|
Name |
Accession |
Description |
Interval |
E-value |
| ClpA |
COG0542 |
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ... |
8-693 |
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: 1085.50 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499409228 8 LDKYGTNLTKTAATNKLDPVIGRDAEIRRVCQILSRRTKNNPVLIGSAGVGKTAIVEGLAQRIVAGDVPESLRNKEIVSL 87
Cdd:COG0542 162 LDKYGRDLTELAREGKLDPVIGRDEEIRRVIQILSRRTKNNPVLIGEPGVGKTAIVEGLAQRIVNGDVPESLKDKRVLSL 241
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499409228 88 DLSALLAGASYRGEFEKRVKNLLEEIQKS--KVIIFIDEVHTLM-----------SagaaegaiaagNMLKPLLARGELR 154
Cdd:COG0542 242 DLGALVAGAKYRGEFEERLKAVLDEVKKSegNIILFIDELHTLVgaggaegamdaA-----------NLLKPALARGELR 310
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499409228 155 LIGATTLDEYREHLEKDPALERRFQQVFVGEPNLEDCIAIMRGLKERYEAHHKVSISDTALVTAVELSSRYITGRQLPDK 234
Cdd:COG0542 311 CIGATTLDEYRKYIEKDAALERRFQPVLVEEPSVEDTISILRGLKERYEAHHGVRITDEALVAAVRLSDRYITDRFLPDK 390
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499409228 235 AIDLLDEAASSLRMEIDSSPVELDQLRREVDRLRLEELALKSENDPTSEQRLRSITNQLSGKQEMLNTLQASWNSERARL 314
Cdd:COG0542 391 AIDLIDEAAARVRMEIDSKPEELDELERRLEQLEIEKEALKKEQDEASFERLAELRDELAELEEELEALKARWEAEKELI 470
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499409228 315 NQIGALKEQIDiakqsadiaqregrledasrLLYATIPQLQKNLAEKLEE-QDSAPLVSDQVMPEDIASVVEGWTGIPVK 393
Cdd:COG0542 471 EEIQELKEELE--------------------QRYGKIPELEKELAELEEElAELAPLLREEVTEEDIAEVVSRWTGIPVG 530
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499409228 394 KLMQKDAKQLLHLEEDLSKSVIAQKVAIGVIADAVRRSRAGLSDPNRPSGTFLFLGPTGVGKTQLVKALASLLYDGE--I 471
Cdd:COG0542 531 KLLEGEREKLLNLEEELHERVIGQDEAVEAVADAIRRSRAGLKDPNRPIGSFLFLGPTGVGKTELAKALAEFLFGDEdaL 610
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499409228 472 VRIDMSEYSEKFSISRLIGAPPGYIGHESAGQLTESVRRRPYSVVLFDEAEKAHPEVFDILLQVLDEGRLTDSHGRTVDF 551
Cdd:COG0542 611 IRIDMSEYMEKHSVSRLIGAPPGYVGYEEGGQLTEAVRRRPYSVVLLDEIEKAHPDVFNILLQVLDDGRLTDGQGRTVDF 690
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499409228 552 RNTIIVLTSNIGSRYLSDISLEATT---AHEYVNDEVRRTFRPEFLNRLDEIVIFEPLSQSDICQIVDLNIESLNKRIKD 628
Cdd:COG0542 691 RNTIIIMTSNIGSELILDLAEDEPDyeeMKEAVMEELKKHFRPEFLNRIDEIIVFHPLSKEELRKIVDLQLKRLRKRLAE 770
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 499409228 629 RRIVVTVSEDLRRWLSKSGYDVIYGARPLRRLIQREIEDRLAKLIIEGLIHDGQTASFDLSGGAV 693
Cdd:COG0542 771 RGITLELTDAAKDFLAEKGYDPEYGARPLKRAIQRELEDPLAEEILAGEIKEGDTITVDVDDGEL 835
|
|
| chaperone_ClpB |
TIGR03346 |
ATP-dependent chaperone ClpB; Members of this protein family are the bacterial ATP-dependent ... |
2-691 |
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: 1012.18 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499409228 2 SESQSE-LDKYGTNLTKTAATNKLDPVIGRDAEIRRVCQILSRRTKNNPVLIGSAGVGKTAIVEGLAQRIVAGDVPESLR 80
Cdd:TIGR03346 149 AEDQYEaLEKYARDLTERAREGKLDPVIGRDEEIRRTIQVLSRRTKNNPVLIGEPGVGKTAIVEGLAQRIVNGDVPEGLK 228
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499409228 81 NKEIVSLDLSALLAGASYRGEFEKRVKNLLEEIQKS--KVIIFIDEVHTLMSAGAAEGAIAAGNMLKPLLARGELRLIGA 158
Cdd:TIGR03346 229 NKRLLALDMGALIAGAKYRGEFEERLKAVLNEVTKSegQIILFIDELHTLVGAGKAEGAMDAGNMLKPALARGELHCIGA 308
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499409228 159 TTLDEYREHLEKDPALERRFQQVFVGEPNLEDCIAIMRGLKERYEAHHKVSISDTALVTAVELSSRYITGRQLPDKAIDL 238
Cdd:TIGR03346 309 TTLDEYRKYIEKDAALERRFQPVFVDEPSVEDTISILRGLKERYEVHHGVRITDPAIVAAATLSHRYITDRFLPDKAIDL 388
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499409228 239 LDEAASSLRMEIDSSPVELDQLRREVDRLRLEELALKSENDPTSEQRLRSITNQLSGKQEMLNTLQASWNSERARLNQIG 318
Cdd:TIGR03346 389 IDEAAARIRMEIDSKPEELDELDRRIIQLEIEREALKKEKDEASKKRLEDLEKELADLEEEYAELEEQWKAEKASIQGIQ 468
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499409228 319 ALKEQIDIAKQSADIAQREGRLEDASRLLYATIPQLQKNL--AEKLEEQDSAPLVSDQVMPEDIASVVEGWTGIPVKKLM 396
Cdd:TIGR03346 469 QIKEEIEQVRLELEQAEREGDLAKAAELQYGKLPELEKQLqaAEQKLGEEQNRLLREEVTAEEIAEVVSRWTGIPVSKML 548
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499409228 397 QKDAKQLLHLEEDLSKSVIAQKVAIGVIADAVRRSRAGLSDPNRPSGTFLFLGPTGVGKTQLVKALASLLYDGE--IVRI 474
Cdd:TIGR03346 549 EGEREKLLHMEEELHERVVGQDEAVEAVSDAIRRSRAGLSDPNRPIGSFLFLGPTGVGKTELAKALAEFLFDSEdaMVRI 628
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499409228 475 DMSEYSEKFSISRLIGAPPGYIGHESAGQLTESVRRRPYSVVLFDEAEKAHPEVFDILLQVLDEGRLTDSHGRTVDFRNT 554
Cdd:TIGR03346 629 DMSEYMEKHSVARLIGAPPGYVGYEEGGQLTEAVRRRPYSVVLFDEVEKAHPDVFNVLLQVLDDGRLTDGQGRTVDFRNT 708
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499409228 555 IIVLTSNIGSRYLSDISLEATTAH--EYVNDEVRRTFRPEFLNRLDEIVIFEPLSQSDICQIVDLNIESLNKRIKDRRIV 632
Cdd:TIGR03346 709 VIIMTSNLGSDFIQELAGGDDYEEmrEAVMEVLRAHFRPEFLNRIDEIVVFHPLGREQIARIVEIQLGRLRKRLAERKIT 788
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....*....
gi 499409228 633 VTVSEDLRRWLSKSGYDVIYGARPLRRLIQREIEDRLAKLIIEGLIHDGQTASFDLSGG 691
Cdd:TIGR03346 789 LELSDAALDFLAEAGYDPVYGARPLKRAIQREIENPLAKKILAGEVAPGDTIRVDVEGG 847
|
|
| PRK10865 |
PRK10865 |
ATP-dependent chaperone ClpB; |
2-696 |
0e+00 |
|
ATP-dependent chaperone ClpB;
Pssm-ID: 182791 [Multi-domain] Cd Length: 857 Bit Score: 783.65 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499409228 2 SESQSE-LDKYGTNLTKTAATNKLDPVIGRDAEIRRVCQILSRRTKNNPVLIGSAGVGKTAIVEGLAQRIVAGDVPESLR 80
Cdd:PRK10865 154 AEDQRQaLKKYTIDLTERAEQGKLDPVIGRDEEIRRTIQVLQRRTKNNPVLIGEPGVGKTAIVEGLAQRIINGEVPEGLK 233
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499409228 81 NKEIVSLDLSALLAGASYRGEFEKRVKNLLEEI--QKSKVIIFIDEVHTLMSAGAAEGAIAAGNMLKPLLARGELRLIGA 158
Cdd:PRK10865 234 GRRVLALDMGALVAGAKYRGEFEERLKGVLNDLakQEGNVILFIDELHTMVGAGKADGAMDAGNMLKPALARGELHCVGA 313
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499409228 159 TTLDEYREHLEKDPALERRFQQVFVGEPNLEDCIAIMRGLKERYEAHHKVSISDTALVTAVELSSRYITGRQLPDKAIDL 238
Cdd:PRK10865 314 TTLDEYRQYIEKDAALERRFQKVFVAEPSVEDTIAILRGLKERYELHHHVQITDPAIVAAATLSHRYIADRQLPDKAIDL 393
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499409228 239 LDEAASSLRMEIDSSPVELDQLRREVDRLRLEELALKSENDPTSEQRLRSITNQLSGKQEMLNTLQASWNSERARLNQIG 318
Cdd:PRK10865 394 IDEAASSIRMQIDSKPEELDRLDRRIIQLKLEQQALMKESDEASKKRLDMLNEELSDKERQYSELEEEWKAEKASLSGTQ 473
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499409228 319 ALKEQIDIAKQSADIAQREGRLEDASRLLYATIPQLQKNLAEKLE-EQDSAPLVSDQVMPEDIASVVEGWTGIPVKKLMQ 397
Cdd:PRK10865 474 TIKAELEQAKIAIEQARRVGDLARMSELQYGKIPELEKQLAAATQlEGKTMRLLRNKVTDAEIAEVLARWTGIPVSRMLE 553
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499409228 398 KDAKQLLHLEEDLSKSVIAQKVAIGVIADAVRRSRAGLSDPNRPSGTFLFLGPTGVGKTQLVKALASLLYDGE--IVRID 475
Cdd:PRK10865 554 SEREKLLRMEQELHHRVIGQNEAVEAVSNAIRRSRAGLSDPNRPIGSFLFLGPTGVGKTELCKALANFMFDSDdaMVRID 633
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499409228 476 MSEYSEKFSISRLIGAPPGYIGHESAGQLTESVRRRPYSVVLFDEAEKAHPEVFDILLQVLDEGRLTDSHGRTVDFRNTI 555
Cdd:PRK10865 634 MSEFMEKHSVSRLVGAPPGYVGYEEGGYLTEAVRRRPYSVILLDEVEKAHPDVFNILLQVLDDGRLTDGQGRTVDFRNTV 713
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499409228 556 IVLTSNIGSRYLSDI--SLEATTAHEYVNDEVRRTFRPEFLNRLDEIVIFEPLSQSDICQIVDLNIESLNKRIKDRRIVV 633
Cdd:PRK10865 714 VIMTSNLGSDLIQERfgELDYAHMKELVLGVVSHNFRPEFINRIDEVVVFHPLGEQHIASIAQIQLQRLYKRLEERGYEI 793
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 499409228 634 TVSEDLRRWLSKSGYDVIYGARPLRRLIQREIEDRLAKLIIEGLIHDGQTASFDLSGGAVNAQ 696
Cdd:PRK10865 794 HISDEALKLLSENGYDPVYGARPLKRAIQQQIENPLAQQILSGELVPGKVIRLEVNDDRIVAV 856
|
|
| clpC |
CHL00095 |
Clp protease ATP binding subunit |
8-687 |
0e+00 |
|
Clp protease ATP binding subunit
Pssm-ID: 214361 [Multi-domain] Cd Length: 821 Bit Score: 732.24 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499409228 8 LDKYGTNLTKTAATNKLDPVIGRDAEIRRVCQILSRRTKNNPVLIGSAGVGKTAIVEGLAQRIVAGDVPESLRNKEIVSL 87
Cdd:CHL00095 162 LEEFGTNLTKEAIDGNLDPVIGREKEIERVIQILGRRTKNNPILIGEPGVGKTAIAEGLAQRIVNRDVPDILEDKLVITL 241
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499409228 88 DLSALLAGASYRGEFEKRVKNLLEEIQKSK-VIIFIDEVHTLMSAGAAEGAIAAGNMLKPLLARGELRLIGATTLDEYRE 166
Cdd:CHL00095 242 DIGLLLAGTKYRGEFEERLKRIFDEIQENNnIILVIDEVHTLIGAGAAEGAIDAANILKPALARGELQCIGATTLDEYRK 321
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499409228 167 HLEKDPALERRFQQVFVGEPNLEDCIAIMRGLKERYEAHHKVSISDTALVTAVELSSRYITGRQLPDKAIDLLDEAASSL 246
Cdd:CHL00095 322 HIEKDPALERRFQPVYVGEPSVEETIEILFGLRSRYEKHHNLSISDKALEAAAKLSDQYIADRFLPDKAIDLLDEAGSRV 401
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499409228 247 RMEIDSSPVELDQLRREV-DRLRLEELALKSENDPTSEQRLrsitnqlsgKQEMlntlqaswnserarlnqigALKEQID 325
Cdd:CHL00095 402 RLINSRLPPAARELDKELrEILKDKDEAIREQDFETAKQLR---------DREM-------------------EVRAQIA 453
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499409228 326 IAKQSadiaqregrledasrllyatipqlQKNLAEKLEEQDSaplvsdqVMPEDIASVVEGWTGIPVKKLMQKDAKQLLH 405
Cdd:CHL00095 454 AIIQS------------------------KKTEEEKRLEVPV-------VTEEDIAEIVSAWTGIPVNKLTKSESEKLLH 502
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499409228 406 LEEDLSKSVIAQKVAIGVIADAVRRSRAGLSDPNRPSGTFLFLGPTGVGKTQLVKALASLLYDGE--IVRIDMSEYSEKF 483
Cdd:CHL00095 503 MEETLHKRIIGQDEAVVAVSKAIRRARVGLKNPNRPIASFLFSGPTGVGKTELTKALASYFFGSEdaMIRLDMSEYMEKH 582
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499409228 484 SISRLIGAPPGYIGHESAGQLTESVRRRPYSVVLFDEAEKAHPEVFDILLQVLDEGRLTDSHGRTVDFRNTIIVLTSNIG 563
Cdd:CHL00095 583 TVSKLIGSPPGYVGYNEGGQLTEAVRKKPYTVVLFDEIEKAHPDIFNLLLQILDDGRLTDSKGRTIDFKNTLIIMTSNLG 662
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499409228 564 SRYLS--------DISLEATTAHEY------VNDEVRRTFRPEFLNRLDEIVIFEPLSQSDICQIVDLNIESLNKRIKDR 629
Cdd:CHL00095 663 SKVIEtnsgglgfELSENQLSEKQYkrlsnlVNEELKQFFRPEFLNRLDEIIVFRQLTKNDVWEIAEIMLKNLFKRLNEQ 742
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....*...
gi 499409228 630 RIVVTVSEDLRRWLSKSGYDVIYGARPLRRLIQREIEDRLAKLIIEGLIHDGQTASFD 687
Cdd:CHL00095 743 GIQLEVTERIKTLLIEEGYNPLYGARPLRRAIMRLLEDPLAEEVLSFKIKPGDIIIVD 800
|
|
| VI_ClpV1 |
TIGR03345 |
type VI secretion ATPase, ClpV1 family; Members of this protein family are homologs of ClpB, ... |
4-680 |
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: 684.36 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499409228 4 SQSELDKYGTNLTKTAATNKLDPVIGRDAEIRRVCQILSRRTKNNPVLIGSAGVGKTAIVEGLAQRIVAGDVPESLRNKE 83
Cdd:TIGR03345 166 GTSALDQYTTDLTAQAREGKIDPVLGRDDEIRQMIDILLRRRQNNPILTGEAGVGKTAVVEGLALRIAAGDVPPALRNVR 245
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499409228 84 IVSLDLSALLAGASYRGEFEKRVKNLLEEIQKSK--VIIFIDEVHTLMSAGAAEGAIAAGNMLKPLLARGELRLIGATTL 161
Cdd:TIGR03345 246 LLSLDLGLLQAGASVKGEFENRLKSVIDEVKASPqpIILFIDEAHTLIGAGGQAGQGDAANLLKPALARGELRTIAATTW 325
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499409228 162 DEYREHLEKDPALERRFQQVFVGEPNLEDCIAIMRGLKERYEAHHKVSISDTALVTAVELSSRYITGRQLPDKAIDLLDE 241
Cdd:TIGR03345 326 AEYKKYFEKDPALTRRFQVVKVEEPDEETAIRMLRGLAPVLEKHHGVLILDEAVVAAVELSHRYIPGRQLPDKAVSLLDT 405
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499409228 242 AASSLRMEIDSSPVELDQLRREVDRLRLEELALKSEN--DPTSEQRLRSITNQLSGKQEMLNTLQASWNSERARLNQIGA 319
Cdd:TIGR03345 406 ACARVALSQNATPAALEDLRRRIAALELELDALEREAalGADHDERLAELRAELAALEAELAALEARWQQEKELVEAILA 485
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499409228 320 LKEQIDiAKQSADiaqregrlEDASRLLYATIPQLQKNLAEKleeQDSAPLVSDQVMPEDIASVVEGWTGIPVKKLMQKD 399
Cdd:TIGR03345 486 LRAELE-ADADAP--------ADDDDALRAQLAELEAALASA---QGEEPLVFPEVDAQAVAEVVADWTGIPVGRMVRDE 553
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499409228 400 AKQLLHLEEDLSKSVIAQKVAIGVIADAVRRSRAGLSDPNRPSGTFLFLGPTGVGKTQLVKALASLLYDGE--IVRIDMS 477
Cdd:TIGR03345 554 IEAVLSLPDRLAERVIGQDHALEAIAERIRTARAGLEDPRKPLGVFLLVGPSGVGKTETALALAELLYGGEqnLITINMS 633
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499409228 478 EYSEKFSISRLIGAPPGYIGHESAGQLTESVRRRPYSVVLFDEAEKAHPEVFDILLQVLDEGRLTDSHGRTVDFRNTIIV 557
Cdd:TIGR03345 634 EFQEAHTVSRLKGSPPGYVGYGEGGVLTEAVRRKPYSVVLLDEVEKAHPDVLELFYQVFDKGVMEDGEGREIDFKNTVIL 713
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499409228 558 LTSNIGSRYLSDISLEATTAH------EYVNDEVRRTFRPEFLNRLdEIVIFEPLSQSDICQIVDLNIESLNKRIKDR-R 630
Cdd:TIGR03345 714 LTSNAGSDLIMALCADPETAPdpeallEALRPELLKVFKPAFLGRM-TVIPYLPLDDDVLAAIVRLKLDRIARRLKENhG 792
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|
gi 499409228 631 IVVTVSEDLRRWLSKSGYDVIYGARPLRRLIQREIEDRLAKLIIEGLIHD 680
Cdd:TIGR03345 793 AELVYSEALVEHIVARCTEVESGARNIDAILNQTLLPELSRQILERLAAG 842
|
|
| ClpA |
TIGR02639 |
ATP-dependent Clp protease ATP-binding subunit clpA; [Protein fate, Degradation of proteins, ... |
5-688 |
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: 630.90 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499409228 5 QSELDKYGTNLTKTAATNKLDPVIGRDAEIRRVCQILSRRTKNNPVLIGSAGVGKTAIVEGLAQRIVAGDVPESLRNKEI 84
Cdd:TIGR02639 161 QDALEKYTVDLTEKAKNGKIDPLIGREDELERTIQVLCRRKKNNPLLVGEPGVGKTAIVEGLALRIAEGKVPERLKNAKI 240
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499409228 85 VSLDLSALLAGASYRGEFEKRVKNLLEEIQK-SKVIIFIDEVHTLM-SAGAAEGAIAAGNMLKPLLARGELRLIGATTLD 162
Cdd:TIGR02639 241 YSLDMGTLLAGTKYRGDFEERLKAVVSEIEKePNAILFIDEIHTIVgAGATSGGSMDASNLLKPALSSGKIRCIGSTTYE 320
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499409228 163 EYREHLEKDPALERRFQQVFVGEPNLEDCIAIMRGLKERYEAHHKVSISDTALVTAVELSSRYITGRQLPDKAIDLLDEA 242
Cdd:TIGR02639 321 EYKNHFEKDRALSRRFQKIDVGEPSIEETVKILKGLKEQYEEFHHVKYSDEALEAAVELSARYINDRFLPDKAIDVIDEA 400
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499409228 243 ASSLRMEIDSSPveldqlrrevdrlrleelalksendptseqrlrsitnqlsgkqemlntlqaswnserarlnqigalke 322
Cdd:TIGR02639 401 GAAFRLRPKAKK-------------------------------------------------------------------- 412
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499409228 323 qidiakqsadiaqregrledasrllyatipqlQKNLAEKleeqdsaplvsdqvmpeDIASVVEGWTGIPVKKLMQKDAKQ 402
Cdd:TIGR02639 413 --------------------------------KANVNVK-----------------DIENVVAKMAKIPVKTVSSDDREQ 443
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499409228 403 LLHLEEDLSKSVIAQKVAIGVIADAVRRSRAGLSDPNRPSGTFLFLGPTGVGKTQLVKALASLLydG-EIVRIDMSEYSE 481
Cdd:TIGR02639 444 LKNLEKNLKAKIFGQDEAIDQLVSAIKRSRAGLGDPNKPVGSFLFVGPTGVGKTELAKQLAEEL--GvHLLRFDMSEYME 521
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499409228 482 KFSISRLIGAPPGYIGHESAGQLTESVRRRPYSVVLFDEAEKAHPEVFDILLQVLDEGRLTDSHGRTVDFRNTIIVLTSN 561
Cdd:TIGR02639 522 KHTVSRLIGSPPGYVGFEQGGLLTDAVRKHPHCVLLLDEIEKAHPDIYNILLQVMDYATLTDNNGRKADFRNVILIMTSN 601
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499409228 562 IGSRYLSD--ISLEATTAHEYVNDEVRRTFRPEFLNRLDEIVIFEPLSQSDICQIVDLNIESLNKRIKDRRIVVTVSEDL 639
Cdd:TIGR02639 602 AGASEMSKppIGFGGENRESKSLKAIKKLFSPEFRNRLDAIIHFNDLSEEMAEKIVKKFLDELQDQLNEKNIELELTDDA 681
|
650 660 670 680
....*....|....*....|....*....|....*....|....*....
gi 499409228 640 RRWLSKSGYDVIYGARPLRRLIQREIEDRLAKLIIEGLIHDGQTASFDL 688
Cdd:TIGR02639 682 KKYLAEKGYDEEFGARPLARVIQEEIKKPLSDEILFGKLKKGGSVKISL 730
|
|
| clpA |
PRK11034 |
ATP-dependent Clp protease ATP-binding subunit; Provisional |
2-689 |
2.59e-166 |
|
ATP-dependent Clp protease ATP-binding subunit; Provisional
Pssm-ID: 236828 [Multi-domain] Cd Length: 758 Bit Score: 496.28 E-value: 2.59e-166
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499409228 2 SESQSELDKYGTNLTKTAATNKLDPVIGRDAEIRRVCQILSRRTKNNPVLIGSAGVGKTAIVEGLAQRIVAGDVPESLRN 81
Cdd:PRK11034 163 AGGEERMENFTTNLNQLARVGGIDPLIGREKELERAIQVLCRRRKNNPLLVGESGVGKTAIAEGLAWRIVQGDVPEVMAD 242
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499409228 82 KEIVSLDLSALLAGASYRGEFEKRVKNLLEEIQK-SKVIIFIDEVHTLM-SAGAAEGAIAAGNMLKPLLARGELRLIGAT 159
Cdd:PRK11034 243 CTIYSLDIGSLLAGTKYRGDFEKRFKALLKQLEQdTNSILFIDEIHTIIgAGAASGGQVDAANLIKPLLSSGKIRVIGST 322
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499409228 160 TLDEYREHLEKDPALERRFQQVFVGEPNLEDCIAIMRGLKERYEAHHKVSISDTALVTAVELSSRYITGRQLPDKAIDLL 239
Cdd:PRK11034 323 TYQEFSNIFEKDRALARRFQKIDITEPSIEETVQIINGLKPKYEAHHDVRYTAKAVRAAVELAVKYINDRHLPDKAIDVI 402
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499409228 240 DEAASslrmeidsspveldqlrrevdrlrleelalksendptseqrlrsitnqlsgkqemlntlqaswnseRARLNQIGA 319
Cdd:PRK11034 403 DEAGA------------------------------------------------------------------RARLMPVSK 416
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499409228 320 LKEQIDIAkqsadiaqregrledasrllyatipqlqknlaekleeqdsaplvsdqvmpeDIASVVEGWTGIPVKKLMQKD 399
Cdd:PRK11034 417 RKKTVNVA---------------------------------------------------DIESVVARIARIPEKSVSQSD 445
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499409228 400 AKQLLHLEEDLSKSVIAQKVAIGVIADAVRRSRAGLSDPNRPSGTFLFLGPTGVGKTQLVKALASLLyDGEIVRIDMSEY 479
Cdd:PRK11034 446 RDTLKNLGDRLKMLVFGQDKAIEALTEAIKMSRAGLGHEHKPVGSFLFAGPTGVGKTEVTVQLSKAL-GIELLRFDMSEY 524
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499409228 480 SEKFSISRLIGAPPGYIGHESAGQLTESVRRRPYSVVLFDEAEKAHPEVFDILLQVLDEGRLTDSHGRTVDFRNTIIVLT 559
Cdd:PRK11034 525 MERHTVSRLIGAPPGYVGFDQGGLLTDAVIKHPHAVLLLDEIEKAHPDVFNLLLQVMDNGTLTDNNGRKADFRNVVLVMT 604
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499409228 560 SNIGSRYLSDISL------EATTAHEyvndEVRRTFRPEFLNRLDEIVIFEPLSQSDICQIVDLNIESLNKRIKDRRIVV 633
Cdd:PRK11034 605 TNAGVRETERKSIglihqdNSTDAME----EIKKIFTPEFRNRLDNIIWFDHLSTDVIHQVVDKFIVELQAQLDQKGVSL 680
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....*.
gi 499409228 634 TVSEDLRRWLSKSGYDVIYGARPLRRLIQREIEDRLAKLIIEGLIHDGQTASFDLS 689
Cdd:PRK11034 681 EVSQEARDWLAEKGYDRAMGARPMARVIQDNLKKPLANELLFGSLVDGGQVTVALD 736
|
|
| RecA-like_ClpB_Hsp104-like |
cd19499 |
Chaperone protein ClpB/Hsp104 subfamily; Bacterial Caseinolytic peptidase B (ClpB) and ... |
403-603 |
8.87e-95 |
|
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: 290.62 E-value: 8.87e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499409228 403 LLHLEEDLSKSVIAQKVAIGVIADAVRRSRAGLSDPNRPSGTFLFLGPTGVGKTQLVKALASLLYDGEI--VRIDMSEYS 480
Cdd:cd19499 2 LLNLEERLHERVVGQDEAVKAVSDAIRRARAGLSDPNRPIGSFLFLGPTGVGKTELAKALAELLFGDEDnlIRIDMSEYM 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499409228 481 EKFSISRLIGAPPGYIGHESAGQLTESVRRRPYSVVLFDEAEKAHPEVFDILLQVLDEGRLTDSHGRTVDFRNTIIVLTS 560
Cdd:cd19499 82 EKHSVSRLIGAPPGYVGYTEGGQLTEAVRRKPYSVVLLDEIEKAHPDVQNLLLQVLDDGRLTDSHGRTVDFKNTIIIMTS 161
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 499409228 561 NIgsrylsdisleattaheyvndevrrtFRPEFLNRLDEIVIF 603
Cdd:cd19499 162 NH--------------------------FRPEFLNRIDEIVVF 178
|
|
| AAA_2 |
pfam07724 |
AAA domain (Cdc48 subfamily); This Pfam entry includes some of the AAA proteins not detected ... |
440-600 |
2.48e-82 |
|
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: 257.89 E-value: 2.48e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499409228 440 RPSGTFLFLGPTGVGKTQLVKALASLLYDGE--IVRIDMSEYSEKFSISRLIGAPPGYIGHESAGQLTESVRRRPYSVVL 517
Cdd:pfam07724 1 RPIGSFLFLGPTGVGKTELAKALAELLFGDEraLIRIDMSEYMEEHSVSRLIGAPPGYVGYEEGGQLTEAVRRKPYSIVL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499409228 518 FDEAEKAHPEVFDILLQVLDEGRLTDSHGRTVDFRNTIIVLTSNIGSRYLSDIS-----LEATTAHEYVNDEVRRTFRPE 592
Cdd:pfam07724 81 IDEIEKAHPGVQNDLLQILEGGTLTDKQGRTVDFKNTLFIMTGNFGSEKISDASrlgdsPDYELLKEEVMDLLKKGFIPE 160
|
....*...
gi 499409228 593 FLNRLDEI 600
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 ... |
187-289 |
5.70e-43 |
|
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: 150.33 E-value: 5.70e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499409228 187 NLEDCIAIMRGLKERYEAHHKVSISDTALVTAVELSSRYITGRQLPDKAIDLLDEAASSLRMEIDSSPVELDQLRREVDR 266
Cdd:pfam17871 1 SVEEAIEILRGLKPKYEKHHGVRISDEALEAAVKLSKRYITDRFLPDKAIDLLDEACARVRLSQESKPEELEDLERELAK 80
|
90 100
....*....|....*....|...
gi 499409228 267 LRLEELALKSENDPTSEQRLRSI 289
Cdd:pfam17871 81 LEIEKEALEREQDFEKAERLAKL 103
|
|
| ClpB_D2-small |
pfam10431 |
C-terminal, D2-small domain, of ClpB protein; This is the C-terminal domain of ClpB protein, ... |
606-683 |
4.38e-26 |
|
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: 102.10 E-value: 4.38e-26
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 499409228 606 LSQSDICQIVDLNIESLNKRIKDRRIVVTVSEDLRRWLSKSGYDVIYGARPLRRLIQREIEDRLAKLIIEGLIHDGQT 683
Cdd:pfam10431 1 LSKEELRKIVDLQLKELQKRLAERGITLELTDAAKDWLAEKGYDPEYGARPLRRAIQREIEDPLAEEILSGELKEGDT 78
|
|
| ClpB_D2-small |
smart01086 |
C-terminal, D2-small domain, of ClpB protein; This is the C-terminal domain of ClpB protein, ... |
606-691 |
2.61e-23 |
|
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: 94.43 E-value: 2.61e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499409228 606 LSQSDICQIVDLNIESLNKRIKDRRIVVTVSEDLRRWLSKSGYDVIYGARPLRRLIQREIEDRLAKLIIEGLIHDGQTAS 685
Cdd:smart01086 1 LDKEDLVRIVDLPLNALQKRLAEKGITLEFTDEALDWLAEKGYDPKYGARPLRRIIQRELEDPLAELILSGELKDGDTVV 80
|
....*.
gi 499409228 686 FDLSGG 691
Cdd:smart01086 81 VDVDDG 86
|
|
| AAA |
cd00009 |
The AAA+ (ATPases Associated with a wide variety of cellular Activities) superfamily ... |
28-186 |
4.36e-19 |
|
The AAA+ (ATPases Associated with a wide variety of cellular Activities) superfamily represents an ancient group of ATPases belonging to the ASCE (for additional strand, catalytic E) division of the P-loop NTPase fold. The ASCE division also includes ABC, RecA-like, VirD4-like, PilT-like, and SF1/2 helicases. Members of the AAA+ ATPases function as molecular chaperons, ATPase subunits of proteases, helicases, or nucleic-acid stimulated ATPases. The AAA+ proteins contain several distinct features in addition to the conserved alpha-beta-alpha core domain structure and the Walker A and B motifs of the P-loop NTPases.
Pssm-ID: 99707 [Multi-domain] Cd Length: 151 Bit Score: 84.51 E-value: 4.36e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499409228 28 IGRDAEIRRVCQILSRRTKNNPVLIGSAGVGKTAIVEGLAQRIVagdvpesLRNKEIVSLDLSALLAGASYRGEFEKRVK 107
Cdd:cd00009 1 VGQEEAIEALREALELPPPKNLLLYGPPGTGKTTLARAIANELF-------RPGAPFLYLNASDLLEGLVVAELFGHFLV 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499409228 108 NLLEEI--QKSKVIIFIDEVHTLMSAGAAEGAIAAGNMLKPLLARGELRLIGATTLDEYRehlEKDPALERRFQQVFVGE 185
Cdd:cd00009 74 RLLFELaeKAKPGVLFIDEIDSLSRGAQNALLRVLETLNDLRIDRENVRVIGATNRPLLG---DLDRALYDRLDIRIVIP 150
|
.
gi 499409228 186 P 186
Cdd:cd00009 151 L 151
|
|
| AAA |
cd00009 |
The AAA+ (ATPases Associated with a wide variety of cellular Activities) superfamily ... |
438-605 |
1.28e-14 |
|
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: 71.79 E-value: 1.28e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499409228 438 PNRPSGTFLFLGPTGVGKTQLVKALA--SLLYDGEIVRIDMSEYSEKFSISRLigappgyIGHESAGQLTESVRRRPYSV 515
Cdd:cd00009 15 ELPPPKNLLLYGPPGTGKTTLARAIAneLFRPGAPFLYLNASDLLEGLVVAEL-------FGHFLVRLLFELAEKAKPGV 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499409228 516 VLFDEAEKAHPEVFDILLQVLDEGRLTdshgrTVDFRNTIIVLTSnigsrylsdisleattaheyvNDEVRRTFRPEFLN 595
Cdd:cd00009 88 LFIDEIDSLSRGAQNALLRVLETLNDL-----RIDRENVRVIGAT---------------------NRPLLGDLDRALYD 141
|
170
....*....|
gi 499409228 596 RLDEIVIFEP 605
Cdd:cd00009 142 RLDIRIVIPL 151
|
|
| AAA_5 |
pfam07728 |
AAA domain (dynein-related subfamily); This Pfam entry includes some of the AAA proteins not ... |
445-571 |
1.51e-12 |
|
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: 65.39 E-value: 1.51e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499409228 445 FLFLGPTGVGKTQLVKALASLLYDGEIVRIDMSEYSEKfsiSRLIGappgyiGHESAGQLTESVRR------RPYSVVLF 518
Cdd:pfam07728 2 VLLVGPPGTGKTELAERLAAALSNRPVFYVQLTRDTTE---EDLFG------RRNIDPGGASWVDGplvraaREGEIAVL 72
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 499409228 519 DEAEKAHPEVFDILLQVLDEGRL-TDSHGRTVDFRNT--IIVLTSNIGSRYLSDIS 571
Cdd:pfam07728 73 DEINRANPDVLNSLLSLLDERRLlLPDGGELVKAAPDgfRLIATMNPLDRGLNELS 128
|
|
| AAA |
pfam00004 |
ATPase family associated with various cellular activities (AAA); AAA family proteins often ... |
51-182 |
3.07e-12 |
|
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: 64.15 E-value: 3.07e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499409228 51 LIGSAGVGKTAIVEGLAQRIvagdvpeslrNKEIVSLDLSALLAgaSYRGEFEKRVKNLLEEIQK-SKVIIFIDEVHTLM 129
Cdd:pfam00004 3 LYGPPGTGKTTLAKAVAKEL----------GAPFIEISGSELVS--KYVGESEKRLRELFEAAKKlAPCVIFIDEIDALA 70
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 499409228 130 SAGAAEGAIAAG---NMLKPLL-----ARGELRLIGATTL-DEYrehlekDPALERRFQQVF 182
Cdd:pfam00004 71 GSRGSGGDSESRrvvNQLLTELdgftsSNSKVIVIAATNRpDKL------DPALLGRFDRII 126
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
441-581 |
1.54e-11 |
|
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: 62.78 E-value: 1.54e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499409228 441 PSGTFLFLGPTGVGKTQLVKALASLL--YDGEIVRIDMSEYSEKFSISRLI----GAPPGYIGHESAGQLTESVRRRPYS 514
Cdd:smart00382 1 PGEVILIVGPPGSGKTTLARALARELgpPGGGVIYIDGEDILEEVLDQLLLiivgGKKASGSGELRLRLALALARKLKPD 80
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 499409228 515 VVLFDEAEKAHPEVFDILLQVLDEGRLTDSHGRtvdFRNTIIVLTSNIGSRYLSDISLEATTAHEYV 581
Cdd:smart00382 81 VLILDEITSLLDAEQEALLLLLEELRLLLLLKS---EKNLTVILTTNDEKDLGPALLRRRFDRRIVL 144
|
|
| SpoVK |
COG0464 |
AAA+-type ATPase, SpoVK/Ycf46/Vps4 family [Cell wall/membrane/envelope biogenesis, Cell cycle ... |
50-275 |
4.74e-09 |
|
AAA+-type ATPase, SpoVK/Ycf46/Vps4 family [Cell wall/membrane/envelope biogenesis, Cell cycle control, cell division, chromosome partitioning, Signal transduction mechanisms];
Pssm-ID: 440232 [Multi-domain] Cd Length: 397 Bit Score: 59.15 E-value: 4.74e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499409228 50 VLIGSAGVGKTAIVEGLAQRIvagdvpeslrNKEIVSLDLSALLAGasYRGEFEKRVKNLLEEI-QKSKVIIFIDEVHTL 128
Cdd:COG0464 195 LLYGPPGTGKTLLARALAGEL----------GLPLIEVDLSDLVSK--YVGETEKNLREVFDKArGLAPCVLFIDEADAL 262
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499409228 129 MSAGAAEGAIAAGNMLKPLLA-----RGELRLIGATTLdeyREHLekDPALERRFQ-QVFVGEPNLEDCIAIMRGLKERY 202
Cdd:COG0464 263 AGKRGEVGDGVGRRVVNTLLTemeelRSDVVVIAATNR---PDLL--DPALLRRFDeIIFFPLPDAEERLEIFRIHLRKR 337
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 499409228 203 EAHHKVSISDTALVTAvELSSRYITgrqlpdkaiDLLDEAAsSLRMEIDSSPVELDQLRREVDRlrlEELALK 275
Cdd:COG0464 338 PLDEDVDLEELAEATE-GLSGADIR---------NVVRRAA-LQALRLGREPVTTEDLLEALER---EDIFLK 396
|
|
| SpoVK |
COG0464 |
AAA+-type ATPase, SpoVK/Ycf46/Vps4 family [Cell wall/membrane/envelope biogenesis, Cell cycle ... |
246-614 |
5.65e-09 |
|
AAA+-type ATPase, SpoVK/Ycf46/Vps4 family [Cell wall/membrane/envelope biogenesis, Cell cycle control, cell division, chromosome partitioning, Signal transduction mechanisms];
Pssm-ID: 440232 [Multi-domain] Cd Length: 397 Bit Score: 58.77 E-value: 5.65e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499409228 246 LRMEIDSSPVELDQLRREVDRLRLEELALKSENDPTSEQRLRSITNQLSGKQEMLNTLQASWNSERARLNQIGALKEQID 325
Cdd:COG0464 1 LAELLALAVALALALLLLDDAALRLLLLLLLALAAALLLLLLLLLLLLLALLLVELLLLLLSGALAALLLLALLLLALLA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499409228 326 IAKQSADIAQREGRLEDASRLLYATIPQLQKNLAEKLEEQDSAPLVSDQVMPEDIASVVEGWTGIPVKKLMQKDAKQLLH 405
Cdd:COG0464 81 LLAALLSALELLLLGELLLLLLLLLLLLLLLLDLERALLELLRESAEALALAAPLVTYEDIGGLEEELLELREAILDDLG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499409228 406 LEEDLSKSViaQKVAIGVIADAVRRSRAGLsdpnRPSGTFLFLGPTGVGKTQLVKALASLLyDGEIVRIDMSEysekfsi 485
Cdd:COG0464 161 GLEEVKEEL--RELVALPLKRPELREEYGL----PPPRGLLLYGPPGTGKTLLARALAGEL-GLPLIEVDLSD------- 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499409228 486 srLIGappGYIGhESAGQLTE---SVRRRPYSVVLFDEAEKAHP-----------EVFDILLQVLDEGRltdshgrtvdf 551
Cdd:COG0464 227 --LVS---KYVG-ETEKNLREvfdKARGLAPCVLFIDEADALAGkrgevgdgvgrRVVNTLLTEMEELR----------- 289
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 499409228 552 RNTIIVLTSNigsrYLSDIsleattaheyvnDevrrtfrPEFLNRLDEIVIFEPLSQSDICQI 614
Cdd:COG0464 290 SDVVVIAATN----RPDLL------------D-------PALLRRFDEIIFFPLPDAEERLEI 329
|
|
| RecA-like_protease |
cd19481 |
proteases similar to RecA; RecA-like NTPases. This family includes the NTP binding domain of ... |
424-561 |
1.37e-07 |
|
proteases similar to RecA; RecA-like NTPases. This family includes the NTP binding domain of F1 and V1 H(+)ATPases, DnaB and related helicases as well as bacterial RecA and related eukaryotic and archaeal recombinases. This group also includes bacterial conjugation proteins and related DNA transfer proteins involved in type II and type IV secretion.
Pssm-ID: 410889 [Multi-domain] Cd Length: 158 Bit Score: 51.51 E-value: 1.37e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499409228 424 IADAVRRSRAGLSDPNRPSGTFLFLGPTGVGKTQLVKALASLLyDGEIVRIDMSEYSEKFSisrligappGYiGHESAGQ 503
Cdd:cd19481 8 AVEAPRRGSRLRRYGLGLPKGILLYGPPGTGKTLLAKALAGEL-GLPLIVVKLSSLLSKYV---------GE-SEKNLRK 76
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499409228 504 LTESVRRRPYSVVLFDEAEKA------------HPEVFDILLQVLDEGRLTDshgrtvdfrNTIIVLTSN 561
Cdd:cd19481 77 IFERARRLAPCILFIDEIDAIgrkrdssgesgeLRRVLNQLLTELDGVNSRS---------KVLVIAATN 137
|
|
| COG1223 |
COG1223 |
Predicted ATPase, AAA+ superfamily [General function prediction only]; |
24-196 |
3.54e-07 |
|
Predicted ATPase, AAA+ superfamily [General function prediction only];
Pssm-ID: 440836 [Multi-domain] Cd Length: 246 Bit Score: 51.81 E-value: 3.54e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499409228 24 LDPVIGrDAEIRRVCQILSRRTKNNPVL-------------IGSAGVGKTAIVEGLAQRIvagdvpeslrNKEIVSLDLS 90
Cdd:COG1223 1 LDDVVG-QEEAKKKLKLIIKELRRRENLrkfglwpprkilfYGPPGTGKTMLAEALAGEL----------KLPLLTVRLD 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499409228 91 ALLAgaSYRGEFEKRVKNLLEEIQKSKVIIFIDEVHTLMSAGAAEGAiaagnmlkpllaRGELR---------------- 154
Cdd:COG1223 70 SLIG--SYLGETARNLRKLFDFARRAPCVIFFDEFDAIAKDRGDQND------------VGEVKrvvnallqeldglpsg 135
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 499409228 155 --LIGATtldeYREHLeKDPALERRFQQVF-VGEPNLEDCIAIMR 196
Cdd:COG1223 136 svVIAAT----NHPEL-LDSALWRRFDEVIeFPLPDKEERKEILE 175
|
|
| RPT1 |
COG1222 |
ATP-dependent 26S proteasome regulatory subunit [Posttranslational modification, protein ... |
24-196 |
2.08e-06 |
|
ATP-dependent 26S proteasome regulatory subunit [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440835 [Multi-domain] Cd Length: 326 Bit Score: 50.39 E-value: 2.08e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499409228 24 LDPVIGRDAEIRRVCQILSRRTKNN---------PV----LIGSAGVGKTaivegLAQRIVAGDVpeslrNKEIVSLDLS 90
Cdd:COG1222 77 FDDIGGLDEQIEEIREAVELPLKNPelfrkygiePPkgvlLYGPPGTGKT-----LLAKAVAGEL-----GAPFIRVRGS 146
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499409228 91 ALLAgaSYRGEFEKRVKNLLEEI-QKSKVIIFIDEVHTLMSAGAAEGAIAAGNMLKP-LLA-------RGELRLIGATTl 161
Cdd:COG1222 147 ELVS--KYIGEGARNVREVFELArEKAPSIIFIDEIDAIAARRTDDGTSGEVQRTVNqLLAeldgfesRGDVLIIAATN- 223
|
170 180 190
....*....|....*....|....*....|....*...
gi 499409228 162 deYREHLekDPALER--RF-QQVFVGEPNLEDCIAIMR 196
Cdd:COG1222 224 --RPDLL--DPALLRpgRFdRVIEVPLPDEEAREEILK 257
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
45-183 |
2.22e-06 |
|
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: 47.75 E-value: 2.22e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499409228 45 TKNNPVLIGSAGVGKTAIVEGLAQRIVAgdvpeslRNKEIVSLDLSALLAGASYR------------GEFEKRVKNLLEE 112
Cdd:smart00382 1 PGEVILIVGPPGSGKTTLARALARELGP-------PGGGVIYIDGEDILEEVLDQllliivggkkasGSGELRLRLALAL 73
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 499409228 113 IQKSKV-IIFIDEVHTLMSAG--AAEGAIAAGNMLKPLLARGELRLIGATTldeyREHLEKDPALERRFQQVFV 183
Cdd:smart00382 74 ARKLKPdVLILDEITSLLDAEqeALLLLLEELRLLLLLKSEKNLTVILTTN----DEKDLGPALLRRRFDRRIV 143
|
|
| AAA |
pfam00004 |
ATPase family associated with various cellular activities (AAA); AAA family proteins often ... |
446-561 |
7.18e-06 |
|
ATPase family associated with various cellular activities (AAA); AAA family proteins often perform chaperone-like functions that assist in the assembly, operation, or disassembly of protein complexes.
Pssm-ID: 459627 [Multi-domain] Cd Length: 130 Bit Score: 46.05 E-value: 7.18e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499409228 446 LFLGPTGVGKTQLVKALASLLYdGEIVRIDMSEYSEKfsisrligappgYIGhESAGQLT---ESVRRRPYSVVLFDEAE 522
Cdd:pfam00004 2 LLYGPPGTGKTTLAKAVAKELG-APFIEISGSELVSK------------YVG-ESEKRLRelfEAAKKLAPCVIFIDEID 67
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 499409228 523 KAHP-----------EVFDILLQVLDegrltdshGRTVDFRNTIIVLTSN 561
Cdd:pfam00004 68 ALAGsrgsggdsesrRVVNQLLTELD--------GFTSSNSKVIVIAATN 109
|
|
| RecA-like_protease |
cd19481 |
proteases similar to RecA; RecA-like NTPases. This family includes the NTP binding domain of ... |
51-181 |
4.06e-05 |
|
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: 44.20 E-value: 4.06e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499409228 51 LIGSAGVGKTAIVEGLAqrivagdvpESLRNKEIVsLDLSALLagASYRGEFEKRVKNLLEEI-QKSKVIIFIDEVHTL- 128
Cdd:cd19481 31 LYGPPGTGKTLLAKALA---------GELGLPLIV-VKLSSLL--SKYVGESEKNLRKIFERArRLAPCILFIDEIDAIg 98
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 499409228 129 -------MSAGAAEGAIAAGNMLKPLLARGELRLIGATTLDEyrehlEKDPALER--RFQQV 181
Cdd:cd19481 99 rkrdssgESGELRRVLNQLLTELDGVNSRSKVLVIAATNRPD-----LLDPALLRpgRFDEV 155
|
|
| AAA_5 |
pfam07728 |
AAA domain (dynein-related subfamily); This Pfam entry includes some of the AAA proteins not ... |
50-178 |
5.58e-05 |
|
AAA domain (dynein-related subfamily); This Pfam entry includes some of the AAA proteins not detected by the pfam00004 model.
Pssm-ID: 400191 [Multi-domain] Cd Length: 135 Bit Score: 43.44 E-value: 5.58e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499409228 50 VLIGSAGVGKTAIVEGLAQRIVAgdvpeslRNKEIVSL--DLSA--LLAGASYRGEFEKRVKNLLEEIQKSKVIIFIDEV 125
Cdd:pfam07728 3 LLVGPPGTGKTELAERLAAALSN-------RPVFYVQLtrDTTEedLFGRRNIDPGGASWVDGPLVRAAREGEIAVLDEI 75
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 499409228 126 HTLMSagaaegaiAAGNMLKPLLARGEL----------------RLIgATTLDEYREHLEKDPALERRF 178
Cdd:pfam07728 76 NRANP--------DVLNSLLSLLDERRLllpdggelvkaapdgfRLI-ATMNPLDRGLNELSPALRSRF 135
|
|
| DNA_pol3_delta2 |
pfam13177 |
DNA polymerase III, delta subunit; DNA polymerase III, delta subunit (EC 2.7.7.7) is required ... |
439-564 |
7.27e-05 |
|
DNA polymerase III, delta subunit; DNA polymerase III, delta subunit (EC 2.7.7.7) is required for, along with delta' subunit, the assembly of the processivity factor beta(2) onto primed DNA in the DNA polymerase III holoenzyme-catalyzed reaction. The delta subunit is also known as HolA.
Pssm-ID: 433013 [Multi-domain] Cd Length: 161 Bit Score: 43.74 E-value: 7.27e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499409228 439 NRPSGTFLFLGPTGVGKTQLVKALASLLYDGE------------IVRIDmseySEKFSISRLIGAPPGYIGHESAGQLTE 506
Cdd:pfam13177 16 GRLSHAYLFSGPEGVGKLELALAFAKALFCEEpgddlpcgqcrsCRRIE----SGNHPDLVIIEPEGQSIKIDQIRELQK 91
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 499409228 507 SVRRRPY----SVVLFDEAEKAHPEVFDILLQVLDEgrltdSHGRTVdfrntIIVLTSNIGS 564
Cdd:pfam13177 92 EFSKSPYegkkKVYIIEDAEKMTASAANSLLKFLEE-----PPGNTV-----IILLTENPSR 143
|
|
| MoxR |
COG0714 |
MoxR-like ATPase [General function prediction only]; MoxR-like ATPase is part of the Pathway ... |
449-561 |
8.11e-05 |
|
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: 45.16 E-value: 8.11e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499409228 449 GPTGVGKTQLVKALASLLyDGEIVRI----DMSEysekfsiSRLIGAppgYIGHESAGQltESVRRRPY--SVVLFDEAE 522
Cdd:COG0714 38 GVPGVGKTTLAKALARAL-GLPFIRIqftpDLLP-------SDILGT---YIYDQQTGE--FEFRPGPLfaNVLLADEIN 104
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 499409228 523 KAHPEVFDILLQVLDEGRLTdSHGRTVDFRNTIIVL-TSN 561
Cdd:COG0714 105 RAPPKTQSALLEAMEERQVT-IPGGTYKLPEPFLVIaTQN 143
|
|
| COG2842 |
COG2842 |
Bacteriophage DNA transposition protein, AAA+ family ATPase [Mobilome: prophages, transposons]; ... |
415-651 |
9.23e-05 |
|
Bacteriophage DNA transposition protein, AAA+ family ATPase [Mobilome: prophages, transposons];
Pssm-ID: 442090 [Multi-domain] Cd Length: 254 Bit Score: 44.56 E-value: 9.23e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499409228 415 IAQKVAIGVIA-DAVRRSRAGLSDPNRPSGTFLFLGPTGVGKTQLVKALASLLYDGEIVRIDMSEYSEKF--SISRLIG- 490
Cdd:COG2842 22 IARWEAPSFVEtKNVRRFAEALDEARALPGIGVVYGESGVGKTTAAREYANRNPNVIYVTASPSWTSKELleELAEELGi 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499409228 491 -APPGYIGhESAGQLTESVRRRPYsVVLFDEAEKAHPEVFDILLQVLDEGrltdshgrtvdfrNTIIVLtsnIGsrylsd 569
Cdd:COG2842 102 pAPPGTIA-DLRDRILERLAGTGR-LLIIDEADHLKPKALEELRDIHDET-------------GVGVVL---IG------ 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499409228 570 isleattaheyvNDEVRRTFR--PEFLNRLDEIVIFEPLSQSDICQIVD----LNIESLNKRIKD------RRIVVTVSE 637
Cdd:COG2842 158 ------------MERLPAKLKryEQLYSRIGFWVEFKPLSLEDVRALAEawgeLTDPDLLELLHRitrgnlRRLDRTLRL 225
|
250
....*....|....
gi 499409228 638 dLRRWLSKSGYDVI 651
Cdd:COG2842 226 -AARAAKRNGLTKI 238
|
|
| MscS_porin |
pfam12795 |
Mechanosensitive ion channel porin domain; The small mechanosensitive channel, MscS, is a part ... |
229-369 |
1.44e-04 |
|
Mechanosensitive ion channel porin domain; The small mechanosensitive channel, MscS, is a part of the turgor-driven solute efflux system that protects bacteria from lysis in the event of osmotic shock. The MscS protein alone is sufficient to form a functional mechanosensitive channel gated directly by tension in the lipid bilayer. The MscS proteins are heptamers of three transmembrane subunits with seven converging M3 domains, and this MscS_porin is towards the N-terminal of the molecules. The high concentration of negative charges at the extracellular entrance of the pore helps select the cations for efflux.
Pssm-ID: 432790 [Multi-domain] Cd Length: 238 Bit Score: 43.83 E-value: 1.44e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499409228 229 RQLPDKAIDLLDEAASS------LRMEIDSSPVELDQLRREVDRLRL-EELALKSENDPTS----EQRLRSITNQLSGKQ 297
Cdd:pfam12795 19 LQDLQQALSLLDKIDASkqraaaYQKALDDAPAELRELRQELAALQAkAEAAPKEILASLSleelEQRLLQTSAQLQELQ 98
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 499409228 298 EMLNTLQASWNSERARL----NQIGALKEQID-IAKQSADIAQREGRLEDASRLLYATIPQLQKNLAEKLE-EQDSAP 369
Cdd:pfam12795 99 NQLAQLNSQLIELQTRPeraqQQLSEARQRLQqIRNRLNGPAPPGEPLSEAQRWALQAELAALKAQIDMLEqELLSNN 176
|
|
| RecA-like_CDC48_NLV2_r1-like |
cd19503 |
first of two ATPase domains of CDC48 and NLV2, and similar ATPase domains; CDC48 in yeast and ... |
51-178 |
3.28e-04 |
|
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: 41.89 E-value: 3.28e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499409228 51 LIGSAGVGKTAIVEGLAQriVAGDVPESLRNKEIVSldlsallagaSYRGEFEKRVKNLLEEIQKSK-VIIFIDEVHTLM 129
Cdd:cd19503 39 LHGPPGTGKTLLARAVAN--EAGANFLSISGPSIVS----------KYLGESEKNLREIFEEARSHApSIIFIDEIDALA 106
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 499409228 130 SAGAAEGAIAAGNMLKPLLA-------RGELRLIGATTldeyR-EHLekDPALER--RF 178
Cdd:cd19503 107 PKREEDQREVERRVVAQLLTlmdgmssRGKVVVIAATN----RpDAI--DPALRRpgRF 159
|
|
| flhF |
PRK05703 |
flagellar biosynthesis protein FlhF; |
218-456 |
3.63e-04 |
|
flagellar biosynthesis protein FlhF;
Pssm-ID: 235570 [Multi-domain] Cd Length: 424 Bit Score: 43.34 E-value: 3.63e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499409228 218 AVELSSRYITGRQLPDKA-IDLLdeAAsslrmeIDSSPVELDQLRREVDRLRLEELAL-KSENDPTSEQRLRSITNQLSG 295
Cdd:PRK05703 26 AVILSNKKVRKGGFLGKKlVEVT--AA------VDEDETPKKNPVLREEKRKPAKSILsLQALLEKRPSRTNSQDALLQA 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499409228 296 KQEMLNTLQASWNSERARLNQIGALKEQIDIAKQSADIAQREGRLED------ASRLLYATIPQLQKNLAEKLEEQDsap 369
Cdd:PRK05703 98 ENALPEWKKELEKPSEPKEEEPKAAAESKVVQKELDELRDELKELKNlledqlSGLRQVERIPPEFAELYKRLKRSG--- 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499409228 370 lvsdqvMPEDIAsvvegwtgipvKKLMQkdakqlLHLEEDLSKSVIAQKVAIGVIADAVRRSragLSDPNRPSGTFLFLG 449
Cdd:PRK05703 175 ------LSPEIA-----------EKLLK------LLLEHMPPRERTAWRYLLELLANMIPVR---VEDILKQGGVVALVG 228
|
....*..
gi 499409228 450 PTGVGKT 456
Cdd:PRK05703 229 PTGVGKT 235
|
|
| AAA_16 |
pfam13191 |
AAA ATPase domain; This family of domains contain a P-loop motif that is characteriztic of the ... |
26-75 |
8.19e-04 |
|
AAA ATPase domain; This family of domains contain a P-loop motif that is characteriztic of the AAA superfamily.
Pssm-ID: 433025 [Multi-domain] Cd Length: 167 Bit Score: 40.56 E-value: 8.19e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 499409228 26 PVIGRDAEIRRVCQILSRRTKNNP---VLIGSAGVGKTAIVEGLAQRIVAGDV 75
Cdd:pfam13191 1 RLVGREEELEQLLDALDRVRSGRPpsvLLTGEAGTGKTTLLRELLRALERDGG 53
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
221-368 |
1.17e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 42.21 E-value: 1.17e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499409228 221 LSSRYITGRQlPDKAIDLLDEAASSLRMEIDSSPVELDQLRREVDRLR-LEELALKSENDPTSEQRLRSITNQLSGKQEM 299
Cdd:COG4913 598 IRSRYVLGFD-NRAKLAALEAELAELEEELAEAEERLEALEAELDALQeRREALQRLAEYSWDEIDVASAEREIAELEAE 676
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 499409228 300 LNTLQASwNSErarlnqIGALKEQIDIAKQSADiaqregRLEDASRLLYATIPQLQKNLAEKLEEQDSA 368
Cdd:COG4913 677 LERLDAS-SDD------LAALEEQLEELEAELE------ELEEELDELKGEIGRLEKELEQAEEELDEL 732
|
|
| PRK13341 |
PRK13341 |
AAA family ATPase; |
48-177 |
1.18e-03 |
|
AAA family ATPase;
Pssm-ID: 237354 [Multi-domain] Cd Length: 725 Bit Score: 42.35 E-value: 1.18e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499409228 48 NPVLIGSAGVGKTAivegLAqRIVAGDVpeslrNKEIVSLdlSALLAGasyrgefekrVKNLLEEIQKS---------KV 118
Cdd:PRK13341 54 SLILYGPPGVGKTT----LA-RIIANHT-----RAHFSSL--NAVLAG----------VKDLRAEVDRAkerlerhgkRT 111
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 499409228 119 IIFIDEVHTLMSagaaegaiAAGNMLKPLLARGELRLIGATTLDEYrehLEKDPALERR 177
Cdd:PRK13341 112 ILFIDEVHRFNK--------AQQDALLPWVENGTITLIGATTENPY---FEVNKALVSR 159
|
|
| PRK13342 |
PRK13342 |
recombination factor protein RarA; Reviewed |
53-251 |
1.34e-03 |
|
recombination factor protein RarA; Reviewed
Pssm-ID: 237355 [Multi-domain] Cd Length: 413 Bit Score: 41.61 E-value: 1.34e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499409228 53 GSAGVGKTAivegLAqRIVAGDVpeslrNKEIVSLdlSALLAGAsyrgefeKRVKNLLEEIQKS-----KVIIFIDEVHT 127
Cdd:PRK13342 43 GPPGTGKTT----LA-RIIAGAT-----DAPFEAL--SAVTSGV-------KDLREVIEEARQRrsagrRTILFIDEIHR 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499409228 128 LmsagaaegaiaagN-----MLKPLLARGELRLIGATTLDEYrehLEKDPALERRfQQVFVGEPnLEDcIAIMRGLKeRY 202
Cdd:PRK13342 104 F-------------NkaqqdALLPHVEDGTITLIGATTENPS---FEVNPALLSR-AQVFELKP-LSE-EDIEQLLK-RA 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 499409228 203 EAHHK---VSISDTALVTAVELSS---RyitgrqlpdKAIDLLdEAASSLRMEID 251
Cdd:PRK13342 164 LEDKErglVELDDEALDALARLANgdaR---------RALNLL-ELAALGVDSIT 208
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
159-367 |
1.61e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 41.82 E-value: 1.61e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499409228 159 TTLDEYREHLEKdpalerrfqqvfvgepnLEDCIAIMRGLKERYEAHHKVSISDTALVTAVELSSRYITGRqlpdkAIDL 238
Cdd:COG4913 235 DDLERAHEALED-----------------AREQIELLEPIRELAERYAAARERLAELEYLRAALRLWFAQR-----RLEL 292
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499409228 239 LDEAASSLRmeidsspVELDQLRREVDRLRLEELALKSENDPTSEQ-------RLRSITNQLSGKQEMLNTLQASWNSER 311
Cdd:COG4913 293 LEAELEELR-------AELARLEAELERLEARLDALREELDELEAQirgnggdRLEQLEREIERLERELEERERRRARLE 365
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 499409228 312 ARLNQIG--------ALKEQIDIAKQSAD-IAQREGRLEDASRLLYATIPQLQKNLAEKLEEQDS 367
Cdd:COG4913 366 ALLAALGlplpasaeEFAALRAEAAALLEaLEEELEALEEALAEAEAALRDLRRELRELEAEIAS 430
|
|
| RecA-like_HslU |
cd19498 |
ATP-dependent protease ATPase subunit HslU; HslU is a component of the ATP-dependent protease ... |
408-523 |
1.67e-03 |
|
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: 40.06 E-value: 1.67e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499409228 408 EDLSKSVIAQKVAIGVIADAVRRS--RAGLSDPNRPSGT---FLFLGPTGVGKTQLVKALASLLyDGEIVRIDMSEYSEK 482
Cdd:cd19498 7 SELDKYIIGQDEAKRAVAIALRNRwrRMQLPEELRDEVTpknILMIGPTGVGKTEIARRLAKLA-GAPFIKVEATKFTEV 85
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 499409228 483 fsisrligappGYIGHEsagqlTESVRRRPYS-VVLFDEAEK 523
Cdd:cd19498 86 -----------GYVGRD-----VESIIRDLVEgIVFIDEIDK 111
|
|
| COG1223 |
COG1223 |
Predicted ATPase, AAA+ superfamily [General function prediction only]; |
441-645 |
1.68e-03 |
|
Predicted ATPase, AAA+ superfamily [General function prediction only];
Pssm-ID: 440836 [Multi-domain] Cd Length: 246 Bit Score: 40.64 E-value: 1.68e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499409228 441 PSGTFLFLGPTGVGKTQLVKALAS-----LLYdgeiVRIDmseysekfsisRLIGAppgYIGhESAGQLT---ESVRRRP 512
Cdd:COG1223 34 PPRKILFYGPPGTGKTMLAEALAGelklpLLT----VRLD-----------SLIGS---YLG-ETARNLRklfDFARRAP 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499409228 513 ySVVLFDEAE---------KAHPE---VFDILLQVLDEGRltdSHGRTVDFRNTIIVLTSNIGSRYLSDISLEATtahey 580
Cdd:COG1223 95 -CVIFFDEFDaiakdrgdqNDVGEvkrVVNALLQELDGLP---SGSVVIAATNHPELLDSALWRRFDEVIEFPLP----- 165
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 499409228 581 vNDEVR--------RTFRPEFLNRLDEIV-IFEPLSQSDICQIVDlniESLNKRIKDRRIVVTVsEDLRRWLSK 645
Cdd:COG1223 166 -DKEERkeilelnlKKFPLPFELDLKKLAkKLEGLSGADIEKVLK---TALKKAILEDREKVTK-EDLEEALKQ 234
|
|
| AAA_22 |
pfam13401 |
AAA domain; |
440-537 |
2.60e-03 |
|
AAA domain;
Pssm-ID: 379165 [Multi-domain] Cd Length: 129 Bit Score: 38.48 E-value: 2.60e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499409228 440 RPSGTFLFL-GPTGVGKTQLVKALASLL--YDGEIVRIDMSEYSEKFSISRLI----GAPPGYIGHESA--GQLTE-SVR 509
Cdd:pfam13401 2 RFGAGILVLtGESGTGKTTLLRRLLEQLpeVRDSVVFVDLPSGTSPKDLLRALlralGLPLSGRLSKEEllAALQQlLLA 81
|
90 100
....*....|....*....|....*...
gi 499409228 510 RRPYSVVLFDEAEKAHPEVFDILLQVLD 537
Cdd:pfam13401 82 LAVAVVLIIDEAQHLSLEALEELRDLLN 109
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
239-368 |
3.85e-03 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 39.52 E-value: 3.85e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499409228 239 LDEAASSLRMEIDSSPVELDQLRREVDRLRLEELALKSEndptseqrLRSITNQLSGKQEMLNTLQASWNSERARLNQIG 318
Cdd:COG1579 15 LDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTE--------LEDLEKEIKRLELEIEEVEARIKKYEEQLGNVR 86
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 499409228 319 ALKEQIDIAKQSADIAQREGRLEDASRLLYATIPQLQKNLAEKLEEQDSA 368
Cdd:COG1579 87 NNKEYEALQKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAEL 136
|
|
| FlhF |
TIGR03499 |
flagellar biosynthetic protein FlhF; [Cellular processes, Chemotaxis and motility] |
218-456 |
4.78e-03 |
|
flagellar biosynthetic protein FlhF; [Cellular processes, Chemotaxis and motility]
Pssm-ID: 274609 [Multi-domain] Cd Length: 282 Bit Score: 39.63 E-value: 4.78e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499409228 218 AVELSSRYITGRQLPDKAIDLLdeAAsslrmeIDSSPVELDQLRREVDRlRLEELALKSENDPTSEQRLRSITNQLSGKQ 297
Cdd:TIGR03499 26 AVILSTRKVRKGLFGKKFVEVT--AA------IDEEEAAAASAEEEASK-ALEQADPKPLSATAEPLELPAPQEEPAAPA 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499409228 298 EMLNTLQASWNSERArlnQIGALKEQIDiakqsadiaqregrlEDASRLLYATIPQLQKNLAEKLEEQDsaplvsdqvMP 377
Cdd:TIGR03499 97 AQAAEPLLPEEELRK---ELEALRELLE---------------RLLAGLAWLQRPPERAKLYERLLEAG---------VS 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499409228 378 EDIAsvvegwtgipvKKLMQKdAKQLLHLEE--DLSKSVIAQKVAIGVIADavrrsraglsDPNRPSGTFLFLGPTGVGK 455
Cdd:TIGR03499 150 EELA-----------RELLEK-LPEDADAEDawRWLREALEGMLPVKPEED----------PILEQGGVIALVGPTGVGK 207
|
.
gi 499409228 456 T 456
Cdd:TIGR03499 208 T 208
|
|
| CDC48 |
TIGR01243 |
AAA family ATPase, CDC48 subfamily; This subfamily of the AAA family ATPases includes two ... |
50-180 |
7.95e-03 |
|
AAA family ATPase, CDC48 subfamily; This subfamily of the AAA family ATPases includes two members each from three archaeal species. It also includes yeast CDC48 (cell division control protein 48) and the human ortholog, transitional endoplasmic reticulum ATPase (valosin-containing protein). These proteins in eukaryotes are involved in the budding and transfer of membrane from the transitional endoplasmic reticulum to the Golgi apparatus.
Pssm-ID: 273521 [Multi-domain] Cd Length: 733 Bit Score: 39.51 E-value: 7.95e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499409228 50 VLIGSAGVGKTAIVEGLAQRIVAGDVpeSLRNKEIVSldlsallagaSYRGEFEKRVKNLLEEIQK-SKVIIFIDEVHTL 128
Cdd:TIGR01243 216 LLYGPPGTGKTLLAKAVANEAGAYFI--SINGPEIMS----------KYYGESEERLREIFKEAEEnAPSIIFIDEIDAI 283
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 499409228 129 MSAGAAEGAIAAGNMLKPLLA-------RGELRLIGATTLDEyrehlEKDPALER--RFQQ 180
Cdd:TIGR01243 284 APKREEVTGEVEKRVVAQLLTlmdglkgRGRVIVIGATNRPD-----ALDPALRRpgRFDR 339
|
|
| |
