|
Name |
Accession |
Description |
Interval |
E-value |
| ClpA |
COG0542 |
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ... |
76-700 |
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: 817.40 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1714390871 76 KGGILEKLGTNLTEQARDGLLDPVIGRENEIQETAEILSRRTKNNPILVGDAGVGKTAVVEGLAQAIVAGKVPETIQDKE 155
Cdd:COG0542 158 KTPALDKYGRDLTELAREGKLDPVIGRDEEIRRVIQILSRRTKNNPVLIGEPGVGKTAIVEGLAQRIVNGDVPESLKDKR 237
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1714390871 156 IYSIDLSSLEAGTQYRGSFEENIKQLVKEVKA-AGNIILFFDEIHQIIGTGATggeDGGKGLADIIKPALSRGELTVIGA 234
Cdd:COG0542 238 VLSLDLGALVAGAKYRGEFEERLKAVLDEVKKsEGNIILFIDELHTLVGAGGA---EGAMDAANLLKPALARGELRCIGA 314
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1714390871 235 TTQDEYRNTILKNAALARRFNDVVINEPTAADTLRILQGVKKLYEKHHHVVLPDDVLKAAVDYSIQYIPQRTLPDKAIDL 314
Cdd:COG0542 315 TTLDEYRKYIEKDAALERRFQPVLVEEPSVEDTISILRGLKERYEAHHGVRITDEALVAAVRLSDRYITDRFLPDKAIDL 394
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1714390871 315 IDMTAAHLAAKNSQ--TDVETLDQRVKKLEAAKEAAVKSED---FTKAADIKKSIEETKQKIKK---------------T 374
Cdd:COG0542 395 IDEAAARVRMEIDSkpEELDELERRLEQLEIEKEALKKEQDeasFERLAELRDELAELEEELEAlkarweaekelieeiQ 474
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1714390871 375 DQKEKITA------------------------------TIDDVAQSVERLTGIPVADMGANDIEHLKNLDKRLKSKVIGQ 424
Cdd:COG0542 475 ELKEELEQrygkipelekelaeleeelaelapllreevTEEDIAEVVSRWTGIPVGKLLEGEREKLLNLEEELHERVIGQ 554
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1714390871 425 DEAVEMVAKAIRRNRAGFSEGDQPIGSFLFVGPTGVGKTELAKQLALDMFGNKNAIIRLDMSEYADRTAVSKLIGTSAGY 504
Cdd:COG0542 555 DEAVEAVADAIRRSRAGLKDPNRPIGSFLFLGPTGVGKTELAKALAEFLFGDEDALIRIDMSEYMEKHSVSRLIGAPPGY 634
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1714390871 505 VGYEDnANTLTERVRRNPYSIVLLDEIEKADPQVLTLLLQVMDDGRLTDGQGNVINFKNTIIIATSNAG------FGNEA 578
Cdd:COG0542 635 VGYEE-GGQLTEAVRRRPYSVVLLDEIEKAHPDVFNILLQVLDDGRLTDGQGRTVDFRNTIIIMTSNIGselildLAEDE 713
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1714390871 579 LSGDKQRDQsLMDKLAPFFRPEFLNRFNGIVEFSHLTKQDLSQIVDLMLADVQKTLAKKSIKLEVTKAAKDWLMEQGYDE 658
Cdd:COG0542 714 PDYEEMKEA-VMEELKKHFRPEFLNRIDEIIVFHPLSKEELRKIVDLQLKRLRKRLAERGITLELTDAAKDFLAEKGYDP 792
|
650 660 670 680
....*....|....*....|....*....|....*....|....
gi 1714390871 659 AMGARPLRRVIEQQIRDKVTDFYLDHL--DVKNLKADLVDGEIV 700
Cdd:COG0542 793 EYGARPLKRAIQRELEDPLAEEILAGEikEGDTITVDVDDGELV 836
|
|
| clpC |
CHL00095 |
Clp protease ATP binding subunit |
61-683 |
0e+00 |
|
Clp protease ATP binding subunit
Pssm-ID: 214361 [Multi-domain] Cd Length: 821 Bit Score: 669.84 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1714390871 61 NKTIEVSKDGKQAFKKGGILEKLGTNLTEQARDGLLDPVIGRENEIQETAEILSRRTKNNPILVGDAGVGKTAVVEGLAQ 140
Cdd:CHL00095 143 GEIIEAILGAEQSRSKTPTLEEFGTNLTKEAIDGNLDPVIGREKEIERVIQILGRRTKNNPILIGEPGVGKTAIAEGLAQ 222
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1714390871 141 AIVAGKVPETIQDKEIYSIDLSSLEAGTQYRGSFEENIKQLVKEVKAAGNIILFFDEIHQIIGTGATggeDGGKGLADII 220
Cdd:CHL00095 223 RIVNRDVPDILEDKLVITLDIGLLLAGTKYRGEFEERLKRIFDEIQENNNIILVIDEVHTLIGAGAA---EGAIDAANIL 299
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1714390871 221 KPALSRGELTVIGATTQDEYRNTILKNAALARRFNDVVINEPTAADTLRILQGVKKLYEKHHHVVLPDDVLKAAVDYSIQ 300
Cdd:CHL00095 300 KPALARGELQCIGATTLDEYRKHIEKDPALERRFQPVYVGEPSVEETIEILFGLRSRYEKHHNLSISDKALEAAAKLSDQ 379
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1714390871 301 YIPQRTLPDKAIDLIDMTAAHLAAKNSQTD--VETLDQRVKKLEAAKEAAVKSEDFTKAADIKKSIEETKQKI------- 371
Cdd:CHL00095 380 YIADRFLPDKAIDLLDEAGSRVRLINSRLPpaARELDKELREILKDKDEAIREQDFETAKQLRDREMEVRAQIaaiiqsk 459
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1714390871 372 --KKTDQKEKITATIDDVAQSVERLTGIPVADMGANDIEHLKNLDKRLKSKVIGQDEAVEMVAKAIRRNRAGFSEGDQPI 449
Cdd:CHL00095 460 ktEEEKRLEVPVVTEEDIAEIVSAWTGIPVNKLTKSESEKLLHMEETLHKRIIGQDEAVVAVSKAIRRARVGLKNPNRPI 539
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1714390871 450 GSFLFVGPTGVGKTELAKQLALDMFGNKNAIIRLDMSEYADRTAVSKLIGTSAGYVGYEDNANtLTERVRRNPYSIVLLD 529
Cdd:CHL00095 540 ASFLFSGPTGVGKTELTKALASYFFGSEDAMIRLDMSEYMEKHTVSKLIGSPPGYVGYNEGGQ-LTEAVRKKPYTVVLFD 618
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1714390871 530 EIEKADPQVLTLLLQVMDDGRLTDGQGNVINFKNTIIIATSNAGF--------GNEALSGDKQRDQSLMDKLA------- 594
Cdd:CHL00095 619 EIEKAHPDIFNLLLQILDDGRLTDSKGRTIDFKNTLIIMTSNLGSkvietnsgGLGFELSENQLSEKQYKRLSnlvneel 698
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1714390871 595 -PFFRPEFLNRFNGIVEFSHLTKQDLSQIVDLMLADVQKTLAKKSIKLEVTKAAKDWLMEQGYDEAMGARPLRRVIEQQI 673
Cdd:CHL00095 699 kQFFRPEFLNRLDEIIVFRQLTKNDVWEIAEIMLKNLFKRLNEQGIQLEVTERIKTLLIEEGYNPLYGARPLRRAIMRLL 778
|
650
....*....|
gi 1714390871 674 RDKVTDFYLD 683
Cdd:CHL00095 779 EDPLAEEVLS 788
|
|
| chaperone_ClpB |
TIGR03346 |
ATP-dependent chaperone ClpB; Members of this protein family are the bacterial ATP-dependent ... |
80-700 |
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: 669.36 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1714390871 80 LEKLGTNLTEQARDGLLDPVIGRENEIQETAEILSRRTKNNPILVGDAGVGKTAVVEGLAQAIVAGKVPETIQDKEIYSI 159
Cdd:TIGR03346 156 LEKYARDLTERAREGKLDPVIGRDEEIRRTIQVLSRRTKNNPVLIGEPGVGKTAIVEGLAQRIVNGDVPEGLKNKRLLAL 235
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1714390871 160 DLSSLEAGTQYRGSFEENIKQLVKEV-KAAGNIILFFDEIHQIIGTGATGGE-DGGkglaDIIKPALSRGELTVIGATTQ 237
Cdd:TIGR03346 236 DMGALIAGAKYRGEFEERLKAVLNEVtKSEGQIILFIDELHTLVGAGKAEGAmDAG----NMLKPALARGELHCIGATTL 311
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1714390871 238 DEYRNTILKNAALARRFNDVVINEPTAADTLRILQGVKKLYEKHHHVVLPDDVLKAAVDYSIQYIPQRTLPDKAIDLIDM 317
Cdd:TIGR03346 312 DEYRKYIEKDAALERRFQPVFVDEPSVEDTISILRGLKERYEVHHGVRITDPAIVAAATLSHRYITDRFLPDKAIDLIDE 391
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1714390871 318 TAAHL----------------------------------AAKNSQTDVE-----------TLDQRVK------------- 339
Cdd:TIGR03346 392 AAARIrmeidskpeeldeldrriiqleierealkkekdeASKKRLEDLEkeladleeeyaELEEQWKaekasiqgiqqik 471
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1714390871 340 -KLEAAK---EAAVKSEDFTKAADIK--------KSIEETKQKIKKTDQ---KEKITAtiDDVAQSVERLTGIPVADMGA 404
Cdd:TIGR03346 472 eEIEQVRlelEQAEREGDLAKAAELQygklpeleKQLQAAEQKLGEEQNrllREEVTA--EEIAEVVSRWTGIPVSKMLE 549
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1714390871 405 NDIEHLKNLDKRLKSKVIGQDEAVEMVAKAIRRNRAGFSEGDQPIGSFLFVGPTGVGKTELAKQLALDMFGNKNAIIRLD 484
Cdd:TIGR03346 550 GEREKLLHMEEELHERVVGQDEAVEAVSDAIRRSRAGLSDPNRPIGSFLFLGPTGVGKTELAKALAEFLFDSEDAMVRID 629
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1714390871 485 MSEYADRTAVSKLIGTSAGYVGYEDnANTLTERVRRNPYSIVLLDEIEKADPQVLTLLLQVMDDGRLTDGQGNVINFKNT 564
Cdd:TIGR03346 630 MSEYMEKHSVARLIGAPPGYVGYEE-GGQLTEAVRRRPYSVVLFDEVEKAHPDVFNVLLQVLDDGRLTDGQGRTVDFRNT 708
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1714390871 565 IIIATSNAGFGN-EALSGDKQRDQ---SLMDKLAPFFRPEFLNRFNGIVEFSHLTKQDLSQIVDLMLADVQKTLAKKSIK 640
Cdd:TIGR03346 709 VIIMTSNLGSDFiQELAGGDDYEEmreAVMEVLRAHFRPEFLNRIDEIVVFHPLGREQIARIVEIQLGRLRKRLAERKIT 788
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1714390871 641 LEVTKAAKDWLMEQGYDEAMGARPLRRVIEQQIRDKVTDFYL--DHLDVKNLKADLVDGEIV 700
Cdd:TIGR03346 789 LELSDAALDFLAEAGYDPVYGARPLKRAIQREIENPLAKKILagEVAPGDTIRVDVEGGRLV 850
|
|
| PRK10865 |
PRK10865 |
ATP-dependent chaperone ClpB; |
67-675 |
0e+00 |
|
ATP-dependent chaperone ClpB;
Pssm-ID: 182791 [Multi-domain] Cd Length: 857 Bit Score: 537.51 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1714390871 67 SKDGKQAFKKGGIleklgtNLTEQARDGLLDPVIGRENEIQETAEILSRRTKNNPILVGDAGVGKTAVVEGLAQAIVAGK 146
Cdd:PRK10865 154 AEDQRQALKKYTI------DLTERAEQGKLDPVIGRDEEIRRTIQVLQRRTKNNPVLIGEPGVGKTAIVEGLAQRIINGE 227
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1714390871 147 VPETIQDKEIYSIDLSSLEAGTQYRGSFEENIKQLVKEV-KAAGNIILFFDEIHQIIGTG-ATGGEDGGkglaDIIKPAL 224
Cdd:PRK10865 228 VPEGLKGRRVLALDMGALVAGAKYRGEFEERLKGVLNDLaKQEGNVILFIDELHTMVGAGkADGAMDAG----NMLKPAL 303
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1714390871 225 SRGELTVIGATTQDEYRNTILKNAALARRFNDVVINEPTAADTLRILQGVKKLYEKHHHVVLPDDVLKAAVDYSIQYIPQ 304
Cdd:PRK10865 304 ARGELHCVGATTLDEYRQYIEKDAALERRFQKVFVAEPSVEDTIAILRGLKERYELHHHVQITDPAIVAAATLSHRYIAD 383
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1714390871 305 RTLPDKAIDLIDMTAAHLAAK--NSQTDVETLDQRVKKLEAAKEAAVKSED----------------------------- 353
Cdd:PRK10865 384 RQLPDKAIDLIDEAASSIRMQidSKPEELDRLDRRIIQLKLEQQALMKESDeaskkrldmlneelsdkerqyseleeewk 463
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1714390871 354 -----FTKAADIKKSIEETKQKIKKTD-------------------QKEKITATIDD---------------VAQSVERL 394
Cdd:PRK10865 464 aekasLSGTQTIKAELEQAKIAIEQARrvgdlarmselqygkipelEKQLAAATQLEgktmrllrnkvtdaeIAEVLARW 543
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1714390871 395 TGIPVADMGANDIEHLKNLDKRLKSKVIGQDEAVEMVAKAIRRNRAGFSEGDQPIGSFLFVGPTGVGKTELAKQLALDMF 474
Cdd:PRK10865 544 TGIPVSRMLESEREKLLRMEQELHHRVIGQNEAVEAVSNAIRRSRAGLSDPNRPIGSFLFLGPTGVGKTELCKALANFMF 623
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1714390871 475 GNKNAIIRLDMSEYADRTAVSKLIGTSAGYVGYEDnANTLTERVRRNPYSIVLLDEIEKADPQVLTLLLQVMDDGRLTDG 554
Cdd:PRK10865 624 DSDDAMVRIDMSEFMEKHSVSRLVGAPPGYVGYEE-GGYLTEAVRRRPYSVILLDEVEKAHPDVFNILLQVLDDGRLTDG 702
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1714390871 555 QGNVINFKNTIIIATSNAG-------FGNEALSGDKqrdQSLMDKLAPFFRPEFLNRFNGIVEFSHLTKQDLSQIVDLML 627
Cdd:PRK10865 703 QGRTVDFRNTVVIMTSNLGsdliqerFGELDYAHMK---ELVLGVVSHNFRPEFINRIDEVVVFHPLGEQHIASIAQIQL 779
|
650 660 670 680
....*....|....*....|....*....|....*....|....*...
gi 1714390871 628 ADVQKTLAKKSIKLEVTKAAKDWLMEQGYDEAMGARPLRRVIEQQIRD 675
Cdd:PRK10865 780 QRLYKRLEERGYEIHISDEALKLLSENGYDPVYGARPLKRAIQQQIEN 827
|
|
| VI_ClpV1 |
TIGR03345 |
type VI secretion ATPase, ClpV1 family; Members of this protein family are homologs of ClpB, ... |
72-685 |
1.17e-180 |
|
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: 536.45 E-value: 1.17e-180
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1714390871 72 QAFKKGGILEKLGTNLTEQARDGLLDPVIGRENEIQETAEILSRRTKNNPILVGDAGVGKTAVVEGLAQAIVAGKVPETI 151
Cdd:TIGR03345 162 AGAAGTSALDQYTTDLTAQAREGKIDPVLGRDDEIRQMIDILLRRRQNNPILTGEAGVGKTAVVEGLALRIAAGDVPPAL 241
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1714390871 152 QDKEIYSIDLSSLEAGTQYRGSFEENIKQLVKEVKAAGN-IILFFDEIHQIIGTGatgGEDGGKGLADIIKPALSRGELT 230
Cdd:TIGR03345 242 RNVRLLSLDLGLLQAGASVKGEFENRLKSVIDEVKASPQpIILFIDEAHTLIGAG---GQAGQGDAANLLKPALARGELR 318
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1714390871 231 VIGATTQDEYRNTILKNAALARRFNDVVINEPTAADTLRILQGVKKLYEKHHHVVLPDDVLKAAVDYSIQYIPQRTLPDK 310
Cdd:TIGR03345 319 TIAATTWAEYKKYFEKDPALTRRFQVVKVEEPDEETAIRMLRGLAPVLEKHHGVLILDEAVVAAVELSHRYIPGRQLPDK 398
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1714390871 311 AIDLIDMTAAHLA-AKNSQTD-VETLDQRVKKLEA-----AKEAAVKSEDFTKAADIKKSIEETKQKIKKTDQ------- 376
Cdd:TIGR03345 399 AVSLLDTACARVAlSQNATPAaLEDLRRRIAALELeldalEREAALGADHDERLAELRAELAALEAELAALEArwqqeke 478
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1714390871 377 --------KEKITATIDD-------------------------------------VAQSVERLTGIPVADMGANDIEHLK 411
Cdd:TIGR03345 479 lveailalRAELEADADApaddddalraqlaeleaalasaqgeeplvfpevdaqaVAEVVADWTGIPVGRMVRDEIEAVL 558
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1714390871 412 NLDKRLKSKVIGQDEAVEMVAKAIRRNRAGFSEGDQPIGSFLFVGPTGVGKTELAKQLALDMFGNKNAIIRLDMSEYADR 491
Cdd:TIGR03345 559 SLPDRLAERVIGQDHALEAIAERIRTARAGLEDPRKPLGVFLLVGPSGVGKTETALALAELLYGGEQNLITINMSEFQEA 638
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1714390871 492 TAVSKLIGTSAGYVGYEDnANTLTERVRRNPYSIVLLDEIEKADPQVLTLLLQVMDDGRLTDGQGNVINFKNTIIIATSN 571
Cdd:TIGR03345 639 HTVSRLKGSPPGYVGYGE-GGVLTEAVRRKPYSVVLLDEVEKAHPDVLELFYQVFDKGVMEDGEGREIDFKNTVILLTSN 717
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1714390871 572 AGFGN-EALSGDKQR-------DQSLMDKLAPFFRPEFLNRFNgIVEFSHLTKQDLSQIVDLMLADVQKTLAKKS-IKLE 642
Cdd:TIGR03345 718 AGSDLiMALCADPETapdpealLEALRPELLKVFKPAFLGRMT-VIPYLPLDDDVLAAIVRLKLDRIARRLKENHgAELV 796
|
650 660 670 680
....*....|....*....|....*....|....*....|...
gi 1714390871 643 VTKAAKDWLMEQGYDEAMGARPLRRVIEQQIRDKVTDFYLDHL 685
Cdd:TIGR03345 797 YSEALVEHIVARCTEVESGARNIDAILNQTLLPELSRQILERL 839
|
|
| clpA |
PRK11034 |
ATP-dependent Clp protease ATP-binding subunit; Provisional |
80-674 |
3.80e-174 |
|
ATP-dependent Clp protease ATP-binding subunit; Provisional
Pssm-ID: 236828 [Multi-domain] Cd Length: 758 Bit Score: 516.70 E-value: 3.80e-174
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1714390871 80 LEKLGTNLTEQARDGLLDPVIGRENEIQETAEILSRRTKNNPILVGDAGVGKTAVVEGLAQAIVAGKVPETIQDKEIYSI 159
Cdd:PRK11034 169 MENFTTNLNQLARVGGIDPLIGREKELERAIQVLCRRRKNNPLLVGESGVGKTAIAEGLAWRIVQGDVPEVMADCTIYSL 248
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1714390871 160 DLSSLEAGTQYRGSFEENIKQLVKEVKAAGNIILFFDEIHQIIGTGATGGedGGKGLADIIKPALSRGELTVIGATTQDE 239
Cdd:PRK11034 249 DIGSLLAGTKYRGDFEKRFKALLKQLEQDTNSILFIDEIHTIIGAGAASG--GQVDAANLIKPLLSSGKIRVIGSTTYQE 326
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1714390871 240 YRNTILKNAALARRFNDVVINEPTAADTLRILQGVKKLYEKHHHVVLPDDVLKAAVDYSIQYIPQRTLPDKAIDLIDmta 319
Cdd:PRK11034 327 FSNIFEKDRALARRFQKIDITEPSIEETVQIINGLKPKYEAHHDVRYTAKAVRAAVELAVKYINDRHLPDKAIDVID--- 403
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1714390871 320 ahlaaknsqtdvetldqrvkkleaakEAAVKSEdFTKAADIKKSIeetkqkikktdqkekitaTIDDVAQSVERLTGIPV 399
Cdd:PRK11034 404 --------------------------EAGARAR-LMPVSKRKKTV------------------NVADIESVVARIARIPE 438
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1714390871 400 ADMGANDIEHLKNLDKRLKSKVIGQDEAVEMVAKAIRRNRAGFSEGDQPIGSFLFVGPTGVGKTELAKQLA--LDMfgnk 477
Cdd:PRK11034 439 KSVSQSDRDTLKNLGDRLKMLVFGQDKAIEALTEAIKMSRAGLGHEHKPVGSFLFAGPTGVGKTEVTVQLSkaLGI---- 514
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1714390871 478 nAIIRLDMSEYADRTAVSKLIGTSAGYVGYeDNANTLTERVRRNPYSIVLLDEIEKADPQVLTLLLQVMDDGRLTDGQGN 557
Cdd:PRK11034 515 -ELLRFDMSEYMERHTVSRLIGAPPGYVGF-DQGGLLTDAVIKHPHAVLLLDEIEKAHPDVFNLLLQVMDNGTLTDNNGR 592
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1714390871 558 VINFKNTIIIATSNAGFGNEALS--GDKQRDQS--LMDKLAPFFRPEFLNRFNGIVEFSHLTKQDLSQIVDLMLADVQKT 633
Cdd:PRK11034 593 KADFRNVVLVMTTNAGVRETERKsiGLIHQDNStdAMEEIKKIFTPEFRNRLDNIIWFDHLSTDVIHQVVDKFIVELQAQ 672
|
570 580 590 600
....*....|....*....|....*....|....*....|.
gi 1714390871 634 LAKKSIKLEVTKAAKDWLMEQGYDEAMGARPLRRVIEQQIR 674
Cdd:PRK11034 673 LDQKGVSLEVSQEARDWLAEKGYDRAMGARPMARVIQDNLK 713
|
|
| RecA-like_ClpB_Hsp104-like |
cd19499 |
Chaperone protein ClpB/Hsp104 subfamily; Bacterial Caseinolytic peptidase B (ClpB) and ... |
410-611 |
4.26e-84 |
|
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: 262.88 E-value: 4.26e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1714390871 410 LKNLDKRLKSKVIGQDEAVEMVAKAIRRNRAGFSEGDQPIGSFLFVGPTGVGKTELAKQLALDMFGNKNAIIRLDMSEYA 489
Cdd:cd19499 2 LLNLEERLHERVVGQDEAVKAVSDAIRRARAGLSDPNRPIGSFLFLGPTGVGKTELAKALAELLFGDEDNLIRIDMSEYM 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1714390871 490 DRTAVSKLIGTSAGYVGYEDNAnTLTERVRRNPYSIVLLDEIEKADPQVLTLLLQVMDDGRLTDGQGNVINFKNTIIIAT 569
Cdd:cd19499 82 EKHSVSRLIGAPPGYVGYTEGG-QLTEAVRRKPYSVVLLDEIEKAHPDVQNLLLQVLDDGRLTDSHGRTVDFKNTIIIMT 160
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1714390871 570 SNagfgnealsgdkqrdqslmdklapFFRPEFLNRFNGIVEF 611
Cdd:cd19499 161 SN------------------------HFRPEFLNRIDEIVVF 178
|
|
| AAA_2 |
pfam07724 |
AAA domain (Cdc48 subfamily); This Pfam entry includes some of the AAA proteins not detected ... |
448-605 |
4.79e-68 |
|
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: 220.53 E-value: 4.79e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1714390871 448 PIGSFLFVGPTGVGKTELAKQLALDMFGNKNAIIRLDMSEYADRTAVSKLIGTSAGYVGYEDNAnTLTERVRRNPYSIVL 527
Cdd:pfam07724 2 PIGSFLFLGPTGVGKTELAKALAELLFGDERALIRIDMSEYMEEHSVSRLIGAPPGYVGYEEGG-QLTEAVRRKPYSIVL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1714390871 528 LDEIEKADPQVLTLLLQVMDDGRLTDGQGNVINFKNTIIIATSNagFGNEALSGDKQRDQS---------LMDKLAPFFR 598
Cdd:pfam07724 81 IDEIEKAHPGVQNDLLQILEGGTLTDKQGRTVDFKNTLFIMTGN--FGSEKISDASRLGDSpdyellkeeVMDLLKKGFI 158
|
....*..
gi 1714390871 599 PEFLNRF 605
Cdd:pfam07724 159 PEFLGRL 165
|
|
| AAA_lid_9 |
pfam17871 |
AAA lid domain; This entry represents the alpha helical AAA+ lid domain that is found to the ... |
263-362 |
1.84e-32 |
|
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: 121.05 E-value: 1.84e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1714390871 263 TAADTLRILQGVKKLYEKHHHVVLPDDVLKAAVDYSIQYIPQRTLPDKAIDLIDMTAAHLAAKNSQT--DVETLDQRVKK 340
Cdd:pfam17871 1 SVEEAIEILRGLKPKYEKHHGVRISDEALEAAVKLSKRYITDRFLPDKAIDLLDEACARVRLSQESKpeELEDLERELAK 80
|
90 100
....*....|....*....|..
gi 1714390871 341 LEAAKEAAVKSEDFTKAADIKK 362
Cdd:pfam17871 81 LEIEKEALEREQDFEKAERLAK 102
|
|
| ClpB_D2-small |
smart01086 |
C-terminal, D2-small domain, of ClpB protein; This is the C-terminal domain of ClpB protein, ... |
614-701 |
5.65e-25 |
|
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: 99.06 E-value: 5.65e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1714390871 614 LTKQDLSQIVDLMLADVQKTLAKKSIKLEVTKAAKDWLMEQGYDEAMGARPLRRVIEQQIRDKVTDFYL--DHLDVKNLK 691
Cdd:smart01086 1 LDKEDLVRIVDLPLNALQKRLAEKGITLEFTDEALDWLAEKGYDPKYGARPLRRIIQRELEDPLAELILsgELKDGDTVV 80
|
90
....*....|
gi 1714390871 692 ADLVDGEIVI 701
Cdd:smart01086 81 VDVDDGELVF 90
|
|
| ClpB_D2-small |
pfam10431 |
C-terminal, D2-small domain, of ClpB protein; This is the C-terminal domain of ClpB protein, ... |
614-701 |
9.84e-25 |
|
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: 98.25 E-value: 9.84e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1714390871 614 LTKQDLSQIVDLMLADVQKTLAKKSIKLEVTKAAKDWLMEQGYDEAMGARPLRRVIEQQIRDKVTDFYLDHldvknlkaD 693
Cdd:pfam10431 1 LSKEELRKIVDLQLKELQKRLAERGITLELTDAAKDWLAEKGYDPEYGARPLRRAIQREIEDPLAEEILSG--------E 72
|
....*...
gi 1714390871 694 LVDGEIVI 701
Cdd:pfam10431 73 LKEGDTVR 80
|
|
| AAA |
cd00009 |
The AAA+ (ATPases Associated with a wide variety of cellular Activities) superfamily ... |
422-612 |
7.46e-18 |
|
The AAA+ (ATPases Associated with a wide variety of cellular Activities) superfamily represents an ancient group of ATPases belonging to the ASCE (for additional strand, catalytic E) division of the P-loop NTPase fold. The ASCE division also includes ABC, RecA-like, VirD4-like, PilT-like, and SF1/2 helicases. Members of the AAA+ ATPases function as molecular chaperons, ATPase subunits of proteases, helicases, or nucleic-acid stimulated ATPases. The AAA+ proteins contain several distinct features in addition to the conserved alpha-beta-alpha core domain structure and the Walker A and B motifs of the P-loop NTPases.
Pssm-ID: 99707 [Multi-domain] Cd Length: 151 Bit Score: 81.04 E-value: 7.46e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1714390871 422 IGQDEAVEMVAKAIRRNragfsegdqPIGSFLFVGPTGVGKTELAKQLALDMFGNKNAIIRLDMSEYADRTAVSKLIGTS 501
Cdd:cd00009 1 VGQEEAIEALREALELP---------PPKNLLLYGPPGTGKTTLARAIANELFRPGAPFLYLNASDLLEGLVVAELFGHF 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1714390871 502 AGYVgyednantLTERVRRNPYSIVLLDEIEKADPQVLTLLLQVMDDGRLTdgqgnVINFKNTIIIATSNagfgnealsg 581
Cdd:cd00009 72 LVRL--------LFELAEKAKPGVLFIDEIDSLSRGAQNALLRVLETLNDL-----RIDRENVRVIGATN---------- 128
|
170 180 190
....*....|....*....|....*....|.
gi 1714390871 582 dkqrdqslmDKLAPFFRPEFLNRFNGIVEFS 612
Cdd:cd00009 129 ---------RPLLGDLDRALYDRLDIRIVIP 150
|
|
| AAA |
cd00009 |
The AAA+ (ATPases Associated with a wide variety of cellular Activities) superfamily ... |
100-258 |
7.44e-17 |
|
The AAA+ (ATPases Associated with a wide variety of cellular Activities) superfamily represents an ancient group of ATPases belonging to the ASCE (for additional strand, catalytic E) division of the P-loop NTPase fold. The ASCE division also includes ABC, RecA-like, VirD4-like, PilT-like, and SF1/2 helicases. Members of the AAA+ ATPases function as molecular chaperons, ATPase subunits of proteases, helicases, or nucleic-acid stimulated ATPases. The AAA+ proteins contain several distinct features in addition to the conserved alpha-beta-alpha core domain structure and the Walker A and B motifs of the P-loop NTPases.
Pssm-ID: 99707 [Multi-domain] Cd Length: 151 Bit Score: 77.96 E-value: 7.44e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1714390871 100 IGRENEIQETAEILSRRTKNNPILVGDAGVGKTAVVEGLAQAIVAGKVPetiqdkeIYSIDLSSLEAGTQYRGSFEENIK 179
Cdd:cd00009 1 VGQEEAIEALREALELPPPKNLLLYGPPGTGKTTLARAIANELFRPGAP-------FLYLNASDLLEGLVVAELFGHFLV 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1714390871 180 QLVKE-VKAAGNIILFFDEIHQIigtgatgGEDGGKGLADIIKPAL----SRGELTVIGATTQDEYrntILKNAALARRF 254
Cdd:cd00009 74 RLLFElAEKAKPGVLFIDEIDSL-------SRGAQNALLRVLETLNdlriDRENVRVIGATNRPLL---GDLDRALYDRL 143
|
....
gi 1714390871 255 NDVV 258
Cdd:cd00009 144 DIRI 147
|
|
| AAA |
pfam00004 |
ATPase family associated with various cellular activities (AAA); AAA family proteins often ... |
122-262 |
5.31e-13 |
|
ATPase family associated with various cellular activities (AAA); AAA family proteins often perform chaperone-like functions that assist in the assembly, operation, or disassembly of protein complexes.
Pssm-ID: 459627 [Multi-domain] Cd Length: 130 Bit Score: 66.46 E-value: 5.31e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1714390871 122 ILVGDAGVGKTAVVEGLAQAIvagkvpetiqDKEIYSIDLSSLEAgtQYRGSFEENIKQLVKEVKAAGNIILFFDEIHQI 201
Cdd:pfam00004 2 LLYGPPGTGKTTLAKAVAKEL----------GAPFIEISGSELVS--KYVGESEKRLRELFEAAKKLAPCVIFIDEIDAL 69
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1714390871 202 IGTGATGGEDGGKGLADIIKPAL-----SRGELTVIGATtqdeyrNTILK-NAALARRFnDVVINEP 262
Cdd:pfam00004 70 AGSRGSGGDSESRRVVNQLLTELdgftsSNSKVIVIAAT------NRPDKlDPALLGRF-DRIIEFP 129
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
453-571 |
6.44e-13 |
|
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a variety of cellular activities. This profile/alignment only detects a fraction of this vast family. The poorly conserved N-terminal helix is missing from the alignment.
Pssm-ID: 214640 [Multi-domain] Cd Length: 148 Bit Score: 66.63 E-value: 6.44e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1714390871 453 LFVGPTGVGKTELAKQLALDMFGNKNAIIRLDMSEYADRTAVSKLIGTSAGYVGY---EDNANTLTERVRRNPYSIVLLD 529
Cdd:smart00382 6 LIVGPPGSGKTTLARALARELGPPGGGVIYIDGEDILEEVLDQLLLIIVGGKKASgsgELRLRLALALARKLKPDVLILD 85
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 1714390871 530 EIEKADPQVLTLLLQVMDDGRLTDgqgNVINFKNTIIIATSN 571
Cdd:smart00382 86 EITSLLDAEQEALLLLLEELRLLL---LLKSEKNLTVILTTN 124
|
|
| SpoVK |
COG0464 |
AAA+-type ATPase, SpoVK/Ycf46/Vps4 family [Cell wall/membrane/envelope biogenesis, Cell cycle ... |
89-272 |
1.33e-11 |
|
AAA+-type ATPase, SpoVK/Ycf46/Vps4 family [Cell wall/membrane/envelope biogenesis, Cell cycle control, cell division, chromosome partitioning, Signal transduction mechanisms];
Pssm-ID: 440232 [Multi-domain] Cd Length: 397 Bit Score: 66.86 E-value: 1.33e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1714390871 89 EQARDGLLDPVIGREN---EIQETAEILSRRTK-------NNP---ILVGDAGVGKTAVVEGLAQAIvagkvpetiqDKE 155
Cdd:COG0464 149 LELREAILDDLGGLEEvkeELRELVALPLKRPElreeyglPPPrglLLYGPPGTGKTLLARALAGEL----------GLP 218
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1714390871 156 IYSIDLSSLEAgtQYRGSFEENIKQLVKEVKAAGNIILFFDEIHQIIGTGATGGEDGGKGLADIIKPAL--SRGELTVIG 233
Cdd:COG0464 219 LIEVDLSDLVS--KYVGETEKNLREVFDKARGLAPCVLFIDEADALAGKRGEVGDGVGRRVVNTLLTEMeeLRSDVVVIA 296
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1714390871 234 ATtqdeYRNTILkNAALARRFNDVV-INEPTAADTLRILQ 272
Cdd:COG0464 297 AT----NRPDLL-DPALLRRFDEIIfFPLPDAEERLEIFR 331
|
|
| RPT1 |
COG1222 |
ATP-dependent 26S proteasome regulatory subunit [Posttranslational modification, protein ... |
419-648 |
1.87e-10 |
|
ATP-dependent 26S proteasome regulatory subunit [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440835 [Multi-domain] Cd Length: 326 Bit Score: 62.72 E-value: 1.87e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1714390871 419 SKVIGQDEAVEMVAKAI---RRNRAGFSE-GDQPIGSFLFVGPTGVGKTELAKQLAldmfGNKNA-IIRLDMSEYadrta 493
Cdd:COG1222 78 DDIGGLDEQIEEIREAVelpLKNPELFRKyGIEPPKGVLLYGPPGTGKTLLAKAVA----GELGApFIRVRGSEL----- 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1714390871 494 VSKLIGTSagyvgyEDNANTLTERVRRNPYSIVLLDEIE------------KADPQVLTLLLQVMDDgrlTDGQGNVinf 561
Cdd:COG1222 149 VSKYIGEG------ARNVREVFELAREKAPSIIFIDEIDaiaarrtddgtsGEVQRTVNQLLAELDG---FESRGDV--- 216
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1714390871 562 kntIIIATSNAgfgnealsgdkqrdqslMDKLAP-FFRPeflNRFNGIVEFSHLTKQDLSQIVDLMLADVQ-------KT 633
Cdd:COG1222 217 ---LIIAATNR-----------------PDLLDPaLLRP---GRFDRVIEVPLPDEEAREEILKIHLRDMPladdvdlDK 273
|
250 260
....*....|....*....|..
gi 1714390871 634 LAKKS-------IKLEVTKAAK 648
Cdd:COG1222 274 LAKLTegfsgadLKAIVTEAGM 295
|
|
| AAA_5 |
pfam07728 |
AAA domain (dynein-related subfamily); This Pfam entry includes some of the AAA proteins not ... |
451-571 |
2.32e-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: 58.84 E-value: 2.32e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1714390871 451 SFLFVGPTGVGKTELAKQLAlDMFGNKNAIIRLdMSEYadrTAVSKLIG---TSAGYVGYEDNAntLTERVRRNpySIVL 527
Cdd:pfam07728 1 GVLLVGPPGTGKTELAERLA-AALSNRPVFYVQ-LTRD---TTEEDLFGrrnIDPGGASWVDGP--LVRAAREG--EIAV 71
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 1714390871 528 LDEIEKADPQVLTLLLQVMDDGRLT--DGqGNVINFKNT--IIIATSN 571
Cdd:pfam07728 72 LDEINRANPDVLNSLLSLLDERRLLlpDG-GELVKAAPDgfRLIATMN 118
|
|
| MoxR |
COG0714 |
MoxR-like ATPase [General function prediction only]; MoxR-like ATPase is part of the Pathway ... |
413-571 |
4.35e-10 |
|
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: 61.34 E-value: 4.35e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1714390871 413 LDKRLKSKVIGQDEAVEMVAKAIrrnragFSEGdqPIgsfLFVGPTGVGKTELAKQLAldmfgnknAIIRLDMSE---YA 489
Cdd:COG0714 6 LRAEIGKVYVGQEELIELVLIAL------LAGG--HL---LLEGVPGVGKTTLAKALA--------RALGLPFIRiqfTP 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1714390871 490 DRTAvSKLIGTSAgyvgYedNANTLTERVRRNPY--SIVLLDEIEKADPQVLTLLLQVMDDGRLT-DGQgnvinfknT-- 564
Cdd:COG0714 67 DLLP-SDILGTYI----Y--DQQTGEFEFRPGPLfaNVLLADEINRAPPKTQSALLEAMEERQVTiPGG--------Tyk 131
|
170
....*....|..
gi 1714390871 565 -----IIIATSN 571
Cdd:COG0714 132 lpepfLVIATQN 143
|
|
| RecA-like_protease |
cd19481 |
proteases similar to RecA; RecA-like NTPases. This family includes the NTP binding domain of ... |
426-571 |
9.51e-10 |
|
proteases similar to RecA; RecA-like NTPases. This family includes the NTP binding domain of F1 and V1 H(+)ATPases, DnaB and related helicases as well as bacterial RecA and related eukaryotic and archaeal recombinases. This group also includes bacterial conjugation proteins and related DNA transfer proteins involved in type II and type IV secretion.
Pssm-ID: 410889 [Multi-domain] Cd Length: 158 Bit Score: 57.68 E-value: 9.51e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1714390871 426 EAVEMVAKAIRRNRAGFSEGDQPIGSFLFVGPTGVGKTELAKQLA----LDMfgnknaiIRLDMSEYADRtavskligts 501
Cdd:cd19481 3 ASLREAVEAPRRGSRLRRYGLGLPKGILLYGPPGTGKTLLAKALAgelgLPL-------IVVKLSSLLSK---------- 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1714390871 502 agYVGY-EDNANTLTERVRRNPYSIVLLDEIEKADP------------QVLTLLLQVMDDGRLTDgqgnvinfkNTIIIA 568
Cdd:cd19481 66 --YVGEsEKNLRKIFERARRLAPCILFIDEIDAIGRkrdssgesgelrRVLNQLLTELDGVNSRS---------KVLVIA 134
|
...
gi 1714390871 569 TSN 571
Cdd:cd19481 135 ATN 137
|
|
| SpoVK |
COG0464 |
AAA+-type ATPase, SpoVK/Ycf46/Vps4 family [Cell wall/membrane/envelope biogenesis, Cell cycle ... |
302-631 |
2.29e-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: 59.92 E-value: 2.29e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1714390871 302 IPQRTLPDKAIDLIDMTAAHLAAKNSQTDVETLDQRVKKLEAAKEAAVKSEDFTKAADIKKSIEETKQKIKKTDQKEKIT 381
Cdd:COG0464 41 LLLLLLLLLALLLVELLLLLLSGALAALLLLALLLLALLALLAALLSALELLLLGELLLLLLLLLLLLLLLLDLERALLE 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1714390871 382 ATIDDVAQSVERLTGIPVADMGANDIEHLKNLDKRLKSkVIGQDE---AVEMVAKAIRRNRAGFSE-GDQPIGSFLFVGP 457
Cdd:COG0464 121 LLRESAEALALAAPLVTYEDIGGLEEELLELREAILDD-LGGLEEvkeELRELVALPLKRPELREEyGLPPPRGLLLYGP 199
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1714390871 458 TGVGKTELAKQLALDMFGNknaIIRLDMSEYadrtaVSKLIGTSAgyvgyednANT--LTERVRRNPYSIVLLDEIEK-- 533
Cdd:COG0464 200 PGTGKTLLARALAGELGLP---LIEVDLSDL-----VSKYVGETE--------KNLreVFDKARGLAPCVLFIDEADAla 263
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1714390871 534 ------ADP---QVLTLLLQVMDDGRltdgqgnvinfKNTIIIATSNagfgnealsgdkqrDQSLMDklapffrPEFLNR 604
Cdd:COG0464 264 gkrgevGDGvgrRVVNTLLTEMEELR-----------SDVVVIAATN--------------RPDLLD-------PALLRR 311
|
330 340
....*....|....*....|....*..
gi 1714390871 605 FNGIVEFSHLTKQDLSQIVDLMLADVQ 631
Cdd:COG0464 312 FDEIIFFPLPDAEERLEIFRIHLRKRP 338
|
|
| COG1223 |
COG1223 |
Predicted ATPase, AAA+ superfamily [General function prediction only]; |
419-683 |
3.82e-08 |
|
Predicted ATPase, AAA+ superfamily [General function prediction only];
Pssm-ID: 440836 [Multi-domain] Cd Length: 246 Bit Score: 54.89 E-value: 3.82e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1714390871 419 SKVIGQDEAVEMVAKAIR-----RNRAGFseGDQPIGSFLFVGPTGVGKTELAKQLA----LDMFgnknaIIRLDmseya 489
Cdd:COG1223 2 DDVVGQEEAKKKLKLIIKelrrrENLRKF--GLWPPRKILFYGPPGTGKTMLAEALAgelkLPLL-----TVRLD----- 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1714390871 490 drTAVSKLIGTSAGyvgyedNANTLTERVRRNPySIVLLDEI-----EKADPQ-------VLTLLLQVMDDGRltdgqgn 557
Cdd:COG1223 70 --SLIGSYLGETAR------NLRKLFDFARRAP-CVIFFDEFdaiakDRGDQNdvgevkrVVNALLQELDGLP------- 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1714390871 558 vinfKNTIIIATSNAgfgNEALsgdkqrDQSLmdklapffrpefLNRFNGIVEFSHLTKQDLSQIVDLMLADVqktlaKK 637
Cdd:COG1223 134 ----SGSVVIAATNH---PELL------DSAL------------WRRFDEVIEFPLPDKEERKEILELNLKKF-----PL 183
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 1714390871 638 SIKLEVTKAAKdwlMEQGYDEAMGARPLRRVIEQQI---RDKVTDFYLD 683
Cdd:COG1223 184 PFELDLKKLAK---KLEGLSGADIEKVLKTALKKAIledREKVTKEDLE 229
|
|
| AAA |
pfam00004 |
ATPase family associated with various cellular activities (AAA); AAA family proteins often ... |
453-612 |
4.88e-08 |
|
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: 52.21 E-value: 4.88e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1714390871 453 LFVGPTGVGKTELAKQLALDMFGNknaIIRLDMSEyadrtAVSKLIGTSAGYVgyednaNTLTERVRRNPYSIVLLDEIE 532
Cdd:pfam00004 2 LLYGPPGTGKTTLAKAVAKELGAP---FIEISGSE-----LVSKYVGESEKRL------RELFEAAKKLAPCVIFIDEID 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1714390871 533 K-----------ADPQVLTLLLQVMDDGRltdgqgnvINFKNTIIIATSNagfgnealsgdkqrdqsLMDKLapffRPEF 601
Cdd:pfam00004 68 AlagsrgsggdsESRRVVNQLLTELDGFT--------SSNSKVIVIAATN-----------------RPDKL----DPAL 118
|
170
....*....|.
gi 1714390871 602 LNRFNGIVEFS 612
Cdd:pfam00004 119 LGRFDRIIEFP 129
|
|
| RecA-like_ClpX |
cd19497 |
ATP-dependent Clp protease ATP-binding subunit ClpX; ClpX is a component of the ATP-dependent ... |
411-533 |
3.65e-07 |
|
ATP-dependent Clp protease ATP-binding subunit ClpX; ClpX is a component of the ATP-dependent protease ClpXP. In ClpXP, ClpX ATPase serves to specifically recognize, unfold, and translocate protein substrates into the chamber of ClpP protease for degradation. This RecA-like_ClpX domain subfamily belongs to the RecA-like NTPase family which includes the NTP binding domain of F1 and V1 H(+)ATPases, DnaB and related helicases as well as bacterial RecA and related eukaryotic and archaeal recombinases. The RecA-like NTPase family also includes bacterial conjugation proteins and related DNA transfer proteins involved in type II and type IV secretion.
Pssm-ID: 410905 [Multi-domain] Cd Length: 251 Bit Score: 51.83 E-value: 3.65e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1714390871 411 KNLDKRLKSKVIGQDEAVEMVAKAI----RRNRAGFSEGDQPI----GSFLFVGPTGVGKTELAKQLA--LDM-FgnknA 479
Cdd:cd19497 4 KEIKEHLDKYVIGQERAKKVLSVAVynhyKRIRNNLKQKDDDVelekSNILLIGPTGSGKTLLAQTLAkiLDVpF----A 79
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1714390871 480 IirldmseyADRTAVskligTSAGYVGyEDNANTLTE-------RVRRNPYSIVLLDEIEK 533
Cdd:cd19497 80 I--------ADATTL-----TEAGYVG-EDVENILLKllqaadyDVERAQRGIVYIDEIDK 126
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
117-262 |
6.38e-07 |
|
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a variety of cellular activities. This profile/alignment only detects a fraction of this vast family. The poorly conserved N-terminal helix is missing from the alignment.
Pssm-ID: 214640 [Multi-domain] Cd Length: 148 Bit Score: 49.29 E-value: 6.38e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1714390871 117 TKNNPILVGDAGVGKTAVVEGLAQAIVAGKVPETIQDKEIYSIDLSS-----LEAGTQYRGSFEENIKQLVKEVKAAGNI 191
Cdd:smart00382 1 PGEVILIVGPPGSGKTTLARALARELGPPGGGVIYIDGEDILEEVLDqllliIVGGKKASGSGELRLRLALALARKLKPD 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1714390871 192 ILFFDEIHQIIGTGATGGEDGGKGLAdIIKPALSRGELTVIGATTqdeyRNTILKNAALARRFNDVVINEP 262
Cdd:smart00382 81 VLILDEITSLLDAEQEALLLLLEELR-LLLLLKSEKNLTVILTTN----DEKDLGPALLRRRFDRRIVLLL 146
|
|
| CDC48 |
TIGR01243 |
AAA family ATPase, CDC48 subfamily; This subfamily of the AAA family ATPases includes two ... |
122-571 |
6.38e-07 |
|
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: 52.99 E-value: 6.38e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1714390871 122 ILVGDAGVGKTAVVEGLAQAIVAgkvpetiqdkeiYSIDLSSLEAGTQYRGSFEENIKQLVKEVKAAGNIILFFDEIHQI 201
Cdd:TIGR01243 216 LLYGPPGTGKTLLAKAVANEAGA------------YFISINGPEIMSKYYGESEERLREIFKEAEENAPSIIFIDEIDAI 283
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1714390871 202 igtGATGGEDGGKGLADIIKPALS-------RGELTVIGATTQDEYRNTILKNAAlarRFN-DVVINEPTAADTLRILQg 273
Cdd:TIGR01243 284 ---APKREEVTGEVEKRVVAQLLTlmdglkgRGRVIVIGATNRPDALDPALRRPG---RFDrEIVIRVPDKRARKEILK- 356
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1714390871 274 vkklyekhhhvvlpddvlkaavdysiqyIPQRTLP---DKAID-LIDMTAAHLAAknsqtDVETLdqrvkkleaAKEAAV 349
Cdd:TIGR01243 357 ----------------------------VHTRNMPlaeDVDLDkLAEVTHGFVGA-----DLAAL---------AKEAAM 394
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1714390871 350 KS-EDFTKAADIKKSIEETKQ------KIKKTDQKEkitaTIDDVAQSVERLTGIPVADMGANDIEHLKNLDKRLKskvi 422
Cdd:TIGR01243 395 AAlRRFIREGKINFEAEEIPAevlkelKVTMKDFME----ALKMVEPSAIREVLVEVPNVRWSDIGGLEEVKQELR---- 466
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1714390871 423 gqdEAVEMVAKAirrnRAGFSE-GDQPIGSFLFVGPTGVGKTELAKQLALDMFGNKNAIIRLDMseyadrtaVSKLIGTS 501
Cdd:TIGR01243 467 ---EAVEWPLKH----PEIFEKmGIRPPKGVLLFGPPGTGKTLLAKAVATESGANFIAVRGPEI--------LSKWVGES 531
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1714390871 502 agyvgyEDNANTLTERVRRNPYSIVLLDEIEKADPQVLTLLLQVMDD----GRLTDGQGNVINfKNTIIIATSN 571
Cdd:TIGR01243 532 ------EKAIREIFRKARQAAPAIIFFDEIDAIAPARGARFDTSVTDrivnQLLTEMDGIQEL-SNVVVIAATN 598
|
|
| RecA-like_HslU |
cd19498 |
ATP-dependent protease ATPase subunit HslU; HslU is a component of the ATP-dependent protease ... |
416-533 |
1.15e-06 |
|
ATP-dependent protease ATPase subunit HslU; HslU is a component of the ATP-dependent protease HslVU. In HslVU, HslU ATPase serves to unfold and translocate protein substrate, and the HslV protease degrades the unfolded proteins. This RecA-like_HslU subfamily belongs to the RecA-like NTPase family which includes the NTP binding domain of F1 and V1 H(+)ATPases, DnaB and related helicases as well as bacterial RecA and related eukaryotic and archaeal recombinases. The RecA-like NTPase family also includes bacterial conjugation proteins and related DNA transfer proteins involved in type II and type IV secretion.
Pssm-ID: 410906 [Multi-domain] Cd Length: 183 Bit Score: 49.30 E-value: 1.15e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1714390871 416 RLKSKVIGQDEAVEMVAKAIRrNRAGFSEGDQPI------GSFLFVGPTGVGKTELAKQLALDMfgnKNAIIRLDMSEYa 489
Cdd:cd19498 8 ELDKYIIGQDEAKRAVAIALR-NRWRRMQLPEELrdevtpKNILMIGPTGVGKTEIARRLAKLA---GAPFIKVEATKF- 82
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 1714390871 490 drtavskligTSAGYVGYEdnantlTERVRRNPYS-IVLLDEIEK 533
Cdd:cd19498 83 ----------TEVGYVGRD------VESIIRDLVEgIVFIDEIDK 111
|
|
| RecA-like_protease |
cd19481 |
proteases similar to RecA; RecA-like NTPases. This family includes the NTP binding domain of ... |
122-260 |
4.06e-06 |
|
proteases similar to RecA; RecA-like NTPases. This family includes the NTP binding domain of F1 and V1 H(+)ATPases, DnaB and related helicases as well as bacterial RecA and related eukaryotic and archaeal recombinases. This group also includes bacterial conjugation proteins and related DNA transfer proteins involved in type II and type IV secretion.
Pssm-ID: 410889 [Multi-domain] Cd Length: 158 Bit Score: 47.28 E-value: 4.06e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1714390871 122 ILVGDAGVGKTAVVEGLAQAIVAgkvpetiqdkEIYSIDLSSLEagTQYRGSFEENIKQLVKEVKAAGNIILFFDEIHQI 201
Cdd:cd19481 30 LLYGPPGTGKTLLAKALAGELGL----------PLIVVKLSSLL--SKYVGESEKNLRKIFERARRLAPCILFIDEIDAI 97
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1714390871 202 IGTGATGGEDGGKGLADI-----IKPALSRGELTVIGATTqdeYRNTILKnaALAR--RFnDVVIN 260
Cdd:cd19481 98 GRKRDSSGESGELRRVLNqllteLDGVNSRSKVLVIAATN---RPDLLDP--ALLRpgRF-DEVIE 157
|
|
| DnaX |
COG2812 |
DNA polymerase III, gamma/tau subunits [Replication, recombination and repair]; |
419-470 |
5.95e-06 |
|
DNA polymerase III, gamma/tau subunits [Replication, recombination and repair];
Pssm-ID: 442061 [Multi-domain] Cd Length: 340 Bit Score: 49.03 E-value: 5.95e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 1714390871 419 SKVIGQDEAVEMVAKAIRRNRagfsegdqpIG-SFLFVGPTGVGKTELAKQLA 470
Cdd:COG2812 10 DDVVGQEHVVRTLKNALASGR---------LAhAYLFTGPRGVGKTTLARILA 53
|
|
| clpX |
PRK05342 |
ATP-dependent Clp protease ATP-binding subunit ClpX; |
421-675 |
7.15e-06 |
|
ATP-dependent Clp protease ATP-binding subunit ClpX;
Pssm-ID: 235422 [Multi-domain] Cd Length: 412 Bit Score: 49.00 E-value: 7.15e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1714390871 421 VIGQDEAVEMVAKAI-----RRNRAGFSEGDQPIG--SFLFVGPTGVGKTELAKQLA--LDM-FgnknAIirldmseyAD 490
Cdd:PRK05342 73 VIGQERAKKVLSVAVynhykRLRHGDKKDDDVELQksNILLIGPTGSGKTLLAQTLAriLDVpF----AI--------AD 140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1714390871 491 RTAVskligTSAGYVGyEDNANTLT----------ERVRRnpySIVLLDEIEK-----ADPQ---------VLTLLLQVM 546
Cdd:PRK05342 141 ATTL-----TEAGYVG-EDVENILLkllqaadydvEKAQR---GIVYIDEIDKiarksENPSitrdvsgegVQQALLKIL 211
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1714390871 547 D---------DGRLTDGQGNV-INFKN-------------TII---IATSNAGFGNEALSG-DKQRDQSLMDKLAP---- 595
Cdd:PRK05342 212 EgtvasvppqGGRKHPQQEFIqVDTTNilficggafdgleKIIkqrLGKKGIGFGAEVKSKkEKRTEGELLKQVEPedli 291
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1714390871 596 -F-FRPEFLNRFNGIVEFSHLTKQDLSQIV----DLMLADVQKTLAKKSIKLEVTKAAKDWLMEQGYDEAMGARPLRRVI 669
Cdd:PRK05342 292 kFgLIPEFIGRLPVVATLEELDEEALVRILtepkNALVKQYQKLFEMDGVELEFTDEALEAIAKKAIERKTGARGLRSIL 371
|
....*.
gi 1714390871 670 EQQIRD 675
Cdd:PRK05342 372 EEILLD 377
|
|
| ClpX |
COG1219 |
ATP-dependent protease Clp, ATPase subunit ClpX [Posttranslational modification, protein ... |
421-675 |
1.87e-05 |
|
ATP-dependent protease Clp, ATPase subunit ClpX [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440832 [Multi-domain] Cd Length: 409 Bit Score: 47.74 E-value: 1.87e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1714390871 421 VIGQDEAVEMVAKAI-----RRNRAGFSEGDQPIG--SFLFVGPTGVGKTELAKQLA--LDM-FgnknAIirldmseyAD 490
Cdd:COG1219 74 VIGQERAKKVLSVAVynhykRLNSGSKDDDDVELEksNILLIGPTGSGKTLLAQTLAriLDVpF----AI--------AD 141
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1714390871 491 RTAVskligTSAGYVGyEDNANTLT----------ERVRRnpySIVLLDEIEK-----ADP------------QVLTLLL 543
Cdd:COG1219 142 ATTL-----TEAGYVG-EDVENILLkllqaadydvEKAER---GIIYIDEIDKiarksENPsitrdvsgegvqQALLKIL 212
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1714390871 544 qvmddgrltdgQGNVINF------KN----TIIIATSN-------A-----------------GFGNEALSGDKQRDQSL 589
Cdd:COG1219 213 -----------EGTVANVppqggrKHpqqeFIQIDTTNilficggAfdglekiierrlgkksiGFGAEVKSKKEKDEGEL 281
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1714390871 590 MDKLAP-----F-FRPEFLNRFNGIVEFSHLTKQDLSQIvdlmL-----ADV---QKTLAKKSIKLEVTKAAKDWLMEQG 655
Cdd:COG1219 282 LKQVEPedlikFgLIPEFIGRLPVIATLEELDEEALVRI----LtepknALVkqyQKLFEMDGVELEFTDEALEAIAKKA 357
|
330 340
....*....|....*....|
gi 1714390871 656 YDEAMGARPLRRVIEQQIRD 675
Cdd:COG1219 358 IERKTGARGLRSILEEILLD 377
|
|
| AAA_16 |
pfam13191 |
AAA ATPase domain; This family of domains contain a P-loop motif that is characteriztic of the ... |
98-144 |
1.47e-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: 42.88 E-value: 1.47e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 1714390871 98 PVIGRENEIQETAEILSRRTKNNP---ILVGDAGVGKTAVVEGLAQAIVA 144
Cdd:pfam13191 1 RLVGREEELEQLLDALDRVRSGRPpsvLLTGEAGTGKTTLLRELLRALER 50
|
|
| PRK13342 |
PRK13342 |
recombination factor protein RarA; Reviewed |
122-298 |
1.64e-04 |
|
recombination factor protein RarA; Reviewed
Pssm-ID: 237355 [Multi-domain] Cd Length: 413 Bit Score: 44.69 E-value: 1.64e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1714390871 122 ILVGDAGVGKTAvvegLAQAIvAGKVpetiqDKEIYSidLSSLEAGtqyrgsfeenIKQLVKEVKAA-------GNIILF 194
Cdd:PRK13342 40 ILWGPPGTGKTT----LARII-AGAT-----DAPFEA--LSAVTSG----------VKDLREVIEEArqrrsagRRTILF 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1714390871 195 FDEIH------QiigtgatggedggkglaDIIKPALSRGELTVIGATTQdeyrN---TIlkNAALARRFNDVVINEPTAA 265
Cdd:PRK13342 98 IDEIHrfnkaqQ-----------------DALLPHVEDGTITLIGATTE----NpsfEV--NPALLSRAQVFELKPLSEE 154
|
170 180 190
....*....|....*....|....*....|...
gi 1714390871 266 DTLRILQGVKKLYEKhHHVVLPDDVLKAAVDYS 298
Cdd:PRK13342 155 DIEQLLKRALEDKER-GLVELDDEALDALARLA 186
|
|
| RPT1 |
COG1222 |
ATP-dependent 26S proteasome regulatory subunit [Posttranslational modification, protein ... |
122-373 |
2.56e-04 |
|
ATP-dependent 26S proteasome regulatory subunit [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440835 [Multi-domain] Cd Length: 326 Bit Score: 43.84 E-value: 2.56e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1714390871 122 ILVGDAGVGKTAvvegLAQAiVAGKVpetiqDKEIYSIDLSSLeagTQ-YRGSFEENIKQLVKEVKAAGNIILFFDEIHQ 200
Cdd:COG1222 116 LLYGPPGTGKTL----LAKA-VAGEL-----GAPFIRVRGSEL---VSkYIGEGARNVREVFELAREKAPSIIFIDEIDA 182
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1714390871 201 IigtGATGGEDGGKGLADIIKPAL--------SRGELTVIGATTqdeyRNTILkNAALAR--RFNDVV-INEPTAADTLR 269
Cdd:COG1222 183 I---AARRTDDGTSGEVQRTVNQLlaeldgfeSRGDVLIIAATN----RPDLL-DPALLRpgRFDRVIeVPLPDEEAREE 254
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1714390871 270 ILqgvkklyeKHHhvvLPDDVLKAAVDYSiqyipqrtlpdkaiDLIDMTAAHLAAknsqtDVETLDQrvkklEAAKEAAV 349
Cdd:COG1222 255 IL--------KIH---LRDMPLADDVDLD--------------KLAKLTEGFSGA-----DLKAIVT-----EAGMFAIR 299
|
250 260
....*....|....*....|....
gi 1714390871 350 KSEDFTKAADIKKSIEETKQKIKK 373
Cdd:COG1222 300 EGRDTVTMEDLEKAIEKVKKKTET 323
|
|
| COG2842 |
COG2842 |
Bacteriophage DNA transposition protein, AAA+ family ATPase [Mobilome: prophages, transposons]; ... |
453-636 |
3.63e-04 |
|
Bacteriophage DNA transposition protein, AAA+ family ATPase [Mobilome: prophages, transposons];
Pssm-ID: 442090 [Multi-domain] Cd Length: 254 Bit Score: 43.02 E-value: 3.63e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1714390871 453 LFVGPTGVGKTELAKQLALDmfgNKNAI-IRLDMSeYADRTAVSKL---IGTSAGYVGYEDNANTLTERVRRNPYSIVlL 528
Cdd:COG2842 54 VVYGESGVGKTTAAREYANR---NPNVIyVTASPS-WTSKELLEELaeeLGIPAPPGTIADLRDRILERLAGTGRLLI-I 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1714390871 529 DEIEKADPQVLTLLLQVMDdgrltdgqgnvinfkntiiiaTSNAGFgneALSGDKQrdqsLMDKLAPFfrPEFLNRFNGI 608
Cdd:COG2842 129 DEADHLKPKALEELRDIHD---------------------ETGVGV---VLIGMER----LPAKLKRY--EQLYSRIGFW 178
|
170 180 190
....*....|....*....|....*....|..
gi 1714390871 609 VEFSHLTKQDLSQIVDLM----LADVQKTLAK 636
Cdd:COG2842 179 VEFKPLSLEDVRALAEAWgeltDPDLLELLHR 210
|
|
| PRK07399 |
PRK07399 |
DNA polymerase III subunit delta'; Validated |
417-470 |
4.31e-04 |
|
DNA polymerase III subunit delta'; Validated
Pssm-ID: 236011 [Multi-domain] Cd Length: 314 Bit Score: 42.97 E-value: 4.31e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 1714390871 417 LKSKVIGQDEAVEMVAKAIRRNRagFSEGdqpigsFLFVGPTGVGKTELAKQLA 470
Cdd:PRK07399 2 LFANLIGQPLAIELLTAAIKQNR--IAPA------YLFAGPEGVGRKLAALCFI 47
|
|
| RecA-like_NVL_r1-like |
cd19518 |
first of two ATPase domains of NVL (nuclear VCP-like protein) and similar ATPase domains; NVL ... |
425-571 |
5.68e-04 |
|
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: 41.24 E-value: 5.68e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1714390871 425 DEAVEMVAKAIRRNRAGFSEGDQPIGSFLFVGPTGVGKTELAKQLALDMfgnknaiiRLDMSEYADRTAVSKLIGTSagy 504
Cdd:cd19518 10 KELCELLIHPILPPEYFQHLGVEPPRGVLLHGPPGCGKTMLANAIAGEL--------KVPFLKISATEIVSGVSGES--- 78
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1714390871 505 vgyEDNANTLTERVRRNPYSIVLLDEIEKADPQ-----------VLTLLLQVMDDGRLTDGQGnvinfKNTIIIATSN 571
Cdd:cd19518 79 ---EEKIRELFDQAISNAPCIVFIDEIDAITPKresaqremerrIVSQLLTCMDELNNEKTAG-----GPVLVIGATN 148
|
|
| FlhF |
TIGR03499 |
flagellar biosynthetic protein FlhF; [Cellular processes, Chemotaxis and motility] |
293-484 |
6.61e-04 |
|
flagellar biosynthetic protein FlhF; [Cellular processes, Chemotaxis and motility]
Pssm-ID: 274609 [Multi-domain] Cd Length: 282 Bit Score: 42.32 E-value: 6.61e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1714390871 293 AAVDYSIQYIPQRTLPDKAidlidmTAAHLAAKNSQTDVETLDQRVKKLEAAKEAAVKSEDFTKAADIKKSIEETKQKIK 372
Cdd:TIGR03499 48 AAIDEEEAAAASAEEEASK------ALEQADPKPLSATAEPLELPAPQEEPAAPAAQAAEPLLPEEELRKELEALRELLE 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1714390871 373 KtdQKEKITATIDDVAQSV--ERLTgipvaDMGANDiEHLKNLDKRLKSKViGQDEAVEMVAKAIRRNRAGFSEGDQPI- 449
Cdd:TIGR03499 122 R--LLAGLAWLQRPPERAKlyERLL-----EAGVSE-ELARELLEKLPEDA-DAEDAWRWLREALEGMLPVKPEEDPILe 192
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1714390871 450 --GSFLFVGPTGVGKT----ELAKQLALdMFGNKN-AIIRLD 484
Cdd:TIGR03499 193 qgGVIALVGPTGVGKTttlaKLAARFAL-EHGKKKvALITTD 233
|
|
| PRK13341 |
PRK13341 |
AAA family ATPase; |
120-298 |
6.77e-04 |
|
AAA family ATPase;
Pssm-ID: 237354 [Multi-domain] Cd Length: 725 Bit Score: 43.12 E-value: 6.77e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1714390871 120 NPILVGDAGVGKTAvvegLAQaIVAGkvpeTIQDKEIYsidLSSLEAGtqyrgsfeenIKQLVKEVKAAGN--------I 191
Cdd:PRK13341 54 SLILYGPPGVGKTT----LAR-IIAN----HTRAHFSS---LNAVLAG----------VKDLRAEVDRAKErlerhgkrT 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1714390871 192 ILFFDEIHQIigtgatggedgGKGLADIIKPALSRGELTVIGATTQDEYRNTilkNAALARRFNDVVINEPTAADTLRIL 271
Cdd:PRK13341 112 ILFIDEVHRF-----------NKAQQDALLPWVENGTITLIGATTENPYFEV---NKALVSRSRLFRLKSLSDEDLHQLL 177
|
170 180 190
....*....|....*....|....*....|..
gi 1714390871 272 QgvKKLYEKHH-----HVVLPDDVLKAAVDYS 298
Cdd:PRK13341 178 K--RALQDKERgygdrKVDLEPEAEKHLVDVA 207
|
|
| RecA-like_NVL_r1-like |
cd19518 |
first of two ATPase domains of NVL (nuclear VCP-like protein) and similar ATPase domains; NVL ... |
122-254 |
7.89e-04 |
|
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: 40.85 E-value: 7.89e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1714390871 122 ILVGDAGVGKTAvvegLAQAIvAG--KVPetiqdkeIYSIDLSSLEAGTQyrGSFEENIKQLVKEVKAAGNIILFFDEIH 199
Cdd:cd19518 38 LLHGPPGCGKTM----LANAI-AGelKVP-------FLKISATEIVSGVS--GESEEKIRELFDQAISNAPCIVFIDEID 103
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1714390871 200 QIIGTGATGGEDGGK--------GLADIIKPALSRGELTVIGATTQDEYRNTILKNAAlarRF 254
Cdd:cd19518 104 AITPKRESAQREMERrivsqlltCMDELNNEKTAGGPVLVIGATNRPDSLDPALRRAG---RF 163
|
|
| RecA-like_Yta7-like |
cd19517 |
ATPase domain of Saccharomyces cerevisiae Yta7 and similar ATPase domains; Saccharomyces ... |
447-559 |
1.17e-03 |
|
ATPase domain of Saccharomyces cerevisiae Yta7 and similar ATPase domains; Saccharomyces cerevisiae Yta7 is a chromatin-associated AAA-ATPase involved in regulation of chromatin dynamics. Its human ortholog ANCCA/ATAD2 transcriptionally activates pathways of malignancy in a broad range of cancers. The RecA-like_Yta7 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: 410925 [Multi-domain] Cd Length: 170 Bit Score: 40.19 E-value: 1.17e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1714390871 447 QPIGSFLFVGPTGVGKTELAKQLALDMfGNKNAIIRLDMSEYADrtAVSKLIGTSagyvgyEDNANTLTERVRRNPYSIV 526
Cdd:cd19517 32 TPPRGVLFHGPPGTGKTLMARALAAEC-SKGGQKVSFFMRKGAD--CLSKWVGEA------ERQLRLLFEEAYRMQPSII 102
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 1714390871 527 LLDEIEKADP-----------QVLTLLLQVMDDgrlTDGQGNVI 559
Cdd:cd19517 103 FFDEIDGLAPvrsskqeqihaSIVSTLLALMDG---LDNRGQVV 143
|
|
| COG1223 |
COG1223 |
Predicted ATPase, AAA+ superfamily [General function prediction only]; |
96-272 |
1.17e-03 |
|
Predicted ATPase, AAA+ superfamily [General function prediction only];
Pssm-ID: 440836 [Multi-domain] Cd Length: 246 Bit Score: 41.02 E-value: 1.17e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1714390871 96 LDPVIGRENEIQETAEILS--------RRTKNNP----ILVGDAGVGKTAVVEGLAQAIvagKVPetiqdkeIYSIDLSS 163
Cdd:COG1223 1 LDDVVGQEEAKKKLKLIIKelrrrenlRKFGLWPprkiLFYGPPGTGKTMLAEALAGEL---KLP-------LLTVRLDS 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1714390871 164 LEagTQYRGSFEENIKQLVKEVKAAGNIIlFFDEIHQIigtgatGGEDGGKGLADIIKPALS---------RGELTVIGA 234
Cdd:COG1223 71 LI--GSYLGETARNLRKLFDFARRAPCVI-FFDEFDAI------AKDRGDQNDVGEVKRVVNallqeldglPSGSVVIAA 141
|
170 180 190
....*....|....*....|....*....|....*....
gi 1714390871 235 TTQDEyrntiLKNAALARRFNDVV-INEPTAADTLRILQ 272
Cdd:COG1223 142 TNHPE-----LLDSALWRRFDEVIeFPLPDKEERKEILE 175
|
|
| HslU |
COG1220 |
ATP-dependent protease HslVU (ClpYQ), ATPase subunit HslU [Posttranslational modification, ... |
413-470 |
1.69e-03 |
|
ATP-dependent protease HslVU (ClpYQ), ATPase subunit HslU [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440833 [Multi-domain] Cd Length: 454 Bit Score: 41.57 E-value: 1.69e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1714390871 413 LDKRlkskVIGQDEAVEMVAKAIRrNRAGFSEGDQPIGS------FLFVGPTGVGKTELAKQLA 470
Cdd:COG1220 13 LDKY----IIGQDEAKRAVAIALR-NRWRRQQLPEELRDeitpknILMIGPTGVGKTEIARRLA 71
|
|
| DNA_pol3_delta2 |
pfam13177 |
DNA polymerase III, delta subunit; DNA polymerase III, delta subunit (EC 2.7.7.7) is required ... |
423-537 |
2.42e-03 |
|
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: 39.12 E-value: 2.42e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1714390871 423 GQDEAVEMVAKAIRRNRAGFSegdqpigsFLFVGPTGVGKTELAKQLALDMF----------GNKNAIIRLDMSEYADRT 492
Cdd:pfam13177 1 GQPEAIQLLQNSLENGRLSHA--------YLFSGPEGVGKLELALAFAKALFceepgddlpcGQCRSCRRIESGNHPDLV 72
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 1714390871 493 AVS---KLIGTsagyvgyeDNANTLTERVRRNPY----SIVLLDEIEKADPQ 537
Cdd:pfam13177 73 IIEpegQSIKI--------DQIRELQKEFSKSPYegkkKVYIIEDAEKMTAS 116
|
|
| RecA-like_PEX1_r2 |
cd19526 |
second of two ATPase domains of Peroxisomal biogenesis factor 1 (PEX1); PEX1(also known as ... |
116-226 |
3.41e-03 |
|
second of two ATPase domains of Peroxisomal biogenesis factor 1 (PEX1); PEX1(also known as Peroxin-1)/PEX6 is a protein unfoldase; PEX1 and PEX6 form a heterohexameric Type-2 AAA-ATPase complex and are essential for peroxisome biogenesis as they are required for the import of folded proteins into the peroxisomal matrix. PEX-1 is required for stability of PEX5. 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: 410934 [Multi-domain] Cd Length: 158 Bit Score: 38.95 E-value: 3.41e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1714390871 116 RTKNNPILVGDAGVGKTAVVEGLAQA----IVAGKVPETIqdkeiysidlssleagTQYRGSFEENIKQLVKEVKAAGNI 191
Cdd:cd19526 25 RLRSGILLYGPPGCGKTLLASAIASEcglnFISVKGPELL----------------NKYIGASEQNVRDLFSRAQSAKPC 88
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1714390871 192 ILFFDEIHQII------GTGAT-----------GGEDGGKGL--------ADIIKPALSR 226
Cdd:cd19526 89 ILFFDEFDSIApkrghdSTGVTdrvvnqlltqlDGVEGLDGVyvlaatsrPDLIDPALLR 148
|
|
| AAA_14 |
pfam13173 |
AAA domain; This family of domains contain a P-loop motif that is characteriztic of the AAA ... |
453-581 |
3.47e-03 |
|
AAA domain; This family of domains contain a P-loop motif that is characteriztic of the AAA superfamily.
Pssm-ID: 463799 [Multi-domain] Cd Length: 128 Bit Score: 37.95 E-value: 3.47e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1714390871 453 LFVGPTGVGKTELAKQLALDMFGNKNaIIRLDMSEYADRTAVSkligtsagyvgyEDNANTLTERVRRNPYsIVLLDEIE 532
Cdd:pfam13173 6 VITGPRQVGKTTLLLQLIKELLPPEN-ILYINLDDPRLLKLAD------------FELLELFLELLYPGKT-YLFLDEIQ 71
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 1714390871 533 KAdPQVLTLLLQVMDDGRLTDgqgnvinfkntIIIATSNAGF----GNEALSG 581
Cdd:pfam13173 72 RV-PDWELALKRLYDDGPNGR-----------VILTGSSALLlskeIAESLAG 112
|
|
| RecA-like_CDC48_NLV2_r1-like |
cd19503 |
first of two ATPase domains of CDC48 and NLV2, and similar ATPase domains; CDC48 in yeast and ... |
122-235 |
3.51e-03 |
|
first of two ATPase domains of CDC48 and NLV2, and similar ATPase domains; CDC48 in yeast and p97 or VCP metazoans is an ATP-dependent molecular chaperone which plays an essential role in many cellular processes, by segregating polyubiquitinated proteins from complexes or membranes. Cdc48/p97 consists of an N-terminal domain and two ATPase domains; this subfamily represents the first of the two ATPase domains. This subfamily also includes the first of the two ATPase domains of NVL (nuclear VCP-like protein) 2, an isoform of NVL mainly present in the nucleolus, which is involved in ribosome biogenesis, in telomerase assembly and the regulation of telomerase activity, and in pre-rRNA processing. This subfamily belongs to the RecA-like NTPase family which includes the NTP binding domain of F1 and V1 H(+)ATPases, DnaB and related helicases as well as bacterial RecA and related eukaryotic and archaeal recombinases. The RecA-like NTPase family also includes bacterial conjugation proteins and related DNA transfer proteins involved in type II and type IV secretion.
Pssm-ID: 410911 [Multi-domain] Cd Length: 165 Bit Score: 38.81 E-value: 3.51e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1714390871 122 ILVGDAGVGKTAVVEGLAQaiVAGKVPETIQDKEIYSidlssleagtQYRGSFEENIKQLVKEVKAAGNIILFFDEIHQI 201
Cdd:cd19503 38 LLHGPPGTGKTLLARAVAN--EAGANFLSISGPSIVS----------KYLGESEKNLREIFEEARSHAPSIIFIDEIDAL 105
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 1714390871 202 IGTGATGGEDGGK-------GLADIIKpalSRGELTVIGAT 235
Cdd:cd19503 106 APKREEDQREVERrvvaqllTLMDGMS---SRGKVVVIAAT 143
|
|
| RecA-like_CDC48_r2-like |
cd19511 |
second of two ATPase domains of CDC48/p97, PEX1 and -6, VAT and NVL, and similar ATPase ... |
122-236 |
3.86e-03 |
|
second of two ATPase domains of CDC48/p97, PEX1 and -6, VAT and NVL, and similar ATPase domains; This subfamily includes the second of two ATPase domains of the molecular chaperone CDC48 in yeast and p97 or VCP in metazoans, Peroxisomal biogenesis factor 1 (PEX1) and -6 (PEX6), Valosin-containing protein-like ATPase (VAT), and nuclear VCP-like protein (NVL). This subfamily belongs to the RecA-like NTPase family which includes the NTP binding domain of F1 and V1 H(+)ATPases, DnaB and related helicases as well as bacterial RecA and related eukaryotic and archaeal recombinases. The RecA-like NTPase family also includes bacterial conjugation proteins and related DNA transfer proteins involved in type II and type IV secretion.
Pssm-ID: 410919 [Multi-domain] Cd Length: 159 Bit Score: 38.42 E-value: 3.86e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1714390871 122 ILVGDAGVGKTAVVEGLAQA----IVAGKVPETIqdkeiysidlssleagTQYRGSFEENIKQLVKEVKAAGNIILFFDE 197
Cdd:cd19511 31 LLYGPPGCGKTLLAKALASEaglnFISVKGPELF----------------SKYVGESERAVREIFQKARQAAPCIIFFDE 94
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 1714390871 198 IHQIigTGATGGEDGGkGLADIIKPAL--------SRGELTVIGATT 236
Cdd:cd19511 95 IDSL--APRRGQSDSS-GVTDRVVSQLlteldgieSLKGVVVIAATN 138
|
|
| PRK10820 |
PRK10820 |
transcriptional regulator TyrR; |
446-549 |
3.88e-03 |
|
transcriptional regulator TyrR;
Pssm-ID: 236769 [Multi-domain] Cd Length: 520 Bit Score: 40.44 E-value: 3.88e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1714390871 446 DQPIgsfLFVGPTGVGKTELAKQLALDMFGNKNAIIRLDMSEYADRTAVSKLIGTSAGYV--------GYEDNANTLTer 517
Cdd:PRK10820 227 DAPL---LITGDTGTGKDLLAYACHLRSPRGKKPFLALNCASIPDDVVESELFGHAPGAYpnalegkkGFFEQANGGS-- 301
|
90 100 110
....*....|....*....|....*....|..
gi 1714390871 518 vrrnpysiVLLDEIEKADPQVLTLLLQVMDDG 549
Cdd:PRK10820 302 --------VLLDEIGEMSPRMQAKLLRFLNDG 325
|
|
| COG3899 |
COG3899 |
Predicted ATPase [General function prediction only]; |
91-144 |
4.30e-03 |
|
Predicted ATPase [General function prediction only];
Pssm-ID: 443106 [Multi-domain] Cd Length: 1244 Bit Score: 40.61 E-value: 4.30e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 1714390871 91 ARDGLLDPVIGRENEIQETAEILSRRTKNNPILV---GDAGVGKTAVVEGLAQAIVA 144
Cdd:COG3899 281 ARRLIPQPLVGREAELAALLAALERARAGRGELVlvsGEAGIGKSRLVRELARRARA 337
|
|
| FlhF |
COG1419 |
Flagellar biosynthesis GTPase FlhF [Cell motility]; |
313-484 |
4.64e-03 |
|
Flagellar biosynthesis GTPase FlhF [Cell motility];
Pssm-ID: 441029 [Multi-domain] Cd Length: 361 Bit Score: 39.85 E-value: 4.64e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1714390871 313 DLIDMTAAHLAAKNSQTDVETLDQRVKKLEAAKE--AAVKSEdftkAADIKKSIEETKQKIKKTdqkekiTATIDDVAQS 390
Cdd:COG1419 41 KKVEVTAAVDEDEAEKAPAAAAAPAAASAAAEEEelEELRRE----LAELKELLEEQLSGLAGE------SARLPPELAE 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1714390871 391 VERLtgipVADMGANDiEHLKNLDKRLKSKvIGQDEAVEMVAKAIRRNragFSEGDQPIGS----FLFVGPTGVGKT-EL 465
Cdd:COG1419 111 LLER----LLEAGVSP-ELARELLEKLPED-LSAEEAWRALLEALARR---LPVAEDPLLDeggvIALVGPTGVGKTtTI 181
|
170 180
....*....|....*....|..
gi 1714390871 466 AKqLALD--MFGNKN-AIIRLD 484
Cdd:COG1419 182 AK-LAARfvLRGKKKvALITTD 202
|
|
| RecA-like_CDC48_NLV2_r1-like |
cd19503 |
first of two ATPase domains of CDC48 and NLV2, and similar ATPase domains; CDC48 in yeast and ... |
425-571 |
4.87e-03 |
|
first of two ATPase domains of CDC48 and NLV2, and similar ATPase domains; CDC48 in yeast and p97 or VCP metazoans is an ATP-dependent molecular chaperone which plays an essential role in many cellular processes, by segregating polyubiquitinated proteins from complexes or membranes. Cdc48/p97 consists of an N-terminal domain and two ATPase domains; this subfamily represents the first of the two ATPase domains. This subfamily also includes the first of the two ATPase domains of NVL (nuclear VCP-like protein) 2, an isoform of NVL mainly present in the nucleolus, which is involved in ribosome biogenesis, in telomerase assembly and the regulation of telomerase activity, and in pre-rRNA processing. This subfamily belongs to the RecA-like NTPase family which includes the NTP binding domain of F1 and V1 H(+)ATPases, DnaB and related helicases as well as bacterial RecA and related eukaryotic and archaeal recombinases. The RecA-like NTPase family also includes bacterial conjugation proteins and related DNA transfer proteins involved in type II and type IV secretion.
Pssm-ID: 410911 [Multi-domain] Cd Length: 165 Bit Score: 38.43 E-value: 4.87e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1714390871 425 DEAVEMVAKAIRRNRAGFSEGDQPIGSFLFVGPTGVGKTELAKQLALDMFGNKNAIIRLDMseyadrtaVSKLIGTSagy 504
Cdd:cd19503 10 ASLKELIELPLKYPELFRALGLKPPRGVLLHGPPGTGKTLLARAVANEAGANFLSISGPSI--------VSKYLGES--- 78
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1714390871 505 vgyEDNANTLTERVRRNPYSIVLLDEI-----------EKADPQVLTLLLQVMDDgrlTDGQGNVinfkntIIIATSN 571
Cdd:cd19503 79 ---EKNLREIFEEARSHAPSIIFIDEIdalapkreedqREVERRVVAQLLTLMDG---MSSRGKV------VVIAATN 144
|
|
| AAA_22 |
pfam13401 |
AAA domain; |
450-550 |
5.75e-03 |
|
AAA domain;
Pssm-ID: 379165 [Multi-domain] Cd Length: 129 Bit Score: 37.71 E-value: 5.75e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1714390871 450 GSFLFVGPTGVGKTELAKQLaLDMFGNKNA-IIRLDMSEYADRTAVSKLIGTSAGYVG-YEDNANTLTERVRRN-----P 522
Cdd:pfam13401 6 GILVLTGESGTGKTTLLRRL-LEQLPEVRDsVVFVDLPSGTSPKDLLRALLRALGLPLsGRLSKEELLAALQQLllalaV 84
|
90 100
....*....|....*....|....*...
gi 1714390871 523 YSIVLLDEIEKADPQVLTLLLQVMDDGR 550
Cdd:pfam13401 85 AVVLIIDEAQHLSLEALEELRDLLNLSS 112
|
|
| CDC48 |
TIGR01243 |
AAA family ATPase, CDC48 subfamily; This subfamily of the AAA family ATPases includes two ... |
390-559 |
7.49e-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: 7.49e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1714390871 390 SVERLTGIPvaDMGANDIEHLKNLDKRLKskvigqdeavEMVAKAIRRNRAGFSEGDQPIGSFLFVGPTGVGKTELAKQL 469
Cdd:TIGR01243 165 REEIERKVP--KVTYEDIGGLKEAKEKIR----------EMVELPMKHPELFEHLGIEPPKGVLLYGPPGTGKTLLAKAV 232
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1714390871 470 ALDMFGNKNAIIRLDMseyadrtaVSKLIGTSagyvgyEDNANTLTERVRRNPYSIVLLDEIEKADPQ-----------V 538
Cdd:TIGR01243 233 ANEAGAYFISINGPEI--------MSKYYGES------EERLREIFKEAEENAPSIIFIDEIDAIAPKreevtgevekrV 298
|
170 180
....*....|....*....|.
gi 1714390871 539 LTLLLQVMDDGRltdGQGNVI 559
Cdd:TIGR01243 299 VAQLLTLMDGLK---GRGRVI 316
|
|
| PRK04195 |
PRK04195 |
replication factor C large subunit; Provisional |
415-530 |
9.15e-03 |
|
replication factor C large subunit; Provisional
Pssm-ID: 235250 [Multi-domain] Cd Length: 482 Bit Score: 39.13 E-value: 9.15e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1714390871 415 KRLkSKVIGQDEAVEMVAKAIRRNRAGfsegdQPIGSFLFVGPTGVGKTELAKQLALDMfgnKNAIIRLDMSEYADRTAV 494
Cdd:PRK04195 11 KTL-SDVVGNEKAKEQLREWIESWLKG-----KPKKALLLYGPPGVGKTSLAHALANDY---GWEVIELNASDQRTADVI 81
|
90 100 110
....*....|....*....|....*....|....*.
gi 1714390871 495 SKLIGTSAGYvgyednaNTLTERVRRnpysIVLLDE 530
Cdd:PRK04195 82 ERVAGEAATS-------GSLFGARRK----LILLDE 106
|
|
| |
