|
Name |
Accession |
Description |
Interval |
E-value |
| ClpA |
COG0542 |
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ... |
1-811 |
0e+00 |
|
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440308 [Multi-domain] Cd Length: 836 Bit Score: 1291.96 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1086031431 1 MFERFTDRARRVVVLAQDEARNLNHNYIGTEHLLLGLITEGEGVAAKALDMMNIERDQVREAVIDIIGEGEKP--VEGHI 78
Cdd:COG0542 2 NFEKFTEKAQEALEAAQELARRLGHQEVEPEHLLLALLEQGEGLAAKLLRKLGVDLDALREELEEALGRLPKVsgSSGQP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1086031431 79 PFTPRAKRIFELSLREALQLGHNYIGTEHLLLGLLKEGEGVAAQVLTKLGADLSQVRQAVIQLLSGYQSDGDNREAvgvs 158
Cdd:COG0542 82 YLSPRLKRVLELAELEARKLGDEYISTEHLLLALLREGEGVAARILKKLGITLEALREALEELRGGSRVTSQNPES---- 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1086031431 159 gnpvrdpgqtNSAILEQFGRNLTQAAREGKLDPVIGRKTEMERVMQVLSRRTKNNPVLIGEPGVGKTAVVEGLAQAIVHG 238
Cdd:COG0542 158 ----------KTPALDKYGRDLTELAREGKLDPVIGRDEEIRRVIQILSRRTKNNPVLIGEPGVGKTAIVEGLAQRIVNG 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1086031431 239 DVPETIKDRQIYSLDMGSLVAGSRYRGDFEERLKKVLKEIRTR-GDIILFIDEIHTLVGAGAAEGSIDAAQMLKPMLARG 317
Cdd:COG0542 228 DVPESLKDKRVLSLDLGALVAGAKYRGEFEERLKAVLDEVKKSeGNIILFIDELHTLVGAGGAEGAMDAANLLKPALARG 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1086031431 318 EIQTIGATTLDEYRKHVEKDAALERRFQPVRVEEPSVDETVGILKGLRDRYEAHHRVIITDEAIRAAAELADRYISDRFL 397
Cdd:COG0542 308 ELRCIGATTLDEYRKYIEKDAALERRFQPVLVEEPSVEDTISILRGLKERYEAHHGVRITDEALVAAVRLSDRYITDRFL 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1086031431 398 PDKAIDLMDEAGARLRIARMTAPPELREIDEKIADVRKAKEAAIDDQD---FERAASLRDEEKKLGEERREKEDAWKGgE 474
Cdd:COG0542 388 PDKAIDLIDEAAARVRMEIDSKPEELDELERRLEQLEIEKEALKKEQDeasFERLAELRDELAELEEELEALKARWEA-E 466
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1086031431 475 REEIAEVTEEE---------------------------------------IAEVLAMSTGIPVVKLTQTESAKLLKMEDE 515
Cdd:COG0542 467 KELIEEIQELKeeleqrygkipelekelaeleeelaelapllreevteedIAEVVSRWTGIPVGKLLEGEREKLLNLEEE 546
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1086031431 516 LHKRVIGQEEAVKALSQSIRRTRSGLKDPKRPGGSFIFAGPTGVGKTELAKALAEFLFGDEDALIQIDMSEFSEKHTASR 595
Cdd:COG0542 547 LHERVIGQDEAVEAVADAIRRSRAGLKDPNRPIGSFLFLGPTGVGKTELAKALAEFLFGDEDALIRIDMSEYMEKHSVSR 626
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1086031431 596 LFGAPPGYVGYDEGGQLTEKVRRRPFSVVLFDEVEKAHPDIFNSLLQILEEGHLTDSQGRKVDFKNTVIIMTTNLGTRDI 675
Cdd:COG0542 627 LIGAPPGYVGYEEGGQLTEAVRRRPYSVVLLDEIEKAHPDVFNILLQVLDDGRLTDGQGRTVDFRNTIIIMTSNIGSELI 706
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1086031431 676 NKGVLTGfqsadnltHDYSRMKSKVNEELKQHFRPEFLNRVDDVIVFPPLTKEQITQIVDLMIGRLAERMEDQNMKLQIT 755
Cdd:COG0542 707 LDLAEDE--------PDYEEMKEAVMEELKKHFRPEFLNRIDEIIVFHPLSKEELRKIVDLQLKRLRKRLAERGITLELT 778
|
810 820 830 840 850
....*....|....*....|....*....|....*....|....*....|....*.
gi 1086031431 756 DAARELLADRGYDPVLGARPLRRAIQRDIEDALSERILFGEIMPGQVVTVDVAGEG 811
Cdd:COG0542 779 DAAKDFLAEKGYDPEYGARPLKRAIQRELEDPLAEEILAGEIKEGDTITVDVDDGE 834
|
|
| clpC |
CHL00095 |
Clp protease ATP binding subunit |
1-812 |
0e+00 |
|
Clp protease ATP binding subunit
Pssm-ID: 214361 [Multi-domain] Cd Length: 821 Bit Score: 1065.06 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1086031431 1 MFERFTDRARRVVVLAQDEARNLNHNYIGTEHLLLGLITEGEGVAAKALDMMNIERDQVREAVIDIIGEGEKPVEGHIPF 80
Cdd:CHL00095 1 MFERFTEKAIKVIMLSQEEARRLGHNFVGTEQILLGLIGEGTGIAARALKSMGVTLKDARIEVEKIIGRGTGFVAVEIPF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1086031431 81 TPRAKRIFELSLREALQLGHNYIGTEHLLLGLLKEGEGVAAQVLTKLGADLSQVRQAVIQLLsGYQSDGDNREAVGVSGN 160
Cdd:CHL00095 81 TPRAKRVLEMSLEEARDLGHNYIGTEHLLLALLEEGEGVAARVLENLGVDLSKIRSLILNLI-GEIIEAILGAEQSRSKT 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1086031431 161 PVrdpgqtnsaiLEQFGRNLTQAAREGKLDPVIGRKTEMERVMQVLSRRTKNNPVLIGEPGVGKTAVVEGLAQAIVHGDV 240
Cdd:CHL00095 160 PT----------LEEFGTNLTKEAIDGNLDPVIGREKEIERVIQILGRRTKNNPILIGEPGVGKTAIAEGLAQRIVNRDV 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1086031431 241 PETIKDRQIYSLDMGSLVAGSRYRGDFEERLKKVLKEIRTRGDIILFIDEIHTLVGAGAAEGSIDAAQMLKPMLARGEIQ 320
Cdd:CHL00095 230 PDILEDKLVITLDIGLLLAGTKYRGEFEERLKRIFDEIQENNNIILVIDEVHTLIGAGAAEGAIDAANILKPALARGELQ 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1086031431 321 TIGATTLDEYRKHVEKDAALERRFQPVRVEEPSVDETVGILKGLRDRYEAHHRVIITDEAIRAAAELADRYISDRFLPDK 400
Cdd:CHL00095 310 CIGATTLDEYRKHIEKDPALERRFQPVYVGEPSVEETIEILFGLRSRYEKHHNLSISDKALEAAAKLSDQYIADRFLPDK 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1086031431 401 AIDLMDEAGARLRIARMTAPPELREIDEKIADVRKAKEAAIDDQDFERAASLRDEEKKLGEERREKEDAWKG--GEREEI 478
Cdd:CHL00095 390 AIDLLDEAGSRVRLINSRLPPAARELDKELREILKDKDEAIREQDFETAKQLRDREMEVRAQIAAIIQSKKTeeEKRLEV 469
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1086031431 479 AEVTEEEIAEVLAMSTGIPVVKLTQTESAKLLKMEDELHKRVIGQEEAVKALSQSIRRTRSGLKDPKRPGGSFIFAGPTG 558
Cdd:CHL00095 470 PVVTEEDIAEIVSAWTGIPVNKLTKSESEKLLHMEETLHKRIIGQDEAVVAVSKAIRRARVGLKNPNRPIASFLFSGPTG 549
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1086031431 559 VGKTELAKALAEFLFGDEDALIQIDMSEFSEKHTASRLFGAPPGYVGYDEGGQLTEKVRRRPFSVVLFDEVEKAHPDIFN 638
Cdd:CHL00095 550 VGKTELTKALASYFFGSEDAMIRLDMSEYMEKHTVSKLIGSPPGYVGYNEGGQLTEAVRKKPYTVVLFDEIEKAHPDIFN 629
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1086031431 639 SLLQILEEGHLTDSQGRKVDFKNTVIIMTTNLGTRDINKGVLT-GFQSADNLTHD--YSRMKSKVNEELKQHFRPEFLNR 715
Cdd:CHL00095 630 LLLQILDDGRLTDSKGRTIDFKNTLIIMTSNLGSKVIETNSGGlGFELSENQLSEkqYKRLSNLVNEELKQFFRPEFLNR 709
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1086031431 716 VDDVIVFPPLTKEQITQIVDLMIGRLAERMEDQNMKLQITDAARELLADRGYDPVLGARPLRRAIQRDIEDALSERILFG 795
Cdd:CHL00095 710 LDEIIVFRQLTKNDVWEIAEIMLKNLFKRLNEQGIQLEVTERIKTLLIEEGYNPLYGARPLRRAIMRLLEDPLAEEVLSF 789
|
810
....*....|....*..
gi 1086031431 796 EIMPGQVVTVDVAGEGD 812
Cdd:CHL00095 790 KIKPGDIIIVDVNDEKE 806
|
|
| chaperone_ClpB |
TIGR03346 |
ATP-dependent chaperone ClpB; Members of this protein family are the bacterial ATP-dependent ... |
5-811 |
0e+00 |
|
ATP-dependent chaperone ClpB; Members of this protein family are the bacterial ATP-dependent chaperone ClpB. This protein belongs to the AAA family, ATPases associated with various cellular activities (pfam00004). This molecular chaperone does not act as a protease, but rather serves to disaggregate misfolded and aggregated proteins. [Protein fate, Protein folding and stabilization]
Pssm-ID: 274529 [Multi-domain] Cd Length: 850 Bit Score: 997.93 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1086031431 5 FTDRARRVVVLAQDEARNLNHNYIGTEHLLLGLITEGEGVAAKALDMMNIERDQVREAVIDIIGEGEKpVEGH---IPFT 81
Cdd:TIGR03346 1 LTEKFQEALQAAQSLALGRDHQQIEPEHLLKALLDQEGGLARPLLQKAGVNVGALRQALEKELERLPK-VSGPggqVYLS 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1086031431 82 PRAKRIFELSLREALQLGHNYIGTEHLLLGLLKEGEGvAAQVLTKLGADLSQVRQAVIQLLSGYQSDGDNREAvgvsgnp 161
Cdd:TIGR03346 80 PDLNRLLNLAEKLAQKRGDEFISSEHLLLALLDDKGT-LGKLLKEAGATADALEAAINAVRGGQKVTDANAED------- 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1086031431 162 vrdpgqtNSAILEQFGRNLTQAAREGKLDPVIGRKTEMERVMQVLSRRTKNNPVLIGEPGVGKTAVVEGLAQAIVHGDVP 241
Cdd:TIGR03346 152 -------QYEALEKYARDLTERAREGKLDPVIGRDEEIRRTIQVLSRRTKNNPVLIGEPGVGKTAIVEGLAQRIVNGDVP 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1086031431 242 ETIKDRQIYSLDMGSLVAGSRYRGDFEERLKKVLKEIR-TRGDIILFIDEIHTLVGAGAAEGSIDAAQMLKPMLARGEIQ 320
Cdd:TIGR03346 225 EGLKNKRLLALDMGALIAGAKYRGEFEERLKAVLNEVTkSEGQIILFIDELHTLVGAGKAEGAMDAGNMLKPALARGELH 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1086031431 321 TIGATTLDEYRKHVEKDAALERRFQPVRVEEPSVDETVGILKGLRDRYEAHHRVIITDEAIRAAAELADRYISDRFLPDK 400
Cdd:TIGR03346 305 CIGATTLDEYRKYIEKDAALERRFQPVFVDEPSVEDTISILRGLKERYEVHHGVRITDPAIVAAATLSHRYITDRFLPDK 384
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1086031431 401 AIDLMDEAGARLRIARMTAPPELREID----------------------------------------------------- 427
Cdd:TIGR03346 385 AIDLIDEAAARIRMEIDSKPEELDELDrriiqleierealkkekdeaskkrledlekeladleeeyaeleeqwkaekasi 464
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1086031431 428 -------EKIADVRKAKEAAIDDQDFERAASLR-----DEEKKLGE-ERREKEDAwkggEREEIAEVTEEEIAEVLAMST 494
Cdd:TIGR03346 465 qgiqqikEEIEQVRLELEQAEREGDLAKAAELQygklpELEKQLQAaEQKLGEEQ----NRLLREEVTAEEIAEVVSRWT 540
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1086031431 495 GIPVVKLTQTESAKLLKMEDELHKRVIGQEEAVKALSQSIRRTRSGLKDPKRPGGSFIFAGPTGVGKTELAKALAEFLFG 574
Cdd:TIGR03346 541 GIPVSKMLEGEREKLLHMEEELHERVVGQDEAVEAVSDAIRRSRAGLSDPNRPIGSFLFLGPTGVGKTELAKALAEFLFD 620
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1086031431 575 DEDALIQIDMSEFSEKHTASRLFGAPPGYVGYDEGGQLTEKVRRRPFSVVLFDEVEKAHPDIFNSLLQILEEGHLTDSQG 654
Cdd:TIGR03346 621 SEDAMVRIDMSEYMEKHSVARLIGAPPGYVGYEEGGQLTEAVRRRPYSVVLFDEVEKAHPDVFNVLLQVLDDGRLTDGQG 700
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1086031431 655 RKVDFKNTVIIMTTNLGTRDINKGVLTGfqsadnlthDYSRMKSKVNEELKQHFRPEFLNRVDDVIVFPPLTKEQITQIV 734
Cdd:TIGR03346 701 RTVDFRNTVIIMTSNLGSDFIQELAGGD---------DYEEMREAVMEVLRAHFRPEFLNRIDEIVVFHPLGREQIARIV 771
|
810 820 830 840 850 860 870
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1086031431 735 DLMIGRLAERMEDQNMKLQITDAARELLADRGYDPVLGARPLRRAIQRDIEDALSERILFGEIMPGQVVTVDVAGEG 811
Cdd:TIGR03346 772 EIQLGRLRKRLAERKITLELSDAALDFLAEAGYDPVYGARPLKRAIQREIENPLAKKILAGEVAPGDTIRVDVEGGR 848
|
|
| ClpA |
TIGR02639 |
ATP-dependent Clp protease ATP-binding subunit clpA; [Protein fate, Degradation of proteins, ... |
5-807 |
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: 764.95 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1086031431 5 FTDRARRVVVLAQDEARNLNHNYIGTEHLLLGLIteGEGVAAKALDMMNIERDQVREAVIDIIGEGEKPVEGHIPFTPRA 84
Cdd:TIGR02639 1 ISEELERILSDALEEAKERRHEFVTLEHLLLALL--DDNEAIEILEECGGDVELLRKRLEDYLEENLPVIPEDIDEEPEQ 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1086031431 85 ----KRIFELSLREALQLGHNYIGTEHLLLGLLKEGEGVAAQVLTKLGADLSQVRQAVIQLLSGYQSDGDNREAVGvsgn 160
Cdd:TIGR02639 79 tvgvQRVIQRALLHVKSAGKKEIDIGDLLVALFDEEDSHASYFLKSQGITRLDILNYISHGISKDDGKDQLGEEAG---- 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1086031431 161 pvrDPGQTNSAILEQFGRNLTQAAREGKLDPVIGRKTEMERVMQVLSRRTKNNPVLIGEPGVGKTAVVEGLAQAIVHGDV 240
Cdd:TIGR02639 155 ---KEEEKGQDALEKYTVDLTEKAKNGKIDPLIGREDELERTIQVLCRRKKNNPLLVGEPGVGKTAIVEGLALRIAEGKV 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1086031431 241 PETIKDRQIYSLDMGSLVAGSRYRGDFEERLKKVLKEIRTRGDIILFIDEIHTLVGAGA-AEGSIDAAQMLKPMLARGEI 319
Cdd:TIGR02639 232 PERLKNAKIYSLDMGTLLAGTKYRGDFEERLKAVVSEIEKEPNAILFIDEIHTIVGAGAtSGGSMDASNLLKPALSSGKI 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1086031431 320 QTIGATTLDEYRKHVEKDAALERRFQPVRVEEPSVDETVGILKGLRDRYEAHHRVIITDEAIRAAAELADRYISDRFLPD 399
Cdd:TIGR02639 312 RCIGSTTYEEYKNHFEKDRALSRRFQKIDVGEPSIEETVKILKGLKEQYEEFHHVKYSDEALEAAVELSARYINDRFLPD 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1086031431 400 KAIDLMDEAGARLRiarmtappeLREIDEKIADVrkakeaaiddqdferaaSLRDeekklgeerrekedawkggereeia 479
Cdd:TIGR02639 392 KAIDVIDEAGAAFR---------LRPKAKKKANV-----------------NVKD------------------------- 420
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1086031431 480 evteeeIAEVLAMSTGIPVVKLTQTESAKLLKMEDELHKRVIGQEEAVKALSQSIRRTRSGLKDPKRPGGSFIFAGPTGV 559
Cdd:TIGR02639 421 ------IENVVAKMAKIPVKTVSSDDREQLKNLEKNLKAKIFGQDEAIDQLVSAIKRSRAGLGDPNKPVGSFLFVGPTGV 494
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1086031431 560 GKTELAKALAEFLfgdEDALIQIDMSEFSEKHTASRLFGAPPGYVGYDEGGQLTEKVRRRPFSVVLFDEVEKAHPDIFNS 639
Cdd:TIGR02639 495 GKTELAKQLAEEL---GVHLLRFDMSEYMEKHTVSRLIGSPPGYVGFEQGGLLTDAVRKHPHCVLLLDEIEKAHPDIYNI 571
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1086031431 640 LLQILEEGHLTDSQGRKVDFKNTVIIMTTNLGTRDINKGVLtGFQSadnlthdySRMKSKVNEELKQHFRPEFLNRVDDV 719
Cdd:TIGR02639 572 LLQVMDYATLTDNNGRKADFRNVILIMTSNAGASEMSKPPI-GFGG--------ENRESKSLKAIKKLFSPEFRNRLDAI 642
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1086031431 720 IVFPPLTKEQITQIVDLMIGRLAERMEDQNMKLQITDAARELLADRGYDPVLGARPLRRAIQRDIEDALSERILFGEIMP 799
Cdd:TIGR02639 643 IHFNDLSEEMAEKIVKKFLDELQDQLNEKNIELELTDDAKKYLAEKGYDEEFGARPLARVIQEEIKKPLSDEILFGKLKK 722
|
....*...
gi 1086031431 800 GQVVTVDV 807
Cdd:TIGR02639 723 GGSVKISL 730
|
|
| PRK10865 |
PRK10865 |
ATP-dependent chaperone ClpB; |
3-810 |
0e+00 |
|
ATP-dependent chaperone ClpB;
Pssm-ID: 182791 [Multi-domain] Cd Length: 857 Bit Score: 764.00 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1086031431 3 ERFTDRARRVVVLAQDEARNLNHNYIGTEHLLLGLITEGEGVAAKALDMMNIERDQVREAVIDIIGEGEKpVEG---HIP 79
Cdd:PRK10865 4 DRLTNKFQLALADAQSLALGHDNQFIEPLHLMSALLNQEGGSVRPLLTSAGINAGQLRTDINQALSRLPQ-VEGtggDVQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1086031431 80 FTPRAKRIFELSLREALQLGHNYIGTEHLLLGLLKEGEGVAaQVLTKLGADLSQVRQAVIQLLSGYQSDGDNREavgvsg 159
Cdd:PRK10865 83 PSQDLVRVLNLCDKLAQKRGDNFISSELFVLAALESRGTLA-DILKAAGATTANITQAIEQMRGGESVNDQGAE------ 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1086031431 160 npvrDPGQTnsaiLEQFGRNLTQAAREGKLDPVIGRKTEMERVMQVLSRRTKNNPVLIGEPGVGKTAVVEGLAQAIVHGD 239
Cdd:PRK10865 156 ----DQRQA----LKKYTIDLTERAEQGKLDPVIGRDEEIRRTIQVLQRRTKNNPVLIGEPGVGKTAIVEGLAQRIINGE 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1086031431 240 VPETIKDRQIYSLDMGSLVAGSRYRGDFEERLKKVLKEI-RTRGDIILFIDEIHTLVGAGAAEGSIDAAQMLKPMLARGE 318
Cdd:PRK10865 228 VPEGLKGRRVLALDMGALVAGAKYRGEFEERLKGVLNDLaKQEGNVILFIDELHTMVGAGKADGAMDAGNMLKPALARGE 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1086031431 319 IQTIGATTLDEYRKHVEKDAALERRFQPVRVEEPSVDETVGILKGLRDRYEAHHRVIITDEAIRAAAELADRYISDRFLP 398
Cdd:PRK10865 308 LHCVGATTLDEYRQYIEKDAALERRFQKVFVAEPSVEDTIAILRGLKERYELHHHVQITDPAIVAAATLSHRYIADRQLP 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1086031431 399 DKAIDLMDEAGARLRIARMTAPPELREIDEKIADVRKAKEA---AIDDQDFERAASLRDEEKKLGEERREKEDAWKGGE- 474
Cdd:PRK10865 388 DKAIDLIDEAASSIRMQIDSKPEELDRLDRRIIQLKLEQQAlmkESDEASKKRLDMLNEELSDKERQYSELEEEWKAEKa 467
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1086031431 475 ---------------------------------------------------------REEIAEVTEEEIAEVLAMSTGIP 497
Cdd:PRK10865 468 slsgtqtikaeleqakiaieqarrvgdlarmselqygkipelekqlaaatqlegktmRLLRNKVTDAEIAEVLARWTGIP 547
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1086031431 498 VVKLTQTESAKLLKMEDELHKRVIGQEEAVKALSQSIRRTRSGLKDPKRPGGSFIFAGPTGVGKTELAKALAEFLFGDED 577
Cdd:PRK10865 548 VSRMLESEREKLLRMEQELHHRVIGQNEAVEAVSNAIRRSRAGLSDPNRPIGSFLFLGPTGVGKTELCKALANFMFDSDD 627
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1086031431 578 ALIQIDMSEFSEKHTASRLFGAPPGYVGYDEGGQLTEKVRRRPFSVVLFDEVEKAHPDIFNSLLQILEEGHLTDSQGRKV 657
Cdd:PRK10865 628 AMVRIDMSEFMEKHSVSRLVGAPPGYVGYEEGGYLTEAVRRRPYSVILLDEVEKAHPDVFNILLQVLDDGRLTDGQGRTV 707
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1086031431 658 DFKNTVIIMTTNLGTRDINK--GVLtgfqsadnlthDYSRMKSKVNEELKQHFRPEFLNRVDDVIVFPPLTKEQITQIVD 735
Cdd:PRK10865 708 DFRNTVVIMTSNLGSDLIQErfGEL-----------DYAHMKELVLGVVSHNFRPEFINRIDEVVVFHPLGEQHIASIAQ 776
|
810 820 830 840 850 860 870
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1086031431 736 LMIGRLAERMEDQNMKLQITDAARELLADRGYDPVLGARPLRRAIQRDIEDALSERILFGEIMPGQVVTVDVAGE 810
Cdd:PRK10865 777 IQLQRLYKRLEERGYEIHISDEALKLLSENGYDPVYGARPLKRAIQQQIENPLAQQILSGELVPGKVIRLEVNDD 851
|
|
| VI_ClpV1 |
TIGR03345 |
type VI secretion ATPase, ClpV1 family; Members of this protein family are homologs of ClpB, ... |
25-793 |
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: 675.51 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1086031431 25 HNYIGTEHLLLGLITEGEGVAAKALDMMNIERDQVREAVIDIIGEGEKPVEGHIPFTPrakrIFELSLREA-----LQLG 99
Cdd:TIGR03345 21 HPEVELEHWLLALLDQPDSDLAAILRHFGVDLGRLKADLARALDKLPRGNTRTPVFSP----HLVELLQEAwllasLELG 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1086031431 100 HNYI--GTEHLLLGLLKEGEGVAAQVLTKLGA-DLSQVRQAVIQLLSGyQSDGDNREAVGVSGNPVRDPGQTNSaiLEQF 176
Cdd:TIGR03345 97 DGRIrsGHLLLALLTDPELRRLLGSISPELAKiDREALREALPALVEG-SAEASAAAADAAPAGAAAGAAGTSA--LDQY 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1086031431 177 GRNLTQAAREGKLDPVIGRKTEMERVMQVLSRRTKNNPVLIGEPGVGKTAVVEGLAQAIVHGDVPETIKDRQIYSLDMGS 256
Cdd:TIGR03345 174 TTDLTAQAREGKIDPVLGRDDEIRQMIDILLRRRQNNPILTGEAGVGKTAVVEGLALRIAAGDVPPALRNVRLLSLDLGL 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1086031431 257 LVAGSRYRGDFEERLKKVLKEI-RTRGDIILFIDEIHTLVGAGAAEGSIDAAQMLKPMLARGEIQTIGATTLDEYRKHVE 335
Cdd:TIGR03345 254 LQAGASVKGEFENRLKSVIDEVkASPQPIILFIDEAHTLIGAGGQAGQGDAANLLKPALARGELRTIAATTWAEYKKYFE 333
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1086031431 336 KDAALERRFQPVRVEEPSVDETVGILKGLRDRYEAHHRVIITDEAIRAAAELADRYISDRFLPDKAIDLMDEAGARLRIA 415
Cdd:TIGR03345 334 KDPALTRRFQVVKVEEPDEETAIRMLRGLAPVLEKHHGVLILDEAVVAAVELSHRYIPGRQLPDKAVSLLDTACARVALS 413
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1086031431 416 RMTAPPELREIDEKIADVRK-----AKEAAIDDQDFERAASLRDEEKKLGEERREKEDAW-------------------- 470
Cdd:TIGR03345 414 QNATPAALEDLRRRIAALELeldalEREAALGADHDERLAELRAELAALEAELAALEARWqqekelveailalraelead 493
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1086031431 471 -------------------------KGGEREEIAEVTEEEIAEVLAMSTGIPVVKLTQTESAKLLKMEDELHKRVIGQEE 525
Cdd:TIGR03345 494 adapaddddalraqlaeleaalasaQGEEPLVFPEVDAQAVAEVVADWTGIPVGRMVRDEIEAVLSLPDRLAERVIGQDH 573
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1086031431 526 AVKALSQSIRRTRSGLKDPKRPGGSFIFAGPTGVGKTELAKALAEFLFGDEDALIQIDMSEFSEKHTASRLFGAPPGYVG 605
Cdd:TIGR03345 574 ALEAIAERIRTARAGLEDPRKPLGVFLLVGPSGVGKTETALALAELLYGGEQNLITINMSEFQEAHTVSRLKGSPPGYVG 653
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1086031431 606 YDEGGQLTEKVRRRPFSVVLFDEVEKAHPDIFNSLLQILEEGHLTDSQGRKVDFKNTVIIMTTNLGTRDINKgvltgfQS 685
Cdd:TIGR03345 654 YGEGGVLTEAVRRKPYSVVLLDEVEKAHPDVLELFYQVFDKGVMEDGEGREIDFKNTVILLTSNAGSDLIMA------LC 727
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1086031431 686 ADNLTH-DYSRMKSKVNEELKQHFRPEFLNRVdDVIVFPPLTKEQITQIVDLMIGRLAERMEDQ-NMKLQITDAARELLA 763
Cdd:TIGR03345 728 ADPETApDPEALLEALRPELLKVFKPAFLGRM-TVIPYLPLDDDVLAAIVRLKLDRIARRLKENhGAELVYSEALVEHIV 806
|
810 820 830
....*....|....*....|....*....|
gi 1086031431 764 DRGYDPVLGARPLRRAIQRDIEDALSERIL 793
Cdd:TIGR03345 807 ARCTEVESGARNIDAILNQTLLPELSRQIL 836
|
|
| clpA |
PRK11034 |
ATP-dependent Clp protease ATP-binding subunit; Provisional |
20-819 |
0e+00 |
|
ATP-dependent Clp protease ATP-binding subunit; Provisional
Pssm-ID: 236828 [Multi-domain] Cd Length: 758 Bit Score: 599.90 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1086031431 20 ARNLNHNYIGTEHLLLGLITEGEgvAAKALDMMNIERDQVREavidiigEGEKPVEGHIPFTPRAKRIFE----LSLREA 95
Cdd:PRK11034 17 AREHRHEFMTVEHLLLALLSNPS--AREALEACSVDLVALRQ-------ELEAFIEQTTPVLPASEEERDtqptLSFQRV 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1086031431 96 LQL--------GHNYIGTEHLLLGLLKEGEGVAAQVLTKlgADLSqvRQAVIQLLSGYQSDGDNREAVGVSGNPVRDPGQ 167
Cdd:PRK11034 88 LQRavfhvqssGRSEVTGANVLVAIFSEQESQAAYLLRK--HEVS--RLDVVNFISHGTRKDEPSQSSDPGSQPNSEEQA 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1086031431 168 TNSAILEQFGRNLTQAAREGKLDPVIGRKTEMERVMQVLSRRTKNNPVLIGEPGVGKTAVVEGLAQAIVHGDVPETIKDR 247
Cdd:PRK11034 164 GGEERMENFTTNLNQLARVGGIDPLIGREKELERAIQVLCRRRKNNPLLVGESGVGKTAIAEGLAWRIVQGDVPEVMADC 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1086031431 248 QIYSLDMGSLVAGSRYRGDFEERLKKVLKEIRTRGDIILFIDEIHTLVGAGAAE-GSIDAAQMLKPMLARGEIQTIGATT 326
Cdd:PRK11034 244 TIYSLDIGSLLAGTKYRGDFEKRFKALLKQLEQDTNSILFIDEIHTIIGAGAASgGQVDAANLIKPLLSSGKIRVIGSTT 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1086031431 327 LDEYRKHVEKDAALERRFQPVRVEEPSVDETVGILKGLRDRYEAHHRVIITDEAIRAAAELADRYISDRFLPDKAIDLMD 406
Cdd:PRK11034 324 YQEFSNIFEKDRALARRFQKIDITEPSIEETVQIINGLKPKYEAHHDVRYTAKAVRAAVELAVKYINDRHLPDKAIDVID 403
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1086031431 407 EAGARLRIarmtAPPELREIDEKIADvrkakeaaiddqdferaaslrdeekklgeerrekedawkggereeiaevteeeI 486
Cdd:PRK11034 404 EAGARARL----MPVSKRKKTVNVAD-----------------------------------------------------I 426
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1086031431 487 AEVLAMSTGIPVVKLTQTESAKLLKMEDELHKRVIGQEEAVKALSQSIRRTRSGLKDPKRPGGSFIFAGPTGVGKTELAK 566
Cdd:PRK11034 427 ESVVARIARIPEKSVSQSDRDTLKNLGDRLKMLVFGQDKAIEALTEAIKMSRAGLGHEHKPVGSFLFAGPTGVGKTEVTV 506
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1086031431 567 ALAEFLfGDEdaLIQIDMSEFSEKHTASRLFGAPPGYVGYDEGGQLTEKVRRRPFSVVLFDEVEKAHPDIFNSLLQILEE 646
Cdd:PRK11034 507 QLSKAL-GIE--LLRFDMSEYMERHTVSRLIGAPPGYVGFDQGGLLTDAVIKHPHAVLLLDEIEKAHPDVFNLLLQVMDN 583
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1086031431 647 GHLTDSQGRKVDFKNTVIIMTTNLGTRDINKGVLtGFQSADNlTHDysrmkskVNEELKQHFRPEFLNRVDDVIVFPPLT 726
Cdd:PRK11034 584 GTLTDNNGRKADFRNVVLVMTTNAGVRETERKSI-GLIHQDN-STD-------AMEEIKKIFTPEFRNRLDNIIWFDHLS 654
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1086031431 727 KEQITQIVDLMIGRLAERMEDQNMKLQITDAARELLADRGYDPVLGARPLRRAIQRDIEDALSERILFGEIMPGQVVTVD 806
Cdd:PRK11034 655 TDVIHQVVDKFIVELQAQLDQKGVSLEVSQEARDWLAEKGYDRAMGARPMARVIQDNLKKPLANELLFGSLVDGGQVTVA 734
|
810
....*....|...
gi 1086031431 807 VAGEGDQREFTFT 819
Cdd:PRK11034 735 LDKEKNELTYGFQ 747
|
|
| RecA-like_ClpB_Hsp104-like |
cd19499 |
Chaperone protein ClpB/Hsp104 subfamily; Bacterial Caseinolytic peptidase B (ClpB) and ... |
508-722 |
1.24e-102 |
|
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: 314.12 E-value: 1.24e-102
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1086031431 508 KLLKMEDELHKRVIGQEEAVKALSQSIRRTRSGLKDPKRPGGSFIFAGPTGVGKTELAKALAEFLFGDEDALIQIDMSEF 587
Cdd:cd19499 1 KLLNLEERLHERVVGQDEAVKAVSDAIRRARAGLSDPNRPIGSFLFLGPTGVGKTELAKALAELLFGDEDNLIRIDMSEY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1086031431 588 SEKHTASRLFGAPPGYVGYDEGGQLTEKVRRRPFSVVLFDEVEKAHPDIFNSLLQILEEGHLTDSQGRKVDFKNTVIIMT 667
Cdd:cd19499 81 MEKHSVSRLIGAPPGYVGYTEGGQLTEAVRRKPYSVVLLDEIEKAHPDVQNLLLQVLDDGRLTDSHGRTVDFKNTIIIMT 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1086031431 668 TNlgtrdinkgvltgfqsadnlthdysrmkskvneelkqHFRPEFLNRVDDVIVF 722
Cdd:cd19499 161 SN-------------------------------------HFRPEFLNRIDEIVVF 178
|
|
| AAA_2 |
pfam07724 |
AAA domain (Cdc48 subfamily); This Pfam entry includes some of the AAA proteins not detected ... |
546-719 |
1.16e-87 |
|
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: 274.84 E-value: 1.16e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1086031431 546 RPGGSFIFAGPTGVGKTELAKALAEFLFGDEDALIQIDMSEFSEKHTASRLFGAPPGYVGYDEGGQLTEKVRRRPFSVVL 625
Cdd:pfam07724 1 RPIGSFLFLGPTGVGKTELAKALAELLFGDERALIRIDMSEYMEEHSVSRLIGAPPGYVGYEEGGQLTEAVRRKPYSIVL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1086031431 626 FDEVEKAHPDIFNSLLQILEEGHLTDSQGRKVDFKNTVIIMTTNLGTRDINKgvltgfQSADNLTHDYSRMKSKVNEELK 705
Cdd:pfam07724 81 IDEIEKAHPGVQNDLLQILEGGTLTDKQGRTVDFKNTLFIMTGNFGSEKISD------ASRLGDSPDYELLKEEVMDLLK 154
|
170
....*....|....
gi 1086031431 706 QHFRPEFLNRVDDV 719
Cdd:pfam07724 155 KGFIPEFLGRLPII 168
|
|
| AAA_lid_9 |
pfam17871 |
AAA lid domain; This entry represents the alpha helical AAA+ lid domain that is found to the ... |
353-456 |
3.57e-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: 3.57e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1086031431 353 SVDETVGILKGLRDRYEAHHRVIITDEAIRAAAELADRYISDRFLPDKAIDLMDEAGARLRIARMTAPPELREIDEKIAD 432
Cdd:pfam17871 1 SVEEAIEILRGLKPKYEKHHGVRISDEALEAAVKLSKRYITDRFLPDKAIDLLDEACARVRLSQESKPEELEDLERELAK 80
|
90 100
....*....|....*....|....
gi 1086031431 433 VRKAKEAAIDDQDFERAASLRDEE 456
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, ... |
725-805 |
2.61e-32 |
|
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: 119.82 E-value: 2.61e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1086031431 725 LTKEQITQIVDLMIGRLAERMEDQNMKLQITDAARELLADRGYDPVLGARPLRRAIQRDIEDALSERILFGEIMPGQVVT 804
Cdd:pfam10431 1 LSKEELRKIVDLQLKELQKRLAERGITLELTDAAKDWLAEKGYDPEYGARPLRRAIQREIEDPLAEEILSGELKEGDTVR 80
|
.
gi 1086031431 805 V 805
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, ... |
725-811 |
4.94e-30 |
|
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: 113.69 E-value: 4.94e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1086031431 725 LTKEQITQIVDLMIGRLAERMEDQNMKLQITDAARELLADRGYDPVLGARPLRRAIQRDIEDALSERILFGEIMPGQVVT 804
Cdd:smart01086 1 LDKEDLVRIVDLPLNALQKRLAEKGITLEFTDEALDWLAEKGYDPKYGARPLRRIIQRELEDPLAELILSGELKDGDTVV 80
|
....*..
gi 1086031431 805 VDVAGEG 811
Cdd:smart01086 81 VDVDDGE 87
|
|
| AAA |
cd00009 |
The AAA+ (ATPases Associated with a wide variety of cellular Activities) superfamily ... |
521-669 |
3.04e-18 |
|
The AAA+ (ATPases Associated with a wide variety of cellular Activities) superfamily represents an ancient group of ATPases belonging to the ASCE (for additional strand, catalytic E) division of the P-loop NTPase fold. The ASCE division also includes ABC, RecA-like, VirD4-like, PilT-like, and SF1/2 helicases. Members of the AAA+ ATPases function as molecular chaperons, ATPase subunits of proteases, helicases, or nucleic-acid stimulated ATPases. The AAA+ proteins contain several distinct features in addition to the conserved alpha-beta-alpha core domain structure and the Walker A and B motifs of the P-loop NTPases.
Pssm-ID: 99707 [Multi-domain] Cd Length: 151 Bit Score: 82.19 E-value: 3.04e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1086031431 521 IGQEEAVKALSQSIRRtrsglkdpkRPGGSFIFAGPTGVGKTELAKALAEFLFGDEDALIQIDMSEFSEKHTASRLFgap 600
Cdd:cd00009 1 VGQEEAIEALREALEL---------PPPKNLLLYGPPGTGKTTLARAIANELFRPGAPFLYLNASDLLEGLVVAELF--- 68
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1086031431 601 pgyvGYDEGGQLTEKVRRRPFSVVLFDEVEKAHPDIFNSLLQILEEGHLTdsqgrKVDFKNTVIIMTTN 669
Cdd:cd00009 69 ----GHFLVRLLFELAEKAKPGVLFIDEIDSLSRGAQNALLRVLETLNDL-----RIDRENVRVIGATN 128
|
|
| AAA |
cd00009 |
The AAA+ (ATPases Associated with a wide variety of cellular Activities) superfamily ... |
193-345 |
6.91e-18 |
|
The AAA+ (ATPases Associated with a wide variety of cellular Activities) superfamily represents an ancient group of ATPases belonging to the ASCE (for additional strand, catalytic E) division of the P-loop NTPase fold. The ASCE division also includes ABC, RecA-like, VirD4-like, PilT-like, and SF1/2 helicases. Members of the AAA+ ATPases function as molecular chaperons, ATPase subunits of proteases, helicases, or nucleic-acid stimulated ATPases. The AAA+ proteins contain several distinct features in addition to the conserved alpha-beta-alpha core domain structure and the Walker A and B motifs of the P-loop NTPases.
Pssm-ID: 99707 [Multi-domain] Cd Length: 151 Bit Score: 81.42 E-value: 6.91e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1086031431 193 IGRKTEMERVMQVLSRRTKNNPVLIGEPGVGKTAVVEGLAQAIVHGDVPetikdrqIYSLDMGSLVAGSRYRGDFEERLK 272
Cdd:cd00009 1 VGQEEAIEALREALELPPPKNLLLYGPPGTGKTTLARAIANELFRPGAP-------FLYLNASDLLEGLVVAELFGHFLV 73
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1086031431 273 KVLKEIRTRGD-IILFIDEIHTLvGAGAAEGSIDAAQMLKPMLA-RGEIQTIGATTLDEYRKhveKDAALERRFQ 345
Cdd:cd00009 74 RLLFELAEKAKpGVLFIDEIDSL-SRGAQNALLRVLETLNDLRIdRENVRVIGATNRPLLGD---LDRALYDRLD 144
|
|
| Clp_N |
pfam02861 |
Clp amino terminal domain, pathogenicity island component; This short domain is found in one ... |
16-68 |
4.66e-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: 67.16 E-value: 4.66e-14
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 1086031431 16 AQDEARNLNHNYIGTEHLLLGLITEGEGVAAKALDMMNIERDQVREAVIDIIG 68
Cdd:pfam02861 1 AQELARALGHQYIGTEHLLLALLEEDDGLAARLLKKAGVDLDALREAIEKLLG 53
|
|
| AAA |
pfam00004 |
ATPase family associated with various cellular activities (AAA); AAA family proteins often ... |
216-345 |
6.28e-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: 69.16 E-value: 6.28e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1086031431 216 LIGEPGVGKTAVVEGLAQAIvhgdvpetikDRQIYSLDMGSLVagSRYRGDFEERLKKVLKEIRTRGDIILFIDEIHTLV 295
Cdd:pfam00004 3 LYGPPGTGKTTLAKAVAKEL----------GAPFIEISGSELV--SKYVGESEKRLRELFEAAKKLAPCVIFIDEIDALA 70
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 1086031431 296 GAGAAEGSIDA----AQMLKPM----LARGEIQTIGATTldeyrkHVEK-DAALERRFQ 345
Cdd:pfam00004 71 GSRGSGGDSESrrvvNQLLTELdgftSSNSKVIVIAATN------RPDKlDPALLGRFD 123
|
|
| AAA_5 |
pfam07728 |
AAA domain (dynein-related subfamily); This Pfam entry includes some of the AAA proteins not ... |
550-677 |
7.13e-14 |
|
AAA domain (dynein-related subfamily); This Pfam entry includes some of the AAA proteins not detected by the pfam00004 model.
Pssm-ID: 400191 [Multi-domain] Cd Length: 135 Bit Score: 69.24 E-value: 7.13e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1086031431 550 SFIFAGPTGVGKTELAKALAEFLFGDEDALIQIdmsefSEKHTASRLFGappgyvGYDEGGQLTEKVRR------RPFSV 623
Cdd:pfam07728 1 GVLLVGPPGTGKTELAERLAAALSNRPVFYVQL-----TRDTTEEDLFG------RRNIDPGGASWVDGplvraaREGEI 69
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 1086031431 624 VLFDEVEKAHPDIFNSLLQILEEGHLTDSQGR---KVDFKNTVIIMTTNLGTRDINK 677
Cdd:pfam07728 70 AVLDEINRANPDVLNSLLSLLDERRLLLPDGGelvKAAPDGFRLIATMNPLDRGLNE 126
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
547-672 |
1.31e-13 |
|
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a variety of cellular activities. This profile/alignment only detects a fraction of this vast family. The poorly conserved N-terminal helix is missing from the alignment.
Pssm-ID: 214640 [Multi-domain] Cd Length: 148 Bit Score: 68.94 E-value: 1.31e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1086031431 547 PGGSFIFAGPTGVGKTELAKALAEFLFGDEDALIQIDMSEFSEKHTASRLFGAPPGYVGYDEGGQ----LTEKVRRRPFS 622
Cdd:smart00382 1 PGEVILIVGPPGSGKTTLARALARELGPPGGGVIYIDGEDILEEVLDQLLLIIVGGKKASGSGELrlrlALALARKLKPD 80
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 1086031431 623 VVLFDEVEKAHPDIFNSLLQILEEGHLTDsqgRKVDFKNTVIIMTTNLGT 672
Cdd:smart00382 81 VLILDEITSLLDAEQEALLLLLEELRLLL---LLKSEKNLTVILTTNDEK 127
|
|
| SpoVK |
COG0464 |
AAA+-type ATPase, SpoVK/Ycf46/Vps4 family [Cell wall/membrane/envelope biogenesis, Cell cycle ... |
369-740 |
1.27e-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: 67.24 E-value: 1.27e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1086031431 369 EAHHRVIITDEAIRAAAELADRYISDRFLPDKAIDLMDEAGARLRIARMTAPPELREIDEKIADVRKAKEAAIDDQDFER 448
Cdd:COG0464 3 ELLALAVALALALLLLDDAALRLLLLLLLALAAALLLLLLLLLLLLLALLLVELLLLLLSGALAALLLLALLLLALLALL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1086031431 449 AASLRDEEKKLGEERREKEDAWKGGEREEIAEVTEEEIAEVLAMSTGIPVVKLTQTESAKLLKMEDELHKR-----VIGQ 523
Cdd:COG0464 83 AALLSALELLLLGELLLLLLLLLLLLLLLLDLERALLELLRESAEALALAAPLVTYEDIGGLEEELLELREailddLGGL 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1086031431 524 EEAVKALSQSIRRTRSGLKDPKR----PGGSFIFAGPTGVGKTELAKALAEFLFGDedaLIQIDMSEF-------SEKHT 592
Cdd:COG0464 163 EEVKEELRELVALPLKRPELREEyglpPPRGLLLYGPPGTGKTLLARALAGELGLP---LIEVDLSDLvskyvgeTEKNL 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1086031431 593 AsRLFgappgyvgydeggqltEKVRRRPFSVVLFDEVEKAHPD-----------IFNSLLQILEEGHltdsqgrkvdfKN 661
Cdd:COG0464 240 R-EVF----------------DKARGLAPCVLFIDEADALAGKrgevgdgvgrrVVNTLLTEMEELR-----------SD 291
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1086031431 662 TVIIMTTNLgtrdinkgvltgFQSADnlthdysrmkskvneelkqhfrPEFLNRVDDVIVFPPLTKEQITQIVDLMIGR 740
Cdd:COG0464 292 VVVIAATNR------------PDLLD----------------------PALLRRFDEIIFFPLPDAEERLEIFRIHLRK 336
|
|
| DnaX |
COG2812 |
DNA polymerase III, gamma/tau subunits [Replication, recombination and repair]; |
520-646 |
9.53e-11 |
|
DNA polymerase III, gamma/tau subunits [Replication, recombination and repair];
Pssm-ID: 442061 [Multi-domain] Cd Length: 340 Bit Score: 64.06 E-value: 9.53e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1086031431 520 VIGQEEAVKALSQSIRRtrsglkdpKRPGGSFIFAGPTGVGKTELAKALAEFLF----GDEDA----------------- 578
Cdd:COG2812 12 VVGQEHVVRTLKNALAS--------GRLAHAYLFTGPRGVGKTTLARILAKALNcengPTGEPcgecescraiaagshpd 83
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1086031431 579 LIQIDmsefsekHTASRLfgappgyvGYDEGGQLTEKVRRRPFS----VVLFDEVEKAHPDIFNSLLQILEE 646
Cdd:COG2812 84 VIEID-------AEASNI--------GVDDIRELIEKVSYAPVEgrykVYIIDEAHMLTTEAFNALLKTLEE 140
|
|
| RecA-like_protease |
cd19481 |
proteases similar to RecA; RecA-like NTPases. This family includes the NTP binding domain of ... |
524-673 |
1.27e-10 |
|
proteases similar to RecA; RecA-like NTPases. This family includes the NTP binding domain of F1 and V1 H(+)ATPases, DnaB and related helicases as well as bacterial RecA and related eukaryotic and archaeal recombinases. This group also includes bacterial conjugation proteins and related DNA transfer proteins involved in type II and type IV secretion.
Pssm-ID: 410889 [Multi-domain] Cd Length: 158 Bit Score: 60.37 E-value: 1.27e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1086031431 524 EEAVKALSQSIRRTRSGLKDPKrpggSFIFAGPTGVGKTELAKALAEFLFGDedaLIQIDMSEFSEKHtasrlfgappGY 603
Cdd:cd19481 6 REAVEAPRRGSRLRRYGLGLPK----GILLYGPPGTGKTLLAKALAGELGLP---LIVVKLSSLLSKY----------VG 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1086031431 604 VGYDEGGQLTEKVRRRPFSVVLFDEVEKAHPD------------IFNSLLQILEEGHLTDsqgrkvdfkNTVIIMTTNLG 671
Cdd:cd19481 69 ESEKNLRKIFERARRLAPCILFIDEIDAIGRKrdssgesgelrrVLNQLLTELDGVNSRS---------KVLVIAATNRP 139
|
..
gi 1086031431 672 TR 673
Cdd:cd19481 140 DL 141
|
|
| SpoVK |
COG0464 |
AAA+-type ATPase, SpoVK/Ycf46/Vps4 family [Cell wall/membrane/envelope biogenesis, Cell cycle ... |
37-362 |
1.28e-10 |
|
AAA+-type ATPase, SpoVK/Ycf46/Vps4 family [Cell wall/membrane/envelope biogenesis, Cell cycle control, cell division, chromosome partitioning, Signal transduction mechanisms];
Pssm-ID: 440232 [Multi-domain] Cd Length: 397 Bit Score: 64.16 E-value: 1.28e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1086031431 37 LITEGEGVAAKALDMMNIERDQVREAVIDIIGEGEKPVEGHIPFTPRAKRIFELSLREALQLGHNYIGTEHLLLGLLKEG 116
Cdd:COG0464 1 LAELLALAVALALALLLLDDAALRLLLLLLLALAAALLLLLLLLLLLLLALLLVELLLLLLSGALAALLLLALLLLALLA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1086031431 117 EGVAAQVLTKLGADLSQVRQAVIQLLSGYQSDGDNREAVGVSGNPVRDPGQTNSAILEQFGRNLT---QAAREGKLDPVI 193
Cdd:COG0464 81 LLAALLSALELLLLGELLLLLLLLLLLLLLLLDLERALLELLRESAEALALAAPLVTYEDIGGLEeelLELREAILDDLG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1086031431 194 GrkteMERVMQVLSRRT---KNNP--------------VLIGEPGVGKTAVVEGLAQAIvhgdvpetikDRQIYSLDMGS 256
Cdd:COG0464 161 G----LEEVKEELRELValpLKRPelreeyglppprglLLYGPPGTGKTLLARALAGEL----------GLPLIEVDLSD 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1086031431 257 LVagSRYRGDFEERLKKVLKEIRTRGDIILFIDEIHTLVGAGAAEGSIDA----AQMLKPM-LARGEIQTIGATtldeYR 331
Cdd:COG0464 227 LV--SKYVGETEKNLREVFDKARGLAPCVLFIDEADALAGKRGEVGDGVGrrvvNTLLTEMeELRSDVVVIAAT----NR 300
|
330 340 350
....*....|....*....|....*....|..
gi 1086031431 332 KHvEKDAALERRFQ-PVRVEEPSVDETVGILK 362
Cdd:COG0464 301 PD-LLDPALLRRFDeIIFFPLPDAEERLEIFR 331
|
|
| DNA_pol3_delta2 |
pfam13177 |
DNA polymerase III, delta subunit; DNA polymerase III, delta subunit (EC 2.7.7.7) is required ... |
522-669 |
1.48e-10 |
|
DNA polymerase III, delta subunit; DNA polymerase III, delta subunit (EC 2.7.7.7) is required for, along with delta' subunit, the assembly of the processivity factor beta(2) onto primed DNA in the DNA polymerase III holoenzyme-catalyzed reaction. The delta subunit is also known as HolA.
Pssm-ID: 433013 [Multi-domain] Cd Length: 161 Bit Score: 60.30 E-value: 1.48e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1086031431 522 GQEEAVKALSQSIRRtrsglkdpKRPGGSFIFAGPTGVGKTELAKALAEFLFGDED----------ALIQIDMSEFSEKH 591
Cdd:pfam13177 1 GQPEAIQLLQNSLEN--------GRLSHAYLFSGPEGVGKLELALAFAKALFCEEPgddlpcgqcrSCRRIESGNHPDLV 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1086031431 592 TASrlfgappgyvgyDEGG--------QLTEKVRRRPF----SVVLFDEVEKAHPDIFNSLLQILEEGHltdsqgrkvdf 659
Cdd:pfam13177 73 IIE------------PEGQsikidqirELQKEFSKSPYegkkKVYIIEDAEKMTASAANSLLKFLEEPP----------- 129
|
170
....*....|
gi 1086031431 660 KNTVIIMTTN 669
Cdd:pfam13177 130 GNTVIILLTE 139
|
|
| HolB |
COG0470 |
DNA polymerase III, delta prime subunit [Replication, recombination and repair]; |
523-669 |
2.02e-09 |
|
DNA polymerase III, delta prime subunit [Replication, recombination and repair];
Pssm-ID: 440238 [Multi-domain] Cd Length: 289 Bit Score: 59.60 E-value: 2.02e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1086031431 523 QEEAVKALSQSIRRtrsglkdpKRPGGSFIFAGPTGVGKTELAKALAEFLFGDEDAliqidmSEFSEKHTASRLF--GAP 600
Cdd:COG0470 1 QEEAWEQLLAAAES--------GRLPHALLLHGPPGIGKTTLALALARDLLCENPE------GGKACGQCHSRLMaaGNH 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1086031431 601 PGY--VGYDEGG---------QLTEKVRRRPFS----VVLFDEVEKAHPDIFNSLLQILEEGHltdsqgrkvdfKNTVII 665
Cdd:COG0470 67 PDLleLNPEEKSdqigidqirELGEFLSLTPLEggrkVVIIDEADAMNEAAANALLKTLEEPP-----------KNTPFI 135
|
....
gi 1086031431 666 MTTN 669
Cdd:COG0470 136 LIAN 139
|
|
| COG1223 |
COG1223 |
Predicted ATPase, AAA+ superfamily [General function prediction only]; |
520-791 |
1.86e-08 |
|
Predicted ATPase, AAA+ superfamily [General function prediction only];
Pssm-ID: 440836 [Multi-domain] Cd Length: 246 Bit Score: 56.05 E-value: 1.86e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1086031431 520 VIGQEEAVKALSQSIRRTRS-------GLKDPKRpggsFIFAGPTGVGKTELAKALAE-----FLFGDEDALIQIDMSEf 587
Cdd:COG1223 4 VVGQEEAKKKLKLIIKELRRrenlrkfGLWPPRK----ILFYGPPGTGKTMLAEALAGelklpLLTVRLDSLIGSYLGE- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1086031431 588 sekhTASRLfgappgyvgydegGQLTEKVRRRPfSVVLFDEVE---------KAHPD---IFNSLLQILEEGHltdsqgr 655
Cdd:COG1223 79 ----TARNL-------------RKLFDFARRAP-CVIFFDEFDaiakdrgdqNDVGEvkrVVNALLQELDGLP------- 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1086031431 656 kvdfKNTVIIMTTNlgtrdinkgvltgfqsadnlthdysrmkskvneelkqhfRPEFLN-----RVDDVIVFPPLTKEQI 730
Cdd:COG1223 134 ----SGSVVIAATN---------------------------------------HPELLDsalwrRFDEVIEFPLPDKEER 170
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1086031431 731 TQIVDLMIGRLAERMEDQNMKLqitdaARELLADRGYDPV-LGARPLRRAI--------QRDIEDALSER 791
Cdd:COG1223 171 KEILELNLKKFPLPFELDLKKL-----AKKLEGLSGADIEkVLKTALKKAIledrekvtKEDLEEALKQR 235
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
210-344 |
2.02e-07 |
|
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a variety of cellular activities. This profile/alignment only detects a fraction of this vast family. The poorly conserved N-terminal helix is missing from the alignment.
Pssm-ID: 214640 [Multi-domain] Cd Length: 148 Bit Score: 51.22 E-value: 2.02e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1086031431 210 TKNNPVLIGEPGVGKTAVVEGLAQAIV--HGDV----PETIKDrQIYSLDMGSLVAGSRYRGDFEERLKKVLKEIRTRGD 283
Cdd:smart00382 1 PGEVILIVGPPGSGKTTLARALARELGppGGGViyidGEDILE-EVLDQLLLIIVGGKKASGSGELRLRLALALARKLKP 79
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1086031431 284 IILFIDEIHTLVGAG--AAEGSIDAAQMLKPMLARGEIQTIGATTldeyRKHVEKDAALERRF 344
Cdd:smart00382 80 DVLILDEITSLLDAEqeALLLLLEELRLLLLLKSEKNLTVILTTN----DEKDLGPALLRRRF 138
|
|
| PRK08691 |
PRK08691 |
DNA polymerase III subunits gamma and tau; Validated |
520-691 |
1.69e-06 |
|
DNA polymerase III subunits gamma and tau; Validated
Pssm-ID: 236333 [Multi-domain] Cd Length: 709 Bit Score: 51.63 E-value: 1.69e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1086031431 520 VIGQEEAVKALSQSIrrtrsglkDPKRPGGSFIFAGPTGVGKTELAKALAEFL----------FGDEDALIQIDMSEFS- 588
Cdd:PRK08691 18 LVGQEHVVKALQNAL--------DEGRLHHAYLLTGTRGVGKTTIARILAKSLncenaqhgepCGVCQSCTQIDAGRYVd 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1086031431 589 --EKHTASRlfgappgyVGYDEGGQLTEKVRRRP----FSVVLFDEVEKAHPDIFNSLLQILEE--GHL------TDSQG 654
Cdd:PRK08691 90 llEIDAASN--------TGIDNIREVLENAQYAPtagkYKVYIIDEVHMLSKSAFNAMLKTLEEppEHVkfilatTDPHK 161
|
170 180 190
....*....|....*....|....*....|....*..
gi 1086031431 655 RKVdfknTVIIMTTNLGTRDinkgvLTGFQSADNLTH 691
Cdd:PRK08691 162 VPV----TVLSRCLQFVLRN-----MTAQQVADHLAH 189
|
|
| RecA-like_protease |
cd19481 |
proteases similar to RecA; RecA-like NTPases. This family includes the NTP binding domain of ... |
216-325 |
2.05e-06 |
|
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: 48.43 E-value: 2.05e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1086031431 216 LIGEPGVGKTAVVEGLAQaivHGDVPEtikdrqiYSLDMGSLVagSRYRGDFEERLKKVLKEIRTRGDIILFIDEIHTLV 295
Cdd:cd19481 31 LYGPPGTGKTLLAKALAG---ELGLPL-------IVVKLSSLL--SKYVGESEKNLRKIFERARRLAPCILFIDEIDAIG 98
|
90 100 110
....*....|....*....|....*....|....*...
gi 1086031431 296 GAGAAEGSIDAA--------QMLKPMLARGEIQTIGAT 325
Cdd:cd19481 99 RKRDSSGESGELrrvlnqllTELDGVNSRSKVLVIAAT 136
|
|
| UVR |
pfam02151 |
UvrB/uvrC motif; |
427-462 |
3.00e-06 |
|
UvrB/uvrC motif;
Pssm-ID: 308001 [Multi-domain] Cd Length: 36 Bit Score: 44.31 E-value: 3.00e-06
10 20 30
....*....|....*....|....*....|....*.
gi 1086031431 427 DEKIADVRKAKEAAIDDQDFERAASLRDEEKKLGEE 462
Cdd:pfam02151 1 KKLIKELEEEMEEAAENEDFEKAAKLRDQINALKKQ 36
|
|
| RecA-like_CDC48_NLV2_r1-like |
cd19503 |
first of two ATPase domains of CDC48 and NLV2, and similar ATPase domains; CDC48 in yeast and ... |
216-325 |
3.60e-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: 47.67 E-value: 3.60e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1086031431 216 LIGEPGVGKTAVVEGLAQAIvhgdvpetikDRQIYSLDMGSLVagSRYRGDFEERLKKVLKEIRTRGDIILFIDEIHTLV 295
Cdd:cd19503 39 LHGPPGTGKTLLARAVANEA----------GANFLSISGPSIV--SKYLGESEKNLREIFEEARSHAPSIIFIDEIDALA 106
|
90 100 110
....*....|....*....|....*....|....*...
gi 1086031431 296 -----GAGAAEGSIdAAQMLKPM---LARGEIQTIGAT 325
Cdd:cd19503 107 pkreeDQREVERRV-VAQLLTLMdgmSSRGKVVVIAAT 143
|
|
| AAA |
pfam00004 |
ATPase family associated with various cellular activities (AAA); AAA family proteins often ... |
552-669 |
4.62e-06 |
|
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: 46.82 E-value: 4.62e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1086031431 552 IFAGPTGVGKTELAKALAEFLFGDedaLIQIDMSEFSEKhtasrlfgappgYVGYDEGG--QLTEKVRRRPFSVVLFDEV 629
Cdd:pfam00004 2 LLYGPPGTGKTTLAKAVAKELGAP---FIEISGSELVSK------------YVGESEKRlrELFEAAKKLAPCVIFIDEI 66
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 1086031431 630 EKAHP-----------DIFNSLLQILEeghltdsqGRKVDFKNTVIIMTTN 669
Cdd:pfam00004 67 DALAGsrgsggdsesrRVVNQLLTELD--------GFTSSNSKVIVIAATN 109
|
|
| RecA-like_HslU |
cd19498 |
ATP-dependent protease ATPase subunit HslU; HslU is a component of the ATP-dependent protease ... |
514-631 |
6.31e-06 |
|
ATP-dependent protease ATPase subunit HslU; HslU is a component of the ATP-dependent protease HslVU. In HslVU, HslU ATPase serves to unfold and translocate protein substrate, and the HslV protease degrades the unfolded proteins. This RecA-like_HslU subfamily belongs to the RecA-like NTPase family which includes the NTP binding domain of F1 and V1 H(+)ATPases, DnaB and related helicases as well as bacterial RecA and related eukaryotic and archaeal recombinases. The RecA-like NTPase family also includes bacterial conjugation proteins and related DNA transfer proteins involved in type II and type IV secretion.
Pssm-ID: 410906 [Multi-domain] Cd Length: 183 Bit Score: 47.37 E-value: 6.31e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1086031431 514 DELHKRVIGQEEAVK----ALSQSIRRTR--SGLKDPKRPGgSFIFAGPTGVGKTELAKALAEFLfgdEDALIQIDMSEF 587
Cdd:cd19498 7 SELDKYIIGQDEAKRavaiALRNRWRRMQlpEELRDEVTPK-NILMIGPTGVGKTEIARRLAKLA---GAPFIKVEATKF 82
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 1086031431 588 SEKhtasrlfgappGYVGYDeggqLTEKVRRRPFSVVLFDEVEK 631
Cdd:cd19498 83 TEV-----------GYVGRD----VESIIRDLVEGIVFIDEIDK 111
|
|
| AAA_5 |
pfam07728 |
AAA domain (dynein-related subfamily); This Pfam entry includes some of the AAA proteins not ... |
215-344 |
1.15e-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: 45.75 E-value: 1.15e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1086031431 215 VLIGEPGVGKTAVVEGLAQAIVhGDVPETIkdrQIYSlDMGS--LVAGSRYRGDFEERLKKVLKEIRTRGDIIlFIDEIH 292
Cdd:pfam07728 3 LLVGPPGTGKTELAERLAAALS-NRPVFYV---QLTR-DTTEedLFGRRNIDPGGASWVDGPLVRAAREGEIA-VLDEIN 76
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 1086031431 293 TLVGAGAAE--GSIDAAQMLKP-----MLARGEIQTIGATTLDEYRKHVEKDAALERRF 344
Cdd:pfam07728 77 RANPDVLNSllSLLDERRLLLPdggelVKAAPDGFRLIATMNPLDRGLNELSPALRSRF 135
|
|
| COG1223 |
COG1223 |
Predicted ATPase, AAA+ superfamily [General function prediction only]; |
189-362 |
1.70e-05 |
|
Predicted ATPase, AAA+ superfamily [General function prediction only];
Pssm-ID: 440836 [Multi-domain] Cd Length: 246 Bit Score: 47.19 E-value: 1.70e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1086031431 189 LDPVIGR---KTEMERVMQVLSRR---------TKNNPVLIGEPGVGKTAVVEGLAQAIvhgDVPetikdrqIYSLDMGS 256
Cdd:COG1223 1 LDDVVGQeeaKKKLKLIIKELRRRenlrkfglwPPRKILFYGPPGTGKTMLAEALAGEL---KLP-------LLTVRLDS 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1086031431 257 LVagSRYRGDFEERLKKVLKEIRTRGDIIlFIDEIHTLvgaGAAEGSIDAA-----------QMLKPMlaRGEIQTIGAT 325
Cdd:COG1223 71 LI--GSYLGETARNLRKLFDFARRAPCVI-FFDEFDAI---AKDRGDQNDVgevkrvvnallQELDGL--PSGSVVIAAT 142
|
170 180 190
....*....|....*....|....*....|....*....
gi 1086031431 326 TldeyrkHVEK-DAALERRFQPV-RVEEPSVDETVGILK 362
Cdd:COG1223 143 N------HPELlDSALWRRFDEViEFPLPDKEERKEILE 175
|
|
| TIGR02928 |
TIGR02928 |
orc1/cdc6 family replication initiation protein; Members of this protein family are found ... |
190-440 |
2.13e-05 |
|
orc1/cdc6 family replication initiation protein; Members of this protein family are found exclusively in the archaea. This set of DNA binding proteins shows homology to the origin recognition complex subunit 1/cell division control protein 6 family in eukaryotes. Several members may be found in genome and interact with each other. [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 274354 [Multi-domain] Cd Length: 365 Bit Score: 47.63 E-value: 2.13e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1086031431 190 DPVIGRKTEMERVMQ----VLSRRTKNNPVLIGEPGVGKTAVVEGL---AQAIVH--GDVPETIK-----DRQIYSLdMG 255
Cdd:TIGR02928 15 DRIVHRDEQIEELAKalrpILRGSRPSNVFIYGKTGTGKTAVTKYVmkeLEEAAEdrDVRVVTVYvncqiLDTLYQV-LV 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1086031431 256 SLVAGSRYRGD--------FEERLKKVLKEIRTRGDIILFI-DEIHTLVGAG----------AAEGSIDAAQmlkpmlar 316
Cdd:TIGR02928 94 ELANQLRGSGEevpttglsTSEVFRRLYKELNERGDSLIIVlDEIDYLVGDDddllyqlsraRSNGDLDNAK-------- 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1086031431 317 geIQTIGATTLDEYRKHVekDAALERRFQPVRVEEPSVDET--VGILKGLRDRyeAHHRVIITDEAIRAAAELADRYISD 394
Cdd:TIGR02928 166 --VGVIGISNDLKFRENL--DPRVKSSLCEEEIIFPPYDAEelRDILENRAEK--AFYDGVLDDGVIPLCAALAAQEHGD 239
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 1086031431 395 -RflpdKAIDLMDEAGarlRIARmtappelREIDEKIA--DVRKAKEAA 440
Cdd:TIGR02928 240 aR----KAIDLLRVAG---EIAE-------REGAERVTedHVEKAQEKI 274
|
|
| RecA-like_ClpX |
cd19497 |
ATP-dependent Clp protease ATP-binding subunit ClpX; ClpX is a component of the ATP-dependent ... |
511-572 |
2.87e-05 |
|
ATP-dependent Clp protease ATP-binding subunit ClpX; ClpX is a component of the ATP-dependent protease ClpXP. In ClpXP, ClpX ATPase serves to specifically recognize, unfold, and translocate protein substrates into the chamber of ClpP protease for degradation. This RecA-like_ClpX domain subfamily belongs to the RecA-like NTPase family which includes the NTP binding domain of F1 and V1 H(+)ATPases, DnaB and related helicases as well as bacterial RecA and related eukaryotic and archaeal recombinases. The RecA-like NTPase family also includes bacterial conjugation proteins and related DNA transfer proteins involved in type II and type IV secretion.
Pssm-ID: 410905 [Multi-domain] Cd Length: 251 Bit Score: 46.44 E-value: 2.87e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1086031431 511 KMEDELHKRVIGQEEAVKALSQSI----RRTRSGLK----DPKRPGGSFIFAGPTGVGKTELAKALAEFL 572
Cdd:cd19497 5 EIKEHLDKYVIGQERAKKVLSVAVynhyKRIRNNLKqkddDVELEKSNILLIGPTGSGKTLLAQTLAKIL 74
|
|
| PRK14969 |
PRK14969 |
DNA polymerase III subunits gamma and tau; Provisional |
521-646 |
3.02e-05 |
|
DNA polymerase III subunits gamma and tau; Provisional
Pssm-ID: 237873 [Multi-domain] Cd Length: 527 Bit Score: 47.44 E-value: 3.02e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1086031431 521 IGQEEAVKALSQSIRRtrsglkdpKRPGGSFIFAGPTGVGKTELAKALAEFL----------FGDEDALIQIDMSEFS-- 588
Cdd:PRK14969 19 VGQEHVVRALTNALEQ--------QRLHHAYLFTGTRGVGKTTLARILAKSLncetgvtatpCGVCSACLEIDSGRFVdl 90
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1086031431 589 -EKHTASRlfgappgyVGYDEGGQLTEKVRRRP----FSVVLFDEVEKAHPDIFNSLLQILEE 646
Cdd:PRK14969 91 iEVDAASN--------TQVDAMRELLDNAQYAPtrgrFKVYIIDEVHMLSKSAFNAMLKTLEE 145
|
|
| RPT1 |
COG1222 |
ATP-dependent 26S proteasome regulatory subunit [Posttranslational modification, protein ... |
520-630 |
5.83e-05 |
|
ATP-dependent 26S proteasome regulatory subunit [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440835 [Multi-domain] Cd Length: 326 Bit Score: 46.15 E-value: 5.83e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1086031431 520 VIGQEEAVKALSQSIRRtrsGLKDP-------KRPGGSFIFAGPTGVGKTELAKALAEFLfgdeDA-LIQIDMSEFSEKh 591
Cdd:COG1222 80 IGGLDEQIEEIREAVEL---PLKNPelfrkygIEPPKGVLLYGPPGTGKTLLAKAVAGEL----GApFIRVRGSELVSK- 151
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 1086031431 592 tasrlfgappgYVGydEGGQLTEKV----RRRPFSVVLFDEVE 630
Cdd:COG1222 152 -----------YIG--EGARNVREVfelaREKAPSIIFIDEID 181
|
|
| PRK14953 |
PRK14953 |
DNA polymerase III subunits gamma and tau; Provisional |
518-646 |
1.02e-04 |
|
DNA polymerase III subunits gamma and tau; Provisional
Pssm-ID: 237867 [Multi-domain] Cd Length: 486 Bit Score: 45.58 E-value: 1.02e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1086031431 518 KRVIGQEEAVKALSQSIRRtrsglkdpKRPGGSFIFAGPTGVGKTELAKALAEFL----------FGDEDALIQIDMSEF 587
Cdd:PRK14953 16 KEVIGQEIVVRILKNAVKL--------QRVSHAYIFAGPRGTGKTTIARILAKVLnclnpqegepCGKCENCVEIDKGSF 87
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1086031431 588 S---EKHTASRLfgappgyvGYDEGGQLTEKVRRRP----FSVVLFDEVEKAHPDIFNSLLQILEE 646
Cdd:PRK14953 88 PdliEIDAASNR--------GIDDIRALRDAVSYTPikgkYKVYIIDEAHMLTKEAFNALLKTLEE 145
|
|
| RPT1 |
COG1222 |
ATP-dependent 26S proteasome regulatory subunit [Posttranslational modification, protein ... |
216-362 |
1.11e-04 |
|
ATP-dependent 26S proteasome regulatory subunit [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440835 [Multi-domain] Cd Length: 326 Bit Score: 45.00 E-value: 1.11e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1086031431 216 LIGEPGVGKTAvvegLAQAIVHgdvpETikDRQIYSLDMGSLVagSRYRGDFEERLKKVLKEIRTRGDIILFIDEIHTLV 295
Cdd:COG1222 117 LYGPPGTGKTL----LAKAVAG----EL--GAPFIRVRGSELV--SKYIGEGARNVREVFELAREKAPSIIFIDEIDAIA 184
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1086031431 296 GAGAAEGSIDAAQMLKPML--------ARGEIQTIGATTldeyrkHVEK-DAALER--RF-QPVRVEEPSVDETVGILK 362
Cdd:COG1222 185 ARRTDDGTSGEVQRTVNQLlaeldgfeSRGDVLIIAATN------RPDLlDPALLRpgRFdRVIEVPLPDEEAREEILK 257
|
|
| MoxR |
COG0714 |
MoxR-like ATPase [General function prediction only]; MoxR-like ATPase is part of the Pathway ... |
511-650 |
1.14e-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: 44.77 E-value: 1.14e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1086031431 511 KMEDELHKRVIGQEEAVKALsqsirrtrsglkdpkrpggsFI--FA-------GPTGVGKTELAKALAEFLFGDedaLIQ 581
Cdd:COG0714 5 RLRAEIGKVYVGQEELIELV--------------------LIalLAgghllleGVPGVGKTTLAKALARALGLP---FIR 61
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1086031431 582 IdmsEFSEKHTASRLFGAppgYVgYDEGGQlTEKVRRRP-F-SVVLFDEVEKAHPDIFNSLLQILEEGHLT 650
Cdd:COG0714 62 I---QFTPDLLPSDILGT---YI-YDQQTG-EFEFRPGPlFaNVLLADEINRAPPKTQSALLEAMEERQVT 124
|
|
| CDC48 |
TIGR01243 |
AAA family ATPase, CDC48 subfamily; This subfamily of the AAA family ATPases includes two ... |
215-669 |
1.85e-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: 45.28 E-value: 1.85e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1086031431 215 VLIGEPGVGKTAVVEGLAQAIvhgdvpetikDRQIYSLDMGSLVagSRYRGDFEERLKKVLKEIRTRGDIILFIDEIHTL 294
Cdd:TIGR01243 216 LLYGPPGTGKTLLAKAVANEA----------GAYFISINGPEIM--SKYYGESEERLREIFKEAEENAPSIIFIDEIDAI 283
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1086031431 295 V-----GAGAAEGSIdAAQMLKPM---LARGEIQTIGATTLDEyrkhvEKDAALER--RF-QPVRVEEPSVDETVGILKg 363
Cdd:TIGR01243 284 ApkreeVTGEVEKRV-VAQLLTLMdglKGRGRVIVIGATNRPD-----ALDPALRRpgRFdREIVIRVPDKRARKEILK- 356
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1086031431 364 lrdrYEAHHRVIITDEAIRAAAELADRYISdrflPDKAIDLMDEAGARLR--IARMTAPPELREIDEKIADvrkakEAAI 441
Cdd:TIGR01243 357 ----VHTRNMPLAEDVDLDKLAEVTHGFVG----ADLAALAKEAAMAALRrfIREGKINFEAEEIPAEVLK-----ELKV 423
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1086031431 442 DDQDFERAasLRDEEKKLgeerrekedawkggereeiaevteeeIAEVLamsTGIPVVKLTQtesakllkmedelhkrVI 521
Cdd:TIGR01243 424 TMKDFMEA--LKMVEPSA--------------------------IREVL---VEVPNVRWSD----------------IG 456
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1086031431 522 GQEEAVKALSQSIRRTrsgLKDPK-------RPGGSFIFAGPTGVGKTELAKALAEflfGDEDALIQIDMSEFSEKhtas 594
Cdd:TIGR01243 457 GLEEVKQELREAVEWP---LKHPEifekmgiRPPKGVLLFGPPGTGKTLLAKAVAT---ESGANFIAVRGPEILSK---- 526
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1086031431 595 rlfgappgYVGYDEGG--QLTEKVRRRPFSVVLFDEVEKAHP----DIFNSLLQILEEGHLTDSQGrKVDFKNTVIIMTT 668
Cdd:TIGR01243 527 --------WVGESEKAirEIFRKARQAAPAIIFFDEIDAIAPargaRFDTSVTDRIVNQLLTEMDG-IQELSNVVVIAAT 597
|
.
gi 1086031431 669 N 669
Cdd:TIGR01243 598 N 598
|
|
| TniB |
pfam05621 |
Bacterial TniB protein; This family consists of several bacterial TniB NTP-binding proteins. ... |
197-350 |
3.78e-04 |
|
Bacterial TniB protein; This family consists of several bacterial TniB NTP-binding proteins. TniB is a probable ATP-binding protein which is involved in Tn5053 mercury resistance transposition. This entry represents a P-loop domain.
Pssm-ID: 428547 Cd Length: 189 Bit Score: 42.19 E-value: 3.78e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1086031431 197 TEMERVMQVLSRRTKNNPVLIGEPGVGKTAVVEGLAQ-------------AIVHGDVPETIKDRQIYSLDMGSLVAGSRY 263
Cdd:pfam05621 21 ERLEDLLDYPKRLRMPNLLLVGDSNNGKTMIVERFARlhpptddedaeivPVVVVQMPPKPDEKRLYVAILEALGAPFRP 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1086031431 264 RG---DFEERLKKVLKEIRTRgdiILFIDEIHTLvgagaAEGSIDAAQMLKPMLAR-GE---IQTIGATTLDEYRkHVEK 336
Cdd:pfam05621 101 RDrlsKLEQQVLRLLRAVGVR---MLIIDEFHNL-----LAGSARKQREFLNVLKSlGNelrIPIVGVGTREAVR-AIRT 171
|
170
....*....|....
gi 1086031431 337 DAALERRFQPVRVE 350
Cdd:pfam05621 172 DPQLASRFEPIALP 185
|
|
| RecA-like_KTNA1 |
cd19522 |
Katanin p60 ATPase-containing subunit A1; Katanin p60 ATPase-containing subunit A1 (KTNA1) is ... |
208-345 |
5.95e-04 |
|
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: 41.51 E-value: 5.95e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1086031431 208 RRTKNNPVLIGEPGVGKTAvvegLAQAIVhgdvpeTIKDRQIYSLDMGSLVagSRYRGDFEERLKKVLKEIRTRGDIILF 287
Cdd:cd19522 30 RRPWKGVLMVGPPGTGKTL----LAKAVA------TECGTTFFNVSSSTLT--SKYRGESEKLVRLLFEMARFYAPTTIF 97
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1086031431 288 IDEIHTLVGAGAAEGSIDAAQMLKPMLARGEIQTIGATTLDEYRKHV----------EKDAALERRFQ 345
Cdd:cd19522 98 IDEIDSICSRRGTSEEHEASRRVKSELLVQMDGVGGASENDDPSKMVmvlaatnfpwDIDEALRRRLE 165
|
|
| PRK07399 |
PRK07399 |
DNA polymerase III subunit delta'; Validated |
515-573 |
6.84e-04 |
|
DNA polymerase III subunit delta'; Validated
Pssm-ID: 236011 [Multi-domain] Cd Length: 314 Bit Score: 42.58 E-value: 6.84e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 1086031431 515 ELHKRVIGQEEAVKALSQSIRRtrsglkdpKRPGGSFIFAGPTGVGKTELAKALAEFLF 573
Cdd:PRK07399 1 NLFANLIGQPLAIELLTAAIKQ--------NRIAPAYLFAGPEGVGRKLAALCFIEGLL 51
|
|
| PRK04195 |
PRK04195 |
replication factor C large subunit; Provisional |
520-569 |
1.15e-03 |
|
replication factor C large subunit; Provisional
Pssm-ID: 235250 [Multi-domain] Cd Length: 482 Bit Score: 42.22 E-value: 1.15e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 1086031431 520 VIGQEEAVKALSQSIRRTRSGlkDPKRPggsFIFAGPTGVGKTELAKALA 569
Cdd:PRK04195 16 VVGNEKAKEQLREWIESWLKG--KPKKA---LLLYGPPGVGKTSLAHALA 60
|
|
| Mg_chelatase |
pfam01078 |
Magnesium chelatase, subunit ChlI; Magnesium-chelatase is a three-component enzyme that ... |
520-670 |
1.82e-03 |
|
Magnesium chelatase, subunit ChlI; Magnesium-chelatase is a three-component enzyme that catalyzes the insertion of Mg2+ into protoporphyrin IX. This is the first unique step in the synthesis of (bacterio)chlorophyll. Due to this, it is thought that Mg-chelatase has an important role in channelling inter- mediates into the (bacterio)chlorophyll branch in response to conditions suitable for photosynthetic growth. ChlI and BchD have molecular weight between 38-42 kDa.
Pssm-ID: 426032 [Multi-domain] Cd Length: 207 Bit Score: 40.60 E-value: 1.82e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1086031431 520 VIGQEEAVKALSQSIrrtrSGlkdpkrpGGSFIFAGPTGVGKTELAKALAEFL--FGDEDAL----IQ-IDMSEFSEKHT 592
Cdd:pfam01078 5 VKGQEQAKRALEIAA----AG-------GHNLLMIGPPGSGKTMLAKRLPGILppLTEAEALevtaIHsVAGLGGDGGLI 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1086031431 593 ASRLFGAP------PGYVGydeGGqltekVRRRPFSV------VLF-DEVEKAHPDIFNSLLQILEEGHLTDSQGR-KVD 658
Cdd:pfam01078 74 RRRPFRAPhhsasaAALVG---GG-----SIPRPGEIslahngVLFlDELPEFKRRVLESLRQPLEDGEITISRARaKVT 145
|
170
....*....|...
gi 1086031431 659 F-KNTVIIMTTNL 670
Cdd:pfam01078 146 FpARFQLVAAMNP 158
|
|
| RecA-like_VPS4-like |
cd19509 |
ATPase domain of VPS4, ATAD1, K, KTNA1, Spastin, FIGL-1 and similar ATPase domains; This ... |
215-345 |
1.82e-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: 40.03 E-value: 1.82e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1086031431 215 VLIGEPGVGKTAvvegLAQAIVhgdvpeTIKDRQIYSLDMGSLVagSRYRGDFEERLKKVLKEIRTRGDIILFIDEIHTL 294
Cdd:cd19509 36 LLYGPPGTGKTL----LARAVA------SESGSTFFSISASSLV--SKWVGESEKIVRALFALARELQPSIIFIDEIDSL 103
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1086031431 295 V---GAGAAEGSID-AAQMLKPM-----LARGEIQTIGATTLDEyrkhvEKDAALERRFQ 345
Cdd:cd19509 104 LserGSGEHEASRRvKTEFLVQMdgvlnKPEDRVLVLGATNRPW-----ELDEAFLRRFE 158
|
|
| hslU |
PRK05201 |
ATP-dependent protease ATPase subunit HslU; |
515-569 |
2.14e-03 |
|
ATP-dependent protease ATPase subunit HslU;
Pssm-ID: 235364 [Multi-domain] Cd Length: 443 Bit Score: 41.22 E-value: 2.14e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1086031431 515 ELHKRVIGQEEAVK----ALSQSIRRTR--SGLKD---PKrpggSFIFAGPTGVGKTELAKALA 569
Cdd:PRK05201 12 ELDKYIIGQDDAKRavaiALRNRWRRMQlpEELRDevtPK----NILMIGPTGVGKTEIARRLA 71
|
|
| PRK05298 |
PRK05298 |
excinuclease ABC subunit UvrB; |
425-467 |
2.68e-03 |
|
excinuclease ABC subunit UvrB;
Pssm-ID: 235395 [Multi-domain] Cd Length: 652 Bit Score: 41.19 E-value: 2.68e-03
10 20 30 40
....*....|....*....|....*....|....*....|...
gi 1086031431 425 EIDEKIADVRKAKEAAIDDQDFERAASLRDEEKKLGEERREKE 467
Cdd:PRK05298 610 ELEKLIKELEKQMKEAAKNLEFEEAARLRDEIKELKEELLGLS 652
|
|
| AAA_16 |
pfam13191 |
AAA ATPase domain; This family of domains contain a P-loop motif that is characteriztic of the ... |
191-236 |
2.92e-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: 39.41 E-value: 2.92e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 1086031431 191 PVIGRKTEMERVMQVLSRRTKNNP---VLIGEPGVGKTAVVEGLAQAIV 236
Cdd:pfam13191 1 RLVGREEELEQLLDALDRVRSGRPpsvLLTGEAGTGKTTLLRELLRALE 49
|
|
| RecA-like_VPS4 |
cd19521 |
ATPase domain of vacuolar protein sorting-associated protein 4; Vacuolar protein ... |
215-345 |
3.91e-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: 39.07 E-value: 3.91e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1086031431 215 VLIGEPGVGKTAvvegLAQAIVhgdvpeTIKDRQIYSLDMGSLVagSRYRGDFEERLKKVLKEIRTRGDIILFIDEIHTL 294
Cdd:cd19521 44 LLYGPPGTGKSY----LAKAVA------TEANSTFFSVSSSDLV--SKWMGESEKLVKQLFAMARENKPSIIFIDEVDSL 111
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1086031431 295 VGAgAAEGSIDAAQMLKP-----MLARGE----IQTIGATTLDeyrkhVEKDAALERRFQ 345
Cdd:cd19521 112 CGT-RGEGESEASRRIKTellvqMNGVGNdsqgVLVLGATNIP-----WQLDSAIRRRFE 165
|
|
| PRK05896 |
PRK05896 |
DNA polymerase III subunits gamma and tau; Validated |
518-569 |
4.11e-03 |
|
DNA polymerase III subunits gamma and tau; Validated
Pssm-ID: 235638 [Multi-domain] Cd Length: 605 Bit Score: 40.60 E-value: 4.11e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 1086031431 518 KRVIGQEEAVKALSQSIRRTrsglkdpKRPGGsFIFAGPTGVGKTELAKALA 569
Cdd:PRK05896 16 KQIIGQELIKKILVNAILNN-------KLTHA-YIFSGPRGIGKTSIAKIFA 59
|
|
| AAA_22 |
pfam13401 |
AAA domain; |
549-645 |
4.29e-03 |
|
AAA domain;
Pssm-ID: 379165 [Multi-domain] Cd Length: 129 Bit Score: 38.09 E-value: 4.29e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1086031431 549 GSFIFAGPTGVGKTELAKALAEFLFGDEDALIQIDMSEFSEKHT-----ASRLFGAPPGYVGYDE-GGQLTEKVRRRPFS 622
Cdd:pfam13401 6 GILVLTGESGTGKTTLLRRLLEQLPEVRDSVVFVDLPSGTSPKDllralLRALGLPLSGRLSKEElLAALQQLLLALAVA 85
|
90 100
....*....|....*....|....
gi 1086031431 623 VVL-FDEVEKAHPDIFNSLLQILE 645
Cdd:pfam13401 86 VVLiIDEAQHLSLEALEELRDLLN 109
|
|
| HslU |
COG1220 |
ATP-dependent protease HslVU (ClpYQ), ATPase subunit HslU [Posttranslational modification, ... |
515-569 |
4.38e-03 |
|
ATP-dependent protease HslVU (ClpYQ), ATPase subunit HslU [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440833 [Multi-domain] Cd Length: 454 Bit Score: 40.42 E-value: 4.38e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1086031431 515 ELHKRVIGQEEAVKALSQSIR-RTR-----SGLKD---PKrpggSFIFAGPTGVGKTELAKALA 569
Cdd:COG1220 12 ELDKYIIGQDEAKRAVAIALRnRWRrqqlpEELRDeitPK----NILMIGPTGVGKTEIARRLA 71
|
|
| Clp_N |
pfam02861 |
Clp amino terminal domain, pathogenicity island component; This short domain is found in one ... |
91-143 |
5.25e-03 |
|
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: 35.57 E-value: 5.25e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 1086031431 91 SLREALQLGHNYIGTEHLLLGLLKEGEGVAAQVLTKLGADLSQVRQAVIQLLS 143
Cdd:pfam02861 1 AQELARALGHQYIGTEHLLLALLEEDDGLAARLLKKAGVDLDALREAIEKLLG 53
|
|
| ftsH |
CHL00176 |
cell division protein; Validated |
196-362 |
5.30e-03 |
|
cell division protein; Validated
Pssm-ID: 214386 [Multi-domain] Cd Length: 638 Bit Score: 40.42 E-value: 5.30e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1086031431 196 KTEMERVMQVLSRRTKNNPV---------LIGEPGVGKTAvvegLAQAIVH-GDVPetikdrqIYSldmgslVAGSRYRG 265
Cdd:CHL00176 192 KEEFEEVVSFLKKPERFTAVgakipkgvlLVGPPGTGKTL----LAKAIAGeAEVP-------FFS------ISGSEFVE 254
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1086031431 266 DFE----ERLKKVLKEIRTRGDIILFIDEIHTL---VGAGAAEGSIDAAQMLKPML-------ARGEIQTIGATTldeyR 331
Cdd:CHL00176 255 MFVgvgaARVRDLFKKAKENSPCIVFIDEIDAVgrqRGAGIGGGNDEREQTLNQLLtemdgfkGNKGVIVIAATN----R 330
|
170 180 190
....*....|....*....|....*....|....
gi 1086031431 332 KHVeKDAALER--RF-QPVRVEEPSVDETVGILK 362
Cdd:CHL00176 331 VDI-LDAALLRpgRFdRQITVSLPDREGRLDILK 363
|
|
| PRK12402 |
PRK12402 |
replication factor C small subunit 2; Reviewed |
515-587 |
5.81e-03 |
|
replication factor C small subunit 2; Reviewed
Pssm-ID: 237090 [Multi-domain] Cd Length: 337 Bit Score: 39.59 E-value: 5.81e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1086031431 515 ELHKRVIGQEEAVKALSQSIrrtrsglKDPKRPggSFIFAGPTGVGKTELAKALAEFLFGD--EDALIQIDMSEF 587
Cdd:PRK12402 12 ALLEDILGQDEVVERLSRAV-------DSPNLP--HLLVQGPPGSGKTAAVRALARELYGDpwENNFTEFNVADF 77
|
|
| RecA-like_FtsH |
cd19501 |
ATP-dependent zinc metalloprotease FtsH; FtsH ATPase is a processive, ATP-dependent zinc ... |
518-630 |
5.91e-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: 5.91e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1086031431 518 KRVIGQEEAVKALSQSIrrtrSGLKDPKR--------PGGsFIFAGPTGVGKTELAKALAeflfGDEDA-LIQIDMSEFS 588
Cdd:cd19501 4 KDVAGCEEAKEELKEVV----EFLKNPEKftklgakiPKG-VLLVGPPGTGKTLLAKAVA----GEAGVpFFSISGSDFV 74
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 1086031431 589 EkhtasrLFGAppgyVGYDEGGQLTEKVRRRPFSVVLFDEVE 630
Cdd:cd19501 75 E------MFVG----VGASRVRDLFEQAKKNAPCIVFIDEID 106
|
|
| PRK14958 |
PRK14958 |
DNA polymerase III subunits gamma and tau; Provisional |
518-646 |
7.24e-03 |
|
DNA polymerase III subunits gamma and tau; Provisional
Pssm-ID: 184922 [Multi-domain] Cd Length: 509 Bit Score: 39.71 E-value: 7.24e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1086031431 518 KRVIGQEEAVKALSQSIrrtrsglkDPKRPGGSFIFAGPTGVGKTELAKALAEFL----------FGDEDALIQIDMSEF 587
Cdd:PRK14958 16 QEVIGQAPVVRALSNAL--------DQQYLHHAYLFTGTRGVGKTTISRILAKCLncekgvsanpCNDCENCREIDEGRF 87
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1086031431 588 S---EKHTASRlfgappgyVGYDEGGQLTEKVRRRP----FSVVLFDEVEKAHPDIFNSLLQILEE 646
Cdd:PRK14958 88 PdlfEVDAASR--------TKVEDTRELLDNIPYAPtkgrFKVYLIDEVHMLSGHSFNALLKTLEE 145
|
|
| UvrB |
COG0556 |
Excinuclease UvrABC helicase subunit UvrB [Replication, recombination and repair]; |
425-462 |
7.37e-03 |
|
Excinuclease UvrABC helicase subunit UvrB [Replication, recombination and repair];
Pssm-ID: 440322 [Multi-domain] Cd Length: 657 Bit Score: 39.99 E-value: 7.37e-03
10 20 30
....*....|....*....|....*....|....*...
gi 1086031431 425 EIDEKIADVRKAKEAAIDDQDFERAASLRDEEKKLGEE 462
Cdd:COG0556 620 ELEKLIKELEKEMKEAAKNLEFEEAARLRDEIKELKKE 657
|
|
| rfc |
PRK00440 |
replication factor C small subunit; Reviewed |
520-575 |
7.84e-03 |
|
replication factor C small subunit; Reviewed
Pssm-ID: 234763 [Multi-domain] Cd Length: 319 Bit Score: 39.09 E-value: 7.84e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 1086031431 520 VIGQEEAVKALSQSIRRtrsglKD-PKrpggsFIFAGPTGVGKTELAKALAEFLFGD 575
Cdd:PRK00440 19 IVGQEEIVERLKSYVKE-----KNmPH-----LLFAGPPGTGKTTAALALARELYGE 65
|
|
| RecA-like_Ycf46-like |
cd19507 |
ATPase domain of Ycf46 and similar ATPase domains; Ycf46 may play a role in the regulation of ... |
216-291 |
7.88e-03 |
|
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: 38.12 E-value: 7.88e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1086031431 216 LIGEPGVGKTAVveglAQAIVHgdvpetIKDRQIYSLDMGSLVAGsrYRGDFEERLKKVLKEIRTRGDIILFIDEI 291
Cdd:cd19507 36 LVGIQGTGKSLT----AKAIAG------VWQLPLLRLDMGRLFGG--LVGESESRLRQMIQTAEAIAPCVLWIDEI 99
|
|
| flhF |
PRK05703 |
flagellar biosynthesis protein FlhF; |
508-569 |
9.89e-03 |
|
flagellar biosynthesis protein FlhF;
Pssm-ID: 235570 [Multi-domain] Cd Length: 424 Bit Score: 39.11 E-value: 9.89e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1086031431 508 KLLKME------DELHKRVI-----GQEEAVKALSQSIRRT-RSGLKDPKRPGGSFIFAGPTGVGK-TELAKaLA 569
Cdd:PRK05703 169 RLKRSGlspeiaEKLLKLLLehmppRERTAWRYLLELLANMiPVRVEDILKQGGVVALVGPTGVGKtTTLAK-LA 242
|
|
| |
