|
Name |
Accession |
Description |
Interval |
E-value |
| clpA |
PRK11034 |
ATP-dependent Clp protease ATP-binding subunit; Provisional |
20-754 |
1.28e-96 |
|
ATP-dependent Clp protease ATP-binding subunit; Provisional
Pssm-ID: 236828 [Multi-domain] Cd Length: 758 Bit Score: 316.39 E-value: 1.28e-96
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501390570 20 ERKHLVFTEEHIFYSLISSEKIKELLSLCTLDFYNFNKILEGFFKQlplresdiSDYLFKMNDLYQEIIDTICYYkkpyR 99
Cdd:PRK11034 19 EHRHEFMTVEHLLLALLSNPSAREALEACSVDLVALRQELEAFIEQ--------TTPVLPASEEERDTQPTLSFQ----R 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501390570 100 LQEKDLLWVLVRKRKNTildallkSGFNL--TIFDKIIEVYDYLGSDLDLSSLeneklvesDLFN---KGI--DRDGGLS 172
Cdd:PRK11034 87 VLQRAVFHVQSSGRSEV-------TGANVlvAIFSEQESQAAYLLRKHEVSRL--------DVVNfisHGTrkDEPSQSS 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501390570 173 IFEEDYFKLEQSDDsldDNNVEDFLVNvIDSLDPNLEKNPLIGRKKELCKLIQVMLRKHKSNPIVFGEPGVGKTILLQGL 252
Cdd:PRK11034 152 DPGSQPNSEEQAGG---EERMENFTTN-LNQLARVGGIDPLIGREKELERAIQVLCRRRKNNPLLVGESGVGKTAIAEGL 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501390570 253 AYMIKAGQVPQELAGYEVYSLDIGRLISGTRYRGDLEDRVNKLLDFLYFKKKVILFIDEIHMIVGAGATSFSNIDVSNLL 332
Cdd:PRK11034 228 AWRIVQGDVPEVMADCTIYSLDIGSLLAGTKYRGDFEKRFKALLKQLEQDTNSILFIDEIHTIIGAGAASGGQVDAANLI 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501390570 333 KPILTLGEVKFIGATTKYEYQKFFLKDKALIRRFHSIELREPSFEDTYIILKGAKEQYEKHHNVEYTDEAIWASITMS-K 411
Cdd:PRK11034 308 KPLLSSGKIRVIGSTTYQEFSNIFEKDRALARRFQKIDITEPSIEETVQIINGLKPKYEAHHDVRYTAKAVRAAVELAvK 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501390570 412 YMKDRFLPDKAFDLLDGLGAKFKL---EGNRKVITADDVRDFVKSMIGTNIFNFDAYDQDLMINLEHKIRESMIIDEEIL 488
Cdd:PRK11034 388 YINDRHLPDKAIDVIDEAGARARLmpvSKRKKTVNVADIESVVARIARIPEKSVSQSDRDTLKNLGDRLKMLVFGQDKAI 467
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501390570 489 SDLILHIKLLRIKFLFKNNTLGIFILMGSSDVDKNKLSGILSEELKIPKLTLGVSEYGDFDGINRLIGPVYGSESYDEFT 568
Cdd:PRK11034 468 EALTEAIKMSRAGLGHEHKPVGSFLFAGPTGVGKTEVTVQLSKALGIELLRFDMSEYMERHTVSRLIGAPPGYVGFDQGG 547
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501390570 569 TFFKFLSKSSSSIIFLSDFDKSSKRVIEFFFEGFNTGRLFDSLGRSVSLSDSIILIDINIEYRELA--SIGFKNE--TLN 644
Cdd:PRK11034 548 LLTDAVIKHPHAVLLLDEIEKAHPDVFNLLLQVMDNGTLTDNNGRKADFRNVVLVMTTNAGVRETErkSIGLIHQdnSTD 627
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501390570 645 GRSLLEKRFSSQFLDLVDHIFFFRPVGESDFEKAIIEEMNNFVKILKNEKIDVFFEENIVDYFQNKTYGSGLGIKSVSKI 724
Cdd:PRK11034 628 AMEEIKKIFTPEFRNRLDNIIWFDHLSTDVIHQVVDKFIVELQAQLDQKGVSLEVSQEARDWLAEKGYDRAMGARPMARV 707
|
730 740 750
....*....|....*....|....*....|
gi 501390570 725 VVKEIGSLLVNDMISKKFKENDKIRVYIDE 754
Cdd:PRK11034 708 IQDNLKKPLANELLFGSLVDGGQVTVALDK 737
|
|
| ClpA |
COG0542 |
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ... |
212-440 |
4.31e-83 |
|
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440308 [Multi-domain] Cd Length: 836 Bit Score: 281.97 E-value: 4.31e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501390570 212 PLIGRKKELCKLIQVMLRKHKSNPIVFGEPGVGKTILLQGLAYMIKAGQVPQELAGYEVYSLDIGRLISGTRYRGDLEDR 291
Cdd:COG0542 180 PVIGRDEEIRRVIQILSRRTKNNPVLIGEPGVGKTAIVEGLAQRIVNGDVPESLKDKRVLSLDLGALVAGAKYRGEFEER 259
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501390570 292 VNKLLDFLY-FKKKVILFIDEIHMIVGAGATSfSNIDVSNLLKPILTLGEVKFIGATTKYEYQKFFLKDKALIRRFHSIE 370
Cdd:COG0542 260 LKAVLDEVKkSEGNIILFIDELHTLVGAGGAE-GAMDAANLLKPALARGELRCIGATTLDEYRKYIEKDAALERRFQPVL 338
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 501390570 371 LREPSFEDTYIILKGAKEQYEKHHNVEYTDEAIWASITMSK-YMKDRFLPDKAFDLLDGLGAKFKLEGNRK 440
Cdd:COG0542 339 VEEPSVEDTISILRGLKERYEAHHGVRITDEALVAAVRLSDrYITDRFLPDKAIDLIDEAAARVRMEIDSK 409
|
|
| VI_ClpV1 |
TIGR03345 |
type VI secretion ATPase, ClpV1 family; Members of this protein family are homologs of ClpB, ... |
212-427 |
2.12e-61 |
|
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: 221.74 E-value: 2.12e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501390570 212 PLIGRKKELCKLIQVMLRKHKSNPIVFGEPGVGKTILLQGLAYMIKAGQVPQELAGYEVYSLDIGRLISGTRYRGDLEDR 291
Cdd:TIGR03345 188 PVLGRDDEIRQMIDILLRRRQNNPILTGEAGVGKTAVVEGLALRIAAGDVPPALRNVRLLSLDLGLLQAGASVKGEFENR 267
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501390570 292 VNKLLDFLyfkKK----VILFIDEIHMIVGAGATSFSNiDVSNLLKPILTLGEVKFIGATTKYEYQKFFLKDKALIRRFH 367
Cdd:TIGR03345 268 LKSVIDEV---KAspqpIILFIDEAHTLIGAGGQAGQG-DAANLLKPALARGELRTIAATTWAEYKKYFEKDPALTRRFQ 343
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 501390570 368 SIELREPSFEDTYIILKGAKEQYEKHHNVEYTDEAIWASITMS-KYMKDRFLPDKAFDLLD 427
Cdd:TIGR03345 344 VVKVEEPDEETAIRMLRGLAPVLEKHHGVLILDEAVVAAVELShRYIPGRQLPDKAVSLLD 404
|
|
| AAA_lid_9 |
pfam17871 |
AAA lid domain; This entry represents the alpha helical AAA+ lid domain that is found to the ... |
375-449 |
1.65e-24 |
|
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: 98.33 E-value: 1.65e-24
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 501390570 375 SFEDTYIILKGAKEQYEKHHNVEYTDEAIWASITMSK-YMKDRFLPDKAFDLLDGLGAKFKLEGNRKVITADDVRD 449
Cdd:pfam17871 1 SVEEAIEILRGLKPKYEKHHGVRISDEALEAAVKLSKrYITDRFLPDKAIDLLDEACARVRLSQESKPEELEDLER 76
|
|
| AAA |
cd00009 |
The AAA+ (ATPases Associated with a wide variety of cellular Activities) superfamily ... |
214-369 |
2.08e-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: 71.02 E-value: 2.08e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501390570 214 IGRKKELCKLIQVMLRKHKSNPIVFGEPGVGKTILLQGLAYMIKagqvpqeLAGYEVYSLDIGRLISGTRYRGDLEDRVN 293
Cdd:cd00009 1 VGQEEAIEALREALELPPPKNLLLYGPPGTGKTTLARAIANELF-------RPGAPFLYLNASDLLEGLVVAELFGHFLV 73
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 501390570 294 KLLDFL-YFKKKVILFIDEIHMI-VGAGATSFSNIDVsnLLKPILTLGEVKFIGATTKYEYQKFflkDKALIRRFHSI 369
Cdd:cd00009 74 RLLFELaEKAKPGVLFIDEIDSLsRGAQNALLRVLET--LNDLRIDRENVRVIGATNRPLLGDL---DRALYDRLDIR 146
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
236-366 |
3.43e-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: 50.45 E-value: 3.43e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501390570 236 IVFGEPGVGKTILLQGLAYMIKAGQVPQ-----ELAGYEVYSLDIGRLISGTRYRGDLEDRVNKLLDFLYFKKKVILFID 310
Cdd:smart00382 6 LIVGPPGSGKTTLARALARELGPPGGGViyidgEDILEEVLDQLLLIIVGGKKASGSGELRLRLALALARKLKPDVLILD 85
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 501390570 311 EIHMIVGAGAT-SFSNIDVSNLLKPILTLGEVKFIGATTKYEyqkfFLKDKALIRRF 366
Cdd:smart00382 86 EITSLLDAEQEaLLLLLEELRLLLLLKSEKNLTVILTTNDEK----DLGPALLRRRF 138
|
|
|
|
Name |
Accession |
Description |
Interval |
E-value |
| clpA |
PRK11034 |
ATP-dependent Clp protease ATP-binding subunit; Provisional |
20-754 |
1.28e-96 |
|
ATP-dependent Clp protease ATP-binding subunit; Provisional
Pssm-ID: 236828 [Multi-domain] Cd Length: 758 Bit Score: 316.39 E-value: 1.28e-96
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501390570 20 ERKHLVFTEEHIFYSLISSEKIKELLSLCTLDFYNFNKILEGFFKQlplresdiSDYLFKMNDLYQEIIDTICYYkkpyR 99
Cdd:PRK11034 19 EHRHEFMTVEHLLLALLSNPSAREALEACSVDLVALRQELEAFIEQ--------TTPVLPASEEERDTQPTLSFQ----R 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501390570 100 LQEKDLLWVLVRKRKNTildallkSGFNL--TIFDKIIEVYDYLGSDLDLSSLeneklvesDLFN---KGI--DRDGGLS 172
Cdd:PRK11034 87 VLQRAVFHVQSSGRSEV-------TGANVlvAIFSEQESQAAYLLRKHEVSRL--------DVVNfisHGTrkDEPSQSS 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501390570 173 IFEEDYFKLEQSDDsldDNNVEDFLVNvIDSLDPNLEKNPLIGRKKELCKLIQVMLRKHKSNPIVFGEPGVGKTILLQGL 252
Cdd:PRK11034 152 DPGSQPNSEEQAGG---EERMENFTTN-LNQLARVGGIDPLIGREKELERAIQVLCRRRKNNPLLVGESGVGKTAIAEGL 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501390570 253 AYMIKAGQVPQELAGYEVYSLDIGRLISGTRYRGDLEDRVNKLLDFLYFKKKVILFIDEIHMIVGAGATSFSNIDVSNLL 332
Cdd:PRK11034 228 AWRIVQGDVPEVMADCTIYSLDIGSLLAGTKYRGDFEKRFKALLKQLEQDTNSILFIDEIHTIIGAGAASGGQVDAANLI 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501390570 333 KPILTLGEVKFIGATTKYEYQKFFLKDKALIRRFHSIELREPSFEDTYIILKGAKEQYEKHHNVEYTDEAIWASITMS-K 411
Cdd:PRK11034 308 KPLLSSGKIRVIGSTTYQEFSNIFEKDRALARRFQKIDITEPSIEETVQIINGLKPKYEAHHDVRYTAKAVRAAVELAvK 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501390570 412 YMKDRFLPDKAFDLLDGLGAKFKL---EGNRKVITADDVRDFVKSMIGTNIFNFDAYDQDLMINLEHKIRESMIIDEEIL 488
Cdd:PRK11034 388 YINDRHLPDKAIDVIDEAGARARLmpvSKRKKTVNVADIESVVARIARIPEKSVSQSDRDTLKNLGDRLKMLVFGQDKAI 467
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501390570 489 SDLILHIKLLRIKFLFKNNTLGIFILMGSSDVDKNKLSGILSEELKIPKLTLGVSEYGDFDGINRLIGPVYGSESYDEFT 568
Cdd:PRK11034 468 EALTEAIKMSRAGLGHEHKPVGSFLFAGPTGVGKTEVTVQLSKALGIELLRFDMSEYMERHTVSRLIGAPPGYVGFDQGG 547
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501390570 569 TFFKFLSKSSSSIIFLSDFDKSSKRVIEFFFEGFNTGRLFDSLGRSVSLSDSIILIDINIEYRELA--SIGFKNE--TLN 644
Cdd:PRK11034 548 LLTDAVIKHPHAVLLLDEIEKAHPDVFNLLLQVMDNGTLTDNNGRKADFRNVVLVMTTNAGVRETErkSIGLIHQdnSTD 627
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501390570 645 GRSLLEKRFSSQFLDLVDHIFFFRPVGESDFEKAIIEEMNNFVKILKNEKIDVFFEENIVDYFQNKTYGSGLGIKSVSKI 724
Cdd:PRK11034 628 AMEEIKKIFTPEFRNRLDNIIWFDHLSTDVIHQVVDKFIVELQAQLDQKGVSLEVSQEARDWLAEKGYDRAMGARPMARV 707
|
730 740 750
....*....|....*....|....*....|
gi 501390570 725 VVKEIGSLLVNDMISKKFKENDKIRVYIDE 754
Cdd:PRK11034 708 IQDNLKKPLANELLFGSLVDGGQVTVALDK 737
|
|
| ClpA |
COG0542 |
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ... |
212-440 |
4.31e-83 |
|
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440308 [Multi-domain] Cd Length: 836 Bit Score: 281.97 E-value: 4.31e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501390570 212 PLIGRKKELCKLIQVMLRKHKSNPIVFGEPGVGKTILLQGLAYMIKAGQVPQELAGYEVYSLDIGRLISGTRYRGDLEDR 291
Cdd:COG0542 180 PVIGRDEEIRRVIQILSRRTKNNPVLIGEPGVGKTAIVEGLAQRIVNGDVPESLKDKRVLSLDLGALVAGAKYRGEFEER 259
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501390570 292 VNKLLDFLY-FKKKVILFIDEIHMIVGAGATSfSNIDVSNLLKPILTLGEVKFIGATTKYEYQKFFLKDKALIRRFHSIE 370
Cdd:COG0542 260 LKAVLDEVKkSEGNIILFIDELHTLVGAGGAE-GAMDAANLLKPALARGELRCIGATTLDEYRKYIEKDAALERRFQPVL 338
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 501390570 371 LREPSFEDTYIILKGAKEQYEKHHNVEYTDEAIWASITMSK-YMKDRFLPDKAFDLLDGLGAKFKLEGNRK 440
Cdd:COG0542 339 VEEPSVEDTISILRGLKERYEAHHGVRITDEALVAAVRLSDrYITDRFLPDKAIDLIDEAAARVRMEIDSK 409
|
|
| clpC |
CHL00095 |
Clp protease ATP binding subunit |
194-761 |
5.92e-83 |
|
Clp protease ATP binding subunit
Pssm-ID: 214361 [Multi-domain] Cd Length: 821 Bit Score: 281.17 E-value: 5.92e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501390570 194 EDFLVNVIDS-LDPNLekNPLIGRKKELCKLIQVMLRKHKSNPIVFGEPGVGKTILLQGLAYMIKAGQVPQELAGYEVYS 272
Cdd:CHL00095 163 EEFGTNLTKEaIDGNL--DPVIGREKEIERVIQILGRRTKNNPILIGEPGVGKTAIAEGLAQRIVNRDVPDILEDKLVIT 240
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501390570 273 LDIGRLISGTRYRGDLEDRVNKLLDFLYFKKKVILFIDEIHMIVGAGATSfSNIDVSNLLKPILTLGEVKFIGATTKYEY 352
Cdd:CHL00095 241 LDIGLLLAGTKYRGEFEERLKRIFDEIQENNNIILVIDEVHTLIGAGAAE-GAIDAANILKPALARGELQCIGATTLDEY 319
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501390570 353 QKFFLKDKALIRRFHSIELREPSFEDTYIILKGAKEQYEKHHNVEYTDEAIWASITMS-KYMKDRFLPDKAFDLLDGLGA 431
Cdd:CHL00095 320 RKHIEKDPALERRFQPVYVGEPSVEETIEILFGLRSRYEKHHNLSISDKALEAAAKLSdQYIADRFLPDKAIDLLDEAGS 399
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501390570 432 KFKLE--------------------------------------------------------------GNRKVITADDVRD 449
Cdd:CHL00095 400 RVRLInsrlppaareldkelreilkdkdeaireqdfetakqlrdremevraqiaaiiqskkteeekrLEVPVVTEEDIAE 479
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501390570 450 FVKSMIGTNIFNFDAYDQDLMINLEHKIRESMIIDEEILSDLILHIKLLRIKFLFKNNTLGIFILMGSSDVDKNKLSGIL 529
Cdd:CHL00095 480 IVSAWTGIPVNKLTKSESEKLLHMEETLHKRIIGQDEAVVAVSKAIRRARVGLKNPNRPIASFLFSGPTGVGKTELTKAL 559
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501390570 530 ------SEELKIpklTLGVSEYGDFDGINRLIGPVYGSESYDEFTTFFKFLSKSSSSIIFLSDFDKSSKRVIEFFFEGFN 603
Cdd:CHL00095 560 asyffgSEDAMI---RLDMSEYMEKHTVSKLIGSPPGYVGYNEGGQLTEAVRKKPYTVVLFDEIEKAHPDIFNLLLQILD 636
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501390570 604 TGRLFDSLGRSVSLSDSIILIDINIEYREL----ASIGFK------NETLNGR------SLLEKRFSSQFLDLVDHIFFF 667
Cdd:CHL00095 637 DGRLTDSKGRTIDFKNTLIIMTSNLGSKVIetnsGGLGFElsenqlSEKQYKRlsnlvnEELKQFFRPEFLNRLDEIIVF 716
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501390570 668 RPVGESDFeKAIIEEM-NNFVKILKNEKIDVFFEENIVDYFQNKTYGSGLGIKSVSKIVVKEIGSLLVNDMISKKFKEND 746
Cdd:CHL00095 717 RQLTKNDV-WEIAEIMlKNLFKRLNEQGIQLEVTERIKTLLIEEGYNPLYGARPLRRAIMRLLEDPLAEEVLSFKIKPGD 795
|
650
....*....|....*
gi 501390570 747 KIRVYIDETMKYELL 761
Cdd:CHL00095 796 IIIVDVNDEKEVKIL 810
|
|
| PRK10865 |
PRK10865 |
ATP-dependent chaperone ClpB; |
211-440 |
1.31e-64 |
|
ATP-dependent chaperone ClpB;
Pssm-ID: 182791 [Multi-domain] Cd Length: 857 Bit Score: 231.27 E-value: 1.31e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501390570 211 NPLIGRKKELCKLIQVMLRKHKSNPIVFGEPGVGKTILLQGLAYMIKAGQVPQELAGYEVYSLDIGRLISGTRYRGDLED 290
Cdd:PRK10865 178 DPVIGRDEEIRRTIQVLQRRTKNNPVLIGEPGVGKTAIVEGLAQRIINGEVPEGLKGRRVLALDMGALVAGAKYRGEFEE 257
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501390570 291 RVNKLLDFLYFKK-KVILFIDEIHMIVGAGATSfSNIDVSNLLKPILTLGEVKFIGATTKYEYQKFFLKDKALIRRFHSI 369
Cdd:PRK10865 258 RLKGVLNDLAKQEgNVILFIDELHTMVGAGKAD-GAMDAGNMLKPALARGELHCVGATTLDEYRQYIEKDAALERRFQKV 336
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 501390570 370 ELREPSFEDTYIILKGAKEQYEKHHNVEYTDEAIWASITMS-KYMKDRFLPDKAFDLLDGLGAKFKLEGNRK 440
Cdd:PRK10865 337 FVAEPSVEDTIAILRGLKERYELHHHVQITDPAIVAAATLShRYIADRQLPDKAIDLIDEAASSIRMQIDSK 408
|
|
| VI_ClpV1 |
TIGR03345 |
type VI secretion ATPase, ClpV1 family; Members of this protein family are homologs of ClpB, ... |
212-427 |
2.12e-61 |
|
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: 221.74 E-value: 2.12e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501390570 212 PLIGRKKELCKLIQVMLRKHKSNPIVFGEPGVGKTILLQGLAYMIKAGQVPQELAGYEVYSLDIGRLISGTRYRGDLEDR 291
Cdd:TIGR03345 188 PVLGRDDEIRQMIDILLRRRQNNPILTGEAGVGKTAVVEGLALRIAAGDVPPALRNVRLLSLDLGLLQAGASVKGEFENR 267
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501390570 292 VNKLLDFLyfkKK----VILFIDEIHMIVGAGATSFSNiDVSNLLKPILTLGEVKFIGATTKYEYQKFFLKDKALIRRFH 367
Cdd:TIGR03345 268 LKSVIDEV---KAspqpIILFIDEAHTLIGAGGQAGQG-DAANLLKPALARGELRTIAATTWAEYKKYFEKDPALTRRFQ 343
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 501390570 368 SIELREPSFEDTYIILKGAKEQYEKHHNVEYTDEAIWASITMS-KYMKDRFLPDKAFDLLD 427
Cdd:TIGR03345 344 VVKVEEPDEETAIRMLRGLAPVLEKHHGVLILDEAVVAAVELShRYIPGRQLPDKAVSLLD 404
|
|
| AAA_lid_9 |
pfam17871 |
AAA lid domain; This entry represents the alpha helical AAA+ lid domain that is found to the ... |
375-449 |
1.65e-24 |
|
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: 98.33 E-value: 1.65e-24
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 501390570 375 SFEDTYIILKGAKEQYEKHHNVEYTDEAIWASITMSK-YMKDRFLPDKAFDLLDGLGAKFKLEGNRKVITADDVRD 449
Cdd:pfam17871 1 SVEEAIEILRGLKPKYEKHHGVRISDEALEAAVKLSKrYITDRFLPDKAIDLLDEACARVRLSQESKPEELEDLER 76
|
|
| AAA |
cd00009 |
The AAA+ (ATPases Associated with a wide variety of cellular Activities) superfamily ... |
214-369 |
2.08e-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: 71.02 E-value: 2.08e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501390570 214 IGRKKELCKLIQVMLRKHKSNPIVFGEPGVGKTILLQGLAYMIKagqvpqeLAGYEVYSLDIGRLISGTRYRGDLEDRVN 293
Cdd:cd00009 1 VGQEEAIEALREALELPPPKNLLLYGPPGTGKTTLARAIANELF-------RPGAPFLYLNASDLLEGLVVAELFGHFLV 73
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 501390570 294 KLLDFL-YFKKKVILFIDEIHMI-VGAGATSFSNIDVsnLLKPILTLGEVKFIGATTKYEYQKFflkDKALIRRFHSI 369
Cdd:cd00009 74 RLLFELaEKAKPGVLFIDEIDSLsRGAQNALLRVLET--LNDLRIDRENVRVIGATNRPLLGDL---DRALYDRLDIR 146
|
|
| AAA |
pfam00004 |
ATPase family associated with various cellular activities (AAA); AAA family proteins often ... |
236-366 |
9.68e-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: 65.69 E-value: 9.68e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501390570 236 IVFGEPGVGKTILLQGLAymikagqvpQELaGYEVYSLDIGRLISGtrYRGDLEDRVNKLLDFLYFKKKVILFIDEIHMI 315
Cdd:pfam00004 2 LLYGPPGTGKTTLAKAVA---------KEL-GAPFIEISGSELVSK--YVGESEKRLRELFEAAKKLAPCVIFIDEIDAL 69
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 501390570 316 VGAGATSFS--NIDVSNLLKPIL-----TLGEVKFIGATTKYEyqkffLKDKALIRRF 366
Cdd:pfam00004 70 AGSRGSGGDseSRRVVNQLLTELdgftsSNSKVIVIAATNRPD-----KLDPALLGRF 122
|
|
| PRK13342 |
PRK13342 |
recombination factor protein RarA; Reviewed |
213-410 |
2.72e-09 |
|
recombination factor protein RarA; Reviewed
Pssm-ID: 237355 [Multi-domain] Cd Length: 413 Bit Score: 60.10 E-value: 2.72e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501390570 213 LIGRKKELCKLIQvmlRKHKSNPIVFGEPGVGKTILlqglAYMIkAGQVpqelaGYEVYSLDIgrLISGTRyrgDLEDRV 292
Cdd:PRK13342 20 LLGPGKPLRRMIE---AGRLSSMILWGPPGTGKTTL----ARII-AGAT-----DAPFEALSA--VTSGVK---DLREVI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501390570 293 NKLLDFLYFKKKVILFIDEIHmivgagatSFSNI--DVsnLLkPILTLGEVKFIGATTkyEyQKFFLKDKALIRRFHSIE 370
Cdd:PRK13342 82 EEARQRRSAGRRTILFIDEIH--------RFNKAqqDA--LL-PHVEDGTITLIGATT--E-NPSFEVNPALLSRAQVFE 147
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 501390570 371 LREPSFEDTYIILKGAKEQYEKHHnVEYTDEAIWASITMS 410
Cdd:PRK13342 148 LKPLSEEDIEQLLKRALEDKERGL-VELDDEALDALARLA 186
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
236-366 |
3.43e-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: 50.45 E-value: 3.43e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501390570 236 IVFGEPGVGKTILLQGLAYMIKAGQVPQ-----ELAGYEVYSLDIGRLISGTRYRGDLEDRVNKLLDFLYFKKKVILFID 310
Cdd:smart00382 6 LIVGPPGSGKTTLARALARELGPPGGGViyidgEDILEEVLDQLLLIIVGGKKASGSGELRLRLALALARKLKPDVLILD 85
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 501390570 311 EIHMIVGAGAT-SFSNIDVSNLLKPILTLGEVKFIGATTKYEyqkfFLKDKALIRRF 366
Cdd:smart00382 86 EITSLLDAEQEaLLLLLEELRLLLLLKSEKNLTVILTTNDEK----DLGPALLRRRF 138
|
|
| COG1223 |
COG1223 |
Predicted ATPase, AAA+ superfamily [General function prediction only]; |
228-384 |
5.00e-07 |
|
Predicted ATPase, AAA+ superfamily [General function prediction only];
Pssm-ID: 440836 [Multi-domain] Cd Length: 246 Bit Score: 51.42 E-value: 5.00e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501390570 228 LRKHKSNP----IVFGEPGVGKTILLQGLAYMIKagqVPqelagyeVYSLDIGRLISgtRYRGDLEDRVNKLLDFLYfKK 303
Cdd:COG1223 27 LRKFGLWPprkiLFYGPPGTGKTMLAEALAGELK---LP-------LLTVRLDSLIG--SYLGETARNLRKLFDFAR-RA 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501390570 304 KVILFIDEIHMIvgAGATSFSNI--DVSNLLKPILTL-----GEVKFIGATTKYEyqkffLKDKALIRRF-HSIELREPS 375
Cdd:COG1223 94 PCVIFFDEFDAI--AKDRGDQNDvgEVKRVVNALLQEldglpSGSVVIAATNHPE-----LLDSALWRRFdEVIEFPLPD 166
|
....*....
gi 501390570 376 FEDTYIILK 384
Cdd:COG1223 167 KEERKEILE 175
|
|
| RarA |
COG2256 |
Replication-associated recombination protein RarA (DNA-dependent ATPase) [Replication, ... |
222-467 |
5.47e-07 |
|
Replication-associated recombination protein RarA (DNA-dependent ATPase) [Replication, recombination and repair];
Pssm-ID: 441857 [Multi-domain] Cd Length: 439 Bit Score: 52.75 E-value: 5.47e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501390570 222 KLIQVMLRKHK-SNPIVFGEPGVGKTILlqglAYMIkAGQVpqelaGYEVYSLDIgrLISGTRyrgDLEDRVNKLLDFLY 300
Cdd:COG2256 38 KPLRRAIEAGRlSSMILWGPPGTGKTTL----ARLI-ANAT-----DAEFVALSA--VTSGVK---DIREVIEEARERRA 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501390570 301 FKKKVILFIDEIHmivgagatSFsnidvsN------LLkPILTLGEVKFIGATTkyEYQKFFLkDKALIRRFHSIELREP 374
Cdd:COG2256 103 YGRRTILFVDEIH--------RF------NkaqqdaLL-PHVEDGTITLIGATT--ENPSFEV-NSALLSRCRVFVLKPL 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501390570 375 SFEDTYIILKGAKEQYEK---HHNVEYTDEAIWASITMSkymkdrflpD----KAFDLLDgLGAKFKLEGNRKVITADDV 447
Cdd:COG2256 165 SEEDLEQLLERALADDERglgGYKLELDDEALEALARLA---------DgdarRALNALE-LAVLSAPPDGVIEITLELV 234
|
250 260
....*....|....*....|....*
gi 501390570 448 RDFvksmIGTNIFNFDA-----YDQ 467
Cdd:COG2256 235 EEA----LQRRALRYDKdgdehYDL 255
|
|
| RecA-like_protease |
cd19481 |
proteases similar to RecA; RecA-like NTPases. This family includes the NTP binding domain of ... |
225-366 |
1.76e-06 |
|
proteases similar to RecA; RecA-like NTPases. This family includes the NTP binding domain of F1 and V1 H(+)ATPases, DnaB and related helicases as well as bacterial RecA and related eukaryotic and archaeal recombinases. This group also includes bacterial conjugation proteins and related DNA transfer proteins involved in type II and type IV secretion.
Pssm-ID: 410889 [Multi-domain] Cd Length: 158 Bit Score: 48.43 E-value: 1.76e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501390570 225 QVMLRKHKSNPIVFGEPGVGKTILLQGLAymikagqvpqELAGYEVYSLDIGRLISgtRYRGDLEDRVNKLLDFLYFKKK 304
Cdd:cd19481 19 RRYGLGLPKGILLYGPPGTGKTLLAKALA----------GELGLPLIVVKLSSLLS--KYVGESEKNLRKIFERARRLAP 86
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 501390570 305 VILFIDEIHMIVGAGATSFSNIDVS-------NLLKPILTLGEVKFIGATTKYEyqkffLKDKALIR--RF 366
Cdd:cd19481 87 CILFIDEIDAIGRKRDSSGESGELRrvlnqllTELDGVNSRSKVLVIAATNRPD-----LLDPALLRpgRF 152
|
|
| SpoVK |
COG0464 |
AAA+-type ATPase, SpoVK/Ycf46/Vps4 family [Cell wall/membrane/envelope biogenesis, Cell cycle ... |
238-384 |
4.33e-06 |
|
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: 49.91 E-value: 4.33e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501390570 238 FGEPGVGKTILLQGLAymikagqvpqELAGYEVYSLDIGRLISGtrYRGDLEDRVNKLLDFLYFKKKVILFIDEIHMIV- 316
Cdd:COG0464 197 YGPPGTGKTLLARALA----------GELGLPLIEVDLSDLVSK--YVGETEKNLREVFDKARGLAPCVLFIDEADALAg 264
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 501390570 317 --GAGATSFSNIDVSNLLK-------PILtlgevkFIGATTkyeyqKFFLKDKALIRRF-HSIELREPSFEDTYIILK 384
Cdd:COG0464 265 krGEVGDGVGRRVVNTLLTemeelrsDVV------VIAATN-----RPDLLDPALLRRFdEIIFFPLPDAEERLEIFR 331
|
|
| RecA-like_ClpB_Hsp104-like |
cd19499 |
Chaperone protein ClpB/Hsp104 subfamily; Bacterial Caseinolytic peptidase B (ClpB) and ... |
505-667 |
7.67e-06 |
|
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: 47.17 E-value: 7.67e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501390570 505 KNNTLGIFILMGSSDVDKNKLSGILSEELKIPK---LTLGVSEYGDFDGINRLIGPVYGSESYDEFTTFFKFLSKSSSSI 581
Cdd:cd19499 37 PNRPIGSFLFLGPTGVGKTELAKALAELLFGDEdnlIRIDMSEYMEKHSVSRLIGAPPGYVGYTEGGQLTEAVRRKPYSV 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501390570 582 IFLSDFDKSSKRVIEFFFEGFNTGRLFDSLGRSVSLSDSIILIDINIeyrelasigfknetlngrsllekrFSSQFLDLV 661
Cdd:cd19499 117 VLLDEIEKAHPDVQNLLLQVLDDGRLTDSHGRTVDFKNTIIIMTSNH------------------------FRPEFLNRI 172
|
....*.
gi 501390570 662 DHIFFF 667
Cdd:cd19499 173 DEIVVF 178
|
|
| PRK13341 |
PRK13341 |
AAA family ATPase; |
233-402 |
5.07e-05 |
|
AAA family ATPase;
Pssm-ID: 237354 [Multi-domain] Cd Length: 725 Bit Score: 46.97 E-value: 5.07e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501390570 233 SNPIVFGEPGVGKTILLQGLAYMIKAgqvpqelagyEVYSLDigRLISGTRyrgDLEDRVNKLLDFL-YFKKKVILFIDE 311
Cdd:PRK13341 53 GSLILYGPPGVGKTTLARIIANHTRA----------HFSSLN--AVLAGVK---DLRAEVDRAKERLeRHGKRTILFIDE 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501390570 312 IHMIvgagatsfsNIDVSNLLKPILTLGEVKFIGATTKYEYqkfFLKDKALIRRFHSIELREPSFEDTYIILKGAKEQYE 391
Cdd:PRK13341 118 VHRF---------NKAQQDALLPWVENGTITLIGATTENPY---FEVNKALVSRSRLFRLKSLSDEDLHQLLKRALQDKE 185
|
170
....*....|....
gi 501390570 392 KHH---NVEYTDEA 402
Cdd:PRK13341 186 RGYgdrKVDLEPEA 199
|
|
| RPT1 |
COG1222 |
ATP-dependent 26S proteasome regulatory subunit [Posttranslational modification, protein ... |
238-384 |
6.21e-05 |
|
ATP-dependent 26S proteasome regulatory subunit [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440835 [Multi-domain] Cd Length: 326 Bit Score: 45.77 E-value: 6.21e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501390570 238 FGEPGVGKTILLQGLAYMIKAGqvpqelagyeVYSLDIGRLISgtRYRGDLEDRVNKLLDFLYFKKKVILFIDEIHMIVG 317
Cdd:COG1222 118 YGPPGTGKTLLAKAVAGELGAP----------FIRVRGSELVS--KYIGEGARNVREVFELAREKAPSIIFIDEIDAIAA 185
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 501390570 318 AGATSFSNIDVSNLLKPILT-------LGEVKFIGATTKYEyqkffLKDKALIR--RF-HSIELREPSFEDTYIILK 384
Cdd:COG1222 186 RRTDDGTSGEVQRTVNQLLAeldgfesRGDVLIIAATNRPD-----LLDPALLRpgRFdRVIEVPLPDEEAREEILK 257
|
|
| RecA-like_NVL_r1-like |
cd19518 |
first of two ATPase domains of NVL (nuclear VCP-like protein) and similar ATPase domains; NVL ... |
218-349 |
2.25e-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: 42.39 E-value: 2.25e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501390570 218 KELCKLIqVMLRKHK-----------SNPIVFGEPGVGKTILLQGLAYMIKagqVPqelagyeVYSLDIGRLISGTRyrG 286
Cdd:cd19518 10 KELCELL-IHPILPPeyfqhlgveppRGVLLHGPPGCGKTMLANAIAGELK---VP-------FLKISATEIVSGVS--G 76
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 501390570 287 DLEDRVNKLLDFLYFKKKVILFIDEIHMIVGAGATSFSNID---VSNLLKPILTL-------GEVKFIGATTK 349
Cdd:cd19518 77 ESEEKIRELFDQAISNAPCIVFIDEIDAITPKRESAQREMErriVSQLLTCMDELnnektagGPVLVIGATNR 149
|
|
|