|
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: 1355.91 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488390569 1 MLFGRLTERAQRVLAHAQEEAIRLNHSNIGTEHLLLGLMKEPEGIAAKVLESFNITEDKVITEVEKLIGHGQEQAGT--- 77
Cdd:COG0542 1 MNFEKFTEKAQEALEAAQELARRLGHQEVEPEHLLLALLEQGEGLAAKLLRKLGVDLDALREELEEALGRLPKVSGSsgq 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488390569 78 LRYTPRAKKVIELSMDEARKLHHNFVGTEHILLGLIRENEGVAARVFANLDLNITKARAQVVKALGspemGTKNAQTNKS 157
Cdd:COG0542 81 PYLSPRLKRVLELAELEARKLGDEYISTEHLLLALLREGEGVAARILKKLGITLEALREALEELRG----GSRVTSQNPE 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488390569 158 NNTPTLDSLARDLTVIAKDGTLDPVIGRTKEITRVIEVLSRRTKNNPVLIGEPGVGKTAIAEGLAQAIINNEVPETLKDK 237
Cdd:COG0542 157 SKTPALDKYGRDLTELAREGKLDPVIGRDEEIRRVIQILSRRTKNNPVLIGEPGVGKTAIVEGLAQRIVNGDVPESLKDK 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488390569 238 RVMSLDMGTVVAGTKYRGEFEERLKKVMEEIHQ-AGNVILFIDELHTLVGAGGAEGAIDASNILKPALARGELQCIGATT 316
Cdd:COG0542 237 RVLSLDLGALVAGAKYRGEFEERLKAVLDEVKKsEGNIILFIDELHTLVGAGGAEGAMDAANLLKPALARGELRCIGATT 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488390569 317 LDEYRKNIEKDAALERRFQPVQVDEPSVEDTIEILKGLRDRYEAHHRINISDQALDAAAKLSDRYVSDRFLPDKAIDLID 396
Cdd:COG0542 317 LDEYRKYIEKDAALERRFQPVLVEEPSVEDTISILRGLKERYEAHHGVRITDEALVAAVRLSDRYITDRFLPDKAIDLID 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488390569 397 EASSKVRLRSHTTPTNLKSIEQEIETVKKEKDAAVHAQE---FENAANLRDKQSKLEKQYEDAKKEWQNAQGGSN----- 468
Cdd:COG0542 397 EAAARVRMEIDSKPEELDELERRLEQLEIEKEALKKEQDeasFERLAELRDELAELEEELEALKARWEAEKELIEeiqel 476
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488390569 469 ---------------------------------TELSQEDIAEVIAGWTGIPLTKINETESDRLLNLEATLHGRVIGQND 515
Cdd:COG0542 477 keeleqrygkipelekelaeleeelaelapllrEEVTEEDIAEVVSRWTGIPVGKLLEGEREKLLNLEEELHERVIGQDE 556
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488390569 516 AVTSISKAVRRARAGLKDPKRPIGSFIFLGPTGVGKTELARALAETMFGEEDAMIRVDMSEFMEKHAVSRLVGAPPGYVG 595
Cdd:COG0542 557 AVEAVADAIRRSRAGLKDPNRPIGSFLFLGPTGVGKTELAKALAEFLFGDEDALIRIDMSEYMEKHSVSRLIGAPPGYVG 636
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488390569 596 HDDGGQLTEKVRRKPYSVILFDEIEKAHPDVFNILLQVLDDGHLTDTKGRRVDFRNTVIIMTSNVGAQELQDQrfagfgg 675
Cdd:COG0542 637 YEEGGQLTEAVRRRPYSVVLLDEIEKAHPDVFNILLQVLDDGRLTDGQGRTVDFRNTIIIMTSNIGSELILDL------- 709
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488390569 676 ASEGQDYETIRKTMMKELKNAFRPEFLNRVDDIIVFHKLSKDELKEIVTMMVNKLTQRLSEQDIQIEVTDKAKEVIAEEG 755
Cdd:COG0542 710 AEDEPDYEEMKEAVMEELKKHFRPEFLNRIDEIIVFHPLSKEELRKIVDLQLKRLRKRLAERGITLELTDAAKDFLAEKG 789
|
810 820 830 840
....*....|....*....|....*....|....*....|....*..
gi 488390569 756 YDPEYGARPLIRAIQKTVEDNLSELILEGNQIEGKAVTIDHDGTEFK 802
Cdd:COG0542 790 YDPEYGARPLKRAIQRELEDPLAEEILAGEIKEGDTITVDVDDGELV 836
|
|
| clpC |
CHL00095 |
Clp protease ATP binding subunit |
3-795 |
0e+00 |
|
Clp protease ATP binding subunit
Pssm-ID: 214361 [Multi-domain] Cd Length: 821 Bit Score: 1104.35 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488390569 3 FGRLTERAQRVLAHAQEEAIRLNHSNIGTEHLLLGLMKEPEGIAAKVLESFNITEDKVITEVEKLIGHGQE-QAGTLRYT 81
Cdd:CHL00095 2 FERFTEKAIKVIMLSQEEARRLGHNFVGTEQILLGLIGEGTGIAARALKSMGVTLKDARIEVEKIIGRGTGfVAVEIPFT 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488390569 82 PRAKKVIELSMDEARKLHHNFVGTEHILLGLIRENEGVAARVFANLDLNITKARAQVVKALGSPEMGTKNAQTNKSNnTP 161
Cdd:CHL00095 82 PRAKRVLEMSLEEARDLGHNYIGTEHLLLALLEEGEGVAARVLENLGVDLSKIRSLILNLIGEIIEAILGAEQSRSK-TP 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488390569 162 TLDSLARDLTVIAKDGTLDPVIGRTKEITRVIEVLSRRTKNNPVLIGEPGVGKTAIAEGLAQAIINNEVPETLKDKRVMS 241
Cdd:CHL00095 161 TLEEFGTNLTKEAIDGNLDPVIGREKEIERVIQILGRRTKNNPILIGEPGVGKTAIAEGLAQRIVNRDVPDILEDKLVIT 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488390569 242 LDMGTVVAGTKYRGEFEERLKKVMEEIHQAGNVILFIDELHTLVGAGGAEGAIDASNILKPALARGELQCIGATTLDEYR 321
Cdd:CHL00095 241 LDIGLLLAGTKYRGEFEERLKRIFDEIQENNNIILVIDEVHTLIGAGAAEGAIDAANILKPALARGELQCIGATTLDEYR 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488390569 322 KNIEKDAALERRFQPVQVDEPSVEDTIEILKGLRDRYEAHHRINISDQALDAAAKLSDRYVSDRFLPDKAIDLIDEASSK 401
Cdd:CHL00095 321 KHIEKDPALERRFQPVYVGEPSVEETIEILFGLRSRYEKHHNLSISDKALEAAAKLSDQYIADRFLPDKAIDLLDEAGSR 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488390569 402 VRLRSHTTPTNLKSIEQEIETVKKEKDAAVHAQEFENAANLRDKQSKLEKQYEDAKKEWQNAQGGSNTEL--SQEDIAEV 479
Cdd:CHL00095 401 VRLINSRLPPAARELDKELREILKDKDEAIREQDFETAKQLRDREMEVRAQIAAIIQSKKTEEEKRLEVPvvTEEDIAEI 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488390569 480 IAGWTGIPLTKINETESDRLLNLEATLHGRVIGQNDAVTSISKAVRRARAGLKDPKRPIGSFIFLGPTGVGKTELARALA 559
Cdd:CHL00095 481 VSAWTGIPVNKLTKSESEKLLHMEETLHKRIIGQDEAVVAVSKAIRRARVGLKNPNRPIASFLFSGPTGVGKTELTKALA 560
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488390569 560 ETMFGEEDAMIRVDMSEFMEKHAVSRLVGAPPGYVGHDDGGQLTEKVRRKPYSVILFDEIEKAHPDVFNILLQVLDDGHL 639
Cdd:CHL00095 561 SYFFGSEDAMIRLDMSEYMEKHTVSKLIGSPPGYVGYNEGGQLTEAVRKKPYTVVLFDEIEKAHPDIFNLLLQILDDGRL 640
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488390569 640 TDTKGRRVDFRNTVIIMTSNVGAQELQDQRF-AGFGGASEGQD---YETIRKTMMKELKNAFRPEFLNRVDDIIVFHKLS 715
Cdd:CHL00095 641 TDSKGRTIDFKNTLIIMTSNLGSKVIETNSGgLGFELSENQLSekqYKRLSNLVNEELKQFFRPEFLNRLDEIIVFRQLT 720
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488390569 716 KDELKEIVTMMVNKLTQRLSEQDIQIEVTDKAKEVIAEEGYDPEYGARPLIRAIQKTVEDNLSELILEGNQIEGKAVTID 795
Cdd:CHL00095 721 KNDVWEIAEIMLKNLFKRLNEQGIQLEVTERIKTLLIEEGYNPLYGARPLRRAIMRLLEDPLAEEVLSFKIKPGDIIIVD 800
|
|
| 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: 1045.70 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488390569 6 LTERAQRVLAHAQEEAIRLNHSNIGTEHLLLGLMKEPEGIAAKVLESFNITEDKVITEVEKLI-------GHGQEqagtL 78
Cdd:TIGR03346 1 LTEKFQEALQAAQSLALGRDHQQIEPEHLLKALLDQEGGLARPLLQKAGVNVGALRQALEKELerlpkvsGPGGQ----V 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488390569 79 RYTPRAKKVIELSMDEARKLHHNFVGTEHILLGLIRENeGVAARVFANLDLNITKARAQVVKALGSPEMGTKNAQtnksN 158
Cdd:TIGR03346 77 YLSPDLNRLLNLAEKLAQKRGDEFISSEHLLLALLDDK-GTLGKLLKEAGATADALEAAINAVRGGQKVTDANAE----D 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488390569 159 NTPTLDSLARDLTVIAKDGTLDPVIGRTKEITRVIEVLSRRTKNNPVLIGEPGVGKTAIAEGLAQAIINNEVPETLKDKR 238
Cdd:TIGR03346 152 QYEALEKYARDLTERAREGKLDPVIGRDEEIRRTIQVLSRRTKNNPVLIGEPGVGKTAIVEGLAQRIVNGDVPEGLKNKR 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488390569 239 VMSLDMGTVVAGTKYRGEFEERLKKVMEEIHQA-GNVILFIDELHTLVGAGGAEGAIDASNILKPALARGELQCIGATTL 317
Cdd:TIGR03346 232 LLALDMGALIAGAKYRGEFEERLKAVLNEVTKSeGQIILFIDELHTLVGAGKAEGAMDAGNMLKPALARGELHCIGATTL 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488390569 318 DEYRKNIEKDAALERRFQPVQVDEPSVEDTIEILKGLRDRYEAHHRINISDQALDAAAKLSDRYVSDRFLPDKAIDLIDE 397
Cdd:TIGR03346 312 DEYRKYIEKDAALERRFQPVFVDEPSVEDTISILRGLKERYEVHHGVRITDPAIVAAATLSHRYITDRFLPDKAIDLIDE 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488390569 398 ASSKVRLRSHTTPTNLKSIEQEI-------ETVKKEKDAAVHA--QEFENA-ANLRDKQSKLEKQYEDAK---------- 457
Cdd:TIGR03346 392 AAARIRMEIDSKPEELDELDRRIiqleierEALKKEKDEASKKrlEDLEKElADLEEEYAELEEQWKAEKasiqgiqqik 471
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488390569 458 ----------------------------------KEWQNAQGGS--------NTELSQEDIAEVIAGWTGIPLTKINETE 495
Cdd:TIGR03346 472 eeieqvrleleqaeregdlakaaelqygklpeleKQLQAAEQKLgeeqnrllREEVTAEEIAEVVSRWTGIPVSKMLEGE 551
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488390569 496 SDRLLNLEATLHGRVIGQNDAVTSISKAVRRARAGLKDPKRPIGSFIFLGPTGVGKTELARALAETMFGEEDAMIRVDMS 575
Cdd:TIGR03346 552 REKLLHMEEELHERVVGQDEAVEAVSDAIRRSRAGLSDPNRPIGSFLFLGPTGVGKTELAKALAEFLFDSEDAMVRIDMS 631
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488390569 576 EFMEKHAVSRLVGAPPGYVGHDDGGQLTEKVRRKPYSVILFDEIEKAHPDVFNILLQVLDDGHLTDTKGRRVDFRNTVII 655
Cdd:TIGR03346 632 EYMEKHSVARLIGAPPGYVGYEEGGQLTEAVRRRPYSVVLFDEVEKAHPDVFNVLLQVLDDGRLTDGQGRTVDFRNTVII 711
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488390569 656 MTSNVGAQELQDQrfagfggaSEGQDYETIRKTMMKELKNAFRPEFLNRVDDIIVFHKLSKDELKEIVTMMVNKLTQRLS 735
Cdd:TIGR03346 712 MTSNLGSDFIQEL--------AGGDDYEEMREAVMEVLRAHFRPEFLNRIDEIVVFHPLGREQIARIVEIQLGRLRKRLA 783
|
810 820 830 840 850 860
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 488390569 736 EQDIQIEVTDKAKEVIAEEGYDPEYGARPLIRAIQKTVEDNLSELILEGNQIEGKAVTIDHDGTEF 801
Cdd:TIGR03346 784 ERKITLELSDAALDFLAEAGYDPVYGARPLKRAIQREIENPLAKKILAGEVAPGDTIRVDVEGGRL 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: 803.29 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488390569 1 MLFGRLTERAQRVLAHAQEEAIRLNHSNIGTEHLLLGLMKEPEGIAAKVLESFNITEDKVITEVEKLIGHGQEQAGT--- 77
Cdd:PRK10865 1 MRLDRLTNKFQLALADAQSLALGHDNQFIEPLHLMSALLNQEGGSVRPLLTSAGINAGQLRTDINQALSRLPQVEGTggd 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488390569 78 LRYTPRAKKVIELSMDEARKLHHNFVGTEHILLGLIrENEGVAARVFANLDLNITKARAQVVKALGSPEMGTKNAQTNKS 157
Cdd:PRK10865 81 VQPSQDLVRVLNLCDKLAQKRGDNFISSELFVLAAL-ESRGTLADILKAAGATTANITQAIEQMRGGESVNDQGAEDQRQ 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488390569 158 nntpTLDSLARDLTVIAKDGTLDPVIGRTKEITRVIEVLSRRTKNNPVLIGEPGVGKTAIAEGLAQAIINNEVPETLKDK 237
Cdd:PRK10865 160 ----ALKKYTIDLTERAEQGKLDPVIGRDEEIRRTIQVLQRRTKNNPVLIGEPGVGKTAIVEGLAQRIINGEVPEGLKGR 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488390569 238 RVMSLDMGTVVAGTKYRGEFEERLKKVMEEI-HQAGNVILFIDELHTLVGAGGAEGAIDASNILKPALARGELQCIGATT 316
Cdd:PRK10865 236 RVLALDMGALVAGAKYRGEFEERLKGVLNDLaKQEGNVILFIDELHTMVGAGKADGAMDAGNMLKPALARGELHCVGATT 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488390569 317 LDEYRKNIEKDAALERRFQPVQVDEPSVEDTIEILKGLRDRYEAHHRINISDQALDAAAKLSDRYVSDRFLPDKAIDLID 396
Cdd:PRK10865 316 LDEYRQYIEKDAALERRFQKVFVAEPSVEDTIAILRGLKERYELHHHVQITDPAIVAAATLSHRYIADRQLPDKAIDLID 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488390569 397 EASSKVRLRSHTTPTNLKSIEQEI-------ETVKKEKDAAVHAQEFENAANLRDKQ---SKLEKQY------------- 453
Cdd:PRK10865 396 EAASSIRMQIDSKPEELDRLDRRIiqlkleqQALMKESDEASKKRLDMLNEELSDKErqySELEEEWkaekaslsgtqti 475
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488390569 454 ----EDAKKEWQNA------------QGGSNTELSQE----------------------DIAEVIAGWTGIPLTKINETE 495
Cdd:PRK10865 476 kaelEQAKIAIEQArrvgdlarmselQYGKIPELEKQlaaatqlegktmrllrnkvtdaEIAEVLARWTGIPVSRMLESE 555
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488390569 496 SDRLLNLEATLHGRVIGQNDAVTSISKAVRRARAGLKDPKRPIGSFIFLGPTGVGKTELARALAETMFGEEDAMIRVDMS 575
Cdd:PRK10865 556 REKLLRMEQELHHRVIGQNEAVEAVSNAIRRSRAGLSDPNRPIGSFLFLGPTGVGKTELCKALANFMFDSDDAMVRIDMS 635
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488390569 576 EFMEKHAVSRLVGAPPGYVGHDDGGQLTEKVRRKPYSVILFDEIEKAHPDVFNILLQVLDDGHLTDTKGRRVDFRNTVII 655
Cdd:PRK10865 636 EFMEKHSVSRLVGAPPGYVGYEEGGYLTEAVRRRPYSVILLDEVEKAHPDVFNILLQVLDDGRLTDGQGRTVDFRNTVVI 715
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488390569 656 MTSNVGAQELQDqRFAGFggasegqDYETIRKTMMKELKNAFRPEFLNRVDDIIVFHKLSKDELKEIVTMMVNKLTQRLS 735
Cdd:PRK10865 716 MTSNLGSDLIQE-RFGEL-------DYAHMKELVLGVVSHNFRPEFINRIDEVVVFHPLGEQHIASIAQIQLQRLYKRLE 787
|
810 820 830 840 850 860
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 488390569 736 EQDIQIEVTDKAKEVIAEEGYDPEYGARPLIRAIQKTVEDNLSELILEGNQIEGKAVTIDHDG 798
Cdd:PRK10865 788 ERGYEIHISDEALKLLSENGYDPVYGARPLKRAIQQQIENPLAQQILSGELVPGKVIRLEVND 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: 772.66 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488390569 6 LTERAQRVLAHAQEEAIRLNHSNIGTEHLLLGLMKEPEGIAakVLESFNITEDKVITEVEKLIGHG-----QEQAGTLRY 80
Cdd:TIGR02639 1 ISEELERILSDALEEAKERRHEFVTLEHLLLALLDDNEAIE--ILEECGGDVELLRKRLEDYLEENlpvipEDIDEEPEQ 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488390569 81 TPRAKKVIELSMDEARKLHHNFVGTEHILLGLIRENEGVAARVFANLDLN-------ITKARAQVVKALGSPEMGTKNAQ 153
Cdd:TIGR02639 79 TVGVQRVIQRALLHVKSAGKKEIDIGDLLVALFDEEDSHASYFLKSQGITrldilnyISHGISKDDGKDQLGEEAGKEEE 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488390569 154 TNKSnntpTLDSLARDLTVIAKDGTLDPVIGRTKEITRVIEVLSRRTKNNPVLIGEPGVGKTAIAEGLAQAIINNEVPET 233
Cdd:TIGR02639 159 KGQD----ALEKYTVDLTEKAKNGKIDPLIGREDELERTIQVLCRRKKNNPLLVGEPGVGKTAIVEGLALRIAEGKVPER 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488390569 234 LKDKRVMSLDMGTVVAGTKYRGEFEERLKKVMEEIHQAGNVILFIDELHTLVGAG-GAEGAIDASNILKPALARGELQCI 312
Cdd:TIGR02639 235 LKNAKIYSLDMGTLLAGTKYRGDFEERLKAVVSEIEKEPNAILFIDEIHTIVGAGaTSGGSMDASNLLKPALSSGKIRCI 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488390569 313 GATTLDEYRKNIEKDAALERRFQPVQVDEPSVEDTIEILKGLRDRYEAHHRINISDQALDAAAKLSDRYVSDRFLPDKAI 392
Cdd:TIGR02639 315 GSTTYEEYKNHFEKDRALSRRFQKIDVGEPSIEETVKILKGLKEQYEEFHHVKYSDEALEAAVELSARYINDRFLPDKAI 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488390569 393 DLIDEASSKVRLRShttptnlksieqeietvKKEKDAAVhaqefenaanlrdkqsklekqyedakkewqnaqggsntelS 472
Cdd:TIGR02639 395 DVIDEAGAAFRLRP-----------------KAKKKANV----------------------------------------N 417
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488390569 473 QEDIAEVIAGWTGIPLTKINETESDRLLNLEATLHGRVIGQNDAVTSISKAVRRARAGLKDPKRPIGSFIFLGPTGVGKT 552
Cdd:TIGR02639 418 VKDIENVVAKMAKIPVKTVSSDDREQLKNLEKNLKAKIFGQDEAIDQLVSAIKRSRAGLGDPNKPVGSFLFVGPTGVGKT 497
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488390569 553 ELARALAETMfgeEDAMIRVDMSEFMEKHAVSRLVGAPPGYVGHDDGGQLTEKVRRKPYSVILFDEIEKAHPDVFNILLQ 632
Cdd:TIGR02639 498 ELAKQLAEEL---GVHLLRFDMSEYMEKHTVSRLIGSPPGYVGFEQGGLLTDAVRKHPHCVLLLDEIEKAHPDIYNILLQ 574
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488390569 633 VLDDGHLTDTKGRRVDFRNTVIIMTSNVGAQELqDQRFAGFGGasegqdyETIRKTMMKELKNAFRPEFLNRVDDIIVFH 712
Cdd:TIGR02639 575 VMDYATLTDNNGRKADFRNVILIMTSNAGASEM-SKPPIGFGG-------ENRESKSLKAIKKLFSPEFRNRLDAIIHFN 646
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488390569 713 KLSKDELKEIVTMMVNKLTQRLSEQDIQIEVTDKAKEVIAEEGYDPEYGARPLIRAIQKTVEDNLSELILEGNQIEGKAV 792
Cdd:TIGR02639 647 DLSEEMAEKIVKKFLDELQDQLNEKNIELELTDDAKKYLAEKGYDEEFGARPLARVIQEEIKKPLSDEILFGKLKKGGSV 726
|
...
gi 488390569 793 TID 795
Cdd:TIGR02639 727 KIS 729
|
|
| VI_ClpV1 |
TIGR03345 |
type VI secretion ATPase, ClpV1 family; Members of this protein family are homologs of ClpB, ... |
6-783 |
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: 709.02 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488390569 6 LTERAQRVLAHAQEEAIRLNHSNIGTEHLLLGLMKEPEGIAAKVLESFNITEDKVITEVEKLIGhgQEQAGTLRYTPRAK 85
Cdd:TIGR03345 1 LNPTSRRALEQAAALCVARGHPEVELEHWLLALLDQPDSDLAAILRHFGVDLGRLKADLARALD--KLPRGNTRTPVFSP 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488390569 86 KVIEL--------SMDearkLHHNFVGTEHILLGLIRENE--GVAARVFANLD-LNITKARAQVVKAL-GSPE------M 147
Cdd:TIGR03345 79 HLVELlqeawllaSLE----LGDGRIRSGHLLLALLTDPElrRLLGSISPELAkIDREALREALPALVeGSAEasaaaaD 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488390569 148 GTKNAQTNKSNNTPTLDSLARDLTVIAKDGTLDPVIGRTKEITRVIEVLSRRTKNNPVLIGEPGVGKTAIAEGLAQAIIN 227
Cdd:TIGR03345 155 AAPAGAAAGAAGTSALDQYTTDLTAQAREGKIDPVLGRDDEIRQMIDILLRRRQNNPILTGEAGVGKTAVVEGLALRIAA 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488390569 228 NEVPETLKDKRVMSLDMGTVVAGTKYRGEFEERLKKVMEEIHQAGN-VILFIDELHTLVGAGGAEGAIDASNILKPALAR 306
Cdd:TIGR03345 235 GDVPPALRNVRLLSLDLGLLQAGASVKGEFENRLKSVIDEVKASPQpIILFIDEAHTLIGAGGQAGQGDAANLLKPALAR 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488390569 307 GELQCIGATTLDEYRKNIEKDAALERRFQPVQVDEPSVEDTIEILKGLRDRYEAHHRINISDQALDAAAKLSDRYVSDRF 386
Cdd:TIGR03345 315 GELRTIAATTWAEYKKYFEKDPALTRRFQVVKVEEPDEETAIRMLRGLAPVLEKHHGVLILDEAVVAAVELSHRYIPGRQ 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488390569 387 LPDKAIDLIDEASSKVRLRSHTTPTNLKSIEQEIETVKKEKDAAVHAQEF-----ENAANLRDKQSKLEKQYEDAKKEWQ 461
Cdd:TIGR03345 395 LPDKAVSLLDTACARVALSQNATPAALEDLRRRIAALELELDALEREAALgadhdERLAELRAELAALEAELAALEARWQ 474
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488390569 462 ------------------------------------------NAQGGS---NTELSQEDIAEVIAGWTGIPLTKINETES 496
Cdd:TIGR03345 475 qekelveailalraeleadadapaddddalraqlaeleaalaSAQGEEplvFPEVDAQAVAEVVADWTGIPVGRMVRDEI 554
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488390569 497 DRLLNLEATLHGRVIGQNDAVTSISKAVRRARAGLKDPKRPIGSFIFLGPTGVGKTELARALAETMFGEEDAMIRVDMSE 576
Cdd:TIGR03345 555 EAVLSLPDRLAERVIGQDHALEAIAERIRTARAGLEDPRKPLGVFLLVGPSGVGKTETALALAELLYGGEQNLITINMSE 634
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488390569 577 FMEKHAVSRLVGAPPGYVGHDDGGQLTEKVRRKPYSVILFDEIEKAHPDVFNILLQVLDDGHLTDTKGRRVDFRNTVIIM 656
Cdd:TIGR03345 635 FQEAHTVSRLKGSPPGYVGYGEGGVLTEAVRRKPYSVVLLDEVEKAHPDVLELFYQVFDKGVMEDGEGREIDFKNTVILL 714
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488390569 657 TSNVGAQELQDQrfagFGGASEGQDYETIRKTMMKELKNAFRPEFLNRVdDIIVFHKLSKDELKEIVTMMVNKLTQRLSE 736
Cdd:TIGR03345 715 TSNAGSDLIMAL----CADPETAPDPEALLEALRPELLKVFKPAFLGRM-TVIPYLPLDDDVLAAIVRLKLDRIARRLKE 789
|
810 820 830 840
....*....|....*....|....*....|....*....|....*...
gi 488390569 737 Q-DIQIEVTDKAKEVIAEEGYDPEYGARPLIRAIQKTVEDNLSELILE 783
Cdd:TIGR03345 790 NhGAELVYSEALVEHIVARCTEVESGARNIDAILNQTLLPELSRQILE 837
|
|
| clpA |
PRK11034 |
ATP-dependent Clp protease ATP-binding subunit; Provisional |
26-804 |
0e+00 |
|
ATP-dependent Clp protease ATP-binding subunit; Provisional
Pssm-ID: 236828 [Multi-domain] Cd Length: 758 Bit Score: 567.16 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488390569 26 HSNIGTEHLLLGLMKEPEgiAAKVLESFNITEDKVITEVEKLIGH----------GQEQAGTLRYtpraKKVIELSMDEA 95
Cdd:PRK11034 22 HEFMTVEHLLLALLSNPS--AREALEACSVDLVALRQELEAFIEQttpvlpaseeERDTQPTLSF----QRVLQRAVFHV 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488390569 96 RKLHHNFVGTEHILLGLIRENEGVAARVFANLDLnitkARAQVVKAL------GSPEMGTKNAQTNKSNNTPT----LDS 165
Cdd:PRK11034 96 QSSGRSEVTGANVLVAIFSEQESQAAYLLRKHEV----SRLDVVNFIshgtrkDEPSQSSDPGSQPNSEEQAGgeerMEN 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488390569 166 LARDLTVIAKDGTLDPVIGRTKEITRVIEVLSRRTKNNPVLIGEPGVGKTAIAEGLAQAIINNEVPETLKDKRVMSLDMG 245
Cdd:PRK11034 172 FTTNLNQLARVGGIDPLIGREKELERAIQVLCRRRKNNPLLVGESGVGKTAIAEGLAWRIVQGDVPEVMADCTIYSLDIG 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488390569 246 TVVAGTKYRGEFEERLKKVMEEIHQAGNVILFIDELHTLVGAGGAEGA-IDASNILKPALARGELQCIGATTLDEYRKNI 324
Cdd:PRK11034 252 SLLAGTKYRGDFEKRFKALLKQLEQDTNSILFIDEIHTIIGAGAASGGqVDAANLIKPLLSSGKIRVIGSTTYQEFSNIF 331
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488390569 325 EKDAALERRFQPVQVDEPSVEDTIEILKGLRDRYEAHHRINISDQALDAAAKLSDRYVSDRFLPDKAIDLIDEASSKVRL 404
Cdd:PRK11034 332 EKDRALARRFQKIDITEPSIEETVQIINGLKPKYEAHHDVRYTAKAVRAAVELAVKYINDRHLPDKAIDVIDEAGARARL 411
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488390569 405 rshtTPTNlksieqeietvKKEKDAAVhaqefenaanlrdkqsklekqyedakkewqnaqggsntelsqEDIAEVIAGWT 484
Cdd:PRK11034 412 ----MPVS-----------KRKKTVNV------------------------------------------ADIESVVARIA 434
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488390569 485 GIPLTKINETESDRLLNLEATLHGRVIGQNDAVTSISKAVRRARAGLKDPKRPIGSFIFLGPTGVGKTELARALAETMFG 564
Cdd:PRK11034 435 RIPEKSVSQSDRDTLKNLGDRLKMLVFGQDKAIEALTEAIKMSRAGLGHEHKPVGSFLFAGPTGVGKTEVTVQLSKALGI 514
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488390569 565 EedaMIRVDMSEFMEKHAVSRLVGAPPGYVGHDDGGQLTEKVRRKPYSVILFDEIEKAHPDVFNILLQVLDDGHLTDTKG 644
Cdd:PRK11034 515 E---LLRFDMSEYMERHTVSRLIGAPPGYVGFDQGGLLTDAVIKHPHAVLLLDEIEKAHPDVFNLLLQVMDNGTLTDNNG 591
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488390569 645 RRVDFRNTVIIMTSNVGAQELQDQRFagfgGASEgQDYETirkTMMKELKNAFRPEFLNRVDDIIVFHKLSKDELKEIVT 724
Cdd:PRK11034 592 RKADFRNVVLVMTTNAGVRETERKSI----GLIH-QDNST---DAMEEIKKIFTPEFRNRLDNIIWFDHLSTDVIHQVVD 663
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488390569 725 MMVNKLTQRLSEQDIQIEVTDKAKEVIAEEGYDPEYGARPLIRAIQKTVEDNLSELILEGNQIEGKAVTI--DHDGTEFK 802
Cdd:PRK11034 664 KFIVELQAQLDQKGVSLEVSQEARDWLAEKGYDRAMGARPMARVIQDNLKKPLANELLFGSLVDGGQVTValDKEKNELT 743
|
..
gi 488390569 803 YD 804
Cdd:PRK11034 744 YG 745
|
|
| RecA-like_ClpB_Hsp104-like |
cd19499 |
Chaperone protein ClpB/Hsp104 subfamily; Bacterial Caseinolytic peptidase B (ClpB) and ... |
498-711 |
1.34e-105 |
|
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: 321.82 E-value: 1.34e-105
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488390569 498 RLLNLEATLHGRVIGQNDAVTSISKAVRRARAGLKDPKRPIGSFIFLGPTGVGKTELARALAETMFGEEDAMIRVDMSEF 577
Cdd:cd19499 1 KLLNLEERLHERVVGQDEAVKAVSDAIRRARAGLSDPNRPIGSFLFLGPTGVGKTELAKALAELLFGDEDNLIRIDMSEY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488390569 578 MEKHAVSRLVGAPPGYVGHDDGGQLTEKVRRKPYSVILFDEIEKAHPDVFNILLQVLDDGHLTDTKGRRVDFRNTVIIMT 657
Cdd:cd19499 81 MEKHSVSRLIGAPPGYVGYTEGGQLTEAVRRKPYSVVLLDEIEKAHPDVQNLLLQVLDDGRLTDSHGRTVDFKNTIIIMT 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 488390569 658 SnvgaqelqdqrfagfggasegqdyetirktmmkelkNAFRPEFLNRVDDIIVF 711
Cdd:cd19499 161 S------------------------------------NHFRPEFLNRIDEIVVF 178
|
|
| AAA_2 |
pfam07724 |
AAA domain (Cdc48 subfamily); This Pfam entry includes some of the AAA proteins not detected ... |
536-708 |
1.12e-91 |
|
AAA domain (Cdc48 subfamily); This Pfam entry includes some of the AAA proteins not detected by the pfam00004 model.
Pssm-ID: 400187 [Multi-domain] Cd Length: 168 Bit Score: 285.24 E-value: 1.12e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488390569 536 RPIGSFIFLGPTGVGKTELARALAETMFGEEDAMIRVDMSEFMEKHAVSRLVGAPPGYVGHDDGGQLTEKVRRKPYSVIL 615
Cdd:pfam07724 1 RPIGSFLFLGPTGVGKTELAKALAELLFGDERALIRIDMSEYMEEHSVSRLIGAPPGYVGYEEGGQLTEAVRRKPYSIVL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488390569 616 FDEIEKAHPDVFNILLQVLDDGHLTDTKGRRVDFRNTVIIMTSNVGAQELQDQRFAGfggasEGQDYETIRKTMMKELKN 695
Cdd:pfam07724 81 IDEIEKAHPGVQNDLLQILEGGTLTDKQGRTVDFKNTLFIMTGNFGSEKISDASRLG-----DSPDYELLKEEVMDLLKK 155
|
170
....*....|...
gi 488390569 696 AFRPEFLNRVDDI 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 |
3.80e-46 |
|
AAA lid domain; This entry represents the alpha helical AAA+ lid domain that is found to the C-terminus of AAA domains.
Pssm-ID: 465544 [Multi-domain] Cd Length: 104 Bit Score: 159.96 E-value: 3.80e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488390569 343 SVEDTIEILKGLRDRYEAHHRINISDQALDAAAKLSDRYVSDRFLPDKAIDLIDEASSKVRLRSHTTPTNLKSIEQEIET 422
Cdd:pfam17871 1 SVEEAIEILRGLKPKYEKHHGVRISDEALEAAVKLSKRYITDRFLPDKAIDLLDEACARVRLSQESKPEELEDLERELAK 80
|
90 100
....*....|....*....|....
gi 488390569 423 VKKEKDAAVHAQEFENAANLRDKQ 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 |
9.78e-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: 9.78e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488390569 714 LSKDELKEIVTMMVNKLTQRLSEQDIQIEVTDKAKEVIAEEGYDPEYGARPLIRAIQKTVEDNLSELILEGNQIEGKAVT 793
Cdd:pfam10431 1 LSKEELRKIVDLQLKELQKRLAERGITLELTDAAKDWLAEKGYDPEYGARPLRRAIQREIEDPLAEEILSGELKEGDTVR 80
|
.
gi 488390569 794 I 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 |
1.27e-27 |
|
C-terminal, D2-small domain, of ClpB protein; This is the C-terminal domain of ClpB protein, referred to as the D2-small domain, and is a mixed alpha-beta structure. Compared with the D1-small domain (included in AAA) it lacks the long coiled-coil insertion, and instead of helix C4 contains a beta-strand (e3) that is part of a three stranded beta-pleated sheet. In Thermophilus the whole protein forms a hexamer with the D1-small and D2-small domains located on the outside of the hexamer, with the long coiled-coil being exposed on the surface. The D2-small domain is essential for oligomerisation, forming a tight interface with the D2-large domain of a neighbouring subunit and thereby providing enough binding energy to stabilise the functional assembly. The domain is associated with two Clp_N at the N-terminus as well as AAA and AAA_2.
Pssm-ID: 198154 [Multi-domain] Cd Length: 90 Bit Score: 106.76 E-value: 1.27e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488390569 714 LSKDELKEIVTMMVNKLTQRLSEQDIQIEVTDKAKEVIAEEGYDPEYGARPLIRAIQKTVEDNLSELILEGNQIEGKAVT 793
Cdd:smart01086 1 LDKEDLVRIVDLPLNALQKRLAEKGITLEFTDEALDWLAEKGYDPKYGARPLRRIIQRELEDPLAELILSGELKDGDTVV 80
|
....*....
gi 488390569 794 IDHDGTEFK 802
Cdd:smart01086 81 VDVDDGELV 89
|
|
| AAA |
cd00009 |
The AAA+ (ATPases Associated with a wide variety of cellular Activities) superfamily ... |
183-335 |
5.38e-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: 87.20 E-value: 5.38e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488390569 183 IGRTKEITRVIEVLSRRTKNNPVLIGEPGVGKTAIAEGLAQAIINNEVPetlkdkrVMSLDMGTVVAGTKYRGEFEERLK 262
Cdd:cd00009 1 VGQEEAIEALREALELPPPKNLLLYGPPGTGKTTLARAIANELFRPGAP-------FLYLNASDLLEGLVVAELFGHFLV 73
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 488390569 263 KVMEEI-HQAGNVILFIDELHTLvGAGGAEGAIDASNILKPALA-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 |
1.47e-19 |
|
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: 86.05 E-value: 1.47e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488390569 511 IGQNDAVTSISKAVRRAraglkdPKRPIgsfIFLGPTGVGKTELARALAETMFGEEDAMIRVDMSEFMEKHAVSRLvgap 590
Cdd:cd00009 1 VGQEEAIEALREALELP------PPKNL---LLYGPPGTGKTTLARAIANELFRPGAPFLYLNASDLLEGLVVAEL---- 67
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 488390569 591 pgyVGHDDGGQLTEKVRRKPYSVILFDEIEKAHPDVFNILLQVLDDGHLTdtkgrRVDFRNTVIIMTSN 659
Cdd:cd00009 68 ---FGHFLVRLLFELAEKAKPGVLFIDEIDSLSRGAQNALLRVLETLNDL-----RIDRENVRVIGATN 128
|
|
| AAA_5 |
pfam07728 |
AAA domain (dynein-related subfamily); This Pfam entry includes some of the AAA proteins not ... |
540-671 |
5.16e-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: 5.16e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488390569 540 SFIFLGPTGVGKTELARALAETMFGEEDAMirVDMSEFMEKhavSRLVG----APPGYVGHDdgGQLTEKVRRKpySVIL 615
Cdd:pfam07728 1 GVLLVGPPGTGKTELAERLAAALSNRPVFY--VQLTRDTTE---EDLFGrrniDPGGASWVD--GPLVRAAREG--EIAV 71
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 488390569 616 FDEIEKAHPDVFNILLQVLDDGHLTDTKGR---RVDFRNTVIIMTSNVGAQELQDQRFA 671
Cdd:pfam07728 72 LDEINRANPDVLNSLLSLLDERRLLLPDGGelvKAAPDGFRLIATMNPLDRGLNELSPA 130
|
|
| Clp_N |
pfam02861 |
Clp amino terminal domain, pathogenicity island component; This short domain is found in one ... |
17-69 |
1.01e-14 |
|
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: 68.70 E-value: 1.01e-14
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 488390569 17 AQEEAIRLNHSNIGTEHLLLGLMKEPEGIAAKVLESFNITEDKVITEVEKLIG 69
Cdd:pfam02861 1 AQELARALGHQYIGTEHLLLALLEEDDGLAARLLKKAGVDLDALREAIEKLLG 53
|
|
| AAA |
pfam00004 |
ATPase family associated with various cellular activities (AAA); AAA family proteins often ... |
206-335 |
1.16e-13 |
|
ATPase family associated with various cellular activities (AAA); AAA family proteins often perform chaperone-like functions that assist in the assembly, operation, or disassembly of protein complexes.
Pssm-ID: 459627 [Multi-domain] Cd Length: 130 Bit Score: 68.39 E-value: 1.16e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488390569 206 LIGEPGVGKTAIAEGLAQAIinnevpetlkDKRVMSLDMGTVVAgtKYRGEFEERLKKVMEEIHQAGNVILFIDELHTLV 285
Cdd:pfam00004 3 LYGPPGTGKTTLAKAVAKEL----------GAPFIEISGSELVS--KYVGESEKRLRELFEAAKKLAPCVIFIDEIDALA 70
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 488390569 286 GAGGAEG---AIDASNILKPAL-----ARGELQCIGATTldeyrkNIEK-DAALERRFQ 335
Cdd:pfam00004 71 GSRGSGGdseSRRVVNQLLTELdgftsSNSKVIVIAATN------RPDKlDPALLGRFD 123
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
542-659 |
1.89e-13 |
|
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a variety of cellular activities. This profile/alignment only detects a fraction of this vast family. The poorly conserved N-terminal helix is missing from the alignment.
Pssm-ID: 214640 [Multi-domain] Cd Length: 148 Bit Score: 68.55 E-value: 1.89e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488390569 542 IFLGPTGVGKTELARALAETMFGEEDAMIRVDMSEFMEKHAVSRLVGAPPGYVGHDDGGQ----LTEKVRRKPYSVILFD 617
Cdd:smart00382 6 LIVGPPGSGKTTLARALARELGPPGGGVIYIDGEDILEEVLDQLLLIIVGGKKASGSGELrlrlALALARKLKPDVLILD 85
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 488390569 618 EIEKAHPDVFNILLQVLDDGHLTDTKGRRvdfRNTVIIMTSN 659
Cdd:smart00382 86 EITSLLDAEQEALLLLLEELRLLLLLKSE---KNLTVILTTN 124
|
|
| Clp_N |
pfam02861 |
Clp amino terminal domain, pathogenicity island component; This short domain is found in one ... |
93-143 |
1.73e-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: 59.84 E-value: 1.73e-11
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 488390569 93 DEARKLHHNFVGTEHILLGLIRENEGVAARVFANLDLNITKARAQVVKALG 143
Cdd:pfam02861 3 ELARALGHQYIGTEHLLLALLEEDDGLAARLLKKAGVDLDALREAIEKLLG 53
|
|
| SpoVK |
COG0464 |
AAA+-type ATPase, SpoVK/Ycf46/Vps4 family [Cell wall/membrane/envelope biogenesis, Cell cycle ... |
205-381 |
2.36e-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: 66.47 E-value: 2.36e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488390569 205 VLIGEPGVGKTAIAEGLAQAIinnevpetlkDKRVMSLDMGTVVAgtKYRGEFEERLKKVMEEIHQAGNVILFIDELHTL 284
Cdd:COG0464 195 LLYGPPGTGKTLLARALAGEL----------GLPLIEVDLSDLVS--KYVGETEKNLREVFDKARGLAPCVLFIDEADAL 262
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488390569 285 VGAGGAEGAIDAS---NILKPALA--RGELQCIGATtldeYRK-NIekDAALERRFQ-PVQVDEPSVEDTIEILKG-LRD 356
Cdd:COG0464 263 AGKRGEVGDGVGRrvvNTLLTEMEelRSDVVVIAAT----NRPdLL--DPALLRRFDeIIFFPLPDAEERLEIFRIhLRK 336
|
170 180
....*....|....*....|....*
gi 488390569 357 RYEAhhriniSDQALDAAAKLSDRY 381
Cdd:COG0464 337 RPLD------EDVDLEELAEATEGL 355
|
|
| RecA-like_protease |
cd19481 |
proteases similar to RecA; RecA-like NTPases. This family includes the NTP binding domain of ... |
515-659 |
2.50e-11 |
|
proteases similar to RecA; RecA-like NTPases. This family includes the NTP binding domain of F1 and V1 H(+)ATPases, DnaB and related helicases as well as bacterial RecA and related eukaryotic and archaeal recombinases. This group also includes bacterial conjugation proteins and related DNA transfer proteins involved in type II and type IV secretion.
Pssm-ID: 410889 [Multi-domain] Cd Length: 158 Bit Score: 62.69 E-value: 2.50e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488390569 515 DAVTSISKAVRRARAGLKDPKRPIGSFIFLGPTGVGKTELARALAetmfGEEDA-MIRVDMSEFMEKHavsrlvgappGY 593
Cdd:cd19481 3 ASLREAVEAPRRGSRLRRYGLGLPKGILLYGPPGTGKTLLAKALA----GELGLpLIVVKLSSLLSKY----------VG 68
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 488390569 594 VGHDDGGQLTEKVRRKPYSVILFDEIEKAHPD------------VFNILLQVLDDGHLTDtkgrrvdfrNTVIIMTSN 659
Cdd:cd19481 69 ESEKNLRKIFERARRLAPCILFIDEIDAIGRKrdssgesgelrrVLNQLLTELDGVNSRS---------KVLVIAATN 137
|
|
| AAA |
pfam00004 |
ATPase family associated with various cellular activities (AAA); AAA family proteins often ... |
542-659 |
1.81e-09 |
|
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: 56.45 E-value: 1.81e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488390569 542 IFLGPTGVGKTELARALAETMFGEedaMIRVDMSEFMEKHavsrlVGAPPGYVghddgGQLTEKVRRKPYSVILFDEIEK 621
Cdd:pfam00004 2 LLYGPPGTGKTTLAKAVAKELGAP---FIEISGSELVSKY-----VGESEKRL-----RELFEAAKKLAPCVIFIDEIDA 68
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 488390569 622 AHP-----------DVFNILLQVLDdghltdtkGRRVDFRNTVIIMTSN 659
Cdd:pfam00004 69 LAGsrgsggdsesrRVVNQLLTELD--------GFTSSNSKVIVIAATN 109
|
|
| SpoVK |
COG0464 |
AAA+-type ATPase, SpoVK/Ycf46/Vps4 family [Cell wall/membrane/envelope biogenesis, Cell cycle ... |
525-742 |
8.61e-09 |
|
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: 58.38 E-value: 8.61e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488390569 525 RRARAGLKDPKRpigsFIFLGPTGVGKTELARALAETMFGEedaMIRVDMSEFMEKhavsrlvgappgYVGHddggqlTE 604
Cdd:COG0464 182 LREEYGLPPPRG----LLLYGPPGTGKTLLARALAGELGLP---LIEVDLSDLVSK------------YVGE------TE 236
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488390569 605 K--------VRRKPYSVILFDEIEKAHPD-----------VFNILLQVLDDGHltdtkgrrvdfRNTVIIMTSNvgaqel 665
Cdd:COG0464 237 KnlrevfdkARGLAPCVLFIDEADALAGKrgevgdgvgrrVVNTLLTEMEELR-----------SDVVVIAATN------ 299
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 488390569 666 qdqrfagfggasegqdyetirktmmkeLKNAFRPEFLNRVDDIIVFHKLSKDELKEIVTMMvnkLTQRLSEQDIQIE 742
Cdd:COG0464 300 ---------------------------RPDLLDPALLRRFDEIIFFPLPDAEERLEIFRIH---LRKRPLDEDVDLE 346
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
200-334 |
1.58e-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: 54.30 E-value: 1.58e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488390569 200 TKNNPVLIGEPGVGKTAIAEGLAQAIINNEVPETLKD-----KRVMSLDMGTVVAGTKYRGEFEERLKKVMEEIHQAGNV 274
Cdd:smart00382 1 PGEVILIVGPPGSGKTTLARALARELGPPGGGVIYIDgedilEEVLDQLLLIIVGGKKASGSGELRLRLALALARKLKPD 80
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 488390569 275 ILFIDELHTLVGAG--GAEGAIDASNILKPALARGELQCIGATTldeyRKNIEKDAALERRF 334
Cdd:smart00382 81 VLILDEITSLLDAEqeALLLLLEELRLLLLLKSEKNLTVILTTN----DEKDLGPALLRRRF 138
|
|
| RecA-like_protease |
cd19481 |
proteases similar to RecA; RecA-like NTPases. This family includes the NTP binding domain of ... |
206-312 |
3.53e-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: 50.74 E-value: 3.53e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488390569 206 LIGEPGVGKTAIAEGLAQaiinnevpETLKDkrVMSLDMGTVVagTKYRGEFEERLKKVMEEIHQAGNVILFIDELHTLV 285
Cdd:cd19481 31 LYGPPGTGKTLLAKALAG--------ELGLP--LIVVKLSSLL--SKYVGESEKNLRKIFERARRLAPCILFIDEIDAIG 98
|
90 100
....*....|....*....|....*..
gi 488390569 286 GAGGAEGAIDASNILKPALargeLQCI 312
Cdd:cd19481 99 RKRDSSGESGELRRVLNQL----LTEL 121
|
|
| RecA-like_HslU |
cd19498 |
ATP-dependent protease ATPase subunit HslU; HslU is a component of the ATP-dependent protease ... |
510-621 |
4.17e-07 |
|
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: 50.84 E-value: 4.17e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488390569 510 VIGQNDAVTSISKAVR------RARAGLKDPKRPiGSFIFLGPTGVGKTELARALAETMfgeEDAMIRVDMSEFMEKhav 583
Cdd:cd19498 13 IIGQDEAKRAVAIALRnrwrrmQLPEELRDEVTP-KNILMIGPTGVGKTEIARRLAKLA---GAPFIKVEATKFTEV--- 85
|
90 100 110
....*....|....*....|....*....|....*....
gi 488390569 584 srlvgappGYVGHDdggqlTEKVRRKPYSVILF-DEIEK 621
Cdd:cd19498 86 --------GYVGRD-----VESIIRDLVEGIVFiDEIDK 111
|
|
| RPT1 |
COG1222 |
ATP-dependent 26S proteasome regulatory subunit [Posttranslational modification, protein ... |
510-620 |
5.11e-07 |
|
ATP-dependent 26S proteasome regulatory subunit [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440835 [Multi-domain] Cd Length: 326 Bit Score: 52.32 E-value: 5.11e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488390569 510 VIGQNDAVTSISKAVRRaraGLKDP-------KRPIGSFIFLGPTGVGKTELARALAetmfGEEDA-MIRVDMSEFMEKh 581
Cdd:COG1222 80 IGGLDEQIEEIREAVEL---PLKNPelfrkygIEPPKGVLLYGPPGTGKTLLAKAVA----GELGApFIRVRGSELVSK- 151
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 488390569 582 avsrlvgappgYVGhdDGGQLTEKV----RRKPYSVILFDEIE 620
Cdd:COG1222 152 -----------YIG--EGARNVREVfelaREKAPSIIFIDEID 181
|
|
| PRK13342 |
PRK13342 |
recombination factor protein RarA; Reviewed |
178-379 |
7.76e-07 |
|
recombination factor protein RarA; Reviewed
Pssm-ID: 237355 [Multi-domain] Cd Length: 413 Bit Score: 52.39 E-value: 7.76e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488390569 178 TLDPVIGRT------KEITRVIEvlsrrTKNNPVLI--GEPGVGKTAIAEGLAQAIinnevpetlkDKRVMSLDmgTVVA 249
Cdd:PRK13342 10 TLDEVVGQEhllgpgKPLRRMIE-----AGRLSSMIlwGPPGTGKTTLARIIAGAT----------DAPFEALS--AVTS 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488390569 250 GTKyrgefeeRLKKVMEEIHQA----GNVILFIDELHTLvgaggaegaidasN-----ILKPALARGELQCIGATTldEy 320
Cdd:PRK13342 73 GVK-------DLREVIEEARQRrsagRRTILFIDEIHRF-------------NkaqqdALLPHVEDGTITLIGATT--E- 129
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 488390569 321 rkN--IEKDAALERRFQpVQVDEP-SVEDTIEILKglrdRYEAHHR---INISDQALDAAAKLSD 379
Cdd:PRK13342 130 --NpsFEVNPALLSRAQ-VFELKPlSEEDIEQLLK----RALEDKErglVELDDEALDALARLAN 187
|
|
| 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 |
7.11e-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: 46.90 E-value: 7.11e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 488390569 206 LIGEPGVGKTAIAEGLAqaiinNEVpetlkDKRVMSLDMGTVVAgtKYRGEFEERLKKVMEEIHQAGNVILFIDELHTL 284
Cdd:cd19503 39 LHGPPGTGKTLLARAVA-----NEA-----GANFLSISGPSIVS--KYLGESEKNLREIFEEARSHAPSIIFIDEIDAL 105
|
|
| CDC48 |
TIGR01243 |
AAA family ATPase, CDC48 subfamily; This subfamily of the AAA family ATPases includes two ... |
205-624 |
9.20e-06 |
|
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: 49.52 E-value: 9.20e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488390569 205 VLIGEPGVGKTAIAEGLAQAIINNEVpeTLKDKRVMSldmgtvvagtKYRGEFEERLKKVMEEIHQAGNVILFIDELHTL 284
Cdd:TIGR01243 216 LLYGPPGTGKTLLAKAVANEAGAYFI--SINGPEIMS----------KYYGESEERLREIFKEAEENAPSIIFIDEIDAI 283
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488390569 285 V-----GAGGAEGAIDAS--NILKPALARGELQCIGATTldeyRKNiEKDAALER--RF-QPVQVDEPSVEDTIEILKgl 354
Cdd:TIGR01243 284 ApkreeVTGEVEKRVVAQllTLMDGLKGRGRVIVIGATN----RPD-ALDPALRRpgRFdREIVIRVPDKRARKEILK-- 356
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488390569 355 rdrYEAHHRINISDQALDAAAKLSDRYVSdrflPDKAIdLIDEASSKVRLRShttpTNLKSIEQEIETVKKE--KDAAVH 432
Cdd:TIGR01243 357 ---VHTRNMPLAEDVDLDKLAEVTHGFVG----ADLAA-LAKEAAMAALRRF----IREGKINFEAEEIPAEvlKELKVT 424
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488390569 433 AQEFENAANLRDKQSKLEKQYEDAKKEWQNAQGgsnTELSQEDIAEVIAgWtgiPLTKINETEsdrllnleatlhgrvig 512
Cdd:TIGR01243 425 MKDFMEALKMVEPSAIREVLVEVPNVRWSDIGG---LEEVKQELREAVE-W---PLKHPEIFE----------------- 480
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488390569 513 qndavtsiskavrraRAGLKDPKrpiGSFIFlGPTGVGKTELARALAETmfgEEDAMIRVDMSEFMEKhavsrlvgappg 592
Cdd:TIGR01243 481 ---------------KMGIRPPK---GVLLF-GPPGTGKTLLAKAVATE---SGANFIAVRGPEILSK------------ 526
|
410 420 430
....*....|....*....|....*....|....
gi 488390569 593 YVGHDDGG--QLTEKVRRKPYSVILFDEIEKAHP 624
Cdd:TIGR01243 527 WVGESEKAirEIFRKARQAAPAIIFFDEIDAIAP 560
|
|
| AAA_22 |
pfam13401 |
AAA domain; |
540-638 |
1.39e-05 |
|
AAA domain;
Pssm-ID: 379165 [Multi-domain] Cd Length: 129 Bit Score: 45.41 E-value: 1.39e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488390569 540 SFIFL-GPTGVGKTELARALAETMFGEEDAMIRVDMSEFMEK----HAVSRLVGAPPGYVG--HDDGGQLTEKV-RRKPY 611
Cdd:pfam13401 6 GILVLtGESGTGKTTLLRRLLEQLPEVRDSVVFVDLPSGTSPkdllRALLRALGLPLSGRLskEELLAALQQLLlALAVA 85
|
90 100
....*....|....*....|....*..
gi 488390569 612 SVILFDEIEKAHPDVFNILLQVLDDGH 638
Cdd:pfam13401 86 VVLIIDEAQHLSLEALEELRDLLNLSS 112
|
|
| RecA-like_KTNA1 |
cd19522 |
Katanin p60 ATPase-containing subunit A1; Katanin p60 ATPase-containing subunit A1 (KTNA1) is ... |
198-335 |
2.65e-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: 45.36 E-value: 2.65e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488390569 198 RRTKNNPVLIGEPGVGKTAIAEGLAqaiinNEVPETLkdkrvmsLDMGTVVAGTKYRGEFEERLKKVMEEIHQAGNVILF 277
Cdd:cd19522 30 RRPWKGVLMVGPPGTGKTLLAKAVA-----TECGTTF-------FNVSSSTLTSKYRGESEKLVRLLFEMARFYAPTTIF 97
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 488390569 278 IDELHTLVGAGGAEGAIDASNILKPALARGELQCIGATTLDEYRKNI----------EKDAALERRFQ 335
Cdd:cd19522 98 IDEIDSICSRRGTSEEHEASRRVKSELLVQMDGVGGASENDDPSKMVmvlaatnfpwDIDEALRRRLE 165
|
|
| DnaX |
COG2812 |
DNA polymerase III, gamma/tau subunits [Replication, recombination and repair]; |
510-631 |
4.51e-05 |
|
DNA polymerase III, gamma/tau subunits [Replication, recombination and repair];
Pssm-ID: 442061 [Multi-domain] Cd Length: 340 Bit Score: 46.34 E-value: 4.51e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488390569 510 VIGQNDAVTSISKAVRRARaglkdpkrpIG-SFIFLGPTGVGKTELARALAETMFGEE----------------DAMIRV 572
Cdd:COG2812 12 VVGQEHVVRTLKNALASGR---------LAhAYLFTGPRGVGKTTLARILAKALNCENgptgepcgecescraiAAGSHP 82
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 488390569 573 DMSEfMEKHAVSRLVgappgyvghDDGGQLTEKVRRKPYS----VILFDEIEKAHPDVFNILL 631
Cdd:COG2812 83 DVIE-IDAEASNIGV---------DDIRELIEKVSYAPVEgrykVYIIDEAHMLTTEAFNALL 135
|
|
| RarA |
COG2256 |
Replication-associated recombination protein RarA (DNA-dependent ATPase) [Replication, ... |
178-379 |
8.66e-05 |
|
Replication-associated recombination protein RarA (DNA-dependent ATPase) [Replication, recombination and repair];
Pssm-ID: 441857 [Multi-domain] Cd Length: 439 Bit Score: 45.82 E-value: 8.66e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488390569 178 TLDPVIGRT------KEITRVIEvlsrrTKNNPVLI--GEPGVGKTAIAEGLAQAIinnevpetlkDKRVMSLDmgTVVA 249
Cdd:COG2256 23 TLDEVVGQEhllgpgKPLRRAIE-----AGRLSSMIlwGPPGTGKTTLARLIANAT----------DAEFVALS--AVTS 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488390569 250 GTKyrgefeeRLKKVMEEIHQA----GNVILFIDELHTLvgaggaegaidasN-----ILKPALARGELQCIGATTldEy 320
Cdd:COG2256 86 GVK-------DIREVIEEARERraygRRTILFVDEIHRF-------------NkaqqdALLPHVEDGTITLIGATT--E- 142
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 488390569 321 rkN--IEKDAALERRFQpVQVDEP-SVEDTIEILK-GLRD--RYEAHHRINISDQALDAAAKLSD 379
Cdd:COG2256 143 --NpsFEVNSALLSRCR-VFVLKPlSEEDLEQLLErALADdeRGLGGYKLELDDEALEALARLAD 204
|
|
| COG1223 |
COG1223 |
Predicted ATPase, AAA+ superfamily [General function prediction only]; |
187-352 |
8.68e-05 |
|
Predicted ATPase, AAA+ superfamily [General function prediction only];
Pssm-ID: 440836 [Multi-domain] Cd Length: 246 Bit Score: 44.87 E-value: 8.68e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488390569 187 KEITRVIEVLSRR---------TKNNPVLIGEPGVGKTAIAEGLAQAIinnevpetlkDKRVMSLDMGTVVagTKYRGEF 257
Cdd:COG1223 12 KKLKLIIKELRRRenlrkfglwPPRKILFYGPPGTGKTMLAEALAGEL----------KLPLLTVRLDSLI--GSYLGET 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488390569 258 EERLKKVMEEIHQAGnVILFIDELHTLvgaggaegaidasnilkpALARGELQCIGA---------TTLDEYRKNI---- 324
Cdd:COG1223 80 ARNLRKLFDFARRAP-CVIFFDEFDAI------------------AKDRGDQNDVGEvkrvvnallQELDGLPSGSvvia 140
|
170 180 190
....*....|....*....|....*....|....*
gi 488390569 325 ------EKDAALERRFQPV-QVDEPSVEDTIEILK 352
Cdd:COG1223 141 atnhpeLLDSALWRRFDEViEFPLPDKEERKEILE 175
|
|
| RPT1 |
COG1222 |
ATP-dependent 26S proteasome regulatory subunit [Posttranslational modification, protein ... |
100-379 |
1.50e-04 |
|
ATP-dependent 26S proteasome regulatory subunit [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440835 [Multi-domain] Cd Length: 326 Bit Score: 44.61 E-value: 1.50e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488390569 100 HNFVGTEHILLGLIRENEGVAARVFANLDLNITKARAQVVKALGSPEMGTKNAQTNKSNNTPTLDSLARDLTviakDGTL 179
Cdd:COG1222 2 NDLLTIDENIKALLALIDALQERLGVELALLLQPVKALELLEEAPALLLNDANLTQKRLGTPRGTAVPAESP----DVTF 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488390569 180 DPVIGRTKEITRVIEVLSRRTKNN---------PV----LIGEPGVGKTAIAEGLAQ----AIINNEVPEtlkdkrVMSl 242
Cdd:COG1222 78 DDIGGLDEQIEEIREAVELPLKNPelfrkygiePPkgvlLYGPPGTGKTLLAKAVAGelgaPFIRVRGSE------LVS- 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488390569 243 dmgtvvagtKYRGEFEERLKKVMEEIHQAGNVILFIDELHTLVGAGGAEGAIDASNILKPAL--------ARGELQCIGA 314
Cdd:COG1222 151 ---------KYIGEGARNVREVFELAREKAPSIIFIDEIDAIAARRTDDGTSGEVQRTVNQLlaeldgfeSRGDVLIIAA 221
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 488390569 315 TtldeyrkNIEK--DAALER--RF-QPVQVDEPSVEDTIEILK-GLRDRyeahhriNISDQ-ALDAAAKLSD 379
Cdd:COG1222 222 T-------NRPDllDPALLRpgRFdRVIEVPLPDEEAREEILKiHLRDM-------PLADDvDLDKLAKLTE 279
|
|
| HolB |
COG0470 |
DNA polymerase III, delta prime subunit [Replication, recombination and repair]; |
513-659 |
2.18e-04 |
|
DNA polymerase III, delta prime subunit [Replication, recombination and repair];
Pssm-ID: 440238 [Multi-domain] Cd Length: 289 Bit Score: 44.20 E-value: 2.18e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488390569 513 QNDAVTSISKAVRRARAGlkdpkrpiGSFIFLGPTGVGKTELARALAETMFGEEDAmirvDMSEFMEKHAVSRLVGAPPG 592
Cdd:COG0470 1 QEEAWEQLLAAAESGRLP--------HALLLHGPPGIGKTTLALALARDLLCENPE----GGKACGQCHSRLMAAGNHPD 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488390569 593 Y--VGHDDGG---------QLTEKVRRKPYS----VILFDEIEKAHPDVFNILLQVLDDGHltdtkgrrvdfRNTVIIMT 657
Cdd:COG0470 69 LleLNPEEKSdqigidqirELGEFLSLTPLEggrkVVIIDEADAMNEAAANALLKTLEEPP-----------KNTPFILI 137
|
..
gi 488390569 658 SN 659
Cdd:COG0470 138 AN 139
|
|
| Zeta_toxin |
pfam06414 |
Zeta toxin; This family consists of several bacterial zeta toxin proteins. Zeta toxin is ... |
532-647 |
2.55e-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: 2.55e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488390569 532 KDPKRPIgsFIFL-GPTGVGKTELARALAETMfGEEDAMIRVDMSEFMEKH----AVSRLVGAPPGYVGHDDGGQLTEKV 606
Cdd:pfam06414 6 TSQERPK--AILLgGQPGAGKTELARALLDEL-GRQGNVVRIDPDDFRELHphyrELQAADPKTASEYTQPDASRWVEKL 82
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 488390569 607 RRKP----YSVILfdEIEKAHPDVFNILLQVLDDghltdtKGRRV 647
Cdd:pfam06414 83 LQHAiengYNIIL--EGTLRSPDVAKKIARALKA------AGYRV 119
|
|
| hslU |
PRK05201 |
ATP-dependent protease ATPase subunit HslU; |
510-597 |
4.00e-04 |
|
ATP-dependent protease ATPase subunit HslU;
Pssm-ID: 235364 [Multi-domain] Cd Length: 443 Bit Score: 43.53 E-value: 4.00e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488390569 510 VIGQNDAVTSISKAVR-RAR-----AGLKD---PKrpigSFIFLGPTGVGKTELARALAETMfgeeDA-MIRVDMSEFME 579
Cdd:PRK05201 17 IIGQDDAKRAVAIALRnRWRrmqlpEELRDevtPK----NILMIGPTGVGKTEIARRLAKLA----NApFIKVEATKFTE 88
|
90
....*....|....*...
gi 488390569 580 khaVsrlvgappGYVGHD 597
Cdd:PRK05201 89 ---V--------GYVGRD 95
|
|
| UVR |
pfam02151 |
UvrB/uvrC motif; |
417-452 |
4.06e-04 |
|
UvrB/uvrC motif;
Pssm-ID: 308001 [Multi-domain] Cd Length: 36 Bit Score: 38.53 E-value: 4.06e-04
10 20 30
....*....|....*....|....*....|....*.
gi 488390569 417 EQEIETVKKEKDAAVHAQEFENAANLRDKQSKLEKQ 452
Cdd:pfam02151 1 KKLIKELEEEMEEAAENEDFEKAAKLRDQINALKKQ 36
|
|
| 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 |
4.11e-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: 41.65 E-value: 4.11e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488390569 205 VLIGEPGVGKTAIAEGLAQA------IINNevPEtlkdkrVMSldmgtvvagtKYRGEFEERLKKVMEEIHQAGNVILFI 278
Cdd:cd19519 38 LLYGPPGTGKTLIARAVANEtgafffLING--PE------IMS----------KLAGESESNLRKAFEEAEKNAPAIIFI 99
|
...
gi 488390569 279 DEL 281
Cdd:cd19519 100 DEI 102
|
|
| AAA_5 |
pfam07728 |
AAA domain (dynein-related subfamily); This Pfam entry includes some of the AAA proteins not ... |
205-334 |
4.19e-04 |
|
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: 41.12 E-value: 4.19e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488390569 205 VLIGEPGVGKTAIAEGLAQAIINNEV----------PETLKDKRVMSLDMGTVVAGTkyrgefeerLKKVMEEIHqagnv 274
Cdd:pfam07728 3 LLVGPPGTGKTELAERLAAALSNRPVfyvqltrdttEEDLFGRRNIDPGGASWVDGP---------LVRAAREGE----- 68
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 488390569 275 ILFIDELHtlvgaggaEGAIDASNILKPAL---------ARGELQC------IGATTLDEYRKNIEKDAALERRF 334
Cdd:pfam07728 69 IAVLDEIN--------RANPDVLNSLLSLLderrlllpdGGELVKAapdgfrLIATMNPLDRGLNELSPALRSRF 135
|
|
| McsA |
COG3880 |
Protein-arginine kinase activator protein McsA [Posttranslational modification, protein ... |
414-452 |
6.72e-04 |
|
Protein-arginine kinase activator protein McsA [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 443088 [Multi-domain] Cd Length: 173 Bit Score: 41.42 E-value: 6.72e-04
10 20 30
....*....|....*....|....*....|....*....
gi 488390569 414 KSIEQEIETVKKEKDAAVHAQEFENAANLRDKQSKLEKQ 452
Cdd:COG3880 129 LRIKREIEELKEELQEAVEKEEYEEAAELRDEIRELEKE 167
|
|
| RecA-like_Ycf46-like |
cd19507 |
ATPase domain of Ycf46 and similar ATPase domains; Ycf46 may play a role in the regulation of ... |
206-281 |
7.90e-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: 40.81 E-value: 7.90e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 488390569 206 LIGEPGVGKTAIAEGLAqaiinNEVPETLkdkrvMSLDMGTVVAGtkYRGEFEERLKKVMEEIHQAGNVILFIDEL 281
Cdd:cd19507 36 LVGIQGTGKSLTAKAIA-----GVWQLPL-----LRLDMGRLFGG--LVGESESRLRQMIQTAEAIAPCVLWIDEI 99
|
|
| RecA-like_FtsH |
cd19501 |
ATP-dependent zinc metalloprotease FtsH; FtsH ATPase is a processive, ATP-dependent zinc ... |
531-620 |
9.59e-04 |
|
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: 40.68 E-value: 9.59e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488390569 531 LKDPKR--------PIGsFIFLGPTGVGKTELARALAetmfGEEDA-MIRVDMSEFMEKhavsrLVGappgyVGHDDGGQ 601
Cdd:cd19501 23 LKNPEKftklgakiPKG-VLLVGPPGTGKTLLAKAVA----GEAGVpFFSISGSDFVEM-----FVG-----VGASRVRD 87
|
90
....*....|....*....
gi 488390569 602 LTEKVRRKPYSVILFDEIE 620
Cdd:cd19501 88 LFEQAKKNAPCIVFIDEID 106
|
|
| HslU |
COG1220 |
ATP-dependent protease HslVU (ClpYQ), ATPase subunit HslU [Posttranslational modification, ... |
510-597 |
1.12e-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: 1.12e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488390569 510 VIGQNDAvtsiSKAV--------RRAR--AGLKD---PKrpigSFIFLGPTGVGKTELARALAetmfgeedamirvdmse 576
Cdd:COG1220 17 IIGQDEA----KRAVaialrnrwRRQQlpEELRDeitPK----NILMIGPTGVGKTEIARRLA----------------- 71
|
90 100 110
....*....|....*....|....*....|..
gi 488390569 577 fmekhavsRLVGAP-----------PGYVGHD 597
Cdd:COG1220 72 --------KLANAPfikveatkfteVGYVGRD 95
|
|
| PRK13341 |
PRK13341 |
AAA family ATPase; |
203-373 |
1.37e-03 |
|
AAA family ATPase;
Pssm-ID: 237354 [Multi-domain] Cd Length: 725 Bit Score: 42.35 E-value: 1.37e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488390569 203 NPVLIGEPGVGKTAiaegLAQAIINNevpetlkdKRVMSLDMGTVVAGTKyrgEFEERLKKVMEEIHQAG-NVILFIDEL 281
Cdd:PRK13341 54 SLILYGPPGVGKTT----LARIIANH--------TRAHFSSLNAVLAGVK---DLRAEVDRAKERLERHGkRTILFIDEV 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488390569 282 HTLVGAGGaegaiDAsniLKPALARGELQCIGATTLDEYrknIEKDAALERRFQPVQVDEPSVEDTIEIL-KGLRDRYEA 360
Cdd:PRK13341 119 HRFNKAQQ-----DA---LLPWVENGTITLIGATTENPY---FEVNKALVSRSRLFRLKSLSDEDLHQLLkRALQDKERG 187
|
170
....*....|....*
gi 488390569 361 HH--RINISDQALDA 373
Cdd:PRK13341 188 YGdrKVDLEPEAEKH 202
|
|
| RecA-like_PAN_like |
cd19502 |
proteasome activating nucleotidase PAN and related proteasome subunits; This subfamily ... |
527-620 |
1.58e-03 |
|
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: 40.01 E-value: 1.58e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488390569 527 ARAGLKDPKrpigSFIFLGPTGVGKTELARALAetmfGEEDA-MIRVDMSEFMEKhavsrlvgappgYVGhdDGGQLTEK 605
Cdd:cd19502 30 EELGIEPPK----GVLLYGPPGTGKTLLAKAVA----NHTDAtFIRVVGSELVQK------------YIG--EGARLVRE 87
|
90
....*....|....*....
gi 488390569 606 V----RRKPYSVILFDEIE 620
Cdd:cd19502 88 LfemaREKAPSIIFIDEID 106
|
|
| AAA_16 |
pfam13191 |
AAA ATPase domain; This family of domains contain a P-loop motif that is characteriztic of the ... |
181-225 |
1.61e-03 |
|
AAA ATPase domain; This family of domains contain a P-loop motif that is characteriztic of the AAA superfamily.
Pssm-ID: 433025 [Multi-domain] Cd Length: 167 Bit Score: 40.18 E-value: 1.61e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*...
gi 488390569 181 PVIGRTKEITRVIEVLSRRTKNNP---VLIGEPGVGKTAIAEGLAQAI 225
Cdd:pfam13191 1 RLVGREEELEQLLDALDRVRSGRPpsvLLTGEAGTGKTTLLRELLRAL 48
|
|
| 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 488390569 510 VIGQNDAVTSISKAVR-------RARAGLKDPKRpigsFIFLGPTGVGKTELARALA-ETMFgeedAMIRVDMSEFmekh 581
Cdd:COG1223 4 VVGQEEAKKKLKLIIKelrrrenLRKFGLWPPRK----ILFYGPPGTGKTMLAEALAgELKL----PLLTVRLDSL---- 71
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 488390569 582 aVSRLVGappgyvghdDGG----QLTEKVRRKPySVILFDEIE---------KAHPD---VFNILLQVLDD 636
Cdd:COG1223 72 -IGSYLG---------ETArnlrKLFDFARRAP-CVIFFDEFDaiakdrgdqNDVGEvkrVVNALLQELDG 131
|
|
| MoxR |
COG0714 |
MoxR-like ATPase [General function prediction only]; MoxR-like ATPase is part of the Pathway ... |
182-225 |
1.76e-03 |
|
MoxR-like ATPase [General function prediction only]; MoxR-like ATPase is part of the Pathway/BioSystem: Cobalamine/B12 biosynthesis
Pssm-ID: 440478 [Multi-domain] Cd Length: 292 Bit Score: 41.31 E-value: 1.76e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 488390569 182 VIGRTKEITRV-IEVLSRRtknnPVLI-GEPGVGKTAIAEGLAQAI 225
Cdd:COG0714 14 YVGQEELIELVlIALLAGG----HLLLeGVPGVGKTTLAKALARAL 55
|
|
| RecA-like_Lon |
cd19500 |
lon protease homolog 2 peroxisomal; Lon protease (also known as Lon peptidase) is an ... |
530-635 |
1.98e-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: 39.85 E-value: 1.98e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488390569 530 GLKDPKRPIGSFI---------------FLGPTGVGKTELARALAETMfGEEDAMIRV-DMSEFMEKHAVSR-LVGAPPG 592
Cdd:cd19500 14 GLEDVKERILEYLavrklkgsmkgpilcLVGPPGVGKTSLGKSIARAL-GRKFVRISLgGVRDEAEIRGHRRtYVGAMPG 92
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 488390569 593 YVghddgGQLTEKVRRK-PysVILFDEIEK----AHPDVFNILLQVLD 635
Cdd:cd19500 93 RI-----IQALKKAGTNnP--VFLLDEIDKigssFRGDPASALLEVLD 133
|
|
| RecA-like_VPS4 |
cd19521 |
ATPase domain of vacuolar protein sorting-associated protein 4; Vacuolar protein ... |
205-335 |
2.14e-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: 39.85 E-value: 2.14e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488390569 205 VLIGEPGVGKTAIAEGLAqaiinnevpeTLKDKRVMSLDMGTVVagTKYRGEFEERLKKVMEEIHQAGNVILFIDELHTL 284
Cdd:cd19521 44 LLYGPPGTGKSYLAKAVA----------TEANSTFFSVSSSDLV--SKWMGESEKLVKQLFAMARENKPSIIFIDEVDSL 111
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 488390569 285 VGAGGaEGAIDASNILKPALARgELQCIGATT---LDEYRKNI--EKDAALERRFQ 335
Cdd:cd19521 112 CGTRG-EGESEASRRIKTELLV-QMNGVGNDSqgvLVLGATNIpwQLDSAIRRRFE 165
|
|
| PRK13342 |
PRK13342 |
recombination factor protein RarA; Reviewed |
510-562 |
3.15e-03 |
|
recombination factor protein RarA; Reviewed
Pssm-ID: 237355 [Multi-domain] Cd Length: 413 Bit Score: 40.84 E-value: 3.15e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 488390569 510 VIGQnDAVTSISKAVRRA-RAGLkdpkrpIGSFIFLGPTGVGKTELARALAETM 562
Cdd:PRK13342 14 VVGQ-EHLLGPGKPLRRMiEAGR------LSSMILWGPPGTGKTTLARIIAGAT 60
|
|
| RecA-like_VCP_r2 |
cd19529 |
second of two ATPase domains of Valosin-containing protein-like ATPase (VAT) and similar ... |
528-624 |
3.60e-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: 39.02 E-value: 3.60e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488390569 528 RAGLKDPKrpigSFIFLGPTGVGKTELARALAEtmfgEEDA-MIRVDMSEFMekhavSRLVGAPPGYVghddgGQLTEKV 606
Cdd:cd19529 21 RLGIRPPK----GILLYGPPGTGKTLLAKAVAT----ESNAnFISVKGPELL-----SKWVGESEKAI-----REIFRKA 82
|
90
....*....|....*...
gi 488390569 607 RRKPYSVILFDEIEKAHP 624
Cdd:cd19529 83 RQVAPCVIFFDEIDSIAP 100
|
|
| RecA-like_ClpX |
cd19497 |
ATP-dependent Clp protease ATP-binding subunit ClpX; ClpX is a component of the ATP-dependent ... |
510-560 |
3.94e-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: 39.89 E-value: 3.94e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 488390569 510 VIGQNDAVTSISKAV----RRARAGLKDPKRPI----GSFIFLGPTGVGKTELARALAE 560
Cdd:cd19497 14 VIGQERAKKVLSVAVynhyKRIRNNLKQKDDDVelekSNILLIGPTGSGKTLLAQTLAK 72
|
|
| clpX |
PRK05342 |
ATP-dependent Clp protease ATP-binding subunit ClpX; |
510-797 |
4.60e-03 |
|
ATP-dependent Clp protease ATP-binding subunit ClpX;
Pssm-ID: 235422 [Multi-domain] Cd Length: 412 Bit Score: 40.14 E-value: 4.60e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488390569 510 VIGQNDAVTSISKAV----RRARAGLKDP------KrpigSFIFL-GPTGVGKTELARALAETM---FgeedAMirVDMS 575
Cdd:PRK05342 73 VIGQERAKKVLSVAVynhyKRLRHGDKKDddvelqK----SNILLiGPTGSGKTLLAQTLARILdvpF----AI--ADAT 142
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488390569 576 EFMEKhavsrlvgappGYVGHD------------DGGqlTEKVRRkpySVILFDEIEK--AHPDVFNI------------ 629
Cdd:PRK05342 143 TLTEA-----------GYVGEDvenillkllqaaDYD--VEKAQR---GIVYIDEIDKiaRKSENPSItrdvsgegvqqa 206
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488390569 630 LLQVLDdG---HLTDTKGRRVDFRNTVIIMTSN---------VGAQELQDQRFA----GFGGASEGQDYETIRKTMMKE- 692
Cdd:PRK05342 207 LLKILE-GtvaSVPPQGGRKHPQQEFIQVDTTNilficggafDGLEKIIKQRLGkkgiGFGAEVKSKKEKRTEGELLKQv 285
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488390569 693 -----LKNAFRPEFLNRVDDIIVFHKLSKDELKEIVTMMVNKLT---QRLSEQD-IQIEVTDKAKEVIAEEGYDPEYGAR 763
Cdd:PRK05342 286 epedlIKFGLIPEFIGRLPVVATLEELDEEALVRILTEPKNALVkqyQKLFEMDgVELEFTDEALEAIAKKAIERKTGAR 365
|
330 340 350
....*....|....*....|....*....|....*
gi 488390569 764 PLiRAIqktVEDNLSELILE-GNQIEGKAVTIDHD 797
Cdd:PRK05342 366 GL-RSI---LEEILLDVMFElPSREDVEKVVITKE 396
|
|
| 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 |
5.42e-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: 5.42e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488390569 527 ARAGLKDPKrpigSFIFLGPTGVGKTELARALAetmfGEEDA-MIRVDMSEFMEKhavsrlvgappgYVGHDDGG--QLT 603
Cdd:cd19511 20 KRLGIRPPK----GVLLYGPPGCGKTLLAKALA----SEAGLnFISVKGPELFSK------------YVGESERAvrEIF 79
|
90
....*....|....*..
gi 488390569 604 EKVRRKPYSVILFDEIE 620
Cdd:cd19511 80 QKARQAAPCIIFFDEID 96
|
|
| RecA-like_VPS4-like |
cd19509 |
ATPase domain of VPS4, ATAD1, K, KTNA1, Spastin, FIGL-1 and similar ATPase domains; This ... |
205-335 |
7.22e-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: 38.10 E-value: 7.22e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488390569 205 VLIGEPGVGKTAIAEGLAqaiinNEVPETLkdkrvMSLDMGTVVAgtKYRGEFEERLKKVMEEIHQAGNVILFIDELHTL 284
Cdd:cd19509 36 LLYGPPGTGKTLLARAVA-----SESGSTF-----FSISASSLVS--KWVGESEKIVRALFALARELQPSIIFIDEIDSL 103
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 488390569 285 VGAGGaEGAIDASNILKPALArgeLQCIGATTLDEYR------KNI--EKDAALERRFQ 335
Cdd:cd19509 104 LSERG-SGEHEASRRVKTEFL---VQMDGVLNKPEDRvlvlgaTNRpwELDEAFLRRFE 158
|
|
| PRK14953 |
PRK14953 |
DNA polymerase III subunits gamma and tau; Provisional |
510-636 |
8.67e-03 |
|
DNA polymerase III subunits gamma and tau; Provisional
Pssm-ID: 237867 [Multi-domain] Cd Length: 486 Bit Score: 39.42 E-value: 8.67e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488390569 510 VIGQNDAVTSISKAVRRARAGlkdpkrpiGSFIFLGPTGVGKTELARALAETM----------FGEEDAMIRVDMSEF-- 577
Cdd:PRK14953 18 VIGQEIVVRILKNAVKLQRVS--------HAYIFAGPRGTGKTTIARILAKVLnclnpqegepCGKCENCVEIDKGSFpd 89
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 488390569 578 -MEKHAVSRLvgappgyvGHDDGGQLTEKVRRKP----YSVILFDEIEKAHPDVFNILLQVLDD 636
Cdd:PRK14953 90 lIEIDAASNR--------GIDDIRALRDAVSYTPikgkYKVYIIDEAHMLTKEAFNALLKTLEE 145
|
|
| |
