|
Name |
Accession |
Description |
Interval |
E-value |
| chaperone_ClpB |
TIGR03346 |
ATP-dependent chaperone ClpB; Members of this protein family are the bacterial ATP-dependent ... |
6-856 |
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: 1481.74 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276770 6 YSERVRGFIQSAQTQALSSNHQQFTPEHLLKVLVDDEEGLAASLIERAGGRAKDVRLGVEAALKAMPQVEGGNGQLYMAQ 85
Cdd:TIGR03346 1 LTEKFQEALQAAQSLALGRDHQQIEPEHLLKALLDQEGGLARPLLQKAGVNVGALRQALEKELERLPKVSGPGGQVYLSP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276770 86 PLAKVFSTAEELAKKAGDSFVTVERLLTALAVEKSAkTADILSKAGVTPTALNQAINDIRKGRTADSASAEQGYDALKKY 165
Cdd:TIGR03346 81 DLNRLLNLAEKLAQKRGDEFISSEHLLLALLDDKGT-LGKLLKEAGATADALEAAINAVRGGQKVTDANAEDQYEALEKY 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276770 166 ARDLTADARAGKLDPVIGRDDEIRRTIQVLSRRTKNNPVLIGEPGVGKTAIAEGLALRIVNGDVPESLKDKQLMALDMGS 245
Cdd:TIGR03346 160 ARDLTERAREGKLDPVIGRDEEIRRTIQVLSRRTKNNPVLIGEPGVGKTAIVEGLAQRIVNGDVPEGLKNKRLLALDMGA 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276770 246 LIAGAKYRGEFEERLKAVLSEVTAADGNIILFIDEMHTLVGAGKADGAMDASNLLKPALARGELHCVGATTLDEYRKHVE 325
Cdd:TIGR03346 240 LIAGAKYRGEFEERLKAVLNEVTKSEGQIILFIDELHTLVGAGKAEGAMDAGNMLKPALARGELHCIGATTLDEYRKYIE 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276770 326 KDAALARRFQPVFVSEPTVEDTVSILRGLKEKYEQHHKVRVSDSALVAAATLSNRYITDRFLPDKAIDLVDEASSRLRMQ 405
Cdd:TIGR03346 320 KDAALERRFQPVFVDEPSVEDTISILRGLKERYEVHHGVRITDPAIVAAATLSHRYITDRFLPDKAIDLIDEAAARIRME 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276770 406 VDSKPEELDEIDRRVMQLKIEREALKAEKDEASRDRLVKLEKELTDLEEESARLTSRWAAEKDKLGLAADLKKQLDEARN 485
Cdd:TIGR03346 400 IDSKPEELDELDRRIIQLEIEREALKKEKDEASKKRLEDLEKELADLEEEYAELEEQWKAEKASIQGIQQIKEEIEQVRL 479
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276770 486 ELAIAQRKGEFQRAGELAYGQIPELEKKLAEAEAQSEEESASgMVEETVKPDHVAHIVSRWTGIPVDKMLEGEREKLLRM 565
Cdd:TIGR03346 480 ELEQAEREGDLAKAAELQYGKLPELEKQLQAAEQKLGEEQNR-LLREEVTAEEIAEVVSRWTGIPVSKMLEGEREKLLHM 558
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276770 566 EDEIAKRVVGQGEAVQSVSKAVRRARAGLQDPNRPIGSFMFLGPTGVGKTELTKALASFLFDDEQAMVRIDMSEFMEKHS 645
Cdd:TIGR03346 559 EEELHERVVGQDEAVEAVSDAIRRSRAGLSDPNRPIGSFLFLGPTGVGKTELAKALAEFLFDSEDAMVRIDMSEYMEKHS 638
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276770 646 VARLIGAPPGYVGYEEGGVLTEAVRRRPYQVILFDEVEKAHPDVFNVLLQVLDDGRLTDGQGRTVDFRNTLIIMTSNLGA 725
Cdd:TIGR03346 639 VARLIGAPPGYVGYEEGGQLTEAVRRRPYSVVLFDEVEKAHPDVFNVLLQVLDDGRLTDGQGRTVDFRNTVIIMTSNLGS 718
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276770 726 EYLVNLGENEDVDKVRTEVMDVVKASFRPEFLNRIDEVILFHRLRRQDMGKIVEIQLQRLERLLADRKITLDLDKDAVEW 805
Cdd:TIGR03346 719 DFIQELAGGDDYEEMREAVMEVLRAHFRPEFLNRIDEIVVFHPLGREQIARIVEIQLGRLRKRLAERKITLELSDAALDF 798
|
810 820 830 840 850
....*....|....*....|....*....|....*....|....*....|.
gi 1998276770 806 LAEKGYDPAYGARPLKRVMQKELQDPLAEKILQGEIFDNSTVKITAGSDRL 856
Cdd:TIGR03346 799 LAEAGYDPVYGARPLKRAIQREIENPLAKKILAGEVAPGDTIRVDVEGGRL 849
|
|
| ClpA |
COG0542 |
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ... |
1-856 |
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: 1468.77 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276770 1 MNFDKYSERVRGFIQSAQTQALSSNHQQFTPEHLLKVLVDDEEGLAASLIERAGGRAKDVRLGVEAALKAMPQVEGGNGQ 80
Cdd:COG0542 1 MNFEKFTEKAQEALEAAQELARRLGHQEVEPEHLLLALLEQGEGLAAKLLRKLGVDLDALREELEEALGRLPKVSGSSGQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276770 81 LYMAQPLAKVFSTAEELAKKAGDSFVTVERLLTALAVEKSAKTADILSKAGVTPTALNQAINDIRKGRTADSASAEQGYD 160
Cdd:COG0542 81 PYLSPRLKRVLELAELEARKLGDEYISTEHLLLALLREGEGVAARILKKLGITLEALREALEELRGGSRVTSQNPESKTP 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276770 161 ALKKYARDLTADARAGKLDPVIGRDDEIRRTIQVLSRRTKNNPVLIGEPGVGKTAIAEGLALRIVNGDVPESLKDKQLMA 240
Cdd:COG0542 161 ALDKYGRDLTELAREGKLDPVIGRDEEIRRVIQILSRRTKNNPVLIGEPGVGKTAIVEGLAQRIVNGDVPESLKDKRVLS 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276770 241 LDMGSLIAGAKYRGEFEERLKAVLSEVTAADGNIILFIDEMHTLVGAGKADGAMDASNLLKPALARGELHCVGATTLDEY 320
Cdd:COG0542 241 LDLGALVAGAKYRGEFEERLKAVLDEVKKSEGNIILFIDELHTLVGAGGAEGAMDAANLLKPALARGELRCIGATTLDEY 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276770 321 RKHVEKDAALARRFQPVFVSEPTVEDTVSILRGLKEKYEQHHKVRVSDSALVAAATLSNRYITDRFLPDKAIDLVDEASS 400
Cdd:COG0542 321 RKYIEKDAALERRFQPVLVEEPSVEDTISILRGLKERYEAHHGVRITDEALVAAVRLSDRYITDRFLPDKAIDLIDEAAA 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276770 401 RLRMQVDSKPEELDEIDRRVMQLKIEREALKAEKDEASRDRLVKLEKELTDLEEESARLTSRWAAEKDKLGLAADLKKQL 480
Cdd:COG0542 401 RVRMEIDSKPEELDELERRLEQLEIEKEALKKEQDEASFERLAELRDELAELEEELEALKARWEAEKELIEEIQELKEEL 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276770 481 DEarnelaiaqrkgefqragelAYGQIPELEKKLAEAEAQSEEESAsgMVEETVKPDHVAHIVSRWTGIPVDKMLEGERE 560
Cdd:COG0542 481 EQ--------------------RYGKIPELEKELAELEEELAELAP--LLREEVTEEDIAEVVSRWTGIPVGKLLEGERE 538
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276770 561 KLLRMEDEIAKRVVGQGEAVQSVSKAVRRARAGLQDPNRPIGSFMFLGPTGVGKTELTKALASFLFDDEQAMVRIDMSEF 640
Cdd:COG0542 539 KLLNLEEELHERVIGQDEAVEAVADAIRRSRAGLKDPNRPIGSFLFLGPTGVGKTELAKALAEFLFGDEDALIRIDMSEY 618
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276770 641 MEKHSVARLIGAPPGYVGYEEGGVLTEAVRRRPYQVILFDEVEKAHPDVFNVLLQVLDDGRLTDGQGRTVDFRNTLIIMT 720
Cdd:COG0542 619 MEKHSVSRLIGAPPGYVGYEEGGQLTEAVRRRPYSVVLLDEIEKAHPDVFNILLQVLDDGRLTDGQGRTVDFRNTIIIMT 698
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276770 721 SNLGAEYLVNLGEN-EDVDKVRTEVMDVVKASFRPEFLNRIDEVILFHRLRRQDMGKIVEIQLQRLERLLADRKITLDLD 799
Cdd:COG0542 699 SNIGSELILDLAEDePDYEEMKEAVMEELKKHFRPEFLNRIDEIIVFHPLSKEELRKIVDLQLKRLRKRLAERGITLELT 778
|
810 820 830 840 850
....*....|....*....|....*....|....*....|....*....|....*..
gi 1998276770 800 KDAVEWLAEKGYDPAYGARPLKRVMQKELQDPLAEKILQGEIFDNSTVKITAGSDRL 856
Cdd:COG0542 779 DAAKDFLAEKGYDPEYGARPLKRAIQRELEDPLAEEILAGEIKEGDTITVDVDDGEL 835
|
|
| PRK10865 |
PRK10865 |
ATP-dependent chaperone ClpB; |
1-856 |
0e+00 |
|
ATP-dependent chaperone ClpB;
Pssm-ID: 182791 [Multi-domain] Cd Length: 857 Bit Score: 1070.24 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276770 1 MNFDKYSERVRGFIQSAQTQALSSNHQQFTPEHLLKVLVDDEEGLAASLIERAGGRAKDVRLGVEAALKAMPQVEGGNGQ 80
Cdd:PRK10865 1 MRLDRLTNKFQLALADAQSLALGHDNQFIEPLHLMSALLNQEGGSVRPLLTSAGINAGQLRTDINQALSRLPQVEGTGGD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276770 81 LYMAQPLAKVFSTAEELAKKAGDSFVTVERLLTAlAVEKSAKTADILSKAGVTPTALNQAINDIRKGRTADSASAEQGYD 160
Cdd:PRK10865 81 VQPSQDLVRVLNLCDKLAQKRGDNFISSELFVLA-ALESRGTLADILKAAGATTANITQAIEQMRGGESVNDQGAEDQRQ 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276770 161 ALKKYARDLTADARAGKLDPVIGRDDEIRRTIQVLSRRTKNNPVLIGEPGVGKTAIAEGLALRIVNGDVPESLKDKQLMA 240
Cdd:PRK10865 160 ALKKYTIDLTERAEQGKLDPVIGRDEEIRRTIQVLQRRTKNNPVLIGEPGVGKTAIVEGLAQRIINGEVPEGLKGRRVLA 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276770 241 LDMGSLIAGAKYRGEFEERLKAVLSEVTAADGNIILFIDEMHTLVGAGKADGAMDASNLLKPALARGELHCVGATTLDEY 320
Cdd:PRK10865 240 LDMGALVAGAKYRGEFEERLKGVLNDLAKQEGNVILFIDELHTMVGAGKADGAMDAGNMLKPALARGELHCVGATTLDEY 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276770 321 RKHVEKDAALARRFQPVFVSEPTVEDTVSILRGLKEKYEQHHKVRVSDSALVAAATLSNRYITDRFLPDKAIDLVDEASS 400
Cdd:PRK10865 320 RQYIEKDAALERRFQKVFVAEPSVEDTIAILRGLKERYELHHHVQITDPAIVAAATLSHRYIADRQLPDKAIDLIDEAAS 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276770 401 RLRMQVDSKPEELDEIDRRVMQLKIEREALKAEKDEASRDRLVKLEKELTDLEEESARLTSRWAAEKDKLGLAADLKKQL 480
Cdd:PRK10865 400 SIRMQIDSKPEELDRLDRRIIQLKLEQQALMKESDEASKKRLDMLNEELSDKERQYSELEEEWKAEKASLSGTQTIKAEL 479
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276770 481 DEARNELAIAQRKGEFQRAGELAYGQIPELEKKLAEAEAQSEEESAsgMVEETVKPDHVAHIVSRWTGIPVDKMLEGERE 560
Cdd:PRK10865 480 EQAKIAIEQARRVGDLARMSELQYGKIPELEKQLAAATQLEGKTMR--LLRNKVTDAEIAEVLARWTGIPVSRMLESERE 557
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276770 561 KLLRMEDEIAKRVVGQGEAVQSVSKAVRRARAGLQDPNRPIGSFMFLGPTGVGKTELTKALASFLFDDEQAMVRIDMSEF 640
Cdd:PRK10865 558 KLLRMEQELHHRVIGQNEAVEAVSNAIRRSRAGLSDPNRPIGSFLFLGPTGVGKTELCKALANFMFDSDDAMVRIDMSEF 637
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276770 641 MEKHSVARLIGAPPGYVGYEEGGVLTEAVRRRPYQVILFDEVEKAHPDVFNVLLQVLDDGRLTDGQGRTVDFRNTLIIMT 720
Cdd:PRK10865 638 MEKHSVSRLVGAPPGYVGYEEGGYLTEAVRRRPYSVILLDEVEKAHPDVFNILLQVLDDGRLTDGQGRTVDFRNTVVIMT 717
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276770 721 SNLGAEYLVNLGENEDVDKVRTEVMDVVKASFRPEFLNRIDEVILFHRLRRQDMGKIVEIQLQRLERLLADRKITLDLDK 800
Cdd:PRK10865 718 SNLGSDLIQERFGELDYAHMKELVLGVVSHNFRPEFINRIDEVVVFHPLGEQHIASIAQIQLQRLYKRLEERGYEIHISD 797
|
810 820 830 840 850
....*....|....*....|....*....|....*....|....*....|....*.
gi 1998276770 801 DAVEWLAEKGYDPAYGARPLKRVMQKELQDPLAEKILQGEIFDNSTVKITAGSDRL 856
Cdd:PRK10865 798 EALKLLSENGYDPVYGARPLKRAIQQQIENPLAQQILSGELVPGKVIRLEVNDDRI 853
|
|
| clpC |
CHL00095 |
Clp protease ATP binding subunit |
3-850 |
0e+00 |
|
Clp protease ATP binding subunit
Pssm-ID: 214361 [Multi-domain] Cd Length: 821 Bit Score: 877.08 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276770 3 FDKYSERVRGFIQSAQTQALSSNHQQFTPEHLLKVLVDDEEGLAASLIERAGGRAKDVRLGVEAALkampqvegGNGQLY 82
Cdd:CHL00095 2 FERFTEKAIKVIMLSQEEARRLGHNFVGTEQILLGLIGEGTGIAARALKSMGVTLKDARIEVEKII--------GRGTGF 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276770 83 MA-----QPLAK-VFSTAEELAKKAGDSFVTVERLLTALAVEKSAKTADILSKAGVT----PTALNQAINDIRKGrTADS 152
Cdd:CHL00095 74 VAveipfTPRAKrVLEMSLEEARDLGHNYIGTEHLLLALLEEGEGVAARVLENLGVDlskiRSLILNLIGEIIEA-ILGA 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276770 153 ASAEQGYDALKKYARDLTADARAGKLDPVIGRDDEIRRTIQVLSRRTKNNPVLIGEPGVGKTAIAEGLALRIVNGDVPES 232
Cdd:CHL00095 153 EQSRSKTPTLEEFGTNLTKEAIDGNLDPVIGREKEIERVIQILGRRTKNNPILIGEPGVGKTAIAEGLAQRIVNRDVPDI 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276770 233 LKDKQLMALDMGSLIAGAKYRGEFEERLKAVLSEVTAADgNIILFIDEMHTLVGAGKADGAMDASNLLKPALARGELHCV 312
Cdd:CHL00095 233 LEDKLVITLDIGLLLAGTKYRGEFEERLKRIFDEIQENN-NIILVIDEVHTLIGAGAAEGAIDAANILKPALARGELQCI 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276770 313 GATTLDEYRKHVEKDAALARRFQPVFVSEPTVEDTVSILRGLKEKYEQHHKVRVSDSALVAAATLSNRYITDRFLPDKAI 392
Cdd:CHL00095 312 GATTLDEYRKHIEKDPALERRFQPVYVGEPSVEETIEILFGLRSRYEKHHNLSISDKALEAAAKLSDQYIADRFLPDKAI 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276770 393 DLVDEASSRLRMQVDSKPEELDEIDRRVmqlkieREALKaEKDEASRDRLVKLEKELTDLEEEsarltsrwaaekdklgl 472
Cdd:CHL00095 392 DLLDEAGSRVRLINSRLPPAARELDKEL------REILK-DKDEAIREQDFETAKQLRDREME----------------- 447
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276770 473 aadLKKQLDearnelAIAQRKgefqragelaygqipelekklaeaeaqsEEESASGMVEETVKPDHVAHIVSRWTGIPVD 552
Cdd:CHL00095 448 ---VRAQIA------AIIQSK----------------------------KTEEEKRLEVPVVTEEDIAEIVSAWTGIPVN 490
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276770 553 KMLEGEREKLLRMEDEIAKRVVGQGEAVQSVSKAVRRARAGLQDPNRPIGSFMFLGPTGVGKTELTKALASFLFDDEQAM 632
Cdd:CHL00095 491 KLTKSESEKLLHMEETLHKRIIGQDEAVVAVSKAIRRARVGLKNPNRPIASFLFSGPTGVGKTELTKALASYFFGSEDAM 570
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276770 633 VRIDMSEFMEKHSVARLIGAPPGYVGYEEGGVLTEAVRRRPYQVILFDEVEKAHPDVFNVLLQVLDDGRLTDGQGRTVDF 712
Cdd:CHL00095 571 IRLDMSEYMEKHTVSKLIGSPPGYVGYNEGGQLTEAVRKKPYTVVLFDEIEKAHPDIFNLLLQILDDGRLTDSKGRTIDF 650
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276770 713 RNTLIIMTSNLGAEYLVNLG------------ENEDVDKVRTEVMDVVKASFRPEFLNRIDEVILFHRLRRQDMGKIVEI 780
Cdd:CHL00095 651 KNTLIIMTSNLGSKVIETNSgglgfelsenqlSEKQYKRLSNLVNEELKQFFRPEFLNRLDEIIVFRQLTKNDVWEIAEI 730
|
810 820 830 840 850 860 870
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276770 781 QLQRLERLLADRKITLDLDKDAVEWLAEKGYDPAYGARPLKRVMQKELQDPLAEKILQGEIFDNSTVKIT 850
Cdd:CHL00095 731 MLKNLFKRLNEQGIQLEVTERIKTLLIEEGYNPLYGARPLRRAIMRLLEDPLAEEVLSFKIKPGDIIIVD 800
|
|
| ClpA |
TIGR02639 |
ATP-dependent Clp protease ATP-binding subunit clpA; [Protein fate, Degradation of proteins, ... |
6-851 |
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: 753.01 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276770 6 YSERVRGFIQSAQTQALSSNHQQFTPEHLLKVLVDDEEGLAasLIERAGGRAKDVRLGVEAALKAMPQVEGGNGQLYMAQ 85
Cdd:TIGR02639 1 ISEELERILSDALEEAKERRHEFVTLEHLLLALLDDNEAIE--ILEECGGDVELLRKRLEDYLEENLPVIPEDIDEEPEQ 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276770 86 PLA--KVFSTAEELAKKAGDSFVTVERLLTALAVEKSAKTADILSKAGVTPTALNQAIND-IRK------GRTADSASAE 156
Cdd:TIGR02639 79 TVGvqRVIQRALLHVKSAGKKEIDIGDLLVALFDEEDSHASYFLKSQGITRLDILNYISHgISKddgkdqLGEEAGKEEE 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276770 157 QGYDALKKYARDLTADARAGKLDPVIGRDDEIRRTIQVLSRRTKNNPVLIGEPGVGKTAIAEGLALRIVNGDVPESLKDK 236
Cdd:TIGR02639 159 KGQDALEKYTVDLTEKAKNGKIDPLIGREDELERTIQVLCRRKKNNPLLVGEPGVGKTAIVEGLALRIAEGKVPERLKNA 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276770 237 QLMALDMGSLIAGAKYRGEFEERLKAVLSEVTAADgNIILFIDEMHTLVGAGK-ADGAMDASNLLKPALARGELHCVGAT 315
Cdd:TIGR02639 239 KIYSLDMGTLLAGTKYRGDFEERLKAVVSEIEKEP-NAILFIDEIHTIVGAGAtSGGSMDASNLLKPALSSGKIRCIGST 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276770 316 TLDEYRKHVEKDAALARRFQPVFVSEPTVEDTVSILRGLKEKYEQHHKVRVSDSALVAAATLSNRYITDRFLPDKAIDLV 395
Cdd:TIGR02639 318 TYEEYKNHFEKDRALSRRFQKIDVGEPSIEETVKILKGLKEQYEEFHHVKYSDEALEAAVELSARYINDRFLPDKAIDVI 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276770 396 DEASSRLRMQVDSKPEeldeidrrvmqlkierealkaekdeasrdrlvklekeltdleeesarltsrwaaekdklglaad 475
Cdd:TIGR02639 398 DEAGAAFRLRPKAKKK---------------------------------------------------------------- 413
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276770 476 lkkqldearnelaiaqrkgefqragelAYGQIPELEKklaeaeaqseeesasgmveetvkpdhvahIVSRWTGIPVDKML 555
Cdd:TIGR02639 414 ---------------------------ANVNVKDIEN-----------------------------VVAKMAKIPVKTVS 437
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276770 556 EGEREKLLRMEDEIAKRVVGQGEAVQSVSKAVRRARAGLQDPNRPIGSFMFLGPTGVGKTELTKALASFLfddEQAMVRI 635
Cdd:TIGR02639 438 SDDREQLKNLEKNLKAKIFGQDEAIDQLVSAIKRSRAGLGDPNKPVGSFLFVGPTGVGKTELAKQLAEEL---GVHLLRF 514
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276770 636 DMSEFMEKHSVARLIGAPPGYVGYEEGGVLTEAVRRRPYQVILFDEVEKAHPDVFNVLLQVLDDGRLTDGQGRTVDFRNT 715
Cdd:TIGR02639 515 DMSEYMEKHTVSRLIGSPPGYVGFEQGGLLTDAVRKHPHCVLLLDEIEKAHPDIYNILLQVMDYATLTDNNGRKADFRNV 594
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276770 716 LIIMTSNLGAEY----LVNLGEnedvDKVRTEVMDVVKASFRPEFLNRIDEVILFHRLRRQDMGKIVEIQLQRLERLLAD 791
Cdd:TIGR02639 595 ILIMTSNAGASEmskpPIGFGG----ENRESKSLKAIKKLFSPEFRNRLDAIIHFNDLSEEMAEKIVKKFLDELQDQLNE 670
|
810 820 830 840 850 860
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276770 792 RKITLDLDKDAVEWLAEKGYDPAYGARPLKRVMQKELQDPLAEKILQGEIFDNSTVKITA 851
Cdd:TIGR02639 671 KNIELELTDDAKKYLAEKGYDEEFGARPLARVIQEEIKKPLSDEILFGKLKKGGSVKISL 730
|
|
| VI_ClpV1 |
TIGR03345 |
type VI secretion ATPase, ClpV1 family; Members of this protein family are homologs of ClpB, ... |
14-838 |
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: 749.85 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276770 14 IQSAQTQALSSNHQQFTPEHLLKVLVDDEEGLAASLIERAGGRAKDVRLGVEAALKAMPQvegGNGQlymaqplAKVFST 93
Cdd:TIGR03345 9 LEQAAALCVARGHPEVELEHWLLALLDQPDSDLAAILRHFGVDLGRLKADLARALDKLPR---GNTR-------TPVFSP 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276770 94 A-EELAKKA--------GDSFVTVERLLTALAVEKSAKT-----ADILSKagVTPTALNQAINDIRKG------------ 147
Cdd:TIGR03345 79 HlVELLQEAwllaslelGDGRIRSGHLLLALLTDPELRRllgsiSPELAK--IDREALREALPALVEGsaeasaaaadaa 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276770 148 RTADSASAEQGyDALKKYARDLTADARAGKLDPVIGRDDEIRRTIQVLSRRTKNNPVLIGEPGVGKTAIAEGLALRIVNG 227
Cdd:TIGR03345 157 PAGAAAGAAGT-SALDQYTTDLTAQAREGKIDPVLGRDDEIRQMIDILLRRRQNNPILTGEAGVGKTAVVEGLALRIAAG 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276770 228 DVPESLKDKQLMALDMGSLIAGAKYRGEFEERLKAVLSEVTAADGNIILFIDEMHTLVGAGKADGAMDASNLLKPALARG 307
Cdd:TIGR03345 236 DVPPALRNVRLLSLDLGLLQAGASVKGEFENRLKSVIDEVKASPQPIILFIDEAHTLIGAGGQAGQGDAANLLKPALARG 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276770 308 ELHCVGATTLDEYRKHVEKDAALARRFQPVFVSEPTVEDTVSILRGLKEKYEQHHKVRVSDSALVAAATLSNRYITDRFL 387
Cdd:TIGR03345 316 ELRTIAATTWAEYKKYFEKDPALTRRFQVVKVEEPDEETAIRMLRGLAPVLEKHHGVLILDEAVVAAVELSHRYIPGRQL 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276770 388 PDKAIDLVDEASSRLRMQVDSKPEELDEIDRRVMQLKIEREALKAE--KDEASRDRLVKLEKELTDLEEESARLTSRWAA 465
Cdd:TIGR03345 396 PDKAVSLLDTACARVALSQNATPAALEDLRRRIAALELELDALEREaaLGADHDERLAELRAELAALEAELAALEARWQQ 475
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276770 466 EKdklglaaDLKKQLDEARNELAIAQRKGEFQRAGELAygQIPELEKKLAEAEAQSEeesasgMVEETVKPDHVAHIVSR 545
Cdd:TIGR03345 476 EK-------ELVEAILALRAELEADADAPADDDDALRA--QLAELEAALASAQGEEP------LVFPEVDAQAVAEVVAD 540
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276770 546 WTGIPVDKMLEGEREKLLRMEDEIAKRVVGQGEAVQSVSKAVRRARAGLQDPNRPIGSFMFLGPTGVGKTELTKALASFL 625
Cdd:TIGR03345 541 WTGIPVGRMVRDEIEAVLSLPDRLAERVIGQDHALEAIAERIRTARAGLEDPRKPLGVFLLVGPSGVGKTETALALAELL 620
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276770 626 FDDEQAMVRIDMSEFMEKHSVARLIGAPPGYVGYEEGGVLTEAVRRRPYQVILFDEVEKAHPDVFNVLLQVLDDGRLTDG 705
Cdd:TIGR03345 621 YGGEQNLITINMSEFQEAHTVSRLKGSPPGYVGYGEGGVLTEAVRRKPYSVVLLDEVEKAHPDVLELFYQVFDKGVMEDG 700
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276770 706 QGRTVDFRNTLIIMTSNLGAEYLVNLGENE----DVDKVRTEVMDVVKASFRPEFLNRIdEVILFHRLRRQDMGKIVEIQ 781
Cdd:TIGR03345 701 EGREIDFKNTVILLTSNAGSDLIMALCADPetapDPEALLEALRPELLKVFKPAFLGRM-TVIPYLPLDDDVLAAIVRLK 779
|
810 820 830 840 850
....*....|....*....|....*....|....*....|....*....|....*...
gi 1998276770 782 LQRLERLLADR-KITLDLDKDAVEWLAEKGYDPAYGARPLKRVMQKELQDPLAEKILQ 838
Cdd:TIGR03345 780 LDRIARRLKENhGAELVYSEALVEHIVARCTEVESGARNIDAILNQTLLPELSRQILE 837
|
|
| clpA |
PRK11034 |
ATP-dependent Clp protease ATP-binding subunit; Provisional |
14-858 |
0e+00 |
|
ATP-dependent Clp protease ATP-binding subunit; Provisional
Pssm-ID: 236828 [Multi-domain] Cd Length: 758 Bit Score: 558.68 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276770 14 IQSAQTQALSSNHQQFTPEHLLKVLVDD---EEGLAASLIERAGGRaKDVRLGVEAALKAMPQveggNGQLYMAQP---L 87
Cdd:PRK11034 10 LNMAFARAREHRHEFMTVEHLLLALLSNpsaREALEACSVDLVALR-QELEAFIEQTTPVLPA----SEEERDTQPtlsF 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276770 88 AKVFSTAEELAKKAGDSFVTVERLLTALAVEKSAKTADILSKAGVTP-TALNQAINDIRKGRTA-------DSASAEQ-- 157
Cdd:PRK11034 85 QRVLQRAVFHVQSSGRSEVTGANVLVAIFSEQESQAAYLLRKHEVSRlDVVNFISHGTRKDEPSqssdpgsQPNSEEQag 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276770 158 GYDALKKYARDLTADARAGKLDPVIGRDDEIRRTIQVLSRRTKNNPVLIGEPGVGKTAIAEGLALRIVNGDVPESLKDKQ 237
Cdd:PRK11034 165 GEERMENFTTNLNQLARVGGIDPLIGREKELERAIQVLCRRRKNNPLLVGESGVGKTAIAEGLAWRIVQGDVPEVMADCT 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276770 238 LMALDMGSLIAGAKYRGEFEERLKAVLSEVtAADGNIILFIDEMHTLVGAGKADGA-MDASNLLKPALARGELHCVGATT 316
Cdd:PRK11034 245 IYSLDIGSLLAGTKYRGDFEKRFKALLKQL-EQDTNSILFIDEIHTIIGAGAASGGqVDAANLIKPLLSSGKIRVIGSTT 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276770 317 LDEYRKHVEKDAALARRFQPVFVSEPTVEDTVSILRGLKEKYEQHHKVRVSDSALVAAATLSNRYITDRFLPDKAIDLVD 396
Cdd:PRK11034 324 YQEFSNIFEKDRALARRFQKIDITEPSIEETVQIINGLKPKYEAHHDVRYTAKAVRAAVELAVKYINDRHLPDKAIDVID 403
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276770 397 EASSRLRMqvdskpeeldeidrrvmqlkierealkaekdeasrdrlvklekeltdleeesarltsrwaaekdklglaadl 476
Cdd:PRK11034 404 EAGARARL------------------------------------------------------------------------ 411
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276770 477 kkqldearneLAIAQRKgefqragelaygqipelekklaeaeaqseeesasgmveETVKPDHVAHIVSRWTGIPVDKMLE 556
Cdd:PRK11034 412 ----------MPVSKRK--------------------------------------KTVNVADIESVVARIARIPEKSVSQ 443
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276770 557 GEREKLLRMEDEIAKRVVGQGEAVQSVSKAVRRARAGLQDPNRPIGSFMFLGPTGVGKTELTKALASFLfddEQAMVRID 636
Cdd:PRK11034 444 SDRDTLKNLGDRLKMLVFGQDKAIEALTEAIKMSRAGLGHEHKPVGSFLFAGPTGVGKTEVTVQLSKAL---GIELLRFD 520
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276770 637 MSEFMEKHSVARLIGAPPGYVGYEEGGVLTEAVRRRPYQVILFDEVEKAHPDVFNVLLQVLDDGRLTDGQGRTVDFRNTL 716
Cdd:PRK11034 521 MSEYMERHTVSRLIGAPPGYVGFDQGGLLTDAVIKHPHAVLLLDEIEKAHPDVFNLLLQVMDNGTLTDNNGRKADFRNVV 600
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276770 717 IIMTSNLGAEYLVNLGENEDVDKVRTEVMDVVKASFRPEFLNRIDEVILFHRLRRQDMGKIVEIQLQRLERLLADRKITL 796
Cdd:PRK11034 601 LVMTTNAGVRETERKSIGLIHQDNSTDAMEEIKKIFTPEFRNRLDNIIWFDHLSTDVIHQVVDKFIVELQAQLDQKGVSL 680
|
810 820 830 840 850 860
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1998276770 797 DLDKDAVEWLAEKGYDPAYGARPLKRVMQKELQDPLAEKILQGEIFDNSTVKITAGSDRLNF 858
Cdd:PRK11034 681 EVSQEARDWLAEKGYDRAMGARPMARVIQDNLKKPLANELLFGSLVDGGQVTVALDKEKNEL 742
|
|
| RecA-like_ClpB_Hsp104-like |
cd19499 |
Chaperone protein ClpB/Hsp104 subfamily; Bacterial Caseinolytic peptidase B (ClpB) and ... |
561-766 |
4.27e-108 |
|
Chaperone protein ClpB/Hsp104 subfamily; Bacterial Caseinolytic peptidase B (ClpB) and eukaryotic Heat shock protein 104 (Hsp104) are ATP-dependent molecular chaperones and essential proteins of the heat-shock response. ClpB/Hsp104 ATPases, in concert with the DnaK/Hsp70 chaperone system, disaggregate and reactivate aggregated proteins. This RecA-like_ClpB_Hsp104_like subfamily belongs to the RecA-like NTPase family which includes the NTP binding domain of F1 and V1 H(+)ATPases, DnaB and related helicases as well as bacterial RecA and related eukaryotic and archaeal recombinases. The RecA-like NTPase family also includes bacterial conjugation proteins and related DNA transfer proteins involved in type II and type IV secretion.
Pssm-ID: 410907 [Multi-domain] Cd Length: 178 Bit Score: 329.91 E-value: 4.27e-108
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276770 561 KLLRMEDEIAKRVVGQGEAVQSVSKAVRRARAGLQDPNRPIGSFMFLGPTGVGKTELTKALASFLFDDEQAMVRIDMSEF 640
Cdd:cd19499 1 KLLNLEERLHERVVGQDEAVKAVSDAIRRARAGLSDPNRPIGSFLFLGPTGVGKTELAKALAELLFGDEDNLIRIDMSEY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276770 641 MEKHSVARLIGAPPGYVGYEEGGVLTEAVRRRPYQVILFDEVEKAHPDVFNVLLQVLDDGRLTDGQGRTVDFRNTLIIMT 720
Cdd:cd19499 81 MEKHSVSRLIGAPPGYVGYTEGGQLTEAVRRKPYSVVLLDEIEKAHPDVQNLLLQVLDDGRLTDSHGRTVDFKNTIIIMT 160
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1998276770 721 SNLgaeylvnlgenedvdkvrtevmdvvkasFRPEFLNRIDEVILF 766
Cdd:cd19499 161 SNH----------------------------FRPEFLNRIDEIVVF 178
|
|
| AAA_2 |
pfam07724 |
AAA domain (Cdc48 subfamily); This Pfam entry includes some of the AAA proteins not detected ... |
599-763 |
3.80e-96 |
|
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: 297.95 E-value: 3.80e-96
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276770 599 RPIGSFMFLGPTGVGKTELTKALASFLFDDEQAMVRIDMSEFMEKHSVARLIGAPPGYVGYEEGGVLTEAVRRRPYQVIL 678
Cdd:pfam07724 1 RPIGSFLFLGPTGVGKTELAKALAELLFGDERALIRIDMSEYMEEHSVSRLIGAPPGYVGYEEGGQLTEAVRRKPYSIVL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276770 679 FDEVEKAHPDVFNVLLQVLDDGRLTDGQGRTVDFRNTLIIMTSNLGAEYL---VNLGENEDVDKVRTEVMDVVKASFRPE 755
Cdd:pfam07724 81 IDEIEKAHPGVQNDLLQILEGGTLTDKQGRTVDFKNTLFIMTGNFGSEKIsdaSRLGDSPDYELLKEEVMDLLKKGFIPE 160
|
....*...
gi 1998276770 756 FLNRIDEV 763
Cdd:pfam07724 161 FLGRLPII 168
|
|
| AAA_lid_9 |
pfam17871 |
AAA lid domain; This entry represents the alpha helical AAA+ lid domain that is found to the ... |
343-446 |
4.07e-47 |
|
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: 163.04 E-value: 4.07e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276770 343 TVEDTVSILRGLKEKYEQHHKVRVSDSALVAAATLSNRYITDRFLPDKAIDLVDEASSRLRMQVDSKPEELDEIDRRVMQ 422
Cdd:pfam17871 1 SVEEAIEILRGLKPKYEKHHGVRISDEALEAAVKLSKRYITDRFLPDKAIDLLDEACARVRLSQESKPEELEDLERELAK 80
|
90 100
....*....|....*....|....
gi 1998276770 423 LKIEREALKAEKDEASRDRLVKLE 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, ... |
769-849 |
3.39e-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: 3.39e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276770 769 LRRQDMGKIVEIQLQRLERLLADRKITLDLDKDAVEWLAEKGYDPAYGARPLKRVMQKELQDPLAEKILQGEIFDNSTVK 848
Cdd:pfam10431 1 LSKEELRKIVDLQLKELQKRLAERGITLELTDAAKDWLAEKGYDPEYGARPLRRAIQREIEDPLAEEILSGELKEGDTVR 80
|
.
gi 1998276770 849 I 849
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, ... |
769-858 |
5.22e-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: 5.22e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276770 769 LRRQDMGKIVEIQLQRLERLLADRKITLDLDKDAVEWLAEKGYDPAYGARPLKRVMQKELQDPLAEKILQGEIFDNSTVK 848
Cdd:smart01086 1 LDKEDLVRIVDLPLNALQKRLAEKGITLEFTDEALDWLAEKGYDPKYGARPLRRIIQRELEDPLAELILSGELKDGDTVV 80
|
90
....*....|
gi 1998276770 849 ITAGSDRLNF 858
Cdd:smart01086 81 VDVDDGELVF 90
|
|
| AAA |
cd00009 |
The AAA+ (ATPases Associated with a wide variety of cellular Activities) superfamily ... |
182-339 |
6.68e-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: 6.68e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276770 182 IGRDDEIRRTIQVLSRRTKNNPVLIGEPGVGKTAIAEGLALRIVNGDVPeslkdkqLMALDMGSLIAGAKYRGEFEERLK 261
Cdd:cd00009 1 VGQEEAIEALREALELPPPKNLLLYGPPGTGKTTLARAIANELFRPGAP-------FLYLNASDLLEGLVVAELFGHFLV 73
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1998276770 262 AVLSEVTAADGNIILFIDEMHTLvGAGKADGAMDASNLLKPALA-RGELHCVGATTLDEYRKhveKDAALARRFQPVFV 339
Cdd:cd00009 74 RLLFELAEKAKPGVLFIDEIDSL-SRGAQNALLRVLETLNDLRIdRENVRVIGATNRPLLGD---LDRALYDRLDIRIV 148
|
|
| AAA |
cd00009 |
The AAA+ (ATPases Associated with a wide variety of cellular Activities) superfamily ... |
574-722 |
2.38e-17 |
|
The AAA+ (ATPases Associated with a wide variety of cellular Activities) superfamily represents an ancient group of ATPases belonging to the ASCE (for additional strand, catalytic E) division of the P-loop NTPase fold. The ASCE division also includes ABC, RecA-like, VirD4-like, PilT-like, and SF1/2 helicases. Members of the AAA+ ATPases function as molecular chaperons, ATPase subunits of proteases, helicases, or nucleic-acid stimulated ATPases. The AAA+ proteins contain several distinct features in addition to the conserved alpha-beta-alpha core domain structure and the Walker A and B motifs of the P-loop NTPases.
Pssm-ID: 99707 [Multi-domain] Cd Length: 151 Bit Score: 79.88 E-value: 2.38e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276770 574 VGQGEAVQSVSKAVRRaraglqdpnRPIGSFMFLGPTGVGKTELTKALASFLFDDEQAMVRIDMSEFMEKHSVARLIgap 653
Cdd:cd00009 1 VGQEEAIEALREALEL---------PPPKNLLLYGPPGTGKTTLARAIANELFRPGAPFLYLNASDLLEGLVVAELF--- 68
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1998276770 654 pgyvGYEEGGVLTEAVRRRPYQVILFDEVEKAHPDVFNVLLQVLDDGRLTdgqgrTVDFRNTLIIMTSN 722
Cdd:cd00009 69 ----GHFLVRLLFELAEKAKPGVLFIDEIDSLSRGAQNALLRVLETLNDL-----RIDRENVRVIGATN 128
|
|
| AAA_5 |
pfam07728 |
AAA domain (dynein-related subfamily); This Pfam entry includes some of the AAA proteins not ... |
603-722 |
5.71e-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: 69.63 E-value: 5.71e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276770 603 SFMFLGPTGVGKTELTKALASFLFDDEQAMVRidMSEFMEKhsvARLIGA--PPGYVGYEEGGVLTEAVRRRpyQVILFD 680
Cdd:pfam07728 1 GVLLVGPPGTGKTELAERLAAALSNRPVFYVQ--LTRDTTE---EDLFGRrnIDPGGASWVDGPLVRAAREG--EIAVLD 73
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 1998276770 681 EVEKAHPDVFNVLLQVLDDGRLTDGQGRT---VDFRNTLIIMTSN 722
Cdd:pfam07728 74 EINRANPDVLNSLLSLLDERRLLLPDGGElvkAAPDGFRLIATMN 118
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
605-728 |
2.71e-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: 68.17 E-value: 2.71e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276770 605 MFLGPTGVGKTELTKALASFLFDDEQAMVRIDMSEFMEKHSVARLIGAPPGYVGYEEGG----VLTEAVRRRPYQVILFD 680
Cdd:smart00382 6 LIVGPPGSGKTTLARALARELGPPGGGVIYIDGEDILEEVLDQLLLIIVGGKKASGSGElrlrLALALARKLKPDVLILD 85
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 1998276770 681 EVEKAHPDVFNVLLQVLDDGRLTDGQGRtvdFRNTLIIMTSNLGAEYL 728
Cdd:smart00382 86 EITSLLDAEQEALLLLLEELRLLLLLKS---EKNLTVILTTNDEKDLG 130
|
|
| Clp_N |
pfam02861 |
Clp amino terminal domain, pathogenicity island component; This short domain is found in one ... |
17-69 |
2.12e-10 |
|
Clp amino terminal domain, pathogenicity island component; This short domain is found in one or two copies at the amino terminus of ClpA and ClpB proteins from bacteria and eukaryotes. The function of these domains is uncertain but they may form a protein binding site. In many bacterial species, including E.coli, this region represents the N-terminus of one of the key components of the pathogenicity island complex that injects toxin from one bacterium into another.
Pssm-ID: 460724 [Multi-domain] Cd Length: 53 Bit Score: 56.76 E-value: 2.12e-10
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 1998276770 17 AQTQALSSNHQQFTPEHLLKVLVDDEEGLAASLIERAGGRAKDVRLGVEAALK 69
Cdd:pfam02861 1 AQELARALGHQYIGTEHLLLALLEEDDGLAARLLKKAGVDLDALREAIEKLLG 53
|
|
| RecA-like_protease |
cd19481 |
proteases similar to RecA; RecA-like NTPases. This family includes the NTP binding domain of ... |
578-766 |
6.70e-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: 58.45 E-value: 6.70e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276770 578 EAVQSVSKAVRRARAGLQDPNRPIGSFMFLGPTGVGKTELTKALASFLFDDeqaMVRIDMSEFMEKHSvarligappgYV 657
Cdd:cd19481 3 ASLREAVEAPRRGSRLRRYGLGLPKGILLYGPPGTGKTLLAKALAGELGLP---LIVVKLSSLLSKYV----------GE 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276770 658 GYEEGGVLTEAVRRRPYQVILFDEVEKAHPD------------VFNVLLQVLDDGRLTDgqgrtvdfrNTLIIMTSNlga 725
Cdd:cd19481 70 SEKNLRKIFERARRLAPCILFIDEIDAIGRKrdssgesgelrrVLNQLLTELDGVNSRS---------KVLVIAATN--- 137
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1998276770 726 eylvnlgenedvdkvRTEVMDvvKASFRPeflNRIDEVILF 766
Cdd:cd19481 138 ---------------RPDLLD--PALLRP---GRFDEVIEF 158
|
|
| Clp_N |
pfam02861 |
Clp amino terminal domain, pathogenicity island component; This short domain is found in one ... |
94-146 |
1.08e-09 |
|
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: 54.83 E-value: 1.08e-09
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 1998276770 94 AEELAKKAGDSFVTVERLLTALAVEKSAKTADILSKAGVTPTALNQAINDIRK 146
Cdd:pfam02861 1 AQELARALGHQYIGTEHLLLALLEEDDGLAARLLKKAGVDLDALREAIEKLLG 53
|
|
| AAA |
pfam00004 |
ATPase family associated with various cellular activities (AAA); AAA family proteins often ... |
205-338 |
5.20e-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: 55.29 E-value: 5.20e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276770 205 LIGEPGVGKTAIAEGLAlrivngdvpeSLKDKQLMALDMGSLIagAKYRGEFEERLKAVLSEVTAAdGNIILFIDEMHTL 284
Cdd:pfam00004 3 LYGPPGTGKTTLAKAVA----------KELGAPFIEISGSELV--SKYVGESEKRLRELFEAAKKL-APCVIFIDEIDAL 69
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1998276770 285 VGAGKADG---AMDASNLLKPAL-----ARGELHCVGATTldeyrkHVEK-DAALARRFQPVF 338
Cdd:pfam00004 70 AGSRGSGGdseSRRVVNQLLTELdgftsSNSKVIVIAATN------RPDKlDPALLGRFDRII 126
|
|
| SpoVK |
COG0464 |
AAA+-type ATPase, SpoVK/Ycf46/Vps4 family [Cell wall/membrane/envelope biogenesis, Cell cycle ... |
38-352 |
5.96e-08 |
|
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: 56.07 E-value: 5.96e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276770 38 LVDDEEGLAASLIERAGGRAKDVRLGVEAALKAMPQVEGGNGQLYMAQPLAKVFSTAEELAKKAGDSFVTVERLLTALAV 117
Cdd:COG0464 16 LLLDDAALRLLLLLLLALAAALLLLLLLLLLLLLALLLVELLLLLLSGALAALLLLALLLLALLALLAALLSALELLLLG 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276770 118 EKSAKTADILSKAGVTPTALNQAINDIRKGRTADSASAEQGYDALKKYARDLTADARAGKLDPVIGRDD---EIRRTIQV 194
Cdd:COG0464 96 ELLLLLLLLLLLLLLLLDLERALLELLRESAEALALAAPLVTYEDIGGLEEELLELREAILDDLGGLEEvkeELRELVAL 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276770 195 LSRRTK-------NNP---VLIGEPGVGKTAIAEGLAlRIVNGDvpeslkdkqLMALDMGSLIagAKYRGEFEERLKAVL 264
Cdd:COG0464 176 PLKRPElreeyglPPPrglLLYGPPGTGKTLLARALA-GELGLP---------LIEVDLSDLV--SKYVGETEKNLREVF 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276770 265 SEVtAADGNIILFIDEMHTLVGA--GKADGAMDA--SNLLKpALA--RGELHCVGATtldeYRKHvEKDAALARRFQ-PV 337
Cdd:COG0464 244 DKA-RGLAPCVLFIDEADALAGKrgEVGDGVGRRvvNTLLT-EMEelRSDVVVIAAT----NRPD-LLDPALLRRFDeII 316
|
330
....*....|....*
gi 1998276770 338 FVSEPTVEDTVSILR 352
Cdd:COG0464 317 FFPLPDAEERLEIFR 331
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
343-514 |
1.09e-06 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 52.61 E-value: 1.09e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276770 343 TVEDTVSILRGLKEKYEQHHKVRVSDSALVAAATLSNRYITDRflpdkAIDLVDEASSRLRMQVDSKPEELDEIDRRVMQ 422
Cdd:COG4913 246 DAREQIELLEPIRELAERYAAARERLAELEYLRAALRLWFAQR-----RLELLEAELEELRAELARLEAELERLEARLDA 320
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276770 423 LKIEREALKAEKDEASRDRLVKLEKELTDLEEESARLTSRWAAEKD---KLGL-----AADLKKQLDEARNELA-IAQRK 493
Cdd:COG4913 321 LREELDELEAQIRGNGGDRLEQLEREIERLERELEERERRRARLEAllaALGLplpasAEEFAALRAEAAALLEaLEEEL 400
|
170 180
....*....|....*....|.
gi 1998276770 494 GEFQRAGELAYGQIPELEKKL 514
Cdd:COG4913 401 EALEEALAEAEAALRDLRREL 421
|
|
| AAA |
pfam00004 |
ATPase family associated with various cellular activities (AAA); AAA family proteins often ... |
605-722 |
2.85e-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: 47.20 E-value: 2.85e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276770 605 MFLGPTGVGKTELTKALASFLFDDeqaMVRIDMSEFMEKHsvarlIGAPPGYVgyeeGGVLTEAVRRRPyQVILFDEVEK 684
Cdd:pfam00004 2 LLYGPPGTGKTTLAKAVAKELGAP---FIEISGSELVSKY-----VGESEKRL----RELFEAAKKLAP-CVIFIDEIDA 68
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 1998276770 685 AHP-----------DVFNVLLQVLDdgrltdgqGRTVDFRNTLIIMTSN 722
Cdd:pfam00004 69 LAGsrgsggdsesrRVVNQLLTELD--------GFTSSNSKVIVIAATN 109
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
199-339 |
3.07e-05 |
|
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: 45.06 E-value: 3.07e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276770 199 TKNNPVLIGEPGVGKTAIAEGLALRI---------VNGDVPESLKDKQLMALdmgsLIAGAKYRGEFEERLKAVLSEVtA 269
Cdd:smart00382 1 PGEVILIVGPPGSGKTTLARALARELgppgggviyIDGEDILEEVLDQLLLI----IVGGKKASGSGELRLRLALALA-R 75
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1998276770 270 ADGNIILFIDEMHTLVGAG--KADGAMDASNLLKPALARGELHCVGATTldeyRKHVEKDAALARRFQPVFV 339
Cdd:smart00382 76 KLKPDVLILDEITSLLDAEqeALLLLLEELRLLLLLKSEKNLTVILTTN----DEKDLGPALLRRRFDRRIV 143
|
|
| SpoVK |
COG0464 |
AAA+-type ATPase, SpoVK/Ycf46/Vps4 family [Cell wall/membrane/envelope biogenesis, Cell cycle ... |
412-809 |
7.27e-05 |
|
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: 46.06 E-value: 7.27e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276770 412 ELDEIDRRVMQLKIEREALKAEKDEASRDRLVKLEKELTDLEEESARLTSRWAAEKDKLGLAADLKKQLDEARNELAIAQ 491
Cdd:COG0464 1 LAELLALAVALALALLLLDDAALRLLLLLLLALAAALLLLLLLLLLLLLALLLVELLLLLLSGALAALLLLALLLLALLA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276770 492 RKGEFQRAGELAYGQIPELEKKLAEAEAQSEEESASGMVEETVKPDHVAHIVSRWTGIPVDKMLEGEREKLLRMEDEiak 571
Cdd:COG0464 81 LLAALLSALELLLLGELLLLLLLLLLLLLLLLDLERALLELLRESAEALALAAPLVTYEDIGGLEEELLELREAILD--- 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276770 572 RVVGQGEAVQSVSKAV--------RRARAGLqdpnRPIGSFMFLGPTGVGKTELTKALASFLfddEQAMVRIDMSEFMEK 643
Cdd:COG0464 158 DLGGLEEVKEELRELValplkrpeLREEYGL----PPPRGLLLYGPPGTGKTLLARALAGEL---GLPLIEVDLSDLVSK 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276770 644 hsvarligappgYVGYEEGGV--LTEAVRRRPYQVILFDEVEKAHPD-----------VFNVLLQVLDDGRltdgqgrtv 710
Cdd:COG0464 231 ------------YVGETEKNLreVFDKARGLAPCVLFIDEADALAGKrgevgdgvgrrVVNTLLTEMEELR--------- 289
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276770 711 dfRNTLIIMTSNlgaeylvnlgenedvdkvRTEVMDvvkasfrPEFLNRIDEVILFHRLRRQDMGKIveiqlqrLERLLA 790
Cdd:COG0464 290 --SDVVVIAATN------------------RPDLLD-------PALLRRFDEIIFFPLPDAEERLEI-------FRIHLR 335
|
410
....*....|....*....
gi 1998276770 791 DRKITLDLDkdaVEWLAEK 809
Cdd:COG0464 336 KRPLDEDVD---LEELAEA 351
|
|
| RecA-like_HslU |
cd19498 |
ATP-dependent protease ATPase subunit HslU; HslU is a component of the ATP-dependent protease ... |
567-684 |
7.91e-05 |
|
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: 44.29 E-value: 7.91e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276770 567 DEIAKRVVGQGEAVQSVSKAVR------RARAGLQDPNRPIGSFMfLGPTGVGKTELTKALASFLfddEQAMVRIDMSEF 640
Cdd:cd19498 7 SELDKYIIGQDEAKRAVAIALRnrwrrmQLPEELRDEVTPKNILM-IGPTGVGKTEIARRLAKLA---GAPFIKVEATKF 82
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 1998276770 641 MEKhsvarligappGYVGYEeggvlTEAVRRRPYQVILF-DEVEK 684
Cdd:cd19498 83 TEV-----------GYVGRD-----VESIIRDLVEGIVFiDEIDK 111
|
|
| COG1223 |
COG1223 |
Predicted ATPase, AAA+ superfamily [General function prediction only]; |
178-335 |
3.29e-04 |
|
Predicted ATPase, AAA+ superfamily [General function prediction only];
Pssm-ID: 440836 [Multi-domain] Cd Length: 246 Bit Score: 43.33 E-value: 3.29e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276770 178 LDPVIGrDDEIRRTIQVLSRRTKNNPVL-------------IGEPGVGKTAIAEGLALRIvngDVPeslkdkqLMALDMG 244
Cdd:COG1223 1 LDDVVG-QEEAKKKLKLIIKELRRRENLrkfglwpprkilfYGPPGTGKTMLAEALAGEL---KLP-------LLTVRLD 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276770 245 SLIAgaKYRGEFEERLKAVLSEVTAADGniILFIDEMHTLvgagkadgamdasnllkpALARGELHCVGA---------T 315
Cdd:COG1223 70 SLIG--SYLGETARNLRKLFDFARRAPC--VIFFDEFDAI------------------AKDRGDQNDVGEvkrvvnallQ 127
|
170 180 190
....*....|....*....|....*....|
gi 1998276770 316 TLDEYRKHV----------EKDAALARRFQ 335
Cdd:COG1223 128 ELDGLPSGSvviaatnhpeLLDSALWRRFD 157
|
|
| RecA-like_protease |
cd19481 |
proteases similar to RecA; RecA-like NTPases. This family includes the NTP binding domain of ... |
205-284 |
4.16e-04 |
|
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: 41.88 E-value: 4.16e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276770 205 LIGEPGVGKTAIAEGLAlrivngdvpESLkDKQLMALDMGSLIagAKYRGEFEERLKAVLSEVTAAdGNIILFIDEMHTL 284
Cdd:cd19481 31 LYGPPGTGKTLLAKALA---------GEL-GLPLIVVKLSSLL--SKYVGESEKNLRKIFERARRL-APCILFIDEIDAI 97
|
|
| AAA_5 |
pfam07728 |
AAA domain (dynein-related subfamily); This Pfam entry includes some of the AAA proteins not ... |
204-334 |
5.00e-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: 5.00e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276770 204 VLIGEPGVGKTAIAEGLALRIVNGDV----------PESLKDKQLMALDMGSLIAGAKYRgEFEERLKAVLSEVTAADGN 273
Cdd:pfam07728 3 LLVGPPGTGKTELAERLAAALSNRPVfyvqltrdttEEDLFGRRNIDPGGASWVDGPLVR-AAREGEIAVLDEINRANPD 81
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1998276770 274 I------ILFIDEMHTLVGAGKADGAMDASNLLkpalargelhcvgATTLDEYRKHVEKDAALARRF 334
Cdd:pfam07728 82 VlnsllsLLDERRLLLPDGGELVKAAPDGFRLI-------------ATMNPLDRGLNELSPALRSRF 135
|
|
| RecA-like_KTNA1 |
cd19522 |
Katanin p60 ATPase-containing subunit A1; Katanin p60 ATPase-containing subunit A1 (KTNA1) is ... |
197-335 |
6.20e-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: 6.20e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276770 197 RRTKNNPVLIGEPGVGKTAIAEGLAlrivngdvpeslKDKQLMALDMGSLIAGAKYRGEfEERLKAVLSEVTAADGNIIL 276
Cdd:cd19522 30 RRPWKGVLMVGPPGTGKTLLAKAVA------------TECGTTFFNVSSSTLTSKYRGE-SEKLVRLLFEMARFYAPTTI 96
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1998276770 277 FIDEMHTLVGAGKADGAMDASNLLKPALARGELHCVGATTLDEYRKHV----------EKDAALARRFQ 335
Cdd:cd19522 97 FIDEIDSICSRRGTSEEHEASRRVKSELLVQMDGVGGASENDDPSKMVmvlaatnfpwDIDEALRRRLE 165
|
|
| AAA_22 |
pfam13401 |
AAA domain; |
603-701 |
6.53e-04 |
|
AAA domain;
Pssm-ID: 379165 [Multi-domain] Cd Length: 129 Bit Score: 40.40 E-value: 6.53e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276770 603 SFMFL-GPTGVGKTELTKALASFLFDDEQAMVRIDMSEFMEK----HSVARLIGAPPGYVGYEE---GGVLTEAVRRRPY 674
Cdd:pfam13401 6 GILVLtGESGTGKTTLLRRLLEQLPEVRDSVVFVDLPSGTSPkdllRALLRALGLPLSGRLSKEellAALQQLLLALAVA 85
|
90 100
....*....|....*....|....*..
gi 1998276770 675 QVILFDEVEKAHPDVFNVLLQVLDDGR 701
Cdd:pfam13401 86 VVLIIDEAQHLSLEALEELRDLLNLSS 112
|
|
| FlhF |
COG1419 |
Flagellar biosynthesis GTPase FlhF [Cell motility]; |
559-615 |
1.10e-03 |
|
Flagellar biosynthesis GTPase FlhF [Cell motility];
Pssm-ID: 441029 [Multi-domain] Cd Length: 361 Bit Score: 42.16 E-value: 1.10e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1998276770 559 REKLLRME--DEIAKRVVGQGEAVQSVSKAVRRARAGLQD----PNRPIGS----FMFLGPTGVGKT 615
Cdd:COG1419 112 LERLLEAGvsPELARELLEKLPEDLSAEEAWRALLEALARrlpvAEDPLLDeggvIALVGPTGVGKT 178
|
|
| RecA-like_ClpX |
cd19497 |
ATP-dependent Clp protease ATP-binding subunit ClpX; ClpX is a component of the ATP-dependent ... |
571-625 |
1.75e-03 |
|
ATP-dependent Clp protease ATP-binding subunit ClpX; ClpX is a component of the ATP-dependent protease ClpXP. In ClpXP, ClpX ATPase serves to specifically recognize, unfold, and translocate protein substrates into the chamber of ClpP protease for degradation. This RecA-like_ClpX domain subfamily belongs to the RecA-like NTPase family which includes the NTP binding domain of F1 and V1 H(+)ATPases, DnaB and related helicases as well as bacterial RecA and related eukaryotic and archaeal recombinases. The RecA-like NTPase family also includes bacterial conjugation proteins and related DNA transfer proteins involved in type II and type IV secretion.
Pssm-ID: 410905 [Multi-domain] Cd Length: 251 Bit Score: 41.05 E-value: 1.75e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1998276770 571 KRVVGQGEAVQSVSKAV----RRARAGLQDPNRPI----GSFMFLGPTGVGKTELTKALASFL 625
Cdd:cd19497 12 KYVIGQERAKKVLSVAVynhyKRIRNNLKQKDDDVelekSNILLIGPTGSGKTLLAQTLAKIL 74
|
|
| flhF |
PRK05703 |
flagellar biosynthesis protein FlhF; |
374-615 |
2.65e-03 |
|
flagellar biosynthesis protein FlhF;
Pssm-ID: 235570 [Multi-domain] Cd Length: 424 Bit Score: 41.03 E-value: 2.65e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276770 374 AATLSNRYITDR-FLPDKAIDLV-----DEASSRLRMQVDSKPEELDEIDRRvmQLKIEREALKAEKDEASRDRLVKLEK 447
Cdd:PRK05703 26 AVILSNKKVRKGgFLGKKLVEVTaavdeDETPKKNPVLREEKRKPAKSILSL--QALLEKRPSRTNSQDALLQAENALPE 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276770 448 ELTDLEEESARLTSRWAAEKDKlglaADLKKQLDEARNELAIAQRKGEFQRAGELAYGQIP----ELEKKLAEAeaqsee 523
Cdd:PRK05703 104 WKKELEKPSEPKEEEPKAAAES----KVVQKELDELRDELKELKNLLEDQLSGLRQVERIPpefaELYKRLKRS------ 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276770 524 esasGMveetvKPDHVAHIVSRwtgipvdkmlegerekLLRMEDEIakrvvgQGEAVQSVSKAVRRA-RAGLQDPNRPIG 602
Cdd:PRK05703 174 ----GL-----SPEIAEKLLKL----------------LLEHMPPR------ERTAWRYLLELLANMiPVRVEDILKQGG 222
|
250
....*....|...
gi 1998276770 603 SFMFLGPTGVGKT 615
Cdd:PRK05703 223 VVALVGPTGVGKT 235
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
389-503 |
3.80e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 41.05 E-value: 3.80e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276770 389 DKAIDLVDEASSRLRMQVDSKPEELD--EIDRRVMQLKIEREALKAEKDE--ASRDRLVKLEKELTDLEEESARLTSRWA 464
Cdd:COG4913 637 EAELDALQERREALQRLAEYSWDEIDvaSAEREIAELEAELERLDASSDDlaALEEQLEELEAELEELEEELDELKGEIG 716
|
90 100 110
....*....|....*....|....*....|....*....
gi 1998276770 465 AEKDKLglaADLKKQLDEARNELAIAQRKGEFQRAGELA 503
Cdd:COG4913 717 RLEKEL---EQAEEELDELQDRLEAAEDLARLELRALLE 752
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
397-513 |
3.90e-03 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 40.79 E-value: 3.90e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276770 397 EASSRLRMQVDSKPEELDEIDRRVMQLKIEREALkaEKDEASRDRLVKLEKELTDLEEESARLTSRWAAEKDKLGLAADL 476
Cdd:PRK02224 558 EAAAEAEEEAEEAREEVAELNSKLAELKERIESL--ERIRTLLAAIADAEDEIERLREKREALAELNDERRERLAEKRER 635
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 1998276770 477 KKQLDEARNELAIAQRKGEFQRAGEL---AYGQIPELEKK 513
Cdd:PRK02224 636 KRELEAEFDEARIEEAREDKERAEEYleqVEEKLDELREE 675
|
|
| PRK09039 |
PRK09039 |
peptidoglycan -binding protein; |
402-495 |
6.90e-03 |
|
peptidoglycan -binding protein;
Pssm-ID: 181619 [Multi-domain] Cd Length: 343 Bit Score: 39.56 E-value: 6.90e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276770 402 LRMQVDSKPEELDEIDRRVMQLKierEALKAEKDEAS--RDRLVKLEKELTDLEEESARLTSRWA----AEKDKLGLAAD 475
Cdd:PRK09039 44 LSREISGKDSALDRLNSQIAELA---DLLSLERQGNQdlQDSVANLRASLSAAEAERSRLQALLAelagAGAAAEGRAGE 120
|
90 100
....*....|....*....|
gi 1998276770 476 LKKQLDEARNELAIAQRKGE 495
Cdd:PRK09039 121 LAQELDSEKQVSARALAQVE 140
|
|
| MoxR |
COG0714 |
MoxR-like ATPase [General function prediction only]; MoxR-like ATPase is part of the Pathway ... |
181-221 |
7.73e-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: 39.38 E-value: 7.73e-03
10 20 30 40
....*....|....*....|....*....|....*....|...
gi 1998276770 181 VIGRDDEIRR-TIQVLSRRtknnPVLI-GEPGVGKTAIAEGLA 221
Cdd:COG0714 14 YVGQEELIELvLIALLAGG----HLLLeGVPGVGKTTLAKALA 52
|
|
| PRK05431 |
PRK05431 |
seryl-tRNA synthetase; Provisional |
393-487 |
9.28e-03 |
|
seryl-tRNA synthetase; Provisional
Pssm-ID: 235461 [Multi-domain] Cd Length: 425 Bit Score: 39.28 E-value: 9.28e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276770 393 DLVDEASSRLRMQVDSkpEELDEIDRRVMQLKIEREALKAEKDEASRD--RLVKLEKELTDLEEESARLtsrwaaeKDKL 470
Cdd:PRK05431 12 EAVKEALAKRGFPLDV--DELLELDEERRELQTELEELQAERNALSKEigQAKRKGEDAEALIAEVKEL-------KEEI 82
|
90
....*....|....*..
gi 1998276770 471 glaADLKKQLDEARNEL 487
Cdd:PRK05431 83 ---KALEAELDELEAEL 96
|
|
| RecA-like_CDC48_NLV2_r1-like |
cd19503 |
first of two ATPase domains of CDC48 and NLV2, and similar ATPase domains; CDC48 in yeast and ... |
205-315 |
9.45e-03 |
|
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: 38.04 E-value: 9.45e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998276770 205 LIGEPGVGKTAIAEGLAlrivngdvPESlkDKQLMALDMGSLIagAKYRGEFEERLKAVLSEVTAADGNIIlFIDEMHTL 284
Cdd:cd19503 39 LHGPPGTGKTLLARAVA--------NEA--GANFLSISGPSIV--SKYLGESEKNLREIFEEARSHAPSII-FIDEIDAL 105
|
90 100 110
....*....|....*....|....*....|....*...
gi 1998276770 285 VGA-GKADGAMDAS------NLLKPALARGELHCVGAT 315
Cdd:cd19503 106 APKrEEDQREVERRvvaqllTLMDGMSSRGKVVVIAAT 143
|
|
| |
