|
Name |
Accession |
Description |
Interval |
E-value |
| clpA |
PRK11034 |
ATP-dependent Clp protease ATP-binding subunit; Provisional |
1-755 |
0e+00 |
|
ATP-dependent Clp protease ATP-binding subunit; Provisional
Pssm-ID: 236828 [Multi-domain] Cd Length: 758 Bit Score: 1524.76 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520910443 1 MLNKELESSLNGAFARARDKRHEFMTVEHLLLALLENDAAKEALLACQADIDTLRRELDTFIDQTTPLIPENDETRETQP 80
Cdd:PRK11034 1 MLNQELELSLNMAFARAREHRHEFMTVEHLLLALLSNPSAREALEACSVDLVALRQELEAFIEQTTPVLPASEEERDTQP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520910443 81 TLSFQRVLQRAVFHVQSSGRSEVTGANVLVAIFSEQESHAAYLLKKNDISRLDIVNYISHGITKASSSGDEPSSDSfgTE 160
Cdd:PRK11034 81 TLSFQRVLQRAVFHVQSSGRSEVTGANVLVAIFSEQESQAAYLLRKHEVSRLDVVNFISHGTRKDEPSQSSDPGSQ--PN 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520910443 161 SGEDVSSDERLESFATNLNHLAKQGQIDPLIGRDKELERTIQVLCRRRKNNPLLVGEAGVGKTAIAEGLAWRIVEGQVPE 240
Cdd:PRK11034 159 SEEQAGGEERMENFTTNLNQLARVGGIDPLIGREKELERAIQVLCRRRKNNPLLVGESGVGKTAIAEGLAWRIVQGDVPE 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520910443 241 VIQNSVIYSLDIGSLLAGTKYRGDFEKRFKSILKQLEKEKDAILFIDEIHTIIGAGAASGGQVDAANLIKPLLSSGKLRC 320
Cdd:PRK11034 239 VMADCTIYSLDIGSLLAGTKYRGDFEKRFKALLKQLEQDTNSILFIDEIHTIIGAGAASGGQVDAANLIKPLLSSGKIRV 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520910443 321 IGSTTYQEYSNIFEKERALSRRFQKIDIVEPSLDDTTKILMGLKPKYEAHHDVRYTKEALRAAVELSAKYINERHLPDKA 400
Cdd:PRK11034 319 IGSTTYQEFSNIFEKDRALARRFQKIDITEPSIEETVQIINGLKPKYEAHHDVRYTAKAVRAAVELAVKYINDRHLPDKA 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520910443 401 IDVIDEAGARVRLMPASRRKKTVGVAEIEAMVAKMARIPEKSVSSSDKDILKNLDKKMKMLVFGQDNAIDVLTESIKLTR 480
Cdd:PRK11034 399 IDVIDEAGARARLMPVSKRKKTVNVADIESVVARIARIPEKSVSQSDRDTLKNLGDRLKMLVFGQDKAIEALTEAIKMSR 478
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520910443 481 AGLGSDNRPVGSFLFAGPTGVGKTEVTVQLSKLLGIELLRFDMSEYGERHSVSRLIGAPPGYVGFDQGGLLTDAVIKHPH 560
Cdd:PRK11034 479 AGLGHEHKPVGSFLFAGPTGVGKTEVTVQLSKALGIELLRFDMSEYMERHTVSRLIGAPPGYVGFDQGGLLTDAVIKHPH 558
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520910443 561 SVVLLDEIEKAHPDIFNLLLQVMDNGTLTDNNGRKADFRNVILVMTTNAGVAETVKKSIGMIQQDHSHDAMAEIKKVFTP 640
Cdd:PRK11034 559 AVLLLDEIEKAHPDVFNLLLQVMDNGTLTDNNGRKADFRNVVLVMTTNAGVRETERKSIGLIHQDNSTDAMEEIKKIFTP 638
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520910443 641 EFRNRLDHIIWFNALDERVIHQVVDKFIVELQVQLDARGVSLEVSEDARHWLAVKGYDREMGARPMGRVIQEQLKKPLAN 720
Cdd:PRK11034 639 EFRNRLDNIIWFDHLSTDVIHQVVDKFIVELQAQLDQKGVSLEVSQEARDWLAEKGYDRAMGARPMARVIQDNLKKPLAN 718
|
730 740 750 760
....*....|....*....|....*....|....*....|
gi 520910443 721 ELLFGSLVDGGTVKVDLNEDQLTFKYMGTRE-----EVVH 755
Cdd:PRK11034 719 ELLFGSLVDGGQVTVALDKEKNELTYGFQSAqkhkaEAAH 758
|
|
| ClpA |
TIGR02639 |
ATP-dependent Clp protease ATP-binding subunit clpA; [Protein fate, Degradation of proteins, ... |
2-737 |
0e+00 |
|
ATP-dependent Clp protease ATP-binding subunit clpA; [Protein fate, Degradation of proteins, peptides, and glycopeptides]
Pssm-ID: 274241 [Multi-domain] Cd Length: 730 Bit Score: 1148.23 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520910443 2 LNKELESSLNGAFARARDKRHEFMTVEHLLLALLENDAAKEALLACQADIDTLRRELDTFIDQTTPLIPEnDETRETQPT 81
Cdd:TIGR02639 1 ISEELERILSDALEEAKERRHEFVTLEHLLLALLDDNEAIEILEECGGDVELLRKRLEDYLEENLPVIPE-DIDEEPEQT 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520910443 82 LSFQRVLQRAVFHVQSSGRSEVTGANVLVAIFSEQESHAAYLLKKNDISRLDIVNYISHGITKASSSGDEPSSDSFGTES 161
Cdd:TIGR02639 80 VGVQRVIQRALLHVKSAGKKEIDIGDLLVALFDEEDSHASYFLKSQGITRLDILNYISHGISKDDGKDQLGEEAGKEEEK 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520910443 162 GEDVssderLESFATNLNHLAKQGQIDPLIGRDKELERTIQVLCRRRKNNPLLVGEAGVGKTAIAEGLAWRIVEGQVPEV 241
Cdd:TIGR02639 160 GQDA-----LEKYTVDLTEKAKNGKIDPLIGREDELERTIQVLCRRKKNNPLLVGEPGVGKTAIVEGLALRIAEGKVPER 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520910443 242 IQNSVIYSLDIGSLLAGTKYRGDFEKRFKSILKQLEKEKDAILFIDEIHTIIGAGAASGGQVDAANLIKPLLSSGKLRCI 321
Cdd:TIGR02639 235 LKNAKIYSLDMGTLLAGTKYRGDFEERLKAVVSEIEKEPNAILFIDEIHTIVGAGATSGGSMDASNLLKPALSSGKIRCI 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520910443 322 GSTTYQEYSNIFEKERALSRRFQKIDIVEPSLDDTTKILMGLKPKYEAHHDVRYTKEALRAAVELSAKYINERHLPDKAI 401
Cdd:TIGR02639 315 GSTTYEEYKNHFEKDRALSRRFQKIDVGEPSIEETVKILKGLKEQYEEFHHVKYSDEALEAAVELSARYINDRFLPDKAI 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520910443 402 DVIDEAGARVRLMPASRRKKTVGVAEIEAMVAKMARIPEKSVSSSDKDILKNLDKKMKMLVFGQDNAIDVLTESIKLTRA 481
Cdd:TIGR02639 395 DVIDEAGAAFRLRPKAKKKANVNVKDIENVVAKMAKIPVKTVSSDDREQLKNLEKNLKAKIFGQDEAIDQLVSAIKRSRA 474
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520910443 482 GLGSDNRPVGSFLFAGPTGVGKTEVTVQLSKLLGIELLRFDMSEYGERHSVSRLIGAPPGYVGFDQGGLLTDAVIKHPHS 561
Cdd:TIGR02639 475 GLGDPNKPVGSFLFVGPTGVGKTELAKQLAEELGVHLLRFDMSEYMEKHTVSRLIGSPPGYVGFEQGGLLTDAVRKHPHC 554
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520910443 562 VVLLDEIEKAHPDIFNLLLQVMDNGTLTDNNGRKADFRNVILVMTTNAGVAETVKKSIGMIQQDHSHDAMAEIKKVFTPE 641
Cdd:TIGR02639 555 VLLLDEIEKAHPDIYNILLQVMDYATLTDNNGRKADFRNVILIMTSNAGASEMSKPPIGFGGENRESKSLKAIKKLFSPE 634
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520910443 642 FRNRLDHIIWFNALDERVIHQVVDKFIVELQVQLDARGVSLEVSEDARHWLAVKGYDREMGARPMGRVIQEQLKKPLANE 721
Cdd:TIGR02639 635 FRNRLDAIIHFNDLSEEMAEKIVKKFLDELQDQLNEKNIELELTDDAKKYLAEKGYDEEFGARPLARVIQEEIKKPLSDE 714
|
730
....*....|....*.
gi 520910443 722 LLFGSLVDGGTVKVDL 737
Cdd:TIGR02639 715 ILFGKLKKGGSVKISL 730
|
|
| ClpA |
COG0542 |
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ... |
2-743 |
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: 840.89 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520910443 2 LNKELESSLNGAFARARDKRHEFMTVEHLLLALLEND--AAKEALLACQADIDTLRRELDTFIDQTtplipENDETRETQ 79
Cdd:COG0542 6 FTEKAQEALEAAQELARRLGHQEVEPEHLLLALLEQGegLAAKLLRKLGVDLDALREELEEALGRL-----PKVSGSSGQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520910443 80 PTLS--FQRVLQRAVFHVQSSGRSEVTGANVLVAIFSEQESHAAYLLKKNDISRLDIVNYIShGITKASSSGDEPSSDSF 157
Cdd:COG0542 81 PYLSprLKRVLELAELEARKLGDEYISTEHLLLALLREGEGVAARILKKLGITLEALREALE-ELRGGSRVTSQNPESKT 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520910443 158 GTesgedvssderLESFATNLNHLAKQGQIDPLIGRDKELERTIQVLCRRRKNNPLLVGEAGVGKTAIAEGLAWRIVEGQ 237
Cdd:COG0542 160 PA-----------LDKYGRDLTELAREGKLDPVIGRDEEIRRVIQILSRRTKNNPVLIGEPGVGKTAIVEGLAQRIVNGD 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520910443 238 VPEVIQNSVIYSLDIGSLLAGTKYRGDFEKRFKSILKQLEK-EKDAILFIDEIHTIIGAGAASgGQVDAANLIKPLLSSG 316
Cdd:COG0542 229 VPESLKDKRVLSLDLGALVAGAKYRGEFEERLKAVLDEVKKsEGNIILFIDELHTLVGAGGAE-GAMDAANLLKPALARG 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520910443 317 KLRCIGSTTYQEYSNIFEKERALSRRFQKIDIVEPSLDDTTKILMGLKPKYEAHHDVRYTKEALRAAVELSAKYINERHL 396
Cdd:COG0542 308 ELRCIGATTLDEYRKYIEKDAALERRFQPVLVEEPSVEDTISILRGLKERYEAHHGVRITDEALVAAVRLSDRYITDRFL 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520910443 397 PDKAIDVIDEAGARVRL----MPAS-----RR------------------------------------------------ 419
Cdd:COG0542 388 PDKAIDLIDEAAARVRMeidsKPEEldeleRRleqleiekealkkeqdeasferlaelrdelaeleeelealkarweaek 467
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520910443 420 -----------------------------------------KKTVGVAEIEAMVAKMARIPEKSVSSSDKDILKNLDKKM 458
Cdd:COG0542 468 elieeiqelkeeleqrygkipelekelaeleeelaelapllREEVTEEDIAEVVSRWTGIPVGKLLEGEREKLLNLEEEL 547
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520910443 459 KMLVFGQDNAIDVLTESIKLTRAGLGSDNRPVGSFLFAGPTGVGKTEVTVQLSKLL-GIE--LLRFDMSEYGERHSVSRL 535
Cdd:COG0542 548 HERVIGQDEAVEAVADAIRRSRAGLKDPNRPIGSFLFLGPTGVGKTELAKALAEFLfGDEdaLIRIDMSEYMEKHSVSRL 627
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520910443 536 IGAPPGYVGFDQGGLLTDAVIKHPHSVVLLDEIEKAHPDIFNLLLQVMDNGTLTDNNGRKADFRNVILVMTTNAGVAETV 615
Cdd:COG0542 628 IGAPPGYVGYEEGGQLTEAVRRRPYSVVLLDEIEKAHPDVFNILLQVLDDGRLTDGQGRTVDFRNTIIIMTSNIGSELIL 707
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520910443 616 KKSIGMIQQDHSHDA-MAEIKKVFTPEFRNRLDHIIWFNALDERVIHQVVDKFIVELQVQLDARGVSLEVSEDARHWLAV 694
Cdd:COG0542 708 DLAEDEPDYEEMKEAvMEELKKHFRPEFLNRIDEIIVFHPLSKEELRKIVDLQLKRLRKRLAERGITLELTDAAKDFLAE 787
|
810 820 830 840
....*....|....*....|....*....|....*....|....*....
gi 520910443 695 KGYDREMGARPMGRVIQEQLKKPLANELLFGSLVDGGTVKVDLNEDQLT 743
Cdd:COG0542 788 KGYDPEYGARPLKRAIQRELEDPLAEEILAGEIKEGDTITVDVDDGELV 836
|
|
| chaperone_ClpB |
TIGR03346 |
ATP-dependent chaperone ClpB; Members of this protein family are the bacterial ATP-dependent ... |
12-743 |
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: 672.05 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520910443 12 GAFARARD----KRHEFMTVEHLLLALLENDA--AKEALLACQADIDTLRRELDTFIDQTTPLipendETRETQPTLS-- 83
Cdd:TIGR03346 7 EALQAAQSlalgRDHQQIEPEHLLKALLDQEGglARPLLQKAGVNVGALRQALEKELERLPKV-----SGPGGQVYLSpd 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520910443 84 FQRVLQRAVFHVQSSGRSEVTGANVLVAIfSEQESHAAYLLKKNDISRLDIVNYIS--HGITKASSSGDEPSSDSfgtes 161
Cdd:TIGR03346 82 LNRLLNLAEKLAQKRGDEFISSEHLLLAL-LDDKGTLGKLLKEAGATADALEAAINavRGGQKVTDANAEDQYEA----- 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520910443 162 gedvssderLESFATNLNHLAKQGQIDPLIGRDKELERTIQVLCRRRKNNPLLVGEAGVGKTAIAEGLAWRIVEGQVPEV 241
Cdd:TIGR03346 156 ---------LEKYARDLTERAREGKLDPVIGRDEEIRRTIQVLSRRTKNNPVLIGEPGVGKTAIVEGLAQRIVNGDVPEG 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520910443 242 IQNSVIYSLDIGSLLAGTKYRGDFEKRFKSILKQLEK-EKDAILFIDEIHTIIGAGAASGGqVDAANLIKPLLSSGKLRC 320
Cdd:TIGR03346 227 LKNKRLLALDMGALIAGAKYRGEFEERLKAVLNEVTKsEGQIILFIDELHTLVGAGKAEGA-MDAGNMLKPALARGELHC 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520910443 321 IGSTTYQEYSNIFEKERALSRRFQKIDIVEPSLDDTTKILMGLKPKYEAHHDVRYTKEALRAAVELSAKYINERHLPDKA 400
Cdd:TIGR03346 306 IGATTLDEYRKYIEKDAALERRFQPVFVDEPSVEDTISILRGLKERYEVHHGVRITDPAIVAAATLSHRYITDRFLPDKA 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520910443 401 IDVIDEAGARVRL----MP--------------------------ASRR------------------------------- 419
Cdd:TIGR03346 386 IDLIDEAAARIRMeidsKPeeldeldrriiqleierealkkekdeASKKrledlekeladleeeyaeleeqwkaekasiq 465
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520910443 420 ----------------------------------------------------------KKTVGVAEIEAMVAKMARIPEK 441
Cdd:TIGR03346 466 giqqikeeieqvrleleqaeregdlakaaelqygklpelekqlqaaeqklgeeqnrllREEVTAEEIAEVVSRWTGIPVS 545
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520910443 442 SVSSSDKDILKNLDKKMKMLVFGQDNAIDVLTESIKLTRAGLGSDNRPVGSFLFAGPTGVGKTEVTVQLSKLL---GIEL 518
Cdd:TIGR03346 546 KMLEGEREKLLHMEEELHERVVGQDEAVEAVSDAIRRSRAGLSDPNRPIGSFLFLGPTGVGKTELAKALAEFLfdsEDAM 625
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520910443 519 LRFDMSEYGERHSVSRLIGAPPGYVGFDQGGLLTDAVIKHPHSVVLLDEIEKAHPDIFNLLLQVMDNGTLTDNNGRKADF 598
Cdd:TIGR03346 626 VRIDMSEYMEKHSVARLIGAPPGYVGYEEGGQLTEAVRRRPYSVVLFDEVEKAHPDVFNVLLQVLDDGRLTDGQGRTVDF 705
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520910443 599 RNVILVMTTNAGVAETVKKSIGMIQQDHSHDAMAEIKKVFTPEFRNRLDHIIWFNALDERVIHQVVDKFIVELQVQLDAR 678
Cdd:TIGR03346 706 RNTVIIMTSNLGSDFIQELAGGDDYEEMREAVMEVLRAHFRPEFLNRIDEIVVFHPLGREQIARIVEIQLGRLRKRLAER 785
|
810 820 830 840 850 860
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 520910443 679 GVSLEVSEDARHWLAVKGYDREMGARPMGRVIQEQLKKPLANELLFGSLVDGGTVKVDLNEDQLT 743
Cdd:TIGR03346 786 KITLELSDAALDFLAEAGYDPVYGARPLKRAIQREIENPLAKKILAGEVAPGDTIRVDVEGGRLV 850
|
|
| clpC |
CHL00095 |
Clp protease ATP binding subunit |
17-740 |
0e+00 |
|
Clp protease ATP binding subunit
Pssm-ID: 214361 [Multi-domain] Cd Length: 821 Bit Score: 648.27 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520910443 17 ARDKRHEFMTVEHLLLALLE--NDAAKEALLACQADIDTLRRE-------LDTFIDQTTPLIPendetRETqptlsfqRV 87
Cdd:CHL00095 20 ARRLGHNFVGTEQILLGLIGegTGIAARALKSMGVTLKDARIEvekiigrGTGFVAVEIPFTP-----RAK-------RV 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520910443 88 LQRAVFHVQSSGRSEVTGANVLVAIFSEQESHAAYLLKK--NDISRL--DIVNYISHGITKASSSGDEpssdsfgtesge 163
Cdd:CHL00095 88 LEMSLEEARDLGHNYIGTEHLLLALLEEGEGVAARVLENlgVDLSKIrsLILNLIGEIIEAILGAEQS------------ 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520910443 164 dVSSDERLESFATNLNHLAKQGQIDPLIGRDKELERTIQVLCRRRKNNPLLVGEAGVGKTAIAEGLAWRIVEGQVPEVIQ 243
Cdd:CHL00095 156 -RSKTPTLEEFGTNLTKEAIDGNLDPVIGREKEIERVIQILGRRTKNNPILIGEPGVGKTAIAEGLAQRIVNRDVPDILE 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520910443 244 NSVIYSLDIGSLLAGTKYRGDFEKRFKSILKQLEKEKDAILFIDEIHTIIGAGAASGGqVDAANLIKPLLSSGKLRCIGS 323
Cdd:CHL00095 235 DKLVITLDIGLLLAGTKYRGEFEERLKRIFDEIQENNNIILVIDEVHTLIGAGAAEGA-IDAANILKPALARGELQCIGA 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520910443 324 TTYQEYSNIFEKERALSRRFQKIDIVEPSLDDTTKILMGLKPKYEAHHDVRYTKEALRAAVELSAKYINERHLPDKAIDV 403
Cdd:CHL00095 314 TTLDEYRKHIEKDPALERRFQPVYVGEPSVEETIEILFGLRSRYEKHHNLSISDKALEAAAKLSDQYIADRFLPDKAIDL 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520910443 404 IDEAGARVRLM-----------------------------------------------------------PASRRKKTVG 424
Cdd:CHL00095 394 LDEAGSRVRLInsrlppaareldkelreilkdkdeaireqdfetakqlrdremevraqiaaiiqskkteeEKRLEVPVVT 473
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520910443 425 VAEIEAMVAKMARIPEKSVSSSDKDILKNLDKKMKMLVFGQDNAIDVLTESIKLTRAGLGSDNRPVGSFLFAGPTGVGKT 504
Cdd:CHL00095 474 EEDIAEIVSAWTGIPVNKLTKSESEKLLHMEETLHKRIIGQDEAVVAVSKAIRRARVGLKNPNRPIASFLFSGPTGVGKT 553
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520910443 505 EVTVQLSKLL-GIE--LLRFDMSEYGERHSVSRLIGAPPGYVGFDQGGLLTDAVIKHPHSVVLLDEIEKAHPDIFNLLLQ 581
Cdd:CHL00095 554 ELTKALASYFfGSEdaMIRLDMSEYMEKHTVSKLIGSPPGYVGYNEGGQLTEAVRKKPYTVVLFDEIEKAHPDIFNLLLQ 633
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520910443 582 VMDNGTLTDNNGRKADFRNVILVMTTNAGvAETVKKSIGMIQQDHSHDAMA-------------EIKKVFTPEFRNRLDH 648
Cdd:CHL00095 634 ILDDGRLTDSKGRTIDFKNTLIIMTSNLG-SKVIETNSGGLGFELSENQLSekqykrlsnlvneELKQFFRPEFLNRLDE 712
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520910443 649 IIWFNALDERVIHQVVDKFIVELQVQLDARGVSLEVSEDARHWLAVKGYDREMGARPMGRVIQEQLKKPLANELLFGSLV 728
Cdd:CHL00095 713 IIVFRQLTKNDVWEIAEIMLKNLFKRLNEQGIQLEVTERIKTLLIEEGYNPLYGARPLRRAIMRLLEDPLAEEVLSFKIK 792
|
810
....*....|..
gi 520910443 729 DGGTVKVDLNED 740
Cdd:CHL00095 793 PGDIIIVDVNDE 804
|
|
| VI_ClpV1 |
TIGR03345 |
type VI secretion ATPase, ClpV1 family; Members of this protein family are homologs of ClpB, ... |
2-723 |
0e+00 |
|
type VI secretion ATPase, ClpV1 family; Members of this protein family are homologs of ClpB, an ATPase associated with chaperone-related functions. These ClpB homologs, designated ClpV1, are a key component of the bacterial pathogenicity-associated type VI secretion system. [Protein fate, Protein and peptide secretion and trafficking, Cellular processes, Pathogenesis]
Pssm-ID: 274528 [Multi-domain] Cd Length: 852 Bit Score: 549.54 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520910443 2 LNKELESSLNGAFARARDKRHEFMTVEHLLLALLENDA--AKEALLACQADIDTLRRELDTFIDQttpLIPENDETretq 79
Cdd:TIGR03345 1 LNPTSRRALEQAAALCVARGHPEVELEHWLLALLDQPDsdLAAILRHFGVDLGRLKADLARALDK---LPRGNTRT---- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520910443 80 PTLS--FQRVLQRAvFHVQSS--GRSEVTGANVLVAIFSEQE-----SHAAYLLKKNDISRLDivnYISHGITKASSSGD 150
Cdd:TIGR03345 74 PVFSphLVELLQEA-WLLASLelGDGRIRSGHLLLALLTDPElrrllGSISPELAKIDREALR---EALPALVEGSAEAS 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520910443 151 EPSSDSFGTESGEDVSSDERLESFATNLNHLAKQGQIDPLIGRDKELERTIQVLCRRRKNNPLLVGEAGVGKTAIAEGLA 230
Cdd:TIGR03345 150 AAAADAAPAGAAAGAAGTSALDQYTTDLTAQAREGKIDPVLGRDDEIRQMIDILLRRRQNNPILTGEAGVGKTAVVEGLA 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520910443 231 WRIVEGQVPEVIQNSVIYSLDIGSLLAGTKYRGDFEKRFKSILKQLEK-EKDAILFIDEIHTIIGAGAASgGQVDAANLI 309
Cdd:TIGR03345 230 LRIAAGDVPPALRNVRLLSLDLGLLQAGASVKGEFENRLKSVIDEVKAsPQPIILFIDEAHTLIGAGGQA-GQGDAANLL 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520910443 310 KPLLSSGKLRCIGSTTYQEYSNIFEKERALSRRFQKIDIVEPSLDDTTKILMGLKPKYEAHHDVRYTKEALRAAVELSAK 389
Cdd:TIGR03345 309 KPALARGELRTIAATTWAEYKKYFEKDPALTRRFQVVKVEEPDEETAIRMLRGLAPVLEKHHGVLILDEAVVAAVELSHR 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520910443 390 YINERHLPDKAIDVIDEAGARVRL----MPAS------------------RRKKTVG----------------------- 424
Cdd:TIGR03345 389 YIPGRQLPDKAVSLLDTACARVALsqnaTPAAledlrrriaaleleldalEREAALGadhderlaelraelaaleaelaa 468
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520910443 425 -----------VAEIEAMVAKMA-----------------RIPEKSVSSSDKD--------------------------- 449
Cdd:TIGR03345 469 learwqqekelVEAILALRAELEadadapaddddalraqlAELEAALASAQGEeplvfpevdaqavaevvadwtgipvgr 548
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520910443 450 --------ILkNLDKKMKMLVFGQDNAIDVLTESIKLTRAGLGSDNRPVGSFLFAGPTGVGKTEVTVQLSKLL-GIE--L 518
Cdd:TIGR03345 549 mvrdeieaVL-SLPDRLAERVIGQDHALEAIAERIRTARAGLEDPRKPLGVFLLVGPSGVGKTETALALAELLyGGEqnL 627
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520910443 519 LRFDMSEYGERHSVSRLIGAPPGYVGFDQGGLLTDAVIKHPHSVVLLDEIEKAHPDIFNLLLQVMDNGTLTDNNGRKADF 598
Cdd:TIGR03345 628 ITINMSEFQEAHTVSRLKGSPPGYVGYGEGGVLTEAVRRKPYSVVLLDEVEKAHPDVLELFYQVFDKGVMEDGEGREIDF 707
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520910443 599 RNVILVMTTNAGVAETVKKSigmIQQDHSHDA-------MAEIKKVFTPEFRNRLDhIIWFNALDERVIHQVVDKFIVEL 671
Cdd:TIGR03345 708 KNTVILLTSNAGSDLIMALC---ADPETAPDPeallealRPELLKVFKPAFLGRMT-VIPYLPLDDDVLAAIVRLKLDRI 783
|
810 820 830 840 850
....*....|....*....|....*....|....*....|....*....|...
gi 520910443 672 QVQLDAR-GVSLEVSEDARHWLAVKGYDREMGARPMGRVIQEQLKKPLANELL 723
Cdd:TIGR03345 784 ARRLKENhGAELVYSEALVEHIVARCTEVESGARNIDAILNQTLLPELSRQIL 836
|
|
| PRK10865 |
PRK10865 |
ATP-dependent chaperone ClpB; |
2-745 |
0e+00 |
|
ATP-dependent chaperone ClpB;
Pssm-ID: 182791 [Multi-domain] Cd Length: 857 Bit Score: 546.75 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520910443 2 LNKELESSLNGAFARARDKRHEFMTVEHLLLALLENDAAKEALLACQADIDTLRreLDTFIDQTTPLIPENDETR-ETQP 80
Cdd:PRK10865 6 LTNKFQLALADAQSLALGHDNQFIEPLHLMSALLNQEGGSVRPLLTSAGINAGQ--LRTDINQALSRLPQVEGTGgDVQP 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520910443 81 TLSFQRVLQRAVFHVQSSGRSEVTGANVLVAIFsEQESHAAYLLKkndisrldivnyiSHGITKASSSgdEPSSDSFGTE 160
Cdd:PRK10865 84 SQDLVRVLNLCDKLAQKRGDNFISSELFVLAAL-ESRGTLADILK-------------AAGATTANIT--QAIEQMRGGE 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520910443 161 SGEDVSS-DER--LESFATNLNHLAKQGQIDPLIGRDKELERTIQVLCRRRKNNPLLVGEAGVGKTAIAEGLAWRIVEGQ 237
Cdd:PRK10865 148 SVNDQGAeDQRqaLKKYTIDLTERAEQGKLDPVIGRDEEIRRTIQVLQRRTKNNPVLIGEPGVGKTAIVEGLAQRIINGE 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520910443 238 VPEVIQNSVIYSLDIGSLLAGTKYRGDFEKRFKSILKQLEK-EKDAILFIDEIHTIIGAGAASGGqVDAANLIKPLLSSG 316
Cdd:PRK10865 228 VPEGLKGRRVLALDMGALVAGAKYRGEFEERLKGVLNDLAKqEGNVILFIDELHTMVGAGKADGA-MDAGNMLKPALARG 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520910443 317 KLRCIGSTTYQEYSNIFEKERALSRRFQKIDIVEPSLDDTTKILMGLKPKYEAHHDVRYTKEALRAAVELSAKYINERHL 396
Cdd:PRK10865 307 ELHCVGATTLDEYRQYIEKDAALERRFQKVFVAEPSVEDTIAILRGLKERYELHHHVQITDPAIVAAATLSHRYIADRQL 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520910443 397 PDKAIDVIDEAGARVRL--------------------------------------------------------------- 413
Cdd:PRK10865 387 PDKAIDLIDEAASSIRMqidskpeeldrldrriiqlkleqqalmkesdeaskkrldmlneelsdkerqyseleeewkaek 466
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520910443 414 -------------------MPASRR------------------------------------KKTVGVAEIEAMVAKMARI 438
Cdd:PRK10865 467 aslsgtqtikaeleqakiaIEQARRvgdlarmselqygkipelekqlaaatqlegktmrllRNKVTDAEIAEVLARWTGI 546
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520910443 439 PEKSVSSSDKDILKNLDKKMKMLVFGQDNAIDVLTESIKLTRAGLGSDNRPVGSFLFAGPTGVGKTEVTVQLSKLL---G 515
Cdd:PRK10865 547 PVSRMLESEREKLLRMEQELHHRVIGQNEAVEAVSNAIRRSRAGLSDPNRPIGSFLFLGPTGVGKTELCKALANFMfdsD 626
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520910443 516 IELLRFDMSEYGERHSVSRLIGAPPGYVGFDQGGLLTDAVIKHPHSVVLLDEIEKAHPDIFNLLLQVMDNGTLTDNNGRK 595
Cdd:PRK10865 627 DAMVRIDMSEFMEKHSVSRLVGAPPGYVGYEEGGYLTEAVRRRPYSVILLDEVEKAHPDVFNILLQVLDDGRLTDGQGRT 706
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520910443 596 ADFRNVILVMTTNAGvAETVKKSIGMIQQDHSHD-AMAEIKKVFTPEFRNRLDHIIWFNALDERVIHQVVDKFIVELQVQ 674
Cdd:PRK10865 707 VDFRNTVVIMTSNLG-SDLIQERFGELDYAHMKElVLGVVSHNFRPEFINRIDEVVVFHPLGEQHIASIAQIQLQRLYKR 785
|
810 820 830 840 850 860 870
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 520910443 675 LDARGVSLEVSEDARHWLAVKGYDREMGARPMGRVIQEQLKKPLANELLFGSLVDGGTVKVDLNEDQLTFK 745
Cdd:PRK10865 786 LEERGYEIHISDEALKLLSENGYDPVYGARPLKRAIQQQIENPLAQQILSGELVPGKVIRLEVNDDRIVAV 856
|
|
| RecA-like_ClpB_Hsp104-like |
cd19499 |
Chaperone protein ClpB/Hsp104 subfamily; Bacterial Caseinolytic peptidase B (ClpB) and ... |
451-652 |
1.65e-83 |
|
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: 1.65e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520910443 451 LKNLDKKMKMLVFGQDNAIDVLTESIKLTRAGLGSDNRPVGSFLFAGPTGVGKTEVTVQLSKLL---GIELLRFDMSEYG 527
Cdd:cd19499 2 LLNLEERLHERVVGQDEAVKAVSDAIRRARAGLSDPNRPIGSFLFLGPTGVGKTELAKALAELLfgdEDNLIRIDMSEYM 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520910443 528 ERHSVSRLIGAPPGYVGFDQGGLLTDAVIKHPHSVVLLDEIEKAHPDIFNLLLQVMDNGTLTDNNGRKADFRNVILVMTT 607
Cdd:cd19499 82 EKHSVSRLIGAPPGYVGYTEGGQLTEAVRRKPYSVVLLDEIEKAHPDVQNLLLQVLDDGRLTDSHGRTVDFKNTIIIMTS 161
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 520910443 608 NAgvaetvkksigmiqqdhshdamaeikkvFTPEFRNRLDHIIWF 652
Cdd:cd19499 162 NH----------------------------FRPEFLNRIDEIVVF 178
|
|
| AAA_2 |
pfam07724 |
AAA domain (Cdc48 subfamily); This Pfam entry includes some of the AAA proteins not detected ... |
488-649 |
7.74e-75 |
|
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: 239.40 E-value: 7.74e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520910443 488 RPVGSFLFAGPTGVGKTEVTVQLSKLLGI---ELLRFDMSEYGERHSVSRLIGAPPGYVGFDQGGLLTDAVIKHPHSVVL 564
Cdd:pfam07724 1 RPIGSFLFLGPTGVGKTELAKALAELLFGderALIRIDMSEYMEEHSVSRLIGAPPGYVGYEEGGQLTEAVRRKPYSIVL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520910443 565 LDEIEKAHPDIFNLLLQVMDNGTLTDNNGRKADFRNVILVMTTNAGVAETVKKSIG---MIQQDHSHDAMAEIKKVFTPE 641
Cdd:pfam07724 81 IDEIEKAHPGVQNDLLQILEGGTLTDKQGRTVDFKNTLFIMTGNFGSEKISDASRLgdsPDYELLKEEVMDLLKKGFIPE 160
|
....*...
gi 520910443 642 FRNRLDHI 649
Cdd:pfam07724 161 FLGRLPII 168
|
|
| AAA_lid_9 |
pfam17871 |
AAA lid domain; This entry represents the alpha helical AAA+ lid domain that is found to the ... |
352-458 |
1.66e-38 |
|
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: 138.39 E-value: 1.66e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520910443 352 SLDDTTKILMGLKPKYEAHHDVRYTKEALRAAVELSAKYINERHLPDKAIDVIDEAGARVRLMPASRRKKtvgVAEIEAM 431
Cdd:pfam17871 1 SVEEAIEILRGLKPKYEKHHGVRISDEALEAAVKLSKRYITDRFLPDKAIDLLDEACARVRLSQESKPEE---LEDLERE 77
|
90 100
....*....|....*....|....*..
gi 520910443 432 VAKMARIPEKSVSSSDKDILKNLDKKM 458
Cdd:pfam17871 78 LAKLEIEKEALEREQDFEKAERLAKLE 104
|
|
| ClpB_D2-small |
smart01086 |
C-terminal, D2-small domain, of ClpB protein; This is the C-terminal domain of ClpB protein, ... |
655-744 |
4.06e-29 |
|
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: 111.00 E-value: 4.06e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520910443 655 LDERVIHQVVDKFIVELQVQLDARGVSLEVSEDARHWLAVKGYDREMGARPMGRVIQEQLKKPLANELLFGSLVDGGTVK 734
Cdd:smart01086 1 LDKEDLVRIVDLPLNALQKRLAEKGITLEFTDEALDWLAEKGYDPKYGARPLRRIIQRELEDPLAELILSGELKDGDTVV 80
|
90
....*....|
gi 520910443 735 VDLNEDQLTF 744
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, ... |
655-735 |
1.07e-28 |
|
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: 109.42 E-value: 1.07e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520910443 655 LDERVIHQVVDKFIVELQVQLDARGVSLEVSEDARHWLAVKGYDREMGARPMGRVIQEQLKKPLANELLFGSLVDGGTVK 734
Cdd:pfam10431 1 LSKEELRKIVDLQLKELQKRLAERGITLELTDAAKDWLAEKGYDPEYGARPLRRAIQREIEDPLAEEILSGELKEGDTVR 80
|
.
gi 520910443 735 V 735
Cdd:pfam10431 81 V 81
|
|
| AAA |
cd00009 |
The AAA+ (ATPases Associated with a wide variety of cellular Activities) superfamily ... |
191-351 |
2.11e-19 |
|
The AAA+ (ATPases Associated with a wide variety of cellular Activities) superfamily represents an ancient group of ATPases belonging to the ASCE (for additional strand, catalytic E) division of the P-loop NTPase fold. The ASCE division also includes ABC, RecA-like, VirD4-like, PilT-like, and SF1/2 helicases. Members of the AAA+ ATPases function as molecular chaperons, ATPase subunits of proteases, helicases, or nucleic-acid stimulated ATPases. The AAA+ proteins contain several distinct features in addition to the conserved alpha-beta-alpha core domain structure and the Walker A and B motifs of the P-loop NTPases.
Pssm-ID: 99707 [Multi-domain] Cd Length: 151 Bit Score: 85.66 E-value: 2.11e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520910443 191 IGRDKELERTIQVLCRRRKNNPLLVGEAGVGKTAIAEGLAWRIVEGQVPeviqnsvIYSLDIGSLLAGTKYRGDFEKRFK 270
Cdd:cd00009 1 VGQEEAIEALREALELPPPKNLLLYGPPGTGKTTLARAIANELFRPGAP-------FLYLNASDLLEGLVVAELFGHFLV 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520910443 271 SILKQL-EKEKDAILFIDEIHTIigAGAASGGQVDAAN-LIKPLLSSGKLRCIGSTTYQEYsniFEKERALSRRFQKIDI 348
Cdd:cd00009 74 RLLFELaEKAKPGVLFIDEIDSL--SRGAQNALLRVLEtLNDLRIDRENVRVIGATNRPLL---GDLDRALYDRLDIRIV 148
|
...
gi 520910443 349 VEP 351
Cdd:cd00009 149 IPL 151
|
|
| AAA |
pfam00004 |
ATPase family associated with various cellular activities (AAA); AAA family proteins often ... |
213-346 |
3.61e-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: 66.85 E-value: 3.61e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520910443 213 LLVGEAGVGKTAIAEGLAWRIvegQVPeviqnsvIYSLDIGSLLAgtKYRGDFEKRFKSILKQLEKEKDAILFIDEIHTI 292
Cdd:pfam00004 2 LLYGPPGTGKTTLAKAVAKEL---GAP-------FIEISGSELVS--KYVGESEKRLRELFEAAKKLAPCVIFIDEIDAL 69
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 520910443 293 IGAGAASGGQV--DAANLIKPLL-----SSGKLRCIGSTTYqeysnIFEKERALSRRFQKI 346
Cdd:pfam00004 70 AGSRGSGGDSEsrRVVNQLLTELdgftsSNSKVIVIAATNR-----PDKLDPALLGRFDRI 125
|
|
| AAA_5 |
pfam07728 |
AAA domain (dynein-related subfamily); This Pfam entry includes some of the AAA proteins not ... |
492-608 |
3.12e-11 |
|
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: 61.54 E-value: 3.12e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520910443 492 SFLFAGPTGVGKTEVTVQLSKLLG-----IELLRFDMSEygerhsvSRLIGappGYVGFDQGGLLTDAVI----KHPHsV 562
Cdd:pfam07728 1 GVLLVGPPGTGKTELAERLAAALSnrpvfYVQLTRDTTE-------EDLFG---RRNIDPGGASWVDGPLvraaREGE-I 69
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 520910443 563 VLLDEIEKAHPDIFNLLLQVMDNGTLTDNNGR---KADFRNVILVMTTN 608
Cdd:pfam07728 70 AVLDEINRANPDVLNSLLSLLDERRLLLPDGGelvKAAPDGFRLIATMN 118
|
|
| AAA |
cd00009 |
The AAA+ (ATPases Associated with a wide variety of cellular Activities) superfamily ... |
463-608 |
3.22e-11 |
|
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: 62.16 E-value: 3.22e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520910443 463 FGQDNAIDVLTESIKLtraglgsdnRPVGSFLFAGPTGVGKTEVT---VQLSKLLGIELLRFDMSEYGERHSVSRLIgap 539
Cdd:cd00009 1 VGQEEAIEALREALEL---------PPPKNLLLYGPPGTGKTTLAraiANELFRPGAPFLYLNASDLLEGLVVAELF--- 68
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 520910443 540 pgyvGFDQGGLLTDAVIKHPHSVVLLDEIEKAHPDIFNLLLQVMDNGtltdnNGRKADFRNVILVMTTN 608
Cdd:cd00009 69 ----GHFLVRLLFELAEKAKPGVLFIDEIDSLSRGAQNALLRVLETL-----NDLRIDRENVRVIGATN 128
|
|
| Clp_N |
pfam02861 |
Clp amino terminal domain, pathogenicity island component; This short domain is found in one ... |
13-63 |
3.46e-10 |
|
Clp amino terminal domain, pathogenicity island component; This short domain is found in one or two copies at the amino terminus of ClpA and ClpB proteins from bacteria and eukaryotes. The function of these domains is uncertain but they may form a protein binding site. In many bacterial species, including E.coli, this region represents the N-terminus of one of the key components of the pathogenicity island complex that injects toxin from one bacterium into another.
Pssm-ID: 460724 [Multi-domain] Cd Length: 53 Bit Score: 55.99 E-value: 3.46e-10
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 520910443 13 AFARARDKRHEFMTVEHLLLALLEND--AAKEALLACQADIDTLRRELDTFID 63
Cdd:pfam02861 1 AQELARALGHQYIGTEHLLLALLEEDdgLAARLLKKAGVDLDALREAIEKLLG 53
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
208-346 |
7.76e-10 |
|
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: 58.15 E-value: 7.76e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520910443 208 RKNNPLLVGEAGVGKTAIAEGLAWRIVEGQVPEVIQN-----SVIYSLDIGSLLAGTKYRGDFEKRFKSILKQLEKEKDA 282
Cdd:smart00382 1 PGEVILIVGPPGSGKTTLARALARELGPPGGGVIYIDgedilEEVLDQLLLIIVGGKKASGSGELRLRLALALARKLKPD 80
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 520910443 283 ILFIDEIHTIIGAGAASGGQVDA-ANLIKPLLSSGKLRCIGSTTYQEysniFEKERALSRRFQKI 346
Cdd:smart00382 81 VLILDEITSLLDAEQEALLLLLEeLRLLLLLKSEKNLTVILTTNDEK----DLGPALLRRRFDRR 141
|
|
| RecA-like_protease |
cd19481 |
proteases similar to RecA; RecA-like NTPases. This family includes the NTP binding domain of ... |
492-608 |
2.73e-08 |
|
proteases similar to RecA; RecA-like NTPases. This family includes the NTP binding domain of F1 and V1 H(+)ATPases, DnaB and related helicases as well as bacterial RecA and related eukaryotic and archaeal recombinases. This group also includes bacterial conjugation proteins and related DNA transfer proteins involved in type II and type IV secretion.
Pssm-ID: 410889 [Multi-domain] Cd Length: 158 Bit Score: 53.83 E-value: 2.73e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520910443 492 SFLFAGPTGVGKTEVTVQLSKLLGIELLRFDMSEYGERHSvsrligappGYVGfDQGGLLTDAVIKHPHSVVLLDEIEKA 571
Cdd:cd19481 28 GILLYGPPGTGKTLLAKALAGELGLPLIVVKLSSLLSKYV---------GESE-KNLRKIFERARRLAPCILFIDEIDAI 97
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 520910443 572 HPD------------IFNLLLQVMDNGTLTDnngrkadfrNVILVMTTN 608
Cdd:cd19481 98 GRKrdssgesgelrrVLNQLLTELDGVNSRS---------KVLVIAATN 137
|
|
| SpoVK |
COG0464 |
AAA+-type ATPase, SpoVK/Ycf46/Vps4 family [Cell wall/membrane/envelope biogenesis, Cell cycle ... |
213-405 |
3.59e-08 |
|
AAA+-type ATPase, SpoVK/Ycf46/Vps4 family [Cell wall/membrane/envelope biogenesis, Cell cycle control, cell division, chromosome partitioning, Signal transduction mechanisms];
Pssm-ID: 440232 [Multi-domain] Cd Length: 397 Bit Score: 56.46 E-value: 3.59e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520910443 213 LLVGEAGVGKTAIAEGLAwRIVEGQVpeviqnsviYSLDIGSLLAgtKYRGDFEKRFKSILKQLEKEKDAILFIDEIHTI 292
Cdd:COG0464 195 LLYGPPGTGKTLLARALA-GELGLPL---------IEVDLSDLVS--KYVGETEKNLREVFDKARGLAPCVLFIDEADAL 262
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520910443 293 IGAGAASGGQVDA----------ANLIKPLLssgklrCIGSTTYQEYSNifekeRALSRRFQ-KIDIVEPSLDDTTKILM 361
Cdd:COG0464 263 AGKRGEVGDGVGRrvvntlltemEELRSDVV------VIAATNRPDLLD-----PALLRRFDeIIFFPLPDAEERLEIFR 331
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 520910443 362 GLKPKYEAHHDVRYTK------------------EALRAAVELSAKYINERHLpDKAIDVID 405
Cdd:COG0464 332 IHLRKRPLDEDVDLEElaeateglsgadirnvvrRAALQALRLGREPVTTEDL-LEALERED 392
|
|
| AAA |
pfam00004 |
ATPase family associated with various cellular activities (AAA); AAA family proteins often ... |
494-652 |
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 520910443 494 LFAGPTGVGKTEVTVQLSKLLGIELLRFDMSEygerhSVSRLIGAPPGYVgfdqGGLLTDAVIKHPhSVVLLDEIEKAHP 573
Cdd:pfam00004 2 LLYGPPGTGKTTLAKAVAKELGAPFIEISGSE-----LVSKYVGESEKRL----RELFEAAKKLAP-CVIFIDEIDALAG 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520910443 574 -----------DIFNLLLQVMDngtltdnnGRKADFRNVILVMTTNagvaetvkkSIGMIqqdhshdamaeikkvfTPEF 642
Cdd:pfam00004 72 srgsggdsesrRVVNQLLTELD--------GFTSSNSKVIVIAATN---------RPDKL----------------DPAL 118
|
170
....*....|
gi 520910443 643 RNRLDHIIWF 652
Cdd:pfam00004 119 LGRFDRIIEF 128
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
494-608 |
6.71e-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: 49.68 E-value: 6.71e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520910443 494 LFAGPTGVGKTEVTVQLSKLL---GIELLRFDMSEYGERHSVSRLIGAPPGYVGFDQGG----LLTDAVIKHPHSVVLLD 566
Cdd:smart00382 6 LIVGPPGSGKTTLARALARELgppGGGVIYIDGEDILEEVLDQLLLIIVGGKKASGSGElrlrLALALARKLKPDVLILD 85
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 520910443 567 EIEKAHPDIFNLLLQVMDNGTLTDNNGRKadfRNVILVMTTN 608
Cdd:smart00382 86 EITSLLDAEQEALLLLLEELRLLLLLKSE---KNLTVILTTN 124
|
|
| RecA-like_protease |
cd19481 |
proteases similar to RecA; RecA-like NTPases. This family includes the NTP binding domain of ... |
213-292 |
1.45e-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: 48.82 E-value: 1.45e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520910443 213 LLVGEAGVGKTAIAEGLAWRIvegqvpeviqNSVIYSLDIGSLLagTKYRGDFEKRFKSILKQLEKEKDAILFIDEIHTI 292
Cdd:cd19481 30 LLYGPPGTGKTLLAKALAGEL----------GLPLIVVKLSSLL--SKYVGESEKNLRKIFERARRLAPCILFIDEIDAI 97
|
|
| COG1223 |
COG1223 |
Predicted ATPase, AAA+ superfamily [General function prediction only]; |
210-406 |
6.35e-06 |
|
Predicted ATPase, AAA+ superfamily [General function prediction only];
Pssm-ID: 440836 [Multi-domain] Cd Length: 246 Bit Score: 48.34 E-value: 6.35e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520910443 210 NNPLLVGEAGVGKTAIAEGLAWRIvegQVPeviqnsvIYSLDIGSLLagTKYRGDFEKRFKSILKQLEKEKdAILFIDEI 289
Cdd:COG1223 36 RKILFYGPPGTGKTMLAEALAGEL---KLP-------LLTVRLDSLI--GSYLGETARNLRKLFDFARRAP-CVIFFDEF 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520910443 290 HTIigagaasGGQVDAANLikpllsSGKLRCIGSTTYQEYSNIFEK-------------ERALSRRFQ-KIDIVEPSLDD 355
Cdd:COG1223 103 DAI-------AKDRGDQND------VGEVKRVVNALLQELDGLPSGsvviaatnhpellDSALWRRFDeVIEFPLPDKEE 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 520910443 356 TTKI----LMGLKPKYEAHHD--------------VRYTKEALRAAVELSAKYINERHLpDKAIDVIDE 406
Cdd:COG1223 170 RKEIlelnLKKFPLPFELDLKklakkleglsgadiEKVLKTALKKAILEDREKVTKEDL-EEALKQRKE 237
|
|
| RecA-like_VPS4-like |
cd19509 |
ATPase domain of VPS4, ATAD1, K, KTNA1, Spastin, FIGL-1 and similar ATPase domains; This ... |
213-345 |
3.54e-05 |
|
ATPase domain of VPS4, ATAD1, K, KTNA1, Spastin, FIGL-1 and similar ATPase domains; This subfamily includes the ATPase domains of vacuolar protein sorting-associated protein 4 (VPS4), ATPase family AAA domain-containing protein 1 (ATAD1, also known as Thorase), Katanin p60 ATPase-containing subunit A1 (KTNA1), Spastin, and Fidgetin-Like 1 (FIGL-1). 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: 410917 [Multi-domain] Cd Length: 163 Bit Score: 44.65 E-value: 3.54e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520910443 213 LLVGEAGVGKTAIAEGLAWRIvegqvpeviqNSVIYSLDIGSLLAgtKYRGDFEKRFKSILKQLEKEKDAILFIDEIHTI 292
Cdd:cd19509 36 LLYGPPGTGKTLLARAVASES----------GSTFFSISASSLVS--KWVGESEKIVRALFALARELQPSIIFIDEIDSL 103
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 520910443 293 IgaGAASGGQVDAANLIKPLL----------SSGKLRCIGSTtyqeySNIFEKERALSRRFQK 345
Cdd:cd19509 104 L--SERGSGEHEASRRVKTEFlvqmdgvlnkPEDRVLVLGAT-----NRPWELDEAFLRRFEK 159
|
|
| PRK13341 |
PRK13341 |
AAA family ATPase; |
185-405 |
4.26e-05 |
|
AAA family ATPase;
Pssm-ID: 237354 [Multi-domain] Cd Length: 725 Bit Score: 46.97 E-value: 4.26e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520910443 185 GQiDPLIGRDKELERTIQVlcrRRKNNPLLVGEAGVGKTAIAeglawRIVEGQVpeviQNSVIYsldIGSLLAGTKyrgD 264
Cdd:PRK13341 32 GQ-DHILGEGRLLRRAIKA---DRVGSLILYGPPGVGKTTLA-----RIIANHT----RAHFSS---LNAVLAGVK---D 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520910443 265 FEKRFKSILKQLEKE-KDAILFIDEIHTIIGAgaasggQVDAanlIKPLLSSGKLRCIGSTTYQEYsniFEKERAL-SR- 341
Cdd:PRK13341 93 LRAEVDRAKERLERHgKRTILFIDEVHRFNKA------QQDA---LLPWVENGTITLIGATTENPY---FEVNKALvSRs 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520910443 342 ---RFQKID------IVEPSLDDTT----KILMGLKPKYEAH------HDVRYTKEALRAAVELSakyinerhlPDKAID 402
Cdd:PRK13341 161 rlfRLKSLSdedlhqLLKRALQDKErgygDRKVDLEPEAEKHlvdvanGDARSLLNALELAVEST---------PPDEDG 231
|
...
gi 520910443 403 VID 405
Cdd:PRK13341 232 LID 234
|
|
| RecA-like_HslU |
cd19498 |
ATP-dependent protease ATPase subunit HslU; HslU is a component of the ATP-dependent protease ... |
494-570 |
6.27e-05 |
|
ATP-dependent protease ATPase subunit HslU; HslU is a component of the ATP-dependent protease HslVU. In HslVU, HslU ATPase serves to unfold and translocate protein substrate, and the HslV protease degrades the unfolded proteins. This RecA-like_HslU subfamily belongs to the RecA-like NTPase family which includes the NTP binding domain of F1 and V1 H(+)ATPases, DnaB and related helicases as well as bacterial RecA and related eukaryotic and archaeal recombinases. The RecA-like NTPase family also includes bacterial conjugation proteins and related DNA transfer proteins involved in type II and type IV secretion.
Pssm-ID: 410906 [Multi-domain] Cd Length: 183 Bit Score: 44.29 E-value: 6.27e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 520910443 494 LFAGPTGVGKTEVTVQLSKLLGIELLRFDMSEYGErhsvsrligapPGYVGFDQGGLLTDAVikhpHSVVLLDEIEK 570
Cdd:cd19498 50 LMIGPTGVGKTEIARRLAKLAGAPFIKVEATKFTE-----------VGYVGRDVESIIRDLV----EGIVFIDEIDK 111
|
|
| CDC48 |
TIGR01243 |
AAA family ATPase, CDC48 subfamily; This subfamily of the AAA family ATPases includes two ... |
213-324 |
9.38e-05 |
|
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: 46.05 E-value: 9.38e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520910443 213 LLVGEAGVGKTAIAEGLAWRIvegqvpeviqNSVIYSLDIGSLLagTKYRGDFEKRFKSILKQLEKEKDAILFIDEIHTI 292
Cdd:TIGR01243 216 LLYGPPGTGKTLLAKAVANEA----------GAYFISINGPEIM--SKYYGESEERLREIFKEAEENAPSIIFIDEIDAI 283
|
90 100 110
....*....|....*....|....*....|....*...
gi 520910443 293 IGAGAASGGQVDAA------NLIKPLLSSGKLRCIGST 324
Cdd:TIGR01243 284 APKREEVTGEVEKRvvaqllTLMDGLKGRGRVIVIGAT 321
|
|
| AAA_16 |
pfam13191 |
AAA ATPase domain; This family of domains contain a P-loop motif that is characteriztic of the ... |
189-290 |
1.54e-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: 1.54e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520910443 189 PLIGRDKELERTIQVLCRRRKNNP---LLVGEAGVGKTAIAEGLA-------WRIVEGQVPEVI----------QNSVIY 248
Cdd:pfam13191 1 RLVGREEELEQLLDALDRVRSGRPpsvLLTGEAGTGKTTLLRELLralerdgGYFLRGKCDENLpyspllealtREGLLR 80
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 520910443 249 SLD---------------IGSLLAGTKYRGDFEKRFKSILKQL-----EKEKDAILFIDEIH 290
Cdd:pfam13191 81 QLLdelesslleawraalLEALAPVPELPGDLAERLLDLLLRLldllaRGERPLVLVLDDLQ 142
|
|
| RecA-like_VPS4 |
cd19521 |
ATPase domain of vacuolar protein sorting-associated protein 4; Vacuolar protein ... |
213-345 |
1.59e-04 |
|
ATPase domain of vacuolar protein sorting-associated protein 4; Vacuolar protein sorting-associated protein 4 (Vps4) is believed to be involved in intracellular protein transport out of a prevacuolar endosomal compartment. 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: 410929 [Multi-domain] Cd Length: 170 Bit Score: 42.93 E-value: 1.59e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520910443 213 LLVGEAGVGKTAIAEGLAWRIvegqvpeviqNSVIYSLDIGSLLagTKYRGDFEKRFKSILKQLEKEKDAILFIDEIHTI 292
Cdd:cd19521 44 LLYGPPGTGKSYLAKAVATEA----------NSTFFSVSSSDLV--SKWMGESEKLVKQLFAMARENKPSIIFIDEVDSL 111
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 520910443 293 igAGAASGGQVDAANLIKPLL---------SSGKLRCIGSTtyqeysNI-FEKERALSRRFQK 345
Cdd:cd19521 112 --CGTRGEGESEASRRIKTELlvqmngvgnDSQGVLVLGAT------NIpWQLDSAIRRRFEK 166
|
|
| RecA-like_Lon |
cd19500 |
lon protease homolog 2 peroxisomal; Lon protease (also known as Lon peptidase) is an ... |
494-608 |
1.60e-04 |
|
lon protease homolog 2 peroxisomal; Lon protease (also known as Lon peptidase) is an evolutionarily conserved ATP-dependent serine protease, present in bacteria and eukaryotic mitochondria and peroxisomes, which mediates the selective degradation of mutant and abnormal proteins as well as certain short-lived regulatory proteins. Lon protease is both an ATP-dependent peptidase and a protein-activated ATPase. This RecA-like Lon 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: 410908 [Multi-domain] Cd Length: 182 Bit Score: 43.32 E-value: 1.60e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520910443 494 LFAGPTGVGKTEVTVQLSKLLGIELLRF------DMSEY-GERHSvsrLIGAPPGYVgfDQGglLTDAVIKHPhsVVLLD 566
Cdd:cd19500 41 CLVGPPGVGKTSLGKSIARALGRKFVRIslggvrDEAEIrGHRRT---YVGAMPGRI--IQA--LKKAGTNNP--VFLLD 111
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 520910443 567 EIEK----AHPDIFNLLLQVMD---NGTLTDNN-GRKADFRNVILVMTTN 608
Cdd:cd19500 112 EIDKigssFRGDPASALLEVLDpeqNSTFSDHYlDVPFDLSKVLFIATAN 161
|
|
| SpoVK |
COG0464 |
AAA+-type ATPase, SpoVK/Ycf46/Vps4 family [Cell wall/membrane/envelope biogenesis, Cell cycle ... |
488-684 |
2.12e-04 |
|
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: 44.52 E-value: 2.12e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520910443 488 RPVGSFLFAGPTGVGKTEVTVQLSKLLGIELLRFDMSEygerhsvsrLIGappGYVG---------FDQgglltdaVIKH 558
Cdd:COG0464 189 PPPRGLLLYGPPGTGKTLLARALAGELGLPLIEVDLSD---------LVS---KYVGeteknlrevFDK-------ARGL 249
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520910443 559 PHSVVLLDEIEKAHPD-----------IFNLLLQVMDNGTltdnngrkadfRNVILVMTTNAgvaetvkksIGMIqqDhs 627
Cdd:COG0464 250 APCVLFIDEADALAGKrgevgdgvgrrVVNTLLTEMEELR-----------SDVVVIAATNR---------PDLL--D-- 305
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 520910443 628 hdamaeikkvftPEFRNRLDHIIWFNALDERVIHQVvdkfiveLQVQLDARGVSLEV 684
Cdd:COG0464 306 ------------PALLRRFDEIIFFPLPDAEERLEI-------FRIHLRKRPLDEDV 343
|
|
| RPT1 |
COG1222 |
ATP-dependent 26S proteasome regulatory subunit [Posttranslational modification, protein ... |
213-442 |
2.90e-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: 2.90e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520910443 213 LLVGEAGVGKTAIAEGLAWRIvegqvpeviqNSVIYSLDIGSLLagTKYRGDFEKRFKSILKQLEKEKDAILFIDEIHTI 292
Cdd:COG1222 116 LLYGPPGTGKTLLAKAVAGEL----------GAPFIRVRGSELV--SKYIGEGARNVREVFELAREKAPSIIFIDEIDAI 183
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520910443 293 IGA--GAASGGQVDaaNLIKPLL-------SSGKLRCIGSTTYQEysnifEKERALSR--RF-QKIDIVEPSLDDTTKIL 360
Cdd:COG1222 184 AARrtDDGTSGEVQ--RTVNQLLaeldgfeSRGDVLIIAATNRPD-----LLDPALLRpgRFdRVIEVPLPDEEAREEIL 256
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520910443 361 MGLKPKYEAHHDVRYTKEALRAAvELSAKYINErhlpdkaidVIDEAGARVrlmpASRRKKTVGVAEIEAMVAKMARIPE 440
Cdd:COG1222 257 KIHLRDMPLADDVDLDKLAKLTE-GFSGADLKA---------IVTEAGMFA----IREGRDTVTMEDLEKAIEKVKKKTE 322
|
..
gi 520910443 441 KS 442
Cdd:COG1222 323 TA 324
|
|
| RecA-like_CDC48_NLV2_r1-like |
cd19503 |
first of two ATPase domains of CDC48 and NLV2, and similar ATPase domains; CDC48 in yeast and ... |
213-324 |
3.79e-04 |
|
first of two ATPase domains of CDC48 and NLV2, and similar ATPase domains; CDC48 in yeast and p97 or VCP metazoans is an ATP-dependent molecular chaperone which plays an essential role in many cellular processes, by segregating polyubiquitinated proteins from complexes or membranes. Cdc48/p97 consists of an N-terminal domain and two ATPase domains; this subfamily represents the first of the two ATPase domains. This subfamily also includes the first of the two ATPase domains of NVL (nuclear VCP-like protein) 2, an isoform of NVL mainly present in the nucleolus, which is involved in ribosome biogenesis, in telomerase assembly and the regulation of telomerase activity, and in pre-rRNA processing. This subfamily belongs to the RecA-like NTPase family which includes the NTP binding domain of F1 and V1 H(+)ATPases, DnaB and related helicases as well as bacterial RecA and related eukaryotic and archaeal recombinases. The RecA-like NTPase family also includes bacterial conjugation proteins and related DNA transfer proteins involved in type II and type IV secretion.
Pssm-ID: 410911 [Multi-domain] Cd Length: 165 Bit Score: 41.89 E-value: 3.79e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520910443 213 LLVGEAGVGKTAIAEGLAwRIVEGQVPEVIQNSVIysldigsllagTKYRGDFEKRFKSILKQLEKEKDAILFIDEIHTI 292
Cdd:cd19503 38 LLHGPPGTGKTLLARAVA-NEAGANFLSISGPSIV-----------SKYLGESEKNLREIFEEARSHAPSIIFIDEIDAL 105
|
90 100 110
....*....|....*....|....*....|....*...
gi 520910443 293 IGAGAASGGQVDAA------NLIKPLLSSGKLRCIGST 324
Cdd:cd19503 106 APKREEDQREVERRvvaqllTLMDGMSSRGKVVVIAAT 143
|
|
| RecA-like_CDC48_r1-like |
cd19519 |
first of two ATPase domains of CDC48 and similar ATPase domains; CDC48 in yeast and p97 or VCP ... |
213-304 |
3.89e-04 |
|
first of two ATPase domains of CDC48 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. CDC48's roles include in the fragmentation of Golgi stacks during mitosis and for their reassembly after mitosis, and in the formation of the nuclear envelope, and of the transitional endoplasmic reticulum (tER). This RecA-like_cdc48_r1-like subfamily belongs to the RecA-like 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: 410927 [Multi-domain] Cd Length: 166 Bit Score: 41.65 E-value: 3.89e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520910443 213 LLVGEAGVGKTAIAEGLA------WRIVEGqvPEVIqnsviysldigsllagTKYRGDFEKRFKSILKQLEKEKDAILFI 286
Cdd:cd19519 38 LLYGPPGTGKTLIARAVAnetgafFFLING--PEIM----------------SKLAGESESNLRKAFEEAEKNAPAIIFI 99
|
90
....*....|....*...
gi 520910443 287 DEIHTIIGAGAASGGQVD 304
Cdd:cd19519 100 DEIDAIAPKREKTHGEVE 117
|
|
| AAA_5 |
pfam07728 |
AAA domain (dynein-related subfamily); This Pfam entry includes some of the AAA proteins not ... |
213-292 |
5.73e-04 |
|
AAA domain (dynein-related subfamily); This Pfam entry includes some of the AAA proteins not detected by the pfam00004 model.
Pssm-ID: 400191 [Multi-domain] Cd Length: 135 Bit Score: 40.74 E-value: 5.73e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520910443 213 LLVGEAGVGKTAIAEGLAwRIVEGQVPEVIQNS-------VIYSLDIGSLLAgtkyrgdfeKRFKSILKQLEKEKdAILF 285
Cdd:pfam07728 3 LLVGPPGTGKTELAERLA-AALSNRPVFYVQLTrdtteedLFGRRNIDPGGA---------SWVDGPLVRAAREG-EIAV 71
|
....*..
gi 520910443 286 IDEIHTI 292
Cdd:pfam07728 72 LDEINRA 78
|
|
| RecA-like_Ycf46-like |
cd19507 |
ATPase domain of Ycf46 and similar ATPase domains; Ycf46 may play a role in the regulation of ... |
213-301 |
1.78e-03 |
|
ATPase domain of Ycf46 and similar ATPase domains; Ycf46 may play a role in the regulation of photosynthesis in cyanobacteria, especially in CO2 uptake and utilization. This subfamily belongs to the RecA-like NTPase family which includes the NTP binding domain of F1 and V1 H(+)ATPases, DnaB and related helicases as well as bacterial RecA and related eukaryotic and archaeal recombinases. The RecA-like NTPase family also includes bacterial conjugation proteins and related DNA transfer proteins involved in type II and type IV secretion.
Pssm-ID: 410915 [Multi-domain] Cd Length: 161 Bit Score: 39.66 E-value: 1.78e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520910443 213 LLVGEAGVGKTAIAEGLA--WrivegQVPeviqnsvIYSLDIGSLLAGtkYRGDFEKRFKSILKQLEKEKDAILFIDEIH 290
Cdd:cd19507 35 LLVGIQGTGKSLTAKAIAgvW-----QLP-------LLRLDMGRLFGG--LVGESESRLRQMIQTAEAIAPCVLWIDEIE 100
|
90
....*....|.
gi 520910443 291 TIIGaGAASGG 301
Cdd:cd19507 101 KGFS-NADSKG 110
|
|
| RecA-like_HslU |
cd19498 |
ATP-dependent protease ATPase subunit HslU; HslU is a component of the ATP-dependent protease ... |
210-313 |
4.83e-03 |
|
ATP-dependent protease ATPase subunit HslU; HslU is a component of the ATP-dependent protease HslVU. In HslVU, HslU ATPase serves to unfold and translocate protein substrate, and the HslV protease degrades the unfolded proteins. This RecA-like_HslU subfamily belongs to the RecA-like NTPase family which includes the NTP binding domain of F1 and V1 H(+)ATPases, DnaB and related helicases as well as bacterial RecA and related eukaryotic and archaeal recombinases. The RecA-like NTPase family also includes bacterial conjugation proteins and related DNA transfer proteins involved in type II and type IV secretion.
Pssm-ID: 410906 [Multi-domain] Cd Length: 183 Bit Score: 38.90 E-value: 4.83e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520910443 210 NNPLLVGEAGVGKTAIAEGLAwRIVEGQVPEViqnsviysldigsllAGTKYR--GDFEKRFKSILKQLekeKDAILFID 287
Cdd:cd19498 47 KNILMIGPTGVGKTEIARRLA-KLAGAPFIKV---------------EATKFTevGYVGRDVESIIRDL---VEGIVFID 107
|
90 100
....*....|....*....|....*.
gi 520910443 288 EIHTIIGAGAASGGQVDAANLIKPLL 313
Cdd:cd19498 108 EIDKIAKRGGSSGPDVSREGVQRDLL 133
|
|
| DNA_pol3_delta2 |
pfam13177 |
DNA polymerase III, delta subunit; DNA polymerase III, delta subunit (EC 2.7.7.7) is required ... |
464-514 |
8.40e-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: 37.57 E-value: 8.40e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 520910443 464 GQDNAIDVLTESIKltraglgsDNRPVGSFLFAGPTGVGKTEVTVQLSKLL 514
Cdd:pfam13177 1 GQPEAIQLLQNSLE--------NGRLSHAYLFSGPEGVGKLELALAFAKAL 43
|
|
| |
