|
Name |
Accession |
Description |
Interval |
E-value |
| VI_ClpV1 |
TIGR03345 |
type VI secretion ATPase, ClpV1 family; Members of this protein family are homologs of ClpB, ... |
11-859 |
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: 1082.66 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887424716 11 LNPYCARAMEGAASLCQTRAHAEIQPEHWLLKLLEQGEGDLTVLARRYEWDMDAIWQDLLGWLDKQPRSIRHRPQLSDAI 90
Cdd:TIGR03345 1 LNPTSRRALEQAAALCVARGHPEVELEHWLLALLDQPDSDLAAILRHFGVDLGRLKADLARALDKLPRGNTRTPVFSPHL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887424716 91 QTLMQEAWLIASLN-GEAQIRSLHLLMALVEKQNLVRcdglwpLLTLGQSQLERLRP-LLDAQSDERPEMQQEAELAQSH 168
Cdd:TIGR03345 81 VELLQEAWLLASLElGDGRIRSGHLLLALLTDPELRR------LLGSISPELAKIDReALREALPALVEGSAEASAAAAD 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887424716 169 GGEVEFVGRPVGTelkegelnpalqNALDKFTLDVTARAKEGNIDPVFGRDTEIRQMVDILSRRRKNNPILVGEPGVGKT 248
Cdd:TIGR03345 155 AAPAGAAAGAAGT------------SALDQYTTDLTAQAREGKIDPVLGRDDEIRQMIDILLRRRQNNPILTGEAGVGKT 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887424716 249 ALVEGLALRIAEGNVPESLRPVSLRTLDLGLLQAGAGVKGEFEQRLKNVIDAVQQSPAPVLLFIDEAHTIIGAGNQAGGA 328
Cdd:TIGR03345 223 AVVEGLALRIAAGDVPPALRNVRLLSLDLGLLQAGASVKGEFENRLKSVIDEVKASPQPIILFIDEAHTLIGAGGQAGQG 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887424716 329 DAANLLKPALARGELRTIAATTWSEYKQYFERDAALERRFQMVKVDEPDDDTACLMLRGLKSRYAVHHKVHITDDAVRAA 408
Cdd:TIGR03345 303 DAANLLKPALARGELRTIAATTWAEYKKYFEKDPALTRRFQVVKVEEPDEETAIRMLRGLAPVLEKHHGVLILDEAVVAA 382
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887424716 409 VTLSRRYLTGRQLPDKAVDLLDTAAARVRMSFDTVPEAVTQLNAQLTALALEEQGLLDDIVSGRNrHGDRLSAIALQRTM 488
Cdd:TIGR03345 383 VELSHRYIPGRQLPDKAVSLLDTACARVALSQNATPAALEDLRRRIAALELELDALEREAALGAD-HDERLAELRAELAA 461
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887424716 489 LDDQLQQLTRVSEQQRATVAELNACRQDI------------SRQAEMAGLQQQLAILQQTDVLVQVDVDTRTVANVIADW 556
Cdd:TIGR03345 462 LEAELAALEARWQQEKELVEAILALRAELeadadapaddddALRAQLAELEAALASAQGEEPLVFPEVDAQAVAEVVADW 541
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887424716 557 TGVPLSSLMKDEQTGLLTLEADIGKRVVGQDTALNAIAQRLRAAKTGLTSENGPQGVFLLVGPSGTGKTETALALADVLY 636
Cdd:TIGR03345 542 TGIPVGRMVRDEIEAVLSLPDRLAERVIGQDHALEAIAERIRTARAGLEDPRKPLGVFLLVGPSGVGKTETALALAELLY 621
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887424716 637 GGEKSLITINLSEYQEPHTVSQLKGSPPGYVGYGQGGILTEAVRKRPYSVVLLDEVEKAHRDVMNLFYQVFDRGFMRDGE 716
Cdd:TIGR03345 622 GGEQNLITINMSEFQEAHTVSRLKGSPPGYVGYGEGGVLTEAVRRKPYSVVLLDEVEKAHPDVLELFYQVFDKGVMEDGE 701
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887424716 717 GREIDFRNTVILMTSNLGSDHLMQLLDEQPDASEAD-LQELLRPILRDHFQPALLARFQTVIYRPLAEAAMRTIVEMKLE 795
Cdd:TIGR03345 702 GREIDFKNTVILLTSNAGSDLIMALCADPETAPDPEaLLEALRPELLKVFKPAFLGRMTVIPYLPLDDDVLAAIVRLKLD 781
|
810 820 830 840 850 860
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1887424716 796 QVSKRLSRHYGLTTHIEASLYDALTAACLLPDTGARNVDSLLNQQILPVLSQQLLTHMAAKQKP 859
Cdd:TIGR03345 782 RIARRLKENHGAELVYSEALVEHIVARCTEVESGARNIDAILNQTLLPELSRQILERLAAGEPI 845
|
|
| ClpA |
COG0542 |
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ... |
8-864 |
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: 1069.32 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887424716 8 LRRLNPYCARAMEGAASLCQTRAHAEIQPEHWLLKLLEQGEGDLTVLARRYEWDMDAIWQDLLGWLDKQPR--SIRHRPQ 85
Cdd:COG0542 3 FEKFTEKAQEALEAAQELARRLGHQEVEPEHLLLALLEQGEGLAAKLLRKLGVDLDALREELEEALGRLPKvsGSSGQPY 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887424716 86 LSDAIQTLMQEAWLIASLNGEAQIRSLHLLMALVEKQNLVRCDglwpLLTLGQSQLERLRPLLDAQSDERPEMQQEAEla 165
Cdd:COG0542 83 LSPRLKRVLELAELEARKLGDEYISTEHLLLALLREGEGVAAR----ILKKLGITLEALREALEELRGGSRVTSQNPE-- 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887424716 166 qshggevefvgrpvgtelkegelnpALQNALDKFTLDVTARAKEGNIDPVFGRDTEIRQMVDILSRRRKNNPILVGEPGV 245
Cdd:COG0542 157 -------------------------SKTPALDKYGRDLTELAREGKLDPVIGRDEEIRRVIQILSRRTKNNPVLIGEPGV 211
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887424716 246 GKTALVEGLALRIAEGNVPESLRPVSLRTLDLGLLQAGAGVKGEFEQRLKNVIDAVQQSPAPVLLFIDEAHTIIGAGNQA 325
Cdd:COG0542 212 GKTAIVEGLAQRIVNGDVPESLKDKRVLSLDLGALVAGAKYRGEFEERLKAVLDEVKKSEGNIILFIDELHTLVGAGGAE 291
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887424716 326 GGADAANLLKPALARGELRTIAATTWSEYKQYFERDAALERRFQMVKVDEPDDDTACLMLRGLKSRYAVHHKVHITDDAV 405
Cdd:COG0542 292 GAMDAANLLKPALARGELRCIGATTLDEYRKYIEKDAALERRFQPVLVEEPSVEDTISILRGLKERYEAHHGVRITDEAL 371
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887424716 406 RAAVTLSRRYLTGRQLPDKAVDLLDTAAARVRMSFDTVPEAVTQLNAQLTALALEEQGLLDDivsGRNRHGDRLSAIALQ 485
Cdd:COG0542 372 VAAVRLSDRYITDRFLPDKAIDLIDEAAARVRMEIDSKPEELDELERRLEQLEIEKEALKKE---QDEASFERLAELRDE 448
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887424716 486 RTMLDDQLQQLTRVSEQQRATVAELNACRQDISRQ-----AEMAGLQQQLAILQQTDVLVQVDVDTRTVANVIADWTGVP 560
Cdd:COG0542 449 LAELEEELEALKARWEAEKELIEEIQELKEELEQRygkipELEKELAELEEELAELAPLLREEVTEEDIAEVVSRWTGIP 528
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887424716 561 LSSLMKDEQTGLLTLEADIGKRVVGQDTALNAIAQRLRAAKTGLTSENGPQGVFLLVGPSGTGKTETALALADVLYGGEK 640
Cdd:COG0542 529 VGKLLEGEREKLLNLEEELHERVIGQDEAVEAVADAIRRSRAGLKDPNRPIGSFLFLGPTGVGKTELAKALAEFLFGDED 608
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887424716 641 SLITINLSEYQEPHTVSQLKGSPPGYVGYGQGGILTEAVRKRPYSVVLLDEVEKAHRDVMNLFYQVFDRGFMRDGEGREI 720
Cdd:COG0542 609 ALIRIDMSEYMEKHSVSRLIGAPPGYVGYEEGGQLTEAVRRRPYSVVLLDEIEKAHPDVFNILLQVLDDGRLTDGQGRTV 688
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887424716 721 DFRNTVILMTSNLGSDHLMQLLDEQPDASEadLQELLRPILRDHFQPALLARF-QTVIYRPLAEAAMRTIVEMKLEQVSK 799
Cdd:COG0542 689 DFRNTIIIMTSNIGSELILDLAEDEPDYEE--MKEAVMEELKKHFRPEFLNRIdEIIVFHPLSKEELRKIVDLQLKRLRK 766
|
810 820 830 840 850 860
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1887424716 800 RLSRHyGLTTHIEASLYDALTAACLLPDTGARNVDSLLNQQILPVLSQQLLTHMAAKQKPLSLTL 864
Cdd:COG0542 767 RLAER-GITLELTDAAKDFLAEKGYDPEYGARPLKRAIQRELEDPLAEEILAGEIKEGDTITVDV 830
|
|
| chaperone_ClpB |
TIGR03346 |
ATP-dependent chaperone ClpB; Members of this protein family are the bacterial ATP-dependent ... |
18-850 |
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: 707.10 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887424716 18 AMEGAASLCQTRAHAEIQPEHWLLKLLEQGEGDLTVLARRYEWDMDAIWQDLLGWLDKQPRSIRH--RPQLSDAIQTLMQ 95
Cdd:TIGR03346 8 ALQAAQSLALGRDHQQIEPEHLLKALLDQEGGLARPLLQKAGVNVGALRQALEKELERLPKVSGPggQVYLSPDLNRLLN 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887424716 96 EAWLIASLNGEAQIRSLHLLMALVEKQnlvrcDGLWPLLTLGQSQLERLRPLLDA------QSDERPEMQQEAelaqshg 169
Cdd:TIGR03346 88 LAEKLAQKRGDEFISSEHLLLALLDDK-----GTLGKLLKEAGATADALEAAINAvrggqkVTDANAEDQYEA------- 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887424716 170 gevefvgrpvgtelkegelnpalqnaLDKFTLDVTARAKEGNIDPVFGRDTEIRQMVDILSRRRKNNPILVGEPGVGKTA 249
Cdd:TIGR03346 156 --------------------------LEKYARDLTERAREGKLDPVIGRDEEIRRTIQVLSRRTKNNPVLIGEPGVGKTA 209
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887424716 250 LVEGLALRIAEGNVPESLRPVSLRTLDLGLLQAGAGVKGEFEQRLKNVIDAVQQSPAPVLLFIDEAHTIIGAGNQAGGAD 329
Cdd:TIGR03346 210 IVEGLAQRIVNGDVPEGLKNKRLLALDMGALIAGAKYRGEFEERLKAVLNEVTKSEGQIILFIDELHTLVGAGKAEGAMD 289
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887424716 330 AANLLKPALARGELRTIAATTWSEYKQYFERDAALERRFQMVKVDEPDDDTACLMLRGLKSRYAVHHKVHITDDAVRAAV 409
Cdd:TIGR03346 290 AGNMLKPALARGELHCIGATTLDEYRKYIEKDAALERRFQPVFVDEPSVEDTISILRGLKERYEVHHGVRITDPAIVAAA 369
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887424716 410 TLSRRYLTGRQLPDKAVDLLDTAAARVRMSFDTVPEAVTQLNAQLTALALEEQGLL--DDIVSgrnrhGDRLSAIALQRT 487
Cdd:TIGR03346 370 TLSHRYITDRFLPDKAIDLIDEAAARIRMEIDSKPEELDELDRRIIQLEIEREALKkeKDEAS-----KKRLEDLEKELA 444
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887424716 488 MLDDQLQQLTRVSEQQRATVAELNACRQDISR------QAEMAG--------------------LQQQLAILQQTDVLVQ 541
Cdd:TIGR03346 445 DLEEEYAELEEQWKAEKASIQGIQQIKEEIEQvrleleQAEREGdlakaaelqygklpelekqlQAAEQKLGEEQNRLLR 524
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887424716 542 VDVDTRTVANVIADWTGVPLSSLMKDEQTGLLTLEADIGKRVVGQDTALNAIAQRLRAAKTGLTSENGPQGVFLLVGPSG 621
Cdd:TIGR03346 525 EEVTAEEIAEVVSRWTGIPVSKMLEGEREKLLHMEEELHERVVGQDEAVEAVSDAIRRSRAGLSDPNRPIGSFLFLGPTG 604
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887424716 622 TGKTETALALADVLYGGEKSLITINLSEYQEPHTVSQLKGSPPGYVGYGQGGILTEAVRKRPYSVVLLDEVEKAHRDVMN 701
Cdd:TIGR03346 605 VGKTELAKALAEFLFDSEDAMVRIDMSEYMEKHSVARLIGAPPGYVGYEEGGQLTEAVRRRPYSVVLFDEVEKAHPDVFN 684
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887424716 702 LFYQVFDRGFMRDGEGREIDFRNTVILMTSNLGSDHLMQLLDEqpdASEADLQELLRPILRDHFQPALLARF-QTVIYRP 780
Cdd:TIGR03346 685 VLLQVLDDGRLTDGQGRTVDFRNTVIIMTSNLGSDFIQELAGG---DDYEEMREAVMEVLRAHFRPEFLNRIdEIVVFHP 761
|
810 820 830 840 850 860 870
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1887424716 781 LAEAAMRTIVEMKLEQVSKRLS-RHYGLttHIEASLYDALTAACLLPDTGARNVDSLLNQQILPVLSQQLL 850
Cdd:TIGR03346 762 LGREQIARIVEIQLGRLRKRLAeRKITL--ELSDAALDFLAEAGYDPVYGARPLKRAIQREIENPLAKKIL 830
|
|
| PRK10865 |
PRK10865 |
ATP-dependent chaperone ClpB; |
193-864 |
0e+00 |
|
ATP-dependent chaperone ClpB;
Pssm-ID: 182791 [Multi-domain] Cd Length: 857 Bit Score: 581.42 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887424716 193 QNALDKFTLDVTARAKEGNIDPVFGRDTEIRQMVDILSRRRKNNPILVGEPGVGKTALVEGLALRIAEGNVPESLRPVSL 272
Cdd:PRK10865 158 RQALKKYTIDLTERAEQGKLDPVIGRDEEIRRTIQVLQRRTKNNPVLIGEPGVGKTAIVEGLAQRIINGEVPEGLKGRRV 237
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887424716 273 RTLDLGLLQAGAGVKGEFEQRLKNVIDAVQQSPAPVLLFIDEAHTIIGAGNQAGGADAANLLKPALARGELRTIAATTWS 352
Cdd:PRK10865 238 LALDMGALVAGAKYRGEFEERLKGVLNDLAKQEGNVILFIDELHTMVGAGKADGAMDAGNMLKPALARGELHCVGATTLD 317
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887424716 353 EYKQYFERDAALERRFQMVKVDEPDDDTACLMLRGLKSRYAVHHKVHITDDAVRAAVTLSRRYLTGRQLPDKAVDLLDTA 432
Cdd:PRK10865 318 EYRQYIEKDAALERRFQKVFVAEPSVEDTIAILRGLKERYELHHHVQITDPAIVAAATLSHRYIADRQLPDKAIDLIDEA 397
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887424716 433 AARVRMSFDTVPEAVTQLNAQLTALALEEQGLlddivsgrNRHGDRLSAIALQrtMLDDQLQQLTR----VSEQQRATVA 508
Cdd:PRK10865 398 ASSIRMQIDSKPEELDRLDRRIIQLKLEQQAL--------MKESDEASKKRLD--MLNEELSDKERqyseLEEEWKAEKA 467
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887424716 509 ELN------------------ACRQ-DISRQAEM---------AGLQQQLAILQQTDVLVQVDVDTRTVANVIADWTGVP 560
Cdd:PRK10865 468 SLSgtqtikaeleqakiaieqARRVgDLARMSELqygkipeleKQLAAATQLEGKTMRLLRNKVTDAEIAEVLARWTGIP 547
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887424716 561 LSSLMKDEQTGLLTLEADIGKRVVGQDTALNAIAQRLRAAKTGLTSENGPQGVFLLVGPSGTGKTETALALADVLYGGEK 640
Cdd:PRK10865 548 VSRMLESEREKLLRMEQELHHRVIGQNEAVEAVSNAIRRSRAGLSDPNRPIGSFLFLGPTGVGKTELCKALANFMFDSDD 627
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887424716 641 SLITINLSEYQEPHTVSQLKGSPPGYVGYGQGGILTEAVRKRPYSVVLLDEVEKAHRDVMNLFYQVFDRGFMRDGEGREI 720
Cdd:PRK10865 628 AMVRIDMSEFMEKHSVSRLVGAPPGYVGYEEGGYLTEAVRRRPYSVILLDEVEKAHPDVFNILLQVLDDGRLTDGQGRTV 707
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887424716 721 DFRNTVILMTSNLGSDhLMQllDEQPDASEADLQELLRPILRDHFQPALLARF-QTVIYRPLAEAAMRTIVEMKLEQVSK 799
Cdd:PRK10865 708 DFRNTVVIMTSNLGSD-LIQ--ERFGELDYAHMKELVLGVVSHNFRPEFINRIdEVVVFHPLGEQHIASIAQIQLQRLYK 784
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1887424716 800 RLSRHyGLTTHIEASLYDALTAACLLPDTGARNVDSLLNQQILPVLSQQLLTHMAAKQKPLSLTL 864
Cdd:PRK10865 785 RLEER-GYEIHISDEALKLLSENGYDPVYGARPLKRAIQQQIENPLAQQILSGELVPGKVIRLEV 848
|
|
| clpC |
CHL00095 |
Clp protease ATP binding subunit |
196-850 |
0e+00 |
|
Clp protease ATP binding subunit
Pssm-ID: 214361 [Multi-domain] Cd Length: 821 Bit Score: 580.86 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887424716 196 LDKFTLDVTARAKEGNIDPVFGRDTEIRQMVDILSRRRKNNPILVGEPGVGKTALVEGLALRIAEGNVPESLRPVSLRTL 275
Cdd:CHL00095 162 LEEFGTNLTKEAIDGNLDPVIGREKEIERVIQILGRRTKNNPILIGEPGVGKTAIAEGLAQRIVNRDVPDILEDKLVITL 241
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887424716 276 DLGLLQAGAGVKGEFEQRLKNVIDAVQQSPApVLLFIDEAHTIIGAGNQAGGADAANLLKPALARGELRTIAATTWSEYK 355
Cdd:CHL00095 242 DIGLLLAGTKYRGEFEERLKRIFDEIQENNN-IILVIDEVHTLIGAGAAEGAIDAANILKPALARGELQCIGATTLDEYR 320
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887424716 356 QYFERDAALERRFQMVKVDEPDDDTACLMLRGLKSRYAVHHKVHITDDAVRAAVTLSRRYLTGRQLPDKAVDLLDTAAAR 435
Cdd:CHL00095 321 KHIEKDPALERRFQPVYVGEPSVEETIEILFGLRSRYEKHHNLSISDKALEAAAKLSDQYIADRFLPDKAIDLLDEAGSR 400
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887424716 436 VRMSFDTVPEAVTQLnaqltalaleeqgllddivsgrnrhgdrlsAIALQRTMLDDQlqqlTRVSEQQRATVAELNACRQ 515
Cdd:CHL00095 401 VRLINSRLPPAAREL------------------------------DKELREILKDKD----EAIREQDFETAKQLRDREM 446
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887424716 516 DISRQAEMAGLQQQLAILQQTDVLVqvdVDTRTVANVIADWTGVPLSSLMKDEQTGLLTLEADIGKRVVGQDTALNAIAQ 595
Cdd:CHL00095 447 EVRAQIAAIIQSKKTEEEKRLEVPV---VTEEDIAEIVSAWTGIPVNKLTKSESEKLLHMEETLHKRIIGQDEAVVAVSK 523
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887424716 596 RLRAAKTGLTSENGPQGVFLLVGPSGTGKTETALALADVLYGGEKSLITINLSEYQEPHTVSQLKGSPPGYVGYGQGGIL 675
Cdd:CHL00095 524 AIRRARVGLKNPNRPIASFLFSGPTGVGKTELTKALASYFFGSEDAMIRLDMSEYMEKHTVSKLIGSPPGYVGYNEGGQL 603
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887424716 676 TEAVRKRPYSVVLLDEVEKAHRDVMNLFYQVFDRGFMRDGEGREIDFRNTVILMTSNLGS------DHLMQLLDEQPDAS 749
Cdd:CHL00095 604 TEAVRKKPYTVVLFDEIEKAHPDIFNLLLQILDDGRLTDSKGRTIDFKNTLIIMTSNLGSkvietnSGGLGFELSENQLS 683
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887424716 750 EAD---LQELLRPILRDHFQPALLARFQTVI-YRPLAEAAMRTIVEMKLEQVSKRLSRHyGLTTHIEASLYDALTAACLL 825
Cdd:CHL00095 684 EKQykrLSNLVNEELKQFFRPEFLNRLDEIIvFRQLTKNDVWEIAEIMLKNLFKRLNEQ-GIQLEVTERIKTLLIEEGYN 762
|
650 660
....*....|....*....|....*
gi 1887424716 826 PDTGARNVDSLLNQQILPVLSQQLL 850
Cdd:CHL00095 763 PLYGARPLRRAIMRLLEDPLAEEVL 787
|
|
| clpA |
PRK11034 |
ATP-dependent Clp protease ATP-binding subunit; Provisional |
11-734 |
2.97e-129 |
|
ATP-dependent Clp protease ATP-binding subunit; Provisional
Pssm-ID: 236828 [Multi-domain] Cd Length: 758 Bit Score: 406.14 E-value: 2.97e-129
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887424716 11 LNPYCARAMEGAASLCQTRAHAEIQPEHWLLKLLEQGEGDLTVLARRYewDMDAIWQDLLGWLDKQ----PRSIRHR--- 83
Cdd:PRK11034 2 LNQELELSLNMAFARAREHRHEFMTVEHLLLALLSNPSAREALEACSV--DLVALRQELEAFIEQTtpvlPASEEERdtq 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887424716 84 PQLSdaIQTLMQEAWLIASLNGEAQIRSLHLLMALVEKQnlvrcdglwplltlgQSQLERLRPLLDAQSDERPEMQQEAE 163
Cdd:PRK11034 80 PTLS--FQRVLQRAVFHVQSSGRSEVTGANVLVAIFSEQ---------------ESQAAYLLRKHEVSRLDVVNFISHGT 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887424716 164 LAQSHGGEVEFVGRPVGTELKEGElnpalqNALDKFTLDVTARAKEGNIDPVFGRDTEIRQMVDILSRRRKNNPILVGEP 243
Cdd:PRK11034 143 RKDEPSQSSDPGSQPNSEEQAGGE------ERMENFTTNLNQLARVGGIDPLIGREKELERAIQVLCRRRKNNPLLVGES 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887424716 244 GVGKTALVEGLALRIAEGNVPESLRPVSLRTLDLGLLQAGAGVKGEFEQRLKNVIDAVQQSPAPVLlFIDEAHTIIGAGN 323
Cdd:PRK11034 217 GVGKTAIAEGLAWRIVQGDVPEVMADCTIYSLDIGSLLAGTKYRGDFEKRFKALLKQLEQDTNSIL-FIDEIHTIIGAGA 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887424716 324 QAGG-ADAANLLKPALARGELRTIAATTWSEYKQYFERDAALERRFQMVKVDEPDDDTACLMLRGLKSRYAVHHKVHITD 402
Cdd:PRK11034 296 ASGGqVDAANLIKPLLSSGKIRVIGSTTYQEFSNIFEKDRALARRFQKIDITEPSIEETVQIINGLKPKYEAHHDVRYTA 375
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887424716 403 DAVRAAVTLSRRYLTGRQLPDKAVDLLDTAAARVRmsfdtvpeavtqlnaqltalaleeqgllddivsgrnrhgdrlsai 482
Cdd:PRK11034 376 KAVRAAVELAVKYINDRHLPDKAIDVIDEAGARAR--------------------------------------------- 410
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887424716 483 alqrtmlddqlqqLTRVSEQQRAtvaelnacrqdisrqaemaglqqqlailqqtdvlvqvdVDTRTVANVIADWTGVPLS 562
Cdd:PRK11034 411 -------------LMPVSKRKKT--------------------------------------VNVADIESVVARIARIPEK 439
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887424716 563 SLMKDEQTGLLTLEADIGKRVVGQDTALNAIAQRLRAAKTGLTSENGPQGVFLLVGPSGTGKTETALALADVLyggEKSL 642
Cdd:PRK11034 440 SVSQSDRDTLKNLGDRLKMLVFGQDKAIEALTEAIKMSRAGLGHEHKPVGSFLFAGPTGVGKTEVTVQLSKAL---GIEL 516
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887424716 643 ITINLSEYQEPHTVSQLKGSPPGYVGYGQGGILTEAVRKRPYSVVLLDEVEKAHRDVMNLFYQVFDRGFMRDGEGREIDF 722
Cdd:PRK11034 517 LRFDMSEYMERHTVSRLIGAPPGYVGFDQGGLLTDAVIKHPHAVLLLDEIEKAHPDVFNLLLQVMDNGTLTDNNGRKADF 596
|
730
....*....|..
gi 1887424716 723 RNTVILMTSNLG 734
Cdd:PRK11034 597 RNVVLVMTTNAG 608
|
|
| RecA-like_ClpB_Hsp104-like |
cd19499 |
Chaperone protein ClpB/Hsp104 subfamily; Bacterial Caseinolytic peptidase B (ClpB) and ... |
572-778 |
2.26e-86 |
|
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: 272.90 E-value: 2.26e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887424716 572 LLTLEADIGKRVVGQDTALNAIAQRLRAAKTGLTSENGPQGVFLLVGPSGTGKTETALALADVLYGGEKSLITINLSEYQ 651
Cdd:cd19499 2 LLNLEERLHERVVGQDEAVKAVSDAIRRARAGLSDPNRPIGSFLFLGPTGVGKTELAKALAELLFGDEDNLIRIDMSEYM 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887424716 652 EPHTVSQLKGSPPGYVGYGQGGILTEAVRKRPYSVVLLDEVEKAHRDVMNLFYQVFDRGFMRDGEGREIDFRNTVILMTS 731
Cdd:cd19499 82 EKHSVSRLIGAPPGYVGYTEGGQLTEAVRRKPYSVVLLDEIEKAHPDVQNLLLQVLDDGRLTDSHGRTVDFKNTIIIMTS 161
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1887424716 732 NlgsdhlmqlldeqpdaseadlqellrpilrdHFQPALLARFQTVIY 778
Cdd:cd19499 162 N-------------------------------HFRPEFLNRIDEIVV 177
|
|
| AAA_2 |
pfam07724 |
AAA domain (Cdc48 subfamily); This Pfam entry includes some of the AAA proteins not detected ... |
610-773 |
3.76e-71 |
|
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: 231.70 E-value: 3.76e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887424716 610 PQGVFLLVGPSGTGKTETALALADVLYGGEKSLITINLSEYQEPHTVSQLKGSPPGYVGYGQGGILTEAVRKRPYSVVLL 689
Cdd:pfam07724 2 PIGSFLFLGPTGVGKTELAKALAELLFGDERALIRIDMSEYMEEHSVSRLIGAPPGYVGYEEGGQLTEAVRRKPYSIVLI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887424716 690 DEVEKAHRDVMNLFYQVFDRGFMRDGEGREIDFRNTVILMTSNLGSDHLMQLLDEQPDASEADLQELLRPILRDHFQPAL 769
Cdd:pfam07724 82 DEIEKAHPGVQNDLLQILEGGTLTDKQGRTVDFKNTLFIMTGNFGSEKISDASRLGDSPDYELLKEEVMDLLKKGFIPEF 161
|
....
gi 1887424716 770 LARF 773
Cdd:pfam07724 162 LGRL 165
|
|
| AAA_lid_9 |
pfam17871 |
AAA lid domain; This entry represents the alpha helical AAA+ lid domain that is found to the ... |
377-467 |
7.97e-39 |
|
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: 139.54 E-value: 7.97e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887424716 377 DDDTACLMLRGLKSRYAVHHKVHITDDAVRAAVTLSRRYLTGRQLPDKAVDLLDTAAARVRMSFDTVPEAVTQLNAQLTA 456
Cdd:pfam17871 1 SVEEAIEILRGLKPKYEKHHGVRISDEALEAAVKLSKRYITDRFLPDKAIDLLDEACARVRLSQESKPEELEDLERELAK 80
|
90
....*....|.
gi 1887424716 457 LALEEQGLLDD 467
Cdd:pfam17871 81 LEIEKEALERE 91
|
|
| AAA |
cd00009 |
The AAA+ (ATPases Associated with a wide variety of cellular Activities) superfamily ... |
584-738 |
5.38e-15 |
|
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: 72.95 E-value: 5.38e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887424716 584 VGQDTALNAIAQRLraaktgltsENGPQGVFLLVGPSGTGKTETALALADVLYGGEKSLITINLSEYQEPHTVSqlkgsp 663
Cdd:cd00009 1 VGQEEAIEALREAL---------ELPPPKNLLLYGPPGTGKTTLARAIANELFRPGAPFLYLNASDLLEGLVVA------ 65
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1887424716 664 pGYVGYGQGGILTEAVRKRPYSVVLLDEVEKAHRDVMNLFYQVFDrgfmrDGEGREIDFRNTVILMTSNLGSDHL 738
Cdd:cd00009 66 -ELFGHFLVRLLFELAEKAKPGVLFIDEIDSLSRGAQNALLRVLE-----TLNDLRIDRENVRVIGATNRPLLGD 134
|
|
| AAA |
cd00009 |
The AAA+ (ATPases Associated with a wide variety of cellular Activities) superfamily ... |
216-376 |
5.49e-15 |
|
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: 72.95 E-value: 5.49e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887424716 216 FGRDTEIRQMVDILSRRRKNNPILVGEPGVGKTALVEGLALRIAEGNVPeslrpvsLRTLDLGLLQAGAGVKGEFEQRLK 295
Cdd:cd00009 1 VGQEEAIEALREALELPPPKNLLLYGPPGTGKTTLARAIANELFRPGAP-------FLYLNASDLLEGLVVAELFGHFLV 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887424716 296 NVIDAVQQSPAPVLLFIDEAHTiIGAGNQAGGADAANLLKPALA-RGELRTIAATTwseYKQYFERDAALERRFQMVKVD 374
Cdd:cd00009 74 RLLFELAEKAKPGVLFIDEIDS-LSRGAQNALLRVLETLNDLRIdRENVRVIGATN---RPLLGDLDRALYDRLDIRIVI 149
|
..
gi 1887424716 375 EP 376
Cdd:cd00009 150 PL 151
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
610-736 |
1.54e-12 |
|
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: 65.86 E-value: 1.54e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887424716 610 PQGVFLLVGPSGTGKTETALALADVLYGGEKSLITINLSEYQEPHTVSQLKGSPPGYVGYGQGG----ILTEAVRKRPYS 685
Cdd:smart00382 1 PGEVILIVGPPGSGKTTLARALARELGPPGGGVIYIDGEDILEEVLDQLLLIIVGGKKASGSGElrlrLALALARKLKPD 80
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 1887424716 686 VVLLDEVEKAHRDVMNLFYQVFDRGFMRDGEGREidfRNTVILMTSNLGSD 736
Cdd:smart00382 81 VLILDEITSLLDAEQEALLLLLEELRLLLLLKSE---KNLTVILTTNDEKD 128
|
|
| AAA_5 |
pfam07728 |
AAA domain (dynein-related subfamily); This Pfam entry includes some of the AAA proteins not ... |
614-732 |
2.03e-10 |
|
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: 59.61 E-value: 2.03e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887424716 614 FLLVGPSGTGKTETALALADVLYGgeKSLITINLSEYQEPhtvSQLKGS--PPGYVGYGQGGILTEAVRKRpySVVLLDE 691
Cdd:pfam07728 2 VLLVGPPGTGKTELAERLAAALSN--RPVFYVQLTRDTTE---EDLFGRrnIDPGGASWVDGPLVRAAREG--EIAVLDE 74
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 1887424716 692 VEKAHRDVMNLFYQVFDRGFMRDGEGREID---FRNTVILMTSN 732
Cdd:pfam07728 75 INRANPDVLNSLLSLLDERRLLLPDGGELVkaaPDGFRLIATMN 118
|
|
| AAA |
pfam00004 |
ATPase family associated with various cellular activities (AAA); AAA family proteins often ... |
238-371 |
6.33e-10 |
|
ATPase family associated with various cellular activities (AAA); AAA family proteins often perform chaperone-like functions that assist in the assembly, operation, or disassembly of protein complexes.
Pssm-ID: 459627 [Multi-domain] Cd Length: 130 Bit Score: 57.99 E-value: 6.33e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887424716 238 ILVGEPGVGKTALVEGLAlriAEGNVPeslrpvsLRTLDLGLLqaGAGVKGEFEQRLKNVIDAVqQSPAPVLLFIDEAHT 317
Cdd:pfam00004 2 LLYGPPGTGKTTLAKAVA---KELGAP-------FIEISGSEL--VSKYVGESEKRLRELFEAA-KKLAPCVIFIDEIDA 68
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1887424716 318 IIGAGNQAG---GADAANLLKPALARGELRT-----IAATTwseykQYFERDAALERRFQMV 371
Cdd:pfam00004 69 LAGSRGSGGdseSRRVVNQLLTELDGFTSSNskvivIAATN-----RPDKLDPALLGRFDRI 125
|
|
| ClpB_D2-small |
pfam10431 |
C-terminal, D2-small domain, of ClpB protein; This is the C-terminal domain of ClpB protein, ... |
781-856 |
1.65e-09 |
|
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: 55.10 E-value: 1.65e-09
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1887424716 781 LAEAAMRTIVEMKLEQVSKRLSRHyGLTTHIEASLYDALTAACLLPDTGARNVDSLLNQQILPVLSQQLLTHMAAK 856
Cdd:pfam10431 1 LSKEELRKIVDLQLKELQKRLAER-GITLELTDAAKDWLAEKGYDPEYGARPLRRAIQREIEDPLAEEILSGELKE 75
|
|
| ClpB_D2-small |
smart01086 |
C-terminal, D2-small domain, of ClpB protein; This is the C-terminal domain of ClpB protein, ... |
781-865 |
5.27e-09 |
|
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: 53.99 E-value: 5.27e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887424716 781 LAEAAMRTIVEMKLEQVSKRLSRHyGLTTHIEASLYDALTAACLLPDTGARNVDSLLNQQILPVLSQQLLTHMAAKQKPL 860
Cdd:smart01086 1 LDKEDLVRIVDLPLNALQKRLAEK-GITLEFTDEALDWLAEKGYDPKYGARPLRRIIQRELEDPLAELILSGELKDGDTV 79
|
....*
gi 1887424716 861 SLTLG 865
Cdd:smart01086 80 VVDVD 84
|
|
| AAA |
pfam00004 |
ATPase family associated with various cellular activities (AAA); AAA family proteins often ... |
615-781 |
5.42e-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: 5.42e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887424716 615 LLVGPSGTGKTETALALADVLYGgekSLITINLSEyqephTVSQLKGSPPGYVgygqGGILTEAVRKRPySVVLLDEVEK 694
Cdd:pfam00004 2 LLYGPPGTGKTTLAKAVAKELGA---PFIEISGSE-----LVSKYVGESEKRL----RELFEAAKKLAP-CVIFIDEIDA 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887424716 695 -----------AHRDVMNLFYQVFDrgfmrdgeGREIDFRNTVILMTSNlgsdhLMQLLDeqpdaseadlqellrpilrd 763
Cdd:pfam00004 69 lagsrgsggdsESRRVVNQLLTELD--------GFTSSNSKVIVIAATN-----RPDKLD-------------------- 115
|
170
....*....|....*...
gi 1887424716 764 hfqPALLARFQTVIYRPL 781
Cdd:pfam00004 116 ---PALLGRFDRIIEFPL 130
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
233-368 |
3.27e-08 |
|
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a variety of cellular activities. This profile/alignment only detects a fraction of this vast family. The poorly conserved N-terminal helix is missing from the alignment.
Pssm-ID: 214640 [Multi-domain] Cd Length: 148 Bit Score: 53.53 E-value: 3.27e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887424716 233 RKNNPILVGEPGVGKTALVEGLALRIAEGNV------PESLRPVSLRTLdLGLLQAGAGVKGEFEQRLKNVIDAVQQSPa 306
Cdd:smart00382 1 PGEVILIVGPPGSGKTTLARALARELGPPGGgviyidGEDILEEVLDQL-LLIIVGGKKASGSGELRLRLALALARKLK- 78
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1887424716 307 PVLLFIDEAHTIIGAGNQAGGADAA--NLLKPALARGELRTIAATTWSEykqyFERDAALERRF 368
Cdd:smart00382 79 PDVLILDEITSLLDAEQEALLLLLEelRLLLLLKSEKNLTVILTTNDEK----DLGPALLRRRF 138
|
|
| RecA-like_protease |
cd19481 |
proteases similar to RecA; RecA-like NTPases. This family includes the NTP binding domain of ... |
590-698 |
3.38e-08 |
|
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: 53.83 E-value: 3.38e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887424716 590 LNAIAQRLRAAKTGLTSENGPQGVfLLVGPSGTGKTETALALAdvlygGE--KSLITINLSEYQEPhtvsqlkgsppgYV 667
Cdd:cd19481 6 REAVEAPRRGSRLRRYGLGLPKGI-LLYGPPGTGKTLLAKALA-----GElgLPLIVVKLSSLLSK------------YV 67
|
90 100 110
....*....|....*....|....*....|...
gi 1887424716 668 GYGQGGI--LTEAVRKRPYSVVLLDEVEKAHRD 698
Cdd:cd19481 68 GESEKNLrkIFERARRLAPCILFIDEIDAIGRK 100
|
|
| SpoVK |
COG0464 |
AAA+-type ATPase, SpoVK/Ycf46/Vps4 family [Cell wall/membrane/envelope biogenesis, Cell cycle ... |
64-379 |
2.34e-07 |
|
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: 54.15 E-value: 2.34e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887424716 64 AIWQDLLGWLDKQPRSIRHRPQLSDAIQTLMQEAWLIASLNGEAQIRSLHLLMALVEKQNLVRCDGLWPLLTLGQSQLER 143
Cdd:COG0464 8 AVALALALLLLDDAALRLLLLLLLALAAALLLLLLLLLLLLLALLLVELLLLLLSGALAALLLLALLLLALLALLAALLS 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887424716 144 LRPLLDAQSDERPEMQQEAELAQSHGGEVEFVGRPVGTELKEGELNPALQNALDKFTLDVTARAKEGNIDPVFGRD---T 220
Cdd:COG0464 88 ALELLLLGELLLLLLLLLLLLLLLLDLERALLELLRESAEALALAAPLVTYEDIGGLEEELLELREAILDDLGGLEevkE 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887424716 221 EIRQMVDILSRRRK-------NNP---ILVGEPGVGKTALVEGLAlriAEGNVPeslrpvsLRTLDLGLLqAGAGVkGEF 290
Cdd:COG0464 168 ELRELVALPLKRPElreeyglPPPrglLLYGPPGTGKTLLARALA---GELGLP-------LIEVDLSDL-VSKYV-GET 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887424716 291 EQRLKNVIDAVQQSpAPVLLFIDEAHTIIGAGNQAGGADA----ANLLKpALA--RGELRTIAATTwseykqYFER-DAA 363
Cdd:COG0464 236 EKNLREVFDKARGL-APCVLFIDEADALAGKRGEVGDGVGrrvvNTLLT-EMEelRSDVVVIAATN------RPDLlDPA 307
|
330
....*....|....*..
gi 1887424716 364 LERRFQ-MVKVDEPDDD 379
Cdd:COG0464 308 LLRRFDeIIFFPLPDAE 324
|
|
| COG1223 |
COG1223 |
Predicted ATPase, AAA+ superfamily [General function prediction only]; |
583-795 |
2.54e-06 |
|
Predicted ATPase, AAA+ superfamily [General function prediction only];
Pssm-ID: 440836 [Multi-domain] Cd Length: 246 Bit Score: 49.88 E-value: 2.54e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887424716 583 VVGQDTALNAIAQ-------RLRAAKTGLTSengPQGVfLLVGPSGTGKTETALALADVLyggEKSLITINLSEyqepht 655
Cdd:COG1223 4 VVGQEEAKKKLKLiikelrrRENLRKFGLWP---PRKI-LFYGPPGTGKTMLAEALAGEL---KLPLLTVRLDS------ 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887424716 656 vsqLKGSppgYVGYGQGGI--LTEAVRKRPySVVLLDEVekahrDVMNLfyqvfDRGFMRD-GEGREIdfRNTVILMTSN 732
Cdd:COG1223 71 ---LIGS---YLGETARNLrkLFDFARRAP-CVIFFDEF-----DAIAK-----DRGDQNDvGEVKRV--VNALLQELDG 131
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1887424716 733 LGSDHLM-------QLLDeqpdaseadlqellrpilrdhfqPALLARFQTVIYRPLA-EAAMRTIVEMKLE 795
Cdd:COG1223 132 LPSGSVViaatnhpELLD-----------------------SALWRRFDEVIEFPLPdKEERKEILELNLK 179
|
|
| AAA_16 |
pfam13191 |
AAA ATPase domain; This family of domains contain a P-loop motif that is characteriztic of the ... |
214-316 |
1.03e-05 |
|
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: 46.73 E-value: 1.03e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887424716 214 PVFGRDTEIRQMVDILSRRRKNNP---ILVGEPGVGKTALVEGLALRIAEGNV--------------------------- 263
Cdd:pfam13191 1 RLVGREEELEQLLDALDRVRSGRPpsvLLTGEAGTGKTTLLRELLRALERDGGyflrgkcdenlpyspllealtregllr 80
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1887424716 264 -----PESLRPVSLRTLDLGLLQAGAGVKGEFEQR----LKNVIDAVQQSPAPVLLFIDEAH 316
Cdd:pfam13191 81 qlldeLESSLLEAWRAALLEALAPVPELPGDLAERlldlLLRLLDLLARGERPLVLVLDDLQ 142
|
|
| SpoVK |
COG0464 |
AAA+-type ATPase, SpoVK/Ycf46/Vps4 family [Cell wall/membrane/envelope biogenesis, Cell cycle ... |
429-787 |
6.46e-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: 46.44 E-value: 6.46e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887424716 429 LDTAAARVRMSFDTVPEAVTQLNAQLTALALEEQGLLDDIVSGRNRHGDRLSAIALQRTMLDDQLQQLTRVSEQQRATVA 508
Cdd:COG0464 1 LAELLALAVALALALLLLDDAALRLLLLLLLALAAALLLLLLLLLLLLLALLLVELLLLLLSGALAALLLLALLLLALLA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887424716 509 ELNAcRQDISRQAEMAGLQQQLAILQQTDVLVQVDVDTRTVANVIADWTGVPLSSLMKDEQTGLLTLEADIGKR-----V 583
Cdd:COG0464 81 LLAA-LLSALELLLLGELLLLLLLLLLLLLLLLDLERALLELLRESAEALALAAPLVTYEDIGGLEEELLELREailddL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887424716 584 VGQDTALNAIAQRLRAAKTGLTSEN----GPQGVFLLVGPSGTGKTETALALADVLyggEKSLITINLSEyqephTVSQl 659
Cdd:COG0464 160 GGLEEVKEELRELVALPLKRPELREeyglPPPRGLLLYGPPGTGKTLLARALAGEL---GLPLIEVDLSD-----LVSK- 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887424716 660 kgsppgYVGYGQGGI---LTEAVRKRPySVVLLDEVEKAHRdvmnlfyqvfDRGFMRDGEGREI---------DFRNTVI 727
Cdd:COG0464 231 ------YVGETEKNLrevFDKARGLAP-CVLFIDEADALAG----------KRGEVGDGVGRRVvntlltemeELRSDVV 293
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1887424716 728 LM-TSNlgsdhLMQLLDeqpdaseadlqellrpilrdhfqPALLARFQTVIYRPLAEAAMR 787
Cdd:COG0464 294 VIaATN-----RPDLLD-----------------------PALLRRFDEIIFFPLPDAEER 326
|
|
| AAA_22 |
pfam13401 |
AAA domain; |
231-316 |
6.50e-05 |
|
AAA domain;
Pssm-ID: 379165 [Multi-domain] Cd Length: 129 Bit Score: 43.48 E-value: 6.50e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887424716 231 RRRKNNPILVGEPGVGKTALVEGLALRIAEGNVP----ESLRPVSLRTLDLGLLQAgAGVKGEFEQRLKNVIDAVQQ--- 303
Cdd:pfam13401 2 RFGAGILVLTGESGTGKTTLLRRLLEQLPEVRDSvvfvDLPSGTSPKDLLRALLRA-LGLPLSGRLSKEELLAALQQlll 80
|
90
....*....|....
gi 1887424716 304 -SPAPVLLFIDEAH 316
Cdd:pfam13401 81 aLAVAVVLIIDEAQ 94
|
|
| RecA-like_protease |
cd19481 |
proteases similar to RecA; RecA-like NTPases. This family includes the NTP binding domain of ... |
238-318 |
1.05e-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: 43.43 E-value: 1.05e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887424716 238 ILVGEPGVGKTALVEGLAlriAEGNVPeslrpvsLRTLDLGLLQAGAgvKGEFEQRLKNVIDAVQQSpAPVLLFIDEAHT 317
Cdd:cd19481 30 LLYGPPGTGKTLLAKALA---GELGLP-------LIVVKLSSLLSKY--VGESEKNLRKIFERARRL-APCILFIDEIDA 96
|
.
gi 1887424716 318 I 318
Cdd:cd19481 97 I 97
|
|
| PRK12723 |
PRK12723 |
flagellar biosynthesis regulator FlhF; Provisional |
586-702 |
1.28e-04 |
|
flagellar biosynthesis regulator FlhF; Provisional
Pssm-ID: 183702 [Multi-domain] Cd Length: 388 Bit Score: 45.28 E-value: 1.28e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887424716 586 QDTALNAIAQRLRAAKTgLTSENGPQgVFLLVGPSGTGKTETALALADV--LYGGEKSL----ITIN---LSEYQEPHTV 656
Cdd:PRK12723 151 RDSVIIYIAKTIKCSGS-IIDNLKKR-VFILVGPTGVGKTTTIAKLAAIygINSDDKSLnikiITIDnyrIGAKKQIQTY 228
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 1887424716 657 SQLKGSPPGYVGYGQgGILTEAVRKRPYSVVLLDEVEKAHRDVMNL 702
Cdd:PRK12723 229 GDIMGIPVKAIESFK-DLKEEITQSKDFDLVLVDTIGKSPKDFMKL 273
|
|
| AAA_22 |
pfam13401 |
AAA domain; |
608-708 |
2.75e-04 |
|
AAA domain;
Pssm-ID: 379165 [Multi-domain] Cd Length: 129 Bit Score: 41.56 E-value: 2.75e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887424716 608 NGPQGVFLLVGPSGTGKTETALALADVLYGGEKSLITINLSEYQEPHTVSQ--LKGSPPGYVGYGQGGILTEAV-----R 680
Cdd:pfam13401 2 RFGAGILVLTGESGTGKTTLLRRLLEQLPEVRDSVVFVDLPSGTSPKDLLRalLRALGLPLSGRLSKEELLAALqqlllA 81
|
90 100
....*....|....*....|....*...
gi 1887424716 681 KRPYSVVLLDEVEKAHRDVMNLFYQVFD 708
Cdd:pfam13401 82 LAVAVVLIIDEAQHLSLEALEELRDLLN 109
|
|
| CDC6 |
COG1474 |
Cdc6-related protein, AAA superfamily ATPase [Replication, recombination and repair]; |
582-705 |
9.78e-04 |
|
Cdc6-related protein, AAA superfamily ATPase [Replication, recombination and repair];
Pssm-ID: 441083 [Multi-domain] Cd Length: 389 Bit Score: 42.53 E-value: 9.78e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887424716 582 RVVGQDTALNAIAQRLRAAKTGLTSENGpqgvfLLVGPSGTGKTETALALADVL------YGGEKSLITINLSEYQEPHT 655
Cdd:COG1474 27 RLPHREEEIEELASALRPALRGERPSNV-----LIYGPTGTGKTAVAKYVLEELeeeaeeRGVDVRVVYVNCRQASTRYR 101
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1887424716 656 V-----SQLK-GSPPGYVGYGQG---GILTEAVRKRPYSVVL-LDEVEKAHRDVMN-LFYQ 705
Cdd:COG1474 102 VlsrilEELGsGEDIPSTGLSTDelfDRLYEALDERDGVLVVvLDEIDYLVDDEGDdLLYQ 162
|
|
| McrB |
COG1401 |
5-methylcytosine-specific restriction endonuclease McrBC, GTP-binding regulatory subunit McrB ... |
441-645 |
1.22e-03 |
|
5-methylcytosine-specific restriction endonuclease McrBC, GTP-binding regulatory subunit McrB [Defense mechanisms];
Pssm-ID: 441011 [Multi-domain] Cd Length: 477 Bit Score: 42.45 E-value: 1.22e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887424716 441 DTVPEAVTQLNAQLTALALEEQGLLDDIVSGRNRHGDRLSAIALQRTMLDDQLQQLTRVSEQQRATVAELNACRQDISRQ 520
Cdd:COG1401 46 LAERLSEELLRADRAARATELVEELSAALEVVVLLLDLEKVELNEKLALSEAAVAIEELYELEADSEIEAVGLLLELAER 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887424716 521 AEMAGLQQQLAILQQTDVLVQVDVDTRTVANVIADWTGVPLSSLMKDEQTGLLTLEADIGKRVVGQDTALNAIAQRLRAA 600
Cdd:COG1401 126 SDALEALERARLLLELADLEERAALETEVLEALEAELEELLAAPEDLSADALAAELSAAEELYSEDLESEDDYLKDLLRE 205
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1887424716 601 KTGLTSENGPQGVF-----LLVGPSGTGKTETALALADVLYGGEKSLITI 645
Cdd:COG1401 206 KFEETLEAFLAALKtkknvILAGPPGTGKTYLARRLAEALGGEDNGRIEF 255
|
|
| FlhF |
COG1419 |
Flagellar biosynthesis GTPase FlhF [Cell motility]; |
589-645 |
2.28e-03 |
|
Flagellar biosynthesis GTPase FlhF [Cell motility];
Pssm-ID: 441029 [Multi-domain] Cd Length: 361 Bit Score: 41.39 E-value: 2.28e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887424716 589 ALNAIAQRLRAAKTGLTSEngpQGVFLLVGPSGTGKTETA--LALADVLYGGEK-SLITI 645
Cdd:COG1419 145 LLEALARRLPVAEDPLLDE---GGVIALVGPTGVGKTTTIakLAARFVLRGKKKvALITT 201
|
|
| RecA-like_Ycf46-like |
cd19507 |
ATPase domain of Ycf46 and similar ATPase domains; Ycf46 may play a role in the regulation of ... |
238-330 |
3.53e-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: 39.27 E-value: 3.53e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887424716 238 ILVGEPGVGKTALVEGLAlriAEGNVPeslrpvsLRTLDLGLLQAGagVKGEFEQRLKNVIDAVQQSpAPVLLFIDEAHT 317
Cdd:cd19507 35 LLVGIQGTGKSLTAKAIA---GVWQLP-------LLRLDMGRLFGG--LVGESESRLRQMIQTAEAI-APCVLWIDEIEK 101
|
90
....*....|...
gi 1887424716 318 iiGAGNQAGGADA 330
Cdd:cd19507 102 --GFSNADSKGDS 112
|
|
| ExeA |
COG3267 |
Type II secretory pathway ATPase component GspA/ExeA/MshM [Intracellular trafficking, ... |
239-316 |
3.66e-03 |
|
Type II secretory pathway ATPase component GspA/ExeA/MshM [Intracellular trafficking, secretion, and vesicular transport, Extracellular structures];
Pssm-ID: 442498 [Multi-domain] Cd Length: 261 Bit Score: 40.16 E-value: 3.66e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887424716 239 LVGEPGVGKTALVEGLALRIAEGNV----------PESLrpvsLRTL--DLGLLQAGAGvKGEFEQRLKNVIDAVQQSPA 306
Cdd:COG3267 48 LTGEVGTGKTTLLRRLLERLPDDVKvayipnpqlsPAEL----LRAIadELGLEPKGAS-KADLLRQLQEFLLELAAAGR 122
|
90
....*....|
gi 1887424716 307 PVLLFIDEAH 316
Cdd:COG3267 123 RVVLIIDEAQ 132
|
|
| NACHT |
pfam05729 |
NACHT domain; This NTPase domain is found in apoptosis proteins as well as those involved in ... |
238-365 |
3.72e-03 |
|
NACHT domain; This NTPase domain is found in apoptosis proteins as well as those involved in MHC transcription activation. This family is closely related to pfam00931.
Pssm-ID: 428606 [Multi-domain] Cd Length: 166 Bit Score: 39.21 E-value: 3.72e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887424716 238 ILVGEPGVGKTALVEGLALRIAEGNVPE--------SLRPVSLRTLDLGLLQAGAGVKGEFEQRLKNVIDAVQQSPAPVL 309
Cdd:pfam05729 4 ILQGEAGSGKTTLLQKLALLWAQGKLPQgfdfvfflPCRELSRSGNARSLADLLFSQWPEPAAPVSEVWAVILELPERLL 83
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1887424716 310 LFID---EAHTIIGAGNQAGGADA--ANLLKPALARGE--LRTIAATTWSEYKQYFERDAALE 365
Cdd:pfam05729 84 LILDgldELVSDLGQLDGPCPVLTllSSLLRKKLLPGAslLLTVRPDALRDLRRGLEEPRYLE 146
|
|
| PRK04195 |
PRK04195 |
replication factor C large subunit; Provisional |
583-692 |
3.90e-03 |
|
replication factor C large subunit; Provisional
Pssm-ID: 235250 [Multi-domain] Cd Length: 482 Bit Score: 40.67 E-value: 3.90e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887424716 583 VVGQDTALNAIAQRLRAAKTGltsenGPQGVFLLVGPSGTGKTETALALA-DvlYGGEksLITINLSEYQephTVSQLKg 661
Cdd:PRK04195 16 VVGNEKAKEQLREWIESWLKG-----KPKKALLLYGPPGVGKTSLAHALAnD--YGWE--VIELNASDQR---TADVIE- 82
|
90 100 110
....*....|....*....|....*....|..
gi 1887424716 662 sppGYVGYG-QGGILTEAVRKrpysVVLLDEV 692
Cdd:PRK04195 83 ---RVAGEAaTSGSLFGARRK----LILLDEV 107
|
|
| RecA-like_NVL_r1-like |
cd19518 |
first of two ATPase domains of NVL (nuclear VCP-like protein) and similar ATPase domains; NVL ... |
238-318 |
3.96e-03 |
|
first of two ATPase domains of NVL (nuclear VCP-like protein) and similar ATPase domains; NVL exists in two forms with N-terminal extensions of different lengths in mammalian cells. NVL has two alternatively spliced isoforms, a short form, NVL1, and a long form, NVL2. NVL2, the major species, is mainly present in the nucleolus, whereas NVL1 is nucleoplasmic. Each has an N-terminal domain, followed by two tandem ATPase domains; this subfamily includes the first of the two ATPase domains. NVL2 is involved in the biogenesis of the 60S ribosome subunit by associating specifically with ribosome protein L5 and modulating the function of DOB1. NVL2 is also required for telomerase assembly and the regulation of telomerase activity, and is involved in pre-rRNA processing. The role of NVL1 is unclear. This RecA-like_NVL_r1-like subfamily belongs to the RecA-like NTPase family which includes the NTP binding domain of F1 and V1 H(+)ATPases, DnaB and related helicases as well as bacterial RecA and related eukaryotic and archaeal recombinases. The RecA-like NTPase family also includes bacterial conjugation proteins and related DNA transfer proteins involved in type II and type IV secretion.
Pssm-ID: 410926 [Multi-domain] Cd Length: 169 Bit Score: 38.92 E-value: 3.96e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887424716 238 ILVGEPGVGKTALVEGLAlriAEGNVPeslrpvslrtldlgLLQAGA-----GVKGEFEQRLKNVID-AVQQspAPVLLF 311
Cdd:cd19518 38 LLHGPPGCGKTMLANAIA---GELKVP--------------FLKISAteivsGVSGESEEKIRELFDqAISN--APCIVF 98
|
....*..
gi 1887424716 312 IDEAHTI 318
Cdd:cd19518 99 IDEIDAI 105
|
|
| Cas3 |
COG1203 |
CRISPR-Cas type I system-associated endonuclease/helicase Cas3 [Defense mechanisms]; ... |
552-632 |
5.28e-03 |
|
CRISPR-Cas type I system-associated endonuclease/helicase Cas3 [Defense mechanisms]; CRISPR-Cas type I system-associated endonuclease/helicase Cas3 is part of the Pathway/BioSystem: CRISPR-Cas system
Pssm-ID: 440816 [Multi-domain] Cd Length: 535 Bit Score: 40.45 E-value: 5.28e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887424716 552 VIADWTGvplSSLMKDEQTGLLTLEADIGKRVVGQDTALNAIAQRLR--AAKTGLTSENGPQGVFLLVGPSGTGKTETAL 629
Cdd:COG1203 89 IDADWLD---SANFDMARQALDHLLAERLERLLPKKSKPRTPINPLQneALELALEAAEEEPGLFILTAPTGGGKTEAAL 165
|
...
gi 1887424716 630 ALA 632
Cdd:COG1203 166 LFA 168
|
|
| RPT1 |
COG1222 |
ATP-dependent 26S proteasome regulatory subunit [Posttranslational modification, protein ... |
610-693 |
5.83e-03 |
|
ATP-dependent 26S proteasome regulatory subunit [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440835 [Multi-domain] Cd Length: 326 Bit Score: 39.99 E-value: 5.83e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887424716 610 PQGVfLLVGPSGTGKTETALALADVLyggEKSLITINLSEYQEPhtvsqlkgsppgYVgyGQGG-----ILTEAVRKRPy 684
Cdd:COG1222 112 PKGV-LLYGPPGTGKTLLAKAVAGEL---GAPFIRVRGSELVSK------------YI--GEGArnvreVFELAREKAP- 172
|
....*....
gi 1887424716 685 SVVLLDEVE 693
Cdd:COG1222 173 SIIFIDEID 181
|
|
| PulE-GspE-like |
cd01129 |
PulE-GspE family; PulE and General secretory pathway protein GspE are ATPases of the type II ... |
608-645 |
7.14e-03 |
|
PulE-GspE family; PulE and General secretory pathway protein GspE are ATPases of the type II secretory pathway, the main terminal branch of the general secretory pathway (GSP). PulE is a cytoplasmic protein of the GSP, which contains an ATP binding site and a tetracysteine motif. This subgroup also includes PilB, a type IV pilus assembly ATPase, DotB, an ATPase of the type IVb secretion system, also known as the dot/icm system, Escherichia coli IncI plasmid-encoded conjugative transfer ATPase TraJ, and HofB.
Pssm-ID: 410873 [Multi-domain] Cd Length: 159 Bit Score: 38.24 E-value: 7.14e-03
10 20 30
....*....|....*....|....*....|....*...
gi 1887424716 608 NGPQGVFLLVGPSGTGKTETALALADVLYGGEKSLITI 645
Cdd:cd01129 8 KRPHGLILVTGPTGSGKTTTLYAMLRELNGPERNIITI 45
|
|
| AAA_24 |
pfam13479 |
AAA domain; This AAA domain is found in a wide variety of presumed phage proteins. |
613-765 |
9.46e-03 |
|
AAA domain; This AAA domain is found in a wide variety of presumed phage proteins.
Pssm-ID: 433243 Cd Length: 199 Bit Score: 38.46 E-value: 9.46e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887424716 613 VFLLVGPSGTGKTETALALADVLY----GGEKSLITINLSEYQEPHTVSQLKgsppGYVGYgqggiLTEAVrKRPYSVVL 688
Cdd:pfam13479 4 KILIYGPSGIGKTTFAKTLPKPLFldteKGSKALDGDRFPDIVIRDSWQDFL----DAIDE-----LTAAE-LADYKTIV 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1887424716 689 LDEVEKAHRDVMNLFYQVFDRGFMRDGEG-------------REID----FRNTVILmTSnlgsdHLMQLLDEQPDAS-- 749
Cdd:pfam13479 74 IDTVDWLERLCLAYICKQNGKGSSIEDGGygkgygelgeefrRLLDalqeLGKNVIF-TA-----HAKTRKDEDPDGEky 147
|
170
....*....|....*....
gi 1887424716 750 ---EADLQELLRPILRDHF 765
Cdd:pfam13479 148 tryEPKLGKKTANELPGEV 166
|
|
| |
