|
Name |
Accession |
Description |
Interval |
E-value |
| clpA |
PRK11034 |
ATP-dependent Clp protease ATP-binding subunit; Provisional |
1-759 |
0e+00 |
|
ATP-dependent Clp protease ATP-binding subunit; Provisional
Pssm-ID: 236828 [Multi-domain] Cd Length: 758 Bit Score: 1589.09 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2021509219 1 MLNQELELSLNMAFARAREHRHEFMTVEHLLLALLSNPSAREALEACSVDLVALRQELEAFIEQTTPVLPATEEERDTQP 80
Cdd:PRK11034 1 MLNQELELSLNMAFARAREHRHEFMTVEHLLLALLSNPSAREALEACSVDLVALRQELEAFIEQTTPVLPASEEERDTQP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2021509219 81 TLSFQRVLQRAVFHVQSSGRSEVTGANVLVAIFSEQESQAAYLLRKHEVSRLDVVNFISHGTRKDEPSQPSENnASQPGN 160
Cdd:PRK11034 81 TLSFQRVLQRAVFHVQSSGRSEVTGANVLVAIFSEQESQAAYLLRKHEVSRLDVVNFISHGTRKDEPSQSSDP-GSQPNS 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2021509219 161 EEQAGGEDRMENFTTNLNQLARVGGIDPLIGRDKELERAIQVLCRRRKNNPLLVGESGVGKTAIAEGLAWRIVQGDVPEV 240
Cdd:PRK11034 160 EEQAGGEERMENFTTNLNQLARVGGIDPLIGREKELERAIQVLCRRRKNNPLLVGESGVGKTAIAEGLAWRIVQGDVPEV 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2021509219 241 MADCTIYSLDIGSLLAGTKYRGDFEKRFKALLKQLEQDTNSILFIDEIHTIIGAGAASGGQVDAANLIKPLLSGGKIRVI 320
Cdd:PRK11034 240 MADCTIYSLDIGSLLAGTKYRGDFEKRFKALLKQLEQDTNSILFIDEIHTIIGAGAASGGQVDAANLIKPLLSSGKIRVI 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2021509219 321 GSTTYQEFSNIFEKDRALARRFQKIDVTEPSVEETVQIINGLKPKYEAHHDVRYTAKAVRAAVELAVKYINDRHLPDKAI 400
Cdd:PRK11034 320 GSTTYQEFSNIFEKDRALARRFQKIDITEPSIEETVQIINGLKPKYEAHHDVRYTAKAVRAAVELAVKYINDRHLPDKAI 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2021509219 401 DVIDEAGARARLMPVSKRKKTVNVADIESVVARIARIPEKSVSRSDRDTLKNLGDRLKMLVFGQDKAIEALTEAIKMARA 480
Cdd:PRK11034 400 DVIDEAGARARLMPVSKRKKTVNVADIESVVARIARIPEKSVSQSDRDTLKNLGDRLKMLVFGQDKAIEALTEAIKMSRA 479
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2021509219 481 GLGHEHKPVGSFLFAGPTGVGKTEVTVQLAKALGIELLRFDMSEYMERHTVSRLIGAPPGYVGFDQGGLLTDAVIKHPHA 560
Cdd:PRK11034 480 GLGHEHKPVGSFLFAGPTGVGKTEVTVQLSKALGIELLRFDMSEYMERHTVSRLIGAPPGYVGFDQGGLLTDAVIKHPHA 559
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2021509219 561 VLLLDEIEKAHPDVFNILLQVMDNGTLTDNNGRKADFRNVVLVMTTNAGVRETERKSIGLIQQDNSTDAMEEIKKIFTPE 640
Cdd:PRK11034 560 VLLLDEIEKAHPDVFNLLLQVMDNGTLTDNNGRKADFRNVVLVMTTNAGVRETERKSIGLIHQDNSTDAMEEIKKIFTPE 639
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2021509219 641 FRNRLDNIIWFDHLSTTVIHQVVDKFIVELQVQLDQKGVSLEVSQEARDWLAEKGYDRAMGARPMARVIQDNLKKPLANE 720
Cdd:PRK11034 640 FRNRLDNIIWFDHLSTDVIHQVVDKFIVELQAQLDQKGVSLEVSQEARDWLAEKGYDRAMGARPMARVIQDNLKKPLANE 719
|
730 740 750
....*....|....*....|....*....|....*....
gi 2021509219 721 LLFGSLVDGGQVTVELDKANNVLTYGFHSAQKHKPEAAH 759
Cdd:PRK11034 720 LLFGSLVDGGQVTVALDKEKNELTYGFQSAQKHKAEAAH 758
|
|
| ClpA |
TIGR02639 |
ATP-dependent Clp protease ATP-binding subunit clpA; [Protein fate, Degradation of proteins, ... |
2-736 |
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: 1126.27 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2021509219 2 LNQELELSLNMAFARAREHRHEFMTVEHLLLALLSNPSAREALEACSVDLVALRQELEAFIEQTTPVLPaTEEERDTQPT 81
Cdd:TIGR02639 1 ISEELERILSDALEEAKERRHEFVTLEHLLLALLDDNEAIEILEECGGDVELLRKRLEDYLEENLPVIP-EDIDEEPEQT 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2021509219 82 LSFQRVLQRAVFHVQSSGRSEVTGANVLVAIFSEQESQAAYLLRKHEVSRLDVVNFISHGTRKDEPSQPSEnnaSQPGNE 161
Cdd:TIGR02639 80 VGVQRVIQRALLHVKSAGKKEIDIGDLLVALFDEEDSHASYFLKSQGITRLDILNYISHGISKDDGKDQLG---EEAGKE 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2021509219 162 EQAGgEDRMENFTTNLNQLARVGGIDPLIGRDKELERAIQVLCRRRKNNPLLVGESGVGKTAIAEGLAWRIVQGDVPEVM 241
Cdd:TIGR02639 157 EEKG-QDALEKYTVDLTEKAKNGKIDPLIGREDELERTIQVLCRRKKNNPLLVGEPGVGKTAIVEGLALRIAEGKVPERL 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2021509219 242 ADCTIYSLDIGSLLAGTKYRGDFEKRFKALLKQLEQDTNSILFIDEIHTIIGAGAASGGQVDAANLIKPLLSGGKIRVIG 321
Cdd:TIGR02639 236 KNAKIYSLDMGTLLAGTKYRGDFEERLKAVVSEIEKEPNAILFIDEIHTIVGAGATSGGSMDASNLLKPALSSGKIRCIG 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2021509219 322 STTYQEFSNIFEKDRALARRFQKIDVTEPSVEETVQIINGLKPKYEAHHDVRYTAKAVRAAVELAVKYINDRHLPDKAID 401
Cdd:TIGR02639 316 STTYEEYKNHFEKDRALSRRFQKIDVGEPSIEETVKILKGLKEQYEEFHHVKYSDEALEAAVELSARYINDRFLPDKAID 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2021509219 402 VIDEAGARARLMPVSKRKKTVNVADIESVVARIARIPEKSVSRSDRDTLKNLGDRLKMLVFGQDKAIEALTEAIKMARAG 481
Cdd:TIGR02639 396 VIDEAGAAFRLRPKAKKKANVNVKDIENVVAKMAKIPVKTVSSDDREQLKNLEKNLKAKIFGQDEAIDQLVSAIKRSRAG 475
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2021509219 482 LGHEHKPVGSFLFAGPTGVGKTEVTVQLAKALGIELLRFDMSEYMERHTVSRLIGAPPGYVGFDQGGLLTDAVIKHPHAV 561
Cdd:TIGR02639 476 LGDPNKPVGSFLFVGPTGVGKTELAKQLAEELGVHLLRFDMSEYMEKHTVSRLIGSPPGYVGFEQGGLLTDAVRKHPHCV 555
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2021509219 562 LLLDEIEKAHPDVFNILLQVMDNGTLTDNNGRKADFRNVVLVMTTNAGVRETERKSIGLIqQDNSTDAMEE-IKKIFTPE 640
Cdd:TIGR02639 556 LLLDEIEKAHPDIYNILLQVMDYATLTDNNGRKADFRNVILIMTSNAGASEMSKPPIGFG-GENRESKSLKaIKKLFSPE 634
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2021509219 641 FRNRLDNIIWFDHLSTTVIHQVVDKFIVELQVQLDQKGVSLEVSQEARDWLAEKGYDRAMGARPMARVIQDNLKKPLANE 720
Cdd:TIGR02639 635 FRNRLDAIIHFNDLSEEMAEKIVKKFLDELQDQLNEKNIELELTDDAKKYLAEKGYDEEFGARPLARVIQEEIKKPLSDE 714
|
730
....*....|....*.
gi 2021509219 721 LLFGSLVDGGQVTVEL 736
Cdd:TIGR02639 715 ILFGKLKKGGSVKISL 730
|
|
| ClpA |
COG0542 |
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ... |
2-738 |
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: 862.85 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2021509219 2 LNQELELSLNMAFARAREHRHEFMTVEHLLLALLSNPS--AREALEACSVDLVALRQELEAFIEQTTPVLPATEeerdtQ 79
Cdd:COG0542 6 FTEKAQEALEAAQELARRLGHQEVEPEHLLLALLEQGEglAAKLLRKLGVDLDALREELEEALGRLPKVSGSSG-----Q 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2021509219 80 PTLS--FQRVLQRAVFHVQSSGRSEVTGANVLVAIFSEQESQAAYLLRKHEVSR---LDVVNFISHGTRKDEPSQPSENN 154
Cdd:COG0542 81 PYLSprLKRVLELAELEARKLGDEYISTEHLLLALLREGEGVAARILKKLGITLealREALEELRGGSRVTSQNPESKTP 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2021509219 155 AsqpgneeqaggedrMENFTTNLNQLARVGGIDPLIGRDKELERAIQVLCRRRKNNPLLVGESGVGKTAIAEGLAWRIVQ 234
Cdd:COG0542 161 A--------------LDKYGRDLTELAREGKLDPVIGRDEEIRRVIQILSRRTKNNPVLIGEPGVGKTAIVEGLAQRIVN 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2021509219 235 GDVPEVMADCTIYSLDIGSLLAGTKYRGDFEKRFKALLKQLEQ-DTNSILFIDEIHTIIGAGAASgGQVDAANLIKPLLS 313
Cdd:COG0542 227 GDVPESLKDKRVLSLDLGALVAGAKYRGEFEERLKAVLDEVKKsEGNIILFIDELHTLVGAGGAE-GAMDAANLLKPALA 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2021509219 314 GGKIRVIGSTTYQEFSNIFEKDRALARRFQKIDVTEPSVEETVQIINGLKPKYEAHHDVRYTAKAVRAAVELAVKYINDR 393
Cdd:COG0542 306 RGELRCIGATTLDEYRKYIEKDAALERRFQPVLVEEPSVEDTISILRGLKERYEAHHGVRITDEALVAAVRLSDRYITDR 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2021509219 394 HLPDKAIDVIDEAGARARLMPVSK-------------------------------------------------------- 417
Cdd:COG0542 386 FLPDKAIDLIDEAAARVRMEIDSKpeeldelerrleqleiekealkkeqdeasferlaelrdelaeleeelealkarwea 465
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2021509219 418 ------------------------------------------RKKTVNVADIESVVARIARIPEKSVSRSDRDTLKNLGD 455
Cdd:COG0542 466 ekelieeiqelkeeleqrygkipelekelaeleeelaelaplLREEVTEEDIAEVVSRWTGIPVGKLLEGEREKLLNLEE 545
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2021509219 456 RLKMLVFGQDKAIEALTEAIKMARAGLGHEHKPVGSFLFAGPTGVGKTEvtvqLAKAL-----GIE--LLRFDMSEYMER 528
Cdd:COG0542 546 ELHERVIGQDEAVEAVADAIRRSRAGLKDPNRPIGSFLFLGPTGVGKTE----LAKALaeflfGDEdaLIRIDMSEYMEK 621
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2021509219 529 HTVSRLIGAPPGYVGFDQGGLLTDAVIKHPHAVLLLDEIEKAHPDVFNILLQVMDNGTLTDNNGRKADFRNVVLVMTTNA 608
Cdd:COG0542 622 HSVSRLIGAPPGYVGYEEGGQLTEAVRRRPYSVVLLDEIEKAHPDVFNILLQVLDDGRLTDGQGRTVDFRNTIIIMTSNI 701
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2021509219 609 GVRE-TERKSIGLIQQDNSTDAMEEIKKIFTPEFRNRLDNIIWFDHLSTTVIHQVVDKFIVELQVQLDQKGVSLEVSQEA 687
Cdd:COG0542 702 GSELiLDLAEDEPDYEEMKEAVMEELKKHFRPEFLNRIDEIIVFHPLSKEELRKIVDLQLKRLRKRLAERGITLELTDAA 781
|
810 820 830 840 850
....*....|....*....|....*....|....*....|....*....|.
gi 2021509219 688 RDWLAEKGYDRAMGARPMARVIQDNLKKPLANELLFGSLVDGGQVTVELDK 738
Cdd:COG0542 782 KDFLAEKGYDPEYGARPLKRAIQRELEDPLAEEILAGEIKEGDTITVDVDD 832
|
|
| chaperone_ClpB |
TIGR03346 |
ATP-dependent chaperone ClpB; Members of this protein family are the bacterial ATP-dependent ... |
17-737 |
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: 680.91 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2021509219 17 AREHRHEFMTVEHLLLALL--SNPSAREALEACSVDLVALRQELEAFIEQTTPVLPATEeerDTQPTLSFQRVLQRAVFH 94
Cdd:TIGR03346 16 ALGRDHQQIEPEHLLKALLdqEGGLARPLLQKAGVNVGALRQALEKELERLPKVSGPGG---QVYLSPDLNRLLNLAEKL 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2021509219 95 VQSSGRSEVTGANVLVAIfSEQESQAAYLLRKHEVSRLDVVNFIsHGTRKDEpsqpsenNASQPGNEEQaggEDRMENFT 174
Cdd:TIGR03346 93 AQKRGDEFISSEHLLLAL-LDDKGTLGKLLKEAGATADALEAAI-NAVRGGQ-------KVTDANAEDQ---YEALEKYA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2021509219 175 TNLNQLARVGGIDPLIGRDKELERAIQVLCRRRKNNPLLVGESGVGKTAIAEGLAWRIVQGDVPEVMADCTIYSLDIGSL 254
Cdd:TIGR03346 161 RDLTERAREGKLDPVIGRDEEIRRTIQVLSRRTKNNPVLIGEPGVGKTAIVEGLAQRIVNGDVPEGLKNKRLLALDMGAL 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2021509219 255 LAGTKYRGDFEKRFKALLKQLE-QDTNSILFIDEIHTIIGAGAASGGqVDAANLIKPLLSGGKIRVIGSTTYQEFSNIFE 333
Cdd:TIGR03346 241 IAGAKYRGEFEERLKAVLNEVTkSEGQIILFIDELHTLVGAGKAEGA-MDAGNMLKPALARGELHCIGATTLDEYRKYIE 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2021509219 334 KDRALARRFQKIDVTEPSVEETVQIINGLKPKYEAHHDVRYTAKAVRAAVELAVKYINDRHLPDKAIDVIDEAGARARL- 412
Cdd:TIGR03346 320 KDAALERRFQPVFVDEPSVEDTISILRGLKERYEVHHGVRITDPAIVAAATLSHRYITDRFLPDKAIDLIDEAAARIRMe 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2021509219 413 ---MP--------------------------------------------------------------------------- 414
Cdd:TIGR03346 400 idsKPeeldeldrriiqleierealkkekdeaskkrledlekeladleeeyaeleeqwkaekasiqgiqqikeeieqvrl 479
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2021509219 415 ---VSKR-------------------------------------KKTVNVADIESVVARIARIPeksVSR---SDRDTLK 451
Cdd:TIGR03346 480 eleQAERegdlakaaelqygklpelekqlqaaeqklgeeqnrllREEVTAEEIAEVVSRWTGIP---VSKmleGEREKLL 556
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2021509219 452 NLGDRLKMLVFGQDKAIEALTEAIKMARAGLGHEHKPVGSFLFAGPTGVGKTEvtvqLAKALGIEL-------LRFDMSE 524
Cdd:TIGR03346 557 HMEEELHERVVGQDEAVEAVSDAIRRSRAGLSDPNRPIGSFLFLGPTGVGKTE----LAKALAEFLfdsedamVRIDMSE 632
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2021509219 525 YMERHTVSRLIGAPPGYVGFDQGGLLTDAVIKHPHAVLLLDEIEKAHPDVFNILLQVMDNGTLTDNNGRKADFRNVVLVM 604
Cdd:TIGR03346 633 YMEKHSVARLIGAPPGYVGYEEGGQLTEAVRRRPYSVVLFDEVEKAHPDVFNVLLQVLDDGRLTDGQGRTVDFRNTVIIM 712
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2021509219 605 TTNAGVRETERKSIGLIQQDNSTDAMEEIKKIFTPEFRNRLDNIIWFDHLSTTVIHQVVDKFIVELQVQLDQKGVSLEVS 684
Cdd:TIGR03346 713 TSNLGSDFIQELAGGDDYEEMREAVMEVLRAHFRPEFLNRIDEIVVFHPLGREQIARIVEIQLGRLRKRLAERKITLELS 792
|
810 820 830 840 850
....*....|....*....|....*....|....*....|....*....|...
gi 2021509219 685 QEARDWLAEKGYDRAMGARPMARVIQDNLKKPLANELLFGSLVDGGQVTVELD 737
Cdd:TIGR03346 793 DAALDFLAEAGYDPVYGARPLKRAIQREIENPLAKKILAGEVAPGDTIRVDVE 845
|
|
| clpC |
CHL00095 |
Clp protease ATP binding subunit |
1-745 |
0e+00 |
|
Clp protease ATP binding subunit
Pssm-ID: 214361 [Multi-domain] Cd Length: 821 Bit Score: 675.23 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2021509219 1 MLNQELelslnmafarAREHRHEFMTVEHLLLALL--SNPSAREALEACSVDLVALRQELEAFIEQTTPVLpATEeerdT 78
Cdd:CHL00095 14 MLSQEE----------ARRLGHNFVGTEQILLGLIgeGTGIAARALKSMGVTLKDARIEVEKIIGRGTGFV-AVE----I 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2021509219 79 QPTLSFQRVLQRAVFHVQSSGRSEVTGANVLVAIFSEQESQAAYLLRKHEVS----RLDVVNFIShgtrkdepsqpsENN 154
Cdd:CHL00095 79 PFTPRAKRVLEMSLEEARDLGHNYIGTEHLLLALLEEGEGVAARVLENLGVDlskiRSLILNLIG------------EII 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2021509219 155 ASQPGNEEQAGGEDRMENFTTNLNQLARVGGIDPLIGRDKELERAIQVLCRRRKNNPLLVGESGVGKTAIAEGLAWRIVQ 234
Cdd:CHL00095 147 EAILGAEQSRSKTPTLEEFGTNLTKEAIDGNLDPVIGREKEIERVIQILGRRTKNNPILIGEPGVGKTAIAEGLAQRIVN 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2021509219 235 GDVPEVMADCTIYSLDIGSLLAGTKYRGDFEKRFKALLKQLEQDTNSILFIDEIHTIIGAGAASGGqVDAANLIKPLLSG 314
Cdd:CHL00095 227 RDVPDILEDKLVITLDIGLLLAGTKYRGEFEERLKRIFDEIQENNNIILVIDEVHTLIGAGAAEGA-IDAANILKPALAR 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2021509219 315 GKIRVIGSTTYQEFSNIFEKDRALARRFQKIDVTEPSVEETVQIINGLKPKYEAHHDVRYTAKAVRAAVELAVKYINDRH 394
Cdd:CHL00095 306 GELQCIGATTLDEYRKHIEKDPALERRFQPVYVGEPSVEETIEILFGLRSRYEKHHNLSISDKALEAAAKLSDQYIADRF 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2021509219 395 LPDKAIDVIDEAGARARLM-----------------------------------------------------------PV 415
Cdd:CHL00095 386 LPDKAIDLLDEAGSRVRLInsrlppaareldkelreilkdkdeaireqdfetakqlrdremevraqiaaiiqskkteeEK 465
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2021509219 416 SKRKKTVNVADIESVVARIARIPEKSVSRSDRDTLKNLGDRLKMLVFGQDKAIEALTEAIKMARAGLGHEHKPVGSFLFA 495
Cdd:CHL00095 466 RLEVPVVTEEDIAEIVSAWTGIPVNKLTKSESEKLLHMEETLHKRIIGQDEAVVAVSKAIRRARVGLKNPNRPIASFLFS 545
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2021509219 496 GPTGVGKTEVTVQLAKAL-GIE--LLRFDMSEYMERHTVSRLIGAPPGYVGFDQGGLLTDAVIKHPHAVLLLDEIEKAHP 572
Cdd:CHL00095 546 GPTGVGKTELTKALASYFfGSEdaMIRLDMSEYMEKHTVSKLIGSPPGYVGYNEGGQLTEAVRKKPYTVVLFDEIEKAHP 625
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2021509219 573 DVFNILLQVMDNGTLTDNNGRKADFRNVVLVMTTNAGVRETERKSIGL-------IQQDNSTDAM-----EEIKKIFTPE 640
Cdd:CHL00095 626 DIFNLLLQILDDGRLTDSKGRTIDFKNTLIIMTSNLGSKVIETNSGGLgfelsenQLSEKQYKRLsnlvnEELKQFFRPE 705
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2021509219 641 FRNRLDNIIWFDHLSTTVIHQVVDKFIVELQVQLDQKGVSLEVSQEARDWLAEKGYDRAMGARPMARVIQDNLKKPLANE 720
Cdd:CHL00095 706 FLNRLDEIIVFRQLTKNDVWEIAEIMLKNLFKRLNEQGIQLEVTERIKTLLIEEGYNPLYGARPLRRAIMRLLEDPLAEE 785
|
810 820
....*....|....*....|....*
gi 2021509219 721 LLFGSLVDGGQVTVELDKANNVLTY 745
Cdd:CHL00095 786 VLSFKIKPGDIIIVDVNDEKEVKIL 810
|
|
| VI_ClpV1 |
TIGR03345 |
type VI secretion ATPase, ClpV1 family; Members of this protein family are homologs of ClpB, ... |
2-722 |
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: 541.84 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2021509219 2 LNQELELSLNMAFARAREHRHEFMTVEHLLLALLSNPS--AREALEACSVDLVALRQELeafieqtTPVLPATEEERDTQ 79
Cdd:TIGR03345 1 LNPTSRRALEQAAALCVARGHPEVELEHWLLALLDQPDsdLAAILRHFGVDLGRLKADL-------ARALDKLPRGNTRT 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2021509219 80 PTLS--FQRVLQRAvFHVQSS--GRSEVTGANVLVAIFSEQE-----SQAAYLLRKHEVSRLD-VVNFISHGTRKDEPSQ 149
Cdd:TIGR03345 74 PVFSphLVELLQEA-WLLASLelGDGRIRSGHLLLALLTDPElrrllGSISPELAKIDREALReALPALVEGSAEASAAA 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2021509219 150 PSENNASQPGneeQAGGEDRMENFTTNLNQLARVGGIDPLIGRDKELERAIQVLCRRRKNNPLLVGESGVGKTAIAEGLA 229
Cdd:TIGR03345 153 ADAAPAGAAA---GAAGTSALDQYTTDLTAQAREGKIDPVLGRDDEIRQMIDILLRRRQNNPILTGEAGVGKTAVVEGLA 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2021509219 230 WRIVQGDVPEVMADCTIYSLDIGSLLAGTKYRGDFEKRFKALLKQLEQ-DTNSILFIDEIHTIIGAGAASgGQVDAANLI 308
Cdd:TIGR03345 230 LRIAAGDVPPALRNVRLLSLDLGLLQAGASVKGEFENRLKSVIDEVKAsPQPIILFIDEAHTLIGAGGQA-GQGDAANLL 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2021509219 309 KPLLSGGKIRVIGSTTYQEFSNIFEKDRALARRFQKIDVTEPSVEETVQIINGLKPKYEAHHDVRYTAKAVRAAVELAVK 388
Cdd:TIGR03345 309 KPALARGELRTIAATTWAEYKKYFEKDPALTRRFQVVKVEEPDEETAIRMLRGLAPVLEKHHGVLILDEAVVAAVELSHR 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2021509219 389 YINDRHLPDKAIDVIDEAGARARL-------------------------------------------------------- 412
Cdd:TIGR03345 389 YIPGRQLPDKAVSLLDTACARVALsqnatpaaledlrrriaaleleldalereaalgadhderlaelraelaaleaelaa 468
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2021509219 413 ---------------------------MPVSKRKKT------------------------VNVADIESVVARIARIPEKS 441
Cdd:TIGR03345 469 learwqqekelveailalraeleadadAPADDDDALraqlaeleaalasaqgeeplvfpeVDAQAVAEVVADWTGIPVGR 548
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2021509219 442 VSRSDRDTLKNLGDRLKMLVFGQDKAIEALTEAIKMARAGLGHEHKPVGSFLFAGPTGVGKTEVTVQLAKAL-GIE--LL 518
Cdd:TIGR03345 549 MVRDEIEAVLSLPDRLAERVIGQDHALEAIAERIRTARAGLEDPRKPLGVFLLVGPSGVGKTETALALAELLyGGEqnLI 628
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2021509219 519 RFDMSEYMERHTVSRLIGAPPGYVGFDQGGLLTDAVIKHPHAVLLLDEIEKAHPDVFNILLQVMDNGTLTDNNGRKADFR 598
Cdd:TIGR03345 629 TINMSEFQEAHTVSRLKGSPPGYVGYGEGGVLTEAVRRKPYSVVLLDEVEKAHPDVLELFYQVFDKGVMEDGEGREIDFK 708
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2021509219 599 NVVLVMTTNAGvreTERKSIGLIQQDNSTDA-------MEEIKKIFTPEFRNRLdNIIWFDHLSTTVIHQVVDKFIVELQ 671
Cdd:TIGR03345 709 NTVILLTSNAG---SDLIMALCADPETAPDPeallealRPELLKVFKPAFLGRM-TVIPYLPLDDDVLAAIVRLKLDRIA 784
|
810 820 830 840 850
....*....|....*....|....*....|....*....|....*....|..
gi 2021509219 672 VQL-DQKGVSLEVSQEARDWLAEKGYDRAMGARPMARVIQDNLKKPLANELL 722
Cdd:TIGR03345 785 RRLkENHGAELVYSEALVEHIVARCTEVESGARNIDAILNQTLLPELSRQIL 836
|
|
| PRK10865 |
PRK10865 |
ATP-dependent chaperone ClpB; |
2-737 |
0e+00 |
|
ATP-dependent chaperone ClpB;
Pssm-ID: 182791 [Multi-domain] Cd Length: 857 Bit Score: 541.74 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2021509219 2 LNQELELSLNMAFARAREHRHEFMTVEHLLLALLSNP--SAREALEACSVDLVALRQELEAFIEQttpvLPATE-EERDT 78
Cdd:PRK10865 6 LTNKFQLALADAQSLALGHDNQFIEPLHLMSALLNQEggSVRPLLTSAGINAGQLRTDINQALSR----LPQVEgTGGDV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2021509219 79 QPTLSFQRVLQRAVFHVQSSGRSEVTGANVLVAIFsEQESQAAYLLRkhevsrldvvnfiSHGTRKDEPSQPSENNASQP 158
Cdd:PRK10865 82 QPSQDLVRVLNLCDKLAQKRGDNFISSELFVLAAL-ESRGTLADILK-------------AAGATTANITQAIEQMRGGE 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2021509219 159 GNEEQaGGEDR---MENFTTNLNQLARVGGIDPLIGRDKELERAIQVLCRRRKNNPLLVGESGVGKTAIAEGLAWRIVQG 235
Cdd:PRK10865 148 SVNDQ-GAEDQrqaLKKYTIDLTERAEQGKLDPVIGRDEEIRRTIQVLQRRTKNNPVLIGEPGVGKTAIVEGLAQRIING 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2021509219 236 DVPEVMADCTIYSLDIGSLLAGTKYRGDFEKRFKALLKQL-EQDTNSILFIDEIHTIIGAGAASGGqVDAANLIKPLLSG 314
Cdd:PRK10865 227 EVPEGLKGRRVLALDMGALVAGAKYRGEFEERLKGVLNDLaKQEGNVILFIDELHTMVGAGKADGA-MDAGNMLKPALAR 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2021509219 315 GKIRVIGSTTYQEFSNIFEKDRALARRFQKIDVTEPSVEETVQIINGLKPKYEAHHDVRYTAKAVRAAVELAVKYINDRH 394
Cdd:PRK10865 306 GELHCVGATTLDEYRQYIEKDAALERRFQKVFVAEPSVEDTIAILRGLKERYELHHHVQITDPAIVAAATLSHRYIADRQ 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2021509219 395 LPDKAIDVIDEAGARARLMPVSK---------------------RKKT-------------------------------- 421
Cdd:PRK10865 386 LPDKAIDLIDEAASSIRMQIDSKpeeldrldrriiqlkleqqalMKESdeaskkrldmlneelsdkerqyseleeewkae 465
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2021509219 422 -----------------------------------------------------------------VNVADIESVVARIAR 436
Cdd:PRK10865 466 kaslsgtqtikaeleqakiaieqarrvgdlarmselqygkipelekqlaaatqlegktmrllrnkVTDAEIAEVLARWTG 545
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2021509219 437 IPEKSVSRSDRDTLKNLGDRLKMLVFGQDKAIEALTEAIKMARAGLGHEHKPVGSFLFAGPTGVGKTEVTVQLAKAL--- 513
Cdd:PRK10865 546 IPVSRMLESEREKLLRMEQELHHRVIGQNEAVEAVSNAIRRSRAGLSDPNRPIGSFLFLGPTGVGKTELCKALANFMfds 625
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2021509219 514 GIELLRFDMSEYMERHTVSRLIGAPPGYVGFDQGGLLTDAVIKHPHAVLLLDEIEKAHPDVFNILLQVMDNGTLTDNNGR 593
Cdd:PRK10865 626 DDAMVRIDMSEFMEKHSVSRLVGAPPGYVGYEEGGYLTEAVRRRPYSVILLDEVEKAHPDVFNILLQVLDDGRLTDGQGR 705
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2021509219 594 KADFRNVVLVMTTNAGVRETERKSIGLIQQDNSTDAMEEIKKIFTPEFRNRLDNIIWFDHLSTTVIHQVVDKFIVELQVQ 673
Cdd:PRK10865 706 TVDFRNTVVIMTSNLGSDLIQERFGELDYAHMKELVLGVVSHNFRPEFINRIDEVVVFHPLGEQHIASIAQIQLQRLYKR 785
|
810 820 830 840 850 860
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2021509219 674 LDQKGVSLEVSQEARDWLAEKGYDRAMGARPMARVIQDNLKKPLANELLFGSLVDGGQVTVELD 737
Cdd:PRK10865 786 LEERGYEIHISDEALKLLSENGYDPVYGARPLKRAIQQQIENPLAQQILSGELVPGKVIRLEVN 849
|
|
| RecA-like_ClpB_Hsp104-like |
cd19499 |
Chaperone protein ClpB/Hsp104 subfamily; Bacterial Caseinolytic peptidase B (ClpB) and ... |
450-651 |
8.47e-87 |
|
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: 271.36 E-value: 8.47e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2021509219 450 LKNLGDRLKMLVFGQDKAIEALTEAIKMARAGLGHEHKPVGSFLFAGPTGVGKTEVTVQLAKAL---GIELLRFDMSEYM 526
Cdd:cd19499 2 LLNLEERLHERVVGQDEAVKAVSDAIRRARAGLSDPNRPIGSFLFLGPTGVGKTELAKALAELLfgdEDNLIRIDMSEYM 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2021509219 527 ERHTVSRLIGAPPGYVGFDQGGLLTDAVIKHPHAVLLLDEIEKAHPDVFNILLQVMDNGTLTDNNGRKADFRNVVLVMTT 606
Cdd:cd19499 82 EKHSVSRLIGAPPGYVGYTEGGQLTEAVRRKPYSVVLLDEIEKAHPDVQNLLLQVLDDGRLTDSHGRTVDFKNTIIIMTS 161
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 2021509219 607 NAgvreterksigliqqdnstdameeikkiFTPEFRNRLDNIIWF 651
Cdd:cd19499 162 NH----------------------------FRPEFLNRIDEIVVF 178
|
|
| AAA_2 |
pfam07724 |
AAA domain (Cdc48 subfamily); This Pfam entry includes some of the AAA proteins not detected ... |
487-648 |
5.46e-77 |
|
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: 245.18 E-value: 5.46e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2021509219 487 KPVGSFLFAGPTGVGKTEVTVQLAKALGI---ELLRFDMSEYMERHTVSRLIGAPPGYVGFDQGGLLTDAVIKHPHAVLL 563
Cdd:pfam07724 1 RPIGSFLFLGPTGVGKTELAKALAELLFGderALIRIDMSEYMEEHSVSRLIGAPPGYVGYEEGGQLTEAVRRKPYSIVL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2021509219 564 LDEIEKAHPDVFNILLQVMDNGTLTDNNGRKADFRNVVLVMTTNAGVRETERKSIGLIQQDNST---DAMEEIKKIFTPE 640
Cdd:pfam07724 81 IDEIEKAHPGVQNDLLQILEGGTLTDKQGRTVDFKNTLFIMTGNFGSEKISDASRLGDSPDYELlkeEVMDLLKKGFIPE 160
|
....*...
gi 2021509219 641 FRNRLDNI 648
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 ... |
351-453 |
5.85e-37 |
|
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: 133.77 E-value: 5.85e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2021509219 351 SVEETVQIINGLKPKYEAHHDVRYTAKAVRAAVELAVKYINDRHLPDKAIDVIDEAGARARLmpvSKRKKTVNVADIESV 430
Cdd:pfam17871 1 SVEEAIEILRGLKPKYEKHHGVRISDEALEAAVKLSKRYITDRFLPDKAIDLLDEACARVRL---SQESKPEELEDLERE 77
|
90 100
....*....|....*....|...
gi 2021509219 431 VARIARIPEKSVSRSDRDTLKNL 453
Cdd:pfam17871 78 LAKLEIEKEALEREQDFEKAERL 100
|
|
| ClpB_D2-small |
pfam10431 |
C-terminal, D2-small domain, of ClpB protein; This is the C-terminal domain of ClpB protein, ... |
654-734 |
9.39e-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, 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: 109.80 E-value: 9.39e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2021509219 654 LSTTVIHQVVDKFIVELQVQLDQKGVSLEVSQEARDWLAEKGYDRAMGARPMARVIQDNLKKPLANELLFGSLVDGGQVT 733
Cdd:pfam10431 1 LSKEELRKIVDLQLKELQKRLAERGITLELTDAAKDWLAEKGYDPEYGARPLRRAIQREIEDPLAEEILSGELKEGDTVR 80
|
.
gi 2021509219 734 V 734
Cdd:pfam10431 81 V 81
|
|
| ClpB_D2-small |
smart01086 |
C-terminal, D2-small domain, of ClpB protein; This is the C-terminal domain of ClpB protein, ... |
654-743 |
7.06e-27 |
|
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: 104.83 E-value: 7.06e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2021509219 654 LSTTVIHQVVDKFIVELQVQLDQKGVSLEVSQEARDWLAEKGYDRAMGARPMARVIQDNLKKPLANELLFGSLVDGGQVT 733
Cdd:smart01086 1 LDKEDLVRIVDLPLNALQKRLAEKGITLEFTDEALDWLAEKGYDPKYGARPLRRIIQRELEDPLAELILSGELKDGDTVV 80
|
90
....*....|
gi 2021509219 734 VELDKANNVL 743
Cdd:smart01086 81 VDVDDGELVF 90
|
|
| AAA |
cd00009 |
The AAA+ (ATPases Associated with a wide variety of cellular Activities) superfamily ... |
190-345 |
7.43e-22 |
|
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: 92.59 E-value: 7.43e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2021509219 190 IGRDKELERAIQVLCRRRKNNPLLVGESGVGKTAIAEGLAWRIVQGDVPevmadctIYSLDIGSLLAGTKYRGDFE-KRF 268
Cdd:cd00009 1 VGQEEAIEALREALELPPPKNLLLYGPPGTGKTTLARAIANELFRPGAP-------FLYLNASDLLEGLVVAELFGhFLV 73
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2021509219 269 KALLKQLEQDTNSILFIDEIHTIigAGAASGGQVDAAN-LIKPLLSGGKIRVIGSTTYqefSNIFEKDRALARRFQKI 345
Cdd:cd00009 74 RLLFELAEKAKPGVLFIDEIDSL--SRGAQNALLRVLEtLNDLRIDRENVRVIGATNR---PLLGDLDRALYDRLDIR 146
|
|
| SpoVK |
COG0464 |
AAA+-type ATPase, SpoVK/Ycf46/Vps4 family [Cell wall/membrane/envelope biogenesis, Cell cycle ... |
17-388 |
3.48e-17 |
|
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: 84.58 E-value: 3.48e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2021509219 17 AREHRHEFMTVEHLLLALLSNPSAREALEACSVDLVALRQELEAFIEQTTPVLPATEEERDTQPTLSFQRVLQRAVFHVQ 96
Cdd:COG0464 1 LAELLALAVALALALLLLDDAALRLLLLLLLALAAALLLLLLLLLLLLLALLLVELLLLLLSGALAALLLLALLLLALLA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2021509219 97 SSGRSEVTGANVLVAIFSEQESQAAYLLRKHEVSRLDVVNFISHGTRKDEPSQPSENNASQPGNEEQAGGEDRMEnfttn 176
Cdd:COG0464 81 LLAALLSALELLLLGELLLLLLLLLLLLLLLLDLERALLELLRESAEALALAAPLVTYEDIGGLEEELLELREAI----- 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2021509219 177 lnqLARVGGIDPLIGRDKELERAIQVLCRRRKNNP-------LLVGESGVGKTAIAEGLAwRIVQGDVpevmadctiYSL 249
Cdd:COG0464 156 ---LDDLGGLEEVKEELRELVALPLKRPELREEYGlppprglLLYGPPGTGKTLLARALA-GELGLPL---------IEV 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2021509219 250 DIGSLLAgtKYRGDFEKRFKALLKQLEQDTNSILFIDEIHTIIGAGAASGGQVDA----------ANLIKPLLsggkirV 319
Cdd:COG0464 223 DLSDLVS--KYVGETEKNLREVFDKARGLAPCVLFIDEADALAGKRGEVGDGVGRrvvntlltemEELRSDVV------V 294
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2021509219 320 IGsTTYQeFSNIfekDRALARRFQ-KIDVTEPSVEETVQIINGLKPKYEAHHDV----------RYTAKAVRAAVELAVK 388
Cdd:COG0464 295 IA-ATNR-PDLL---DPALLRRFDeIIFFPLPDAEERLEIFRIHLRKRPLDEDVdleelaeateGLSGADIRNVVRRAAL 369
|
|
| AAA |
pfam00004 |
ATPase family associated with various cellular activities (AAA); AAA family proteins often ... |
212-345 |
1.06e-16 |
|
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: 76.86 E-value: 1.06e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2021509219 212 LLVGESGVGKTAIAEGLAWrivqgdvpevMADCTIYSLDIGSLLAgtKYRGDFEKRFKALLKQLEQDTNSILFIDEIHTI 291
Cdd:pfam00004 2 LLYGPPGTGKTTLAKAVAK----------ELGAPFIEISGSELVS--KYVGESEKRLRELFEAAKKLAPCVIFIDEIDAL 69
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2021509219 292 IGAGAASGGQV--DAANLIKPLLSG-----GKIRVIGSTTYqefsnIFEKDRALARRFQKI 345
Cdd:pfam00004 70 AGSRGSGGDSEsrRVVNQLLTELDGftssnSKVIVIAATNR-----PDKLDPALLGRFDRI 125
|
|
| AAA |
cd00009 |
The AAA+ (ATPases Associated with a wide variety of cellular Activities) superfamily ... |
462-618 |
1.81e-13 |
|
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: 68.33 E-value: 1.81e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2021509219 462 FGQDKAIEALTEAIkmaraglghEHKPVGSFLFAGPTGVGKTEVTVQLAKAL---GIELLRFDMSEYMERHTVSRLIgap 538
Cdd:cd00009 1 VGQEEAIEALREAL---------ELPPPKNLLLYGPPGTGKTTLARAIANELfrpGAPFLYLNASDLLEGLVVAELF--- 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2021509219 539 pgyvGFDQGGLLTDAVIKHPHAVLLLDEIEKAHPDVFNILLQVMDNGtltdnNGRKADFRNVVLVMTTNAGVRETERKSI 618
Cdd:cd00009 69 ----GHFLVRLLFELAEKAKPGVLFIDEIDSLSRGAQNALLRVLETL-----NDLRIDRENVRVIGATNRPLLGDLDRAL 139
|
|
| AAA_5 |
pfam07728 |
AAA domain (dynein-related subfamily); This Pfam entry includes some of the AAA proteins not ... |
491-607 |
5.04e-13 |
|
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: 66.55 E-value: 5.04e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2021509219 491 SFLFAGPTGVGKTEVTVQLAKAL-GIELLRFDMSEYMerhTVSRLIGappGYVGFDQGGLLTDAVI----KHPHaVLLLD 565
Cdd:pfam07728 1 GVLLVGPPGTGKTELAERLAAALsNRPVFYVQLTRDT---TEEDLFG---RRNIDPGGASWVDGPLvraaREGE-IAVLD 73
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 2021509219 566 EIEKAHPDVFNILLQVMDNGTLTDNNGR---KADFRNVVLVMTTN 607
Cdd:pfam07728 74 EINRANPDVLNSLLSLLDERRLLLPDGGelvKAAPDGFRLIATMN 118
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
207-345 |
2.66e-12 |
|
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a variety of cellular activities. This profile/alignment only detects a fraction of this vast family. The poorly conserved N-terminal helix is missing from the alignment.
Pssm-ID: 214640 [Multi-domain] Cd Length: 148 Bit Score: 65.09 E-value: 2.66e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2021509219 207 RKNNPLLVGESGVGKTAIAEGLAWRIVQGDVPEVMADCTIYSLDIGSLL-----AGTKYRGDFEKRFKALLKQLEQDTNS 281
Cdd:smart00382 1 PGEVILIVGPPGSGKTTLARALARELGPPGGGVIYIDGEDILEEVLDQLlliivGGKKASGSGELRLRLALALARKLKPD 80
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2021509219 282 ILFIDEIHTIIGAGAASGGQVDA-ANLIKPLLSGGKIRVIGSTTYQEFSnifeKDRALARRFQKI 345
Cdd:smart00382 81 VLILDEITSLLDAEQEALLLLLEeLRLLLLLKSEKNLTVILTTNDEKDL----GPALLRRRFDRR 141
|
|
| Clp_N |
pfam02861 |
Clp amino terminal domain, pathogenicity island component; This short domain is found in one ... |
13-63 |
1.29e-11 |
|
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: 59.84 E-value: 1.29e-11
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 2021509219 13 AFARAREHRHEFMTVEHLLLALLSNPS--AREALEACSVDLVALRQELEAFIE 63
Cdd:pfam02861 1 AQELARALGHQYIGTEHLLLALLEEDDglAARLLKKAGVDLDALREAIEKLLG 53
|
|
| RecA-like_protease |
cd19481 |
proteases similar to RecA; RecA-like NTPases. This family includes the NTP binding domain of ... |
212-345 |
4.63e-10 |
|
proteases similar to RecA; RecA-like NTPases. This family includes the NTP binding domain of F1 and V1 H(+)ATPases, DnaB and related helicases as well as bacterial RecA and related eukaryotic and archaeal recombinases. This group also includes bacterial conjugation proteins and related DNA transfer proteins involved in type II and type IV secretion.
Pssm-ID: 410889 [Multi-domain] Cd Length: 158 Bit Score: 58.83 E-value: 4.63e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2021509219 212 LLVGESGVGKTAIAEGLAwrivqgdvpeVMADCTIYSLDIGSLLagTKYRGDFEKRFKALLKQLEQDTNSILFIDEIHTI 291
Cdd:cd19481 30 LLYGPPGTGKTLLAKALA----------GELGLPLIVVKLSSLL--SKYVGESEKNLRKIFERARRLAPCILFIDEIDAI 97
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2021509219 292 IGAGAASGGQVDAA-------NLIKPLLSGGKIRVIGSTtyqefSNIFEKDRALAR--RFQKI 345
Cdd:cd19481 98 GRKRDSSGESGELRrvlnqllTELDGVNSRSKVLVIAAT-----NRPDLLDPALLRpgRFDEV 155
|
|
| RecA-like_protease |
cd19481 |
proteases similar to RecA; RecA-like NTPases. This family includes the NTP binding domain of ... |
467-607 |
9.42e-10 |
|
proteases similar to RecA; RecA-like NTPases. This family includes the NTP binding domain of F1 and V1 H(+)ATPases, DnaB and related helicases as well as bacterial RecA and related eukaryotic and archaeal recombinases. This group also includes bacterial conjugation proteins and related DNA transfer proteins involved in type II and type IV secretion.
Pssm-ID: 410889 [Multi-domain] Cd Length: 158 Bit Score: 58.06 E-value: 9.42e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2021509219 467 AIEALTEAIKMARAGL----GHEHKPVGsFLFAGPTGVGKTEVTVQLAKALGIELLRFDMSEYMERHTvsrligappGYV 542
Cdd:cd19481 1 LKASLREAVEAPRRGSrlrrYGLGLPKG-ILLYGPPGTGKTLLAKALAGELGLPLIVVKLSSLLSKYV---------GES 70
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2021509219 543 GfDQGGLLTDAVIKHPHAVLLLDEIEKAHPD------------VFNILLQVMDNGTLTDnngrkadfrNVVLVMTTN 607
Cdd:cd19481 71 E-KNLRKIFERARRLAPCILFIDEIDAIGRKrdssgesgelrrVLNQLLTELDGVNSRS---------KVLVIAATN 137
|
|
| AAA |
pfam00004 |
ATPase family associated with various cellular activities (AAA); AAA family proteins often ... |
493-652 |
1.66e-09 |
|
ATPase family associated with various cellular activities (AAA); AAA family proteins often perform chaperone-like functions that assist in the assembly, operation, or disassembly of protein complexes.
Pssm-ID: 459627 [Multi-domain] Cd Length: 130 Bit Score: 56.45 E-value: 1.66e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2021509219 493 LFAGPTGVGKTEVTVQLAKALGIELLRFDMSEymerhTVSRLIGAPPGYVgfdqGGLLTDAVIKHPHaVLLLDEIEKAHP 572
Cdd:pfam00004 2 LLYGPPGTGKTTLAKAVAKELGAPFIEISGSE-----LVSKYVGESEKRL----RELFEAAKKLAPC-VIFIDEIDALAG 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2021509219 573 -----------DVFNILLQVMDngtltdnnGRKADFRNVVLVMTTNagvreterkSIGLIqqdnstdameeikkifTPEF 641
Cdd:pfam00004 72 srgsggdsesrRVVNQLLTELD--------GFTSSNSKVIVIAATN---------RPDKL----------------DPAL 118
|
170
....*....|.
gi 2021509219 642 RNRLDNIIWFD 652
Cdd:pfam00004 119 LGRFDRIIEFP 129
|
|
| COG1223 |
COG1223 |
Predicted ATPase, AAA+ superfamily [General function prediction only]; |
209-405 |
2.12e-09 |
|
Predicted ATPase, AAA+ superfamily [General function prediction only];
Pssm-ID: 440836 [Multi-domain] Cd Length: 246 Bit Score: 58.74 E-value: 2.12e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2021509219 209 NNPLLVGESGVGKTAIAEGLAWRIvqgDVPevmadctIYSLDIGSLLagTKYRGDFEKRFKALLKQLEQdTNSILFIDEI 288
Cdd:COG1223 36 RKILFYGPPGTGKTMLAEALAGEL---KLP-------LLTVRLDSLI--GSYLGETARNLRKLFDFARR-APCVIFFDEF 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2021509219 289 HTIigaGAASGGQVDAA------NLIKPLLSG--GKIRVIGSTTYQEFSnifekDRALARRFQ-KIDVTEPSVEETVQI- 358
Cdd:COG1223 103 DAI---AKDRGDQNDVGevkrvvNALLQELDGlpSGSVVIAATNHPELL-----DSALWRRFDeVIEFPLPDKEERKEIl 174
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2021509219 359 ---INGLKPKYEAHHDV----------RYTAKAVRAAVELAV----KYINDRHLpDKAIDVIDE 405
Cdd:COG1223 175 elnLKKFPLPFELDLKKlakkleglsgADIEKVLKTALKKAIledrEKVTKEDL-EEALKQRKE 237
|
|
| RPT1 |
COG1222 |
ATP-dependent 26S proteasome regulatory subunit [Posttranslational modification, protein ... |
212-441 |
1.47e-08 |
|
ATP-dependent 26S proteasome regulatory subunit [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440835 [Multi-domain] Cd Length: 326 Bit Score: 56.94 E-value: 1.47e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2021509219 212 LLVGESGVGKTAIAEGLAWRivqgdvpevmADCTIYSLDIGSLLagTKYRGDFEKRFKALLKQLEQDTNSILFIDEIHTI 291
Cdd:COG1222 116 LLYGPPGTGKTLLAKAVAGE----------LGAPFIRVRGSELV--SKYIGEGARNVREVFELAREKAPSIIFIDEIDAI 183
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2021509219 292 IGA--GAASGGQVDaaNLIKPLL-------SGGKIRVIGSTTYQEfsnifEKDRALAR--RF-QKIDVTEPSVEETVQII 359
Cdd:COG1222 184 AARrtDDGTSGEVQ--RTVNQLLaeldgfeSRGDVLIIAATNRPD-----LLDPALLRpgRFdRVIEVPLPDEEAREEIL 256
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2021509219 360 NGLKPKYEAHHDVRYTAKAVRA----AVELAVkyindrhlpdkaidVIDEAGARArlmpVSKRKKTVNVADIESVVARIA 435
Cdd:COG1222 257 KIHLRDMPLADDVDLDKLAKLTegfsGADLKA--------------IVTEAGMFA----IREGRDTVTMEDLEKAIEKVK 318
|
....*.
gi 2021509219 436 RIPEKS 441
Cdd:COG1222 319 KKTETA 324
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
493-607 |
3.22e-08 |
|
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a variety of cellular activities. This profile/alignment only detects a fraction of this vast family. The poorly conserved N-terminal helix is missing from the alignment.
Pssm-ID: 214640 [Multi-domain] Cd Length: 148 Bit Score: 53.15 E-value: 3.22e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2021509219 493 LFAGPTGVGKTEVTVQLAKAL---GIELLRFDMSEYMERHTVSRLIGAPPGYVGFDQGG----LLTDAVIKHPHAVLLLD 565
Cdd:smart00382 6 LIVGPPGSGKTTLARALARELgppGGGVIYIDGEDILEEVLDQLLLIIVGGKKASGSGElrlrLALALARKLKPDVLILD 85
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 2021509219 566 EIEKAHPDVFNILLQVMDNGTLTDnngRKADFRNVVLVMTTN 607
Cdd:smart00382 86 EITSLLDAEQEALLLLLEELRLLL---LLKSEKNLTVILTTN 124
|
|
| RecA-like_VPS4-like |
cd19509 |
ATPase domain of VPS4, ATAD1, K, KTNA1, Spastin, FIGL-1 and similar ATPase domains; This ... |
212-344 |
1.38e-07 |
|
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: 51.97 E-value: 1.38e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2021509219 212 LLVGESGVGKTAIAEGLAWRIvqgdvpevmaDCTIYSLDIGSLLAgtKYRGDFEKRFKALLKQLEQDTNSILFIDEIHTI 291
Cdd:cd19509 36 LLYGPPGTGKTLLARAVASES----------GSTFFSISASSLVS--KWVGESEKIVRALFALARELQPSIIFIDEIDSL 103
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2021509219 292 IgaGAASGGQVDAANLIKPLL----------SGGKIRVIGSTtyqefSNIFEKDRALARRFQK 344
Cdd:cd19509 104 L--SERGSGEHEASRRVKTEFlvqmdgvlnkPEDRVLVLGAT-----NRPWELDEAFLRRFEK 159
|
|
| SpoVK |
COG0464 |
AAA+-type ATPase, SpoVK/Ycf46/Vps4 family [Cell wall/membrane/envelope biogenesis, Cell cycle ... |
335-607 |
2.48e-07 |
|
AAA+-type ATPase, SpoVK/Ycf46/Vps4 family [Cell wall/membrane/envelope biogenesis, Cell cycle control, cell division, chromosome partitioning, Signal transduction mechanisms];
Pssm-ID: 440232 [Multi-domain] Cd Length: 397 Bit Score: 53.76 E-value: 2.48e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2021509219 335 DRALARRFQKIDVTEPSVEETVQIINGLKPKYEAHHDVRYTAKAVRAAVELAVKYINDRHLPDKAIDVIDEAGARARLMP 414
Cdd:COG0464 34 AAALLLLLLLLLLLLLALLLVELLLLLLSGALAALLLLALLLLALLALLAALLSALELLLLGELLLLLLLLLLLLLLLLD 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2021509219 415 VSKRKKTVNVADIESVVARIARIPEKSVSRSDRDTLKNLGDRLKMLVfGQDKAIEALTEAIK--------MARAGLgheh 486
Cdd:COG0464 114 LERALLELLRESAEALALAAPLVTYEDIGGLEEELLELREAILDDLG-GLEEVKEELRELVAlplkrpelREEYGL---- 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2021509219 487 KPVGSFLFAGPTGVGKTEVTVQLAKALGIELLRFDMSEymerhtvsrLIGappGYVG---------FDQgglltdaVIKH 557
Cdd:COG0464 189 PPPRGLLLYGPPGTGKTLLARALAGELGLPLIEVDLSD---------LVS---KYVGeteknlrevFDK-------ARGL 249
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2021509219 558 PHAVLLLDEIEKAHPD-----------VFNILLQVMDNGTltdnngrkadfRNVVLVMTTN 607
Cdd:COG0464 250 APCVLFIDEADALAGKrgevgdgvgrrVVNTLLTEMEELR-----------SDVVVIAATN 299
|
|
| RecA-like_VPS4 |
cd19521 |
ATPase domain of vacuolar protein sorting-associated protein 4; Vacuolar protein ... |
212-344 |
3.23e-07 |
|
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: 51.02 E-value: 3.23e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2021509219 212 LLVGESGVGKTAIAEGLAwrivqgdvpeVMADCTIYSLDIGSLLagTKYRGDFEKRFKALLKQLEQDTNSILFIDEIHTI 291
Cdd:cd19521 44 LLYGPPGTGKSYLAKAVA----------TEANSTFFSVSSSDLV--SKWMGESEKLVKQLFAMARENKPSIIFIDEVDSL 111
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2021509219 292 igAGAASGGQVDAANLIKPLL---------SGGKIRVIGSTtyqefsNI-FEKDRALARRFQK 344
Cdd:cd19521 112 --CGTRGEGESEASRRIKTELlvqmngvgnDSQGVLVLGAT------NIpWQLDSAIRRRFEK 166
|
|
| CDC48 |
TIGR01243 |
AAA family ATPase, CDC48 subfamily; This subfamily of the AAA family ATPases includes two ... |
212-516 |
1.82e-06 |
|
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: 51.45 E-value: 1.82e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2021509219 212 LLVGESGVGKTAIAEGLAWRI----VQGDVPEVMadctiysldigsllagTKYRGDFEKRFKALLKQLEQDTNSILFIDE 287
Cdd:TIGR01243 216 LLYGPPGTGKTLLAKAVANEAgayfISINGPEIM----------------SKYYGESEERLREIFKEAEENAPSIIFIDE 279
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2021509219 288 IHTIIGAGAASGGQVDAA------NLIKPLLSGGKIRVIGSTTYQEfsnifEKDRALAR--RFQK-IDVTEPSVEETVQI 358
Cdd:TIGR01243 280 IDAIAPKREEVTGEVEKRvvaqllTLMDGLKGRGRVIVIGATNRPD-----ALDPALRRpgRFDReIVIRVPDKRARKEI 354
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2021509219 359 INGLKPKYEAHHDVR----------YTAKAVRAAVELAVKYINDRHLPDKAIDVIDEAGARARL--MPVSKRKKTVNVAD 426
Cdd:TIGR01243 355 LKVHTRNMPLAEDVDldklaevthgFVGADLAALAKEAAMAALRRFIREGKINFEAEEIPAEVLkeLKVTMKDFMEALKM 434
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2021509219 427 IESVVARIARIPEKSVSRSDRDTLKNLGDRLKMLVFGQDKAIEALteaikmARAGLgheHKPVGSFLFaGPTGVGKTevt 506
Cdd:TIGR01243 435 VEPSAIREVLVEVPNVRWSDIGGLEEVKQELREAVEWPLKHPEIF------EKMGI---RPPKGVLLF-GPPGTGKT--- 501
|
330
....*....|
gi 2021509219 507 vQLAKALGIE 516
Cdd:TIGR01243 502 -LLAKAVATE 510
|
|
| RecA-like_Lon |
cd19500 |
lon protease homolog 2 peroxisomal; Lon protease (also known as Lon peptidase) is an ... |
493-607 |
7.27e-06 |
|
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: 47.17 E-value: 7.27e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2021509219 493 LFAGPTGVGKTEVTVQLAKALGIELLRF------DMSEYM-ERHTvsrLIGAPPGYVgfDQGglLTDAVIKHPhaVLLLD 565
Cdd:cd19500 41 CLVGPPGVGKTSLGKSIARALGRKFVRIslggvrDEAEIRgHRRT---YVGAMPGRI--IQA--LKKAGTNNP--VFLLD 111
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 2021509219 566 EIEK----AHPDVFNILLQVMD---NGTLTDNN-GRKADFRNVVLVMTTN 607
Cdd:cd19500 112 EIDKigssFRGDPASALLEVLDpeqNSTFSDHYlDVPFDLSKVLFIATAN 161
|
|
| RecA-like_KTNA1 |
cd19522 |
Katanin p60 ATPase-containing subunit A1; Katanin p60 ATPase-containing subunit A1 (KTNA1) is ... |
205-344 |
9.36e-06 |
|
Katanin p60 ATPase-containing subunit A1; Katanin p60 ATPase-containing subunit A1 (KTNA1) is the catalytic subunit of the Katanin complex which is severs microtubules in an ATP-dependent manner, and is implicated in multiple aspects of microtubule dynamics. In addition to the p60 catalytic ATPase subunit, Katanin contains an accessory subunit (p80 or p80-like). The microtubule-severing activity of the ATPase is essential for female meiotic spindle assembly, and male gamete production; and the katanin complex severing microtubules is under tight regulation during the transition from the meiotic to mitotic stage to allow proper embryogenesis. 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: 410930 [Multi-domain] Cd Length: 170 Bit Score: 46.52 E-value: 9.36e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2021509219 205 RRRKNNPLLVGESGVGKTAIAEGLAwrivqgdvpevmADCTIYSLDIGSLLAGTKYRGDFEKRFKALLKQLEQDTNSILF 284
Cdd:cd19522 30 RRPWKGVLMVGPPGTGKTLLAKAVA------------TECGTTFFNVSSSTLTSKYRGESEKLVRLLFEMARFYAPTTIF 97
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2021509219 285 IDEIHTIIGAgAASGGQVDAANLIKPLLSGGKIRVIGSTTYQEFSNI----------FEKDRALARRFQK 344
Cdd:cd19522 98 IDEIDSICSR-RGTSEEHEASRRVKSELLVQMDGVGGASENDDPSKMvmvlaatnfpWDIDEALRRRLEK 166
|
|
| DnaX |
COG2812 |
DNA polymerase III, gamma/tau subunits [Replication, recombination and repair]; |
461-513 |
9.76e-06 |
|
DNA polymerase III, gamma/tau subunits [Replication, recombination and repair];
Pssm-ID: 442061 [Multi-domain] Cd Length: 340 Bit Score: 48.26 E-value: 9.76e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 2021509219 461 VFGQDKAIEALTEAIKMARagLGHehkpvgSFLFAGPTGVGKTEVTVQLAKAL 513
Cdd:COG2812 12 VVGQEHVVRTLKNALASGR--LAH------AYLFTGPRGVGKTTLARILAKAL 56
|
|
| AAA_16 |
pfam13191 |
AAA ATPase domain; This family of domains contain a P-loop motif that is characteriztic of the ... |
188-247 |
4.20e-05 |
|
AAA ATPase domain; This family of domains contain a P-loop motif that is characteriztic of the AAA superfamily.
Pssm-ID: 433025 [Multi-domain] Cd Length: 167 Bit Score: 44.80 E-value: 4.20e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2021509219 188 PLIGRDKELERAIQVLCRRRKNNP---LLVGESGVGKTAIAEGLAWRIVQGDVPEVMADCTIY 247
Cdd:pfam13191 1 RLVGREEELEQLLDALDRVRSGRPpsvLLTGEAGTGKTTLLRELLRALERDGGYFLRGKCDEN 63
|
|
| RecA-like_HslU |
cd19498 |
ATP-dependent protease ATPase subunit HslU; HslU is a component of the ATP-dependent protease ... |
449-569 |
4.42e-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: 44.68 E-value: 4.42e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2021509219 449 TLKNLGDRLKMLVFGQDKAIEALTEAIK------MARAGLGHEHKPvGSFLFAGPTGVGKTEVTVQLAKALGIELLRFDM 522
Cdd:cd19498 1 TPREIVSELDKYIIGQDEAKRAVAIALRnrwrrmQLPEELRDEVTP-KNILMIGPTGVGKTEIARRLAKLAGAPFIKVEA 79
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 2021509219 523 SEYMErhtvsrligapPGYVGFDQGGLLTDAVikhpHAVLLLDEIEK 569
Cdd:cd19498 80 TKFTE-----------VGYVGRDVESIIRDLV----EGIVFIDEIDK 111
|
|
| RecA-like_CDC48_r1-like |
cd19519 |
first of two ATPase domains of CDC48 and similar ATPase domains; CDC48 in yeast and p97 or VCP ... |
212-346 |
6.10e-05 |
|
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: 43.96 E-value: 6.10e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2021509219 212 LLVGESGVGKTAIAEGLA------WRIVQGdvPEVMadctiysldigsllagTKYRGDFEKRFKALLKQLEQDTNSILFI 285
Cdd:cd19519 38 LLYGPPGTGKTLIARAVAnetgafFFLING--PEIM----------------SKLAGESESNLRKAFEEAEKNAPAIIFI 99
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2021509219 286 DEIHTIIGAGAASGGQVD---AANLIKpLLSGGKIR----VIGSTtyqefSNIFEKDRALaRRFQKID 346
Cdd:cd19519 100 DEIDAIAPKREKTHGEVErriVSQLLT-LMDGLKQRahviVMAAT-----NRPNSIDPAL-RRFGRFD 160
|
|
| RecA-like_CDC48_NLV2_r1-like |
cd19503 |
first of two ATPase domains of CDC48 and NLV2, and similar ATPase domains; CDC48 in yeast and ... |
212-323 |
7.03e-05 |
|
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: 43.82 E-value: 7.03e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2021509219 212 LLVGESGVGKTAIAEGLAWRivqgdvpevmADCTIYSLDIGSLLAgtKYRGDFEKRFKALLKQLEQDTNSILFIDEIHTI 291
Cdd:cd19503 38 LLHGPPGTGKTLLARAVANE----------AGANFLSISGPSIVS--KYLGESEKNLREIFEEARSHAPSIIFIDEIDAL 105
|
90 100 110
....*....|....*....|....*....|....*....
gi 2021509219 292 IGAGAASGGQVD---AANLIKpLLSG----GKIRVIGST 323
Cdd:cd19503 106 APKREEDQREVErrvVAQLLT-LMDGmssrGKVVVIAAT 143
|
|
| RecA-like_ClpX |
cd19497 |
ATP-dependent Clp protease ATP-binding subunit ClpX; ClpX is a component of the ATP-dependent ... |
208-291 |
9.01e-05 |
|
ATP-dependent Clp protease ATP-binding subunit ClpX; ClpX is a component of the ATP-dependent protease ClpXP. In ClpXP, ClpX ATPase serves to specifically recognize, unfold, and translocate protein substrates into the chamber of ClpP protease for degradation. This RecA-like_ClpX domain subfamily belongs to the RecA-like NTPase family which includes the NTP binding domain of F1 and V1 H(+)ATPases, DnaB and related helicases as well as bacterial RecA and related eukaryotic and archaeal recombinases. The RecA-like NTPase family also includes bacterial conjugation proteins and related DNA transfer proteins involved in type II and type IV secretion.
Pssm-ID: 410905 [Multi-domain] Cd Length: 251 Bit Score: 44.90 E-value: 9.01e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2021509219 208 KNNPLLVGESGVGKTAIAEGLAwRIVqgDVPEVMADCTiysldigSLL-AGtkYRG-DFEKRFKALLK----QLEQDTNS 281
Cdd:cd19497 50 KSNILLIGPTGSGKTLLAQTLA-KIL--DVPFAIADAT-------TLTeAG--YVGeDVENILLKLLQaadyDVERAQRG 117
|
90
....*....|
gi 2021509219 282 ILFIDEIHTI 291
Cdd:cd19497 118 IVYIDEIDKI 127
|
|
| RecA-like_Ycf46-like |
cd19507 |
ATPase domain of Ycf46 and similar ATPase domains; Ycf46 may play a role in the regulation of ... |
212-322 |
1.14e-04 |
|
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: 43.13 E-value: 1.14e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2021509219 212 LLVGESGVGKTAIAEGLA--WRIvqgdvpevmadcTIYSLDIGSLLAGtkYRGDFEKRFKALLKQLEQDTNSILFIDEIH 289
Cdd:cd19507 35 LLVGIQGTGKSLTAKAIAgvWQL------------PLLRLDMGRLFGG--LVGESESRLRQMIQTAEAIAPCVLWIDEIE 100
|
90 100 110
....*....|....*....|....*....|...
gi 2021509219 290 TIIGaGAASGGQvdaanlikpllSGGKIRVIGS 322
Cdd:cd19507 101 KGFS-NADSKGD-----------SGTSSRVLGT 121
|
|
| DNA_pol3_delta2 |
pfam13177 |
DNA polymerase III, delta subunit; DNA polymerase III, delta subunit (EC 2.7.7.7) is required ... |
463-513 |
3.03e-04 |
|
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: 41.81 E-value: 3.03e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 2021509219 463 GQDKAIEALTEAIKMARagLGHehkpvgSFLFAGPTGVGKTEVTVQLAKAL 513
Cdd:pfam13177 1 GQPEAIQLLQNSLENGR--LSH------AYLFSGPEGVGKLELALAFAKAL 43
|
|
| RecA-like_spastin |
cd19524 |
ATPase domain of spastin; Spastin is an ATP-dependent microtubule-severing protein involved in ... |
212-344 |
4.35e-04 |
|
ATPase domain of spastin; Spastin is an ATP-dependent microtubule-severing protein involved in microtubule dynamics; it specifically recognizes and cuts microtubules that are polyglutamylated. 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: 410932 [Multi-domain] Cd Length: 164 Bit Score: 41.76 E-value: 4.35e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2021509219 212 LLVGESGVGKTAIAEGLAwrivqgdvpevmADCTIYSLDIGSLLAGTKYRGDFEKRFKALLKQLEQDTNSILFIDEIHTI 291
Cdd:cd19524 37 LLFGPPGNGKTMLAKAVA------------AESNATFFNISAASLTSKYVGEGEKLVRALFAVARELQPSIIFIDEVDSL 104
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2021509219 292 IgaGAASGGQVDAANLIKP--------LLSGGKIRVI--GSTTYQEfsnifEKDRALARRFQK 344
Cdd:cd19524 105 L--SERSEGEHEASRRLKTefliefdgVQSNGDDRVLvmGATNRPQ-----ELDDAVLRRFTK 160
|
|
| RecA-like_Figl-1 |
cd19525 |
ATPase domain of Fidgetin-Like 1 (FIGL-1); FIGL-1 may participate in DNA repair in the nucleus; ... |
212-344 |
6.13e-04 |
|
ATPase domain of Fidgetin-Like 1 (FIGL-1); FIGL-1 may participate in DNA repair in the nucleus; it may be involved in DNA double-strand break repair via homologous recombination. Caenorhabditis elegans FIGL-1 is a nuclear protein and controls the mitotic progression in the germ line and mouse FIGL-1 may be involved in the control of male meiosis. human FIGL-1 has been shown to be a centrosome protein involved in ciliogenesis perhaps as a microtubule-severing protein. 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: 410933 [Multi-domain] Cd Length: 186 Bit Score: 41.51 E-value: 6.13e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2021509219 212 LLVGESGVGKTAIAEGLAWRivqgdvpevmADCTIYSLDIGSLLagTKYRGDFEKRFKALLKQLEQDTNSILFIDEIHTI 291
Cdd:cd19525 59 LLFGPPGTGKTLIGKCIASQ----------SGATFFSISASSLT--SKWVGEGEKMVRALFSVARCKQPAVIFIDEIDSL 126
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2021509219 292 IgaGAASGGQVDAANLIKPLL----------SGGKIRVIGSTTYQEfsnifEKDRALARRFQK 344
Cdd:cd19525 127 L--SQRGEGEHESSRRIKTEFlvqldgattsSEDRILVVGATNRPQ-----EIDEAARRRLVK 182
|
|
| PRK13341 |
PRK13341 |
AAA family ATPase; |
185-341 |
6.29e-04 |
|
AAA family ATPase;
Pssm-ID: 237354 [Multi-domain] Cd Length: 725 Bit Score: 43.12 E-value: 6.29e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2021509219 185 GIDPLIGRDKELERAIQVlcrRRKNNPLLVGESGVGKTAIAEGLAwRIVQGDVpevmadctiysLDIGSLLAGTKyrgDF 264
Cdd:PRK13341 32 GQDHILGEGRLLRRAIKA---DRVGSLILYGPPGVGKTTLARIIA-NHTRAHF-----------SSLNAVLAGVK---DL 93
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2021509219 265 EKRFKALLKQLEQ-DTNSILFIDEIHTIIGAgaasggQVDAanlIKPLLSGGKIRVIGSTTYQEFsniFEKDRALARR 341
Cdd:PRK13341 94 RAEVDRAKERLERhGKRTILFIDEVHRFNKA------QQDA---LLPWVENGTITLIGATTENPY---FEVNKALVSR 159
|
|
| PRK13342 |
PRK13342 |
recombination factor protein RarA; Reviewed |
189-289 |
1.06e-03 |
|
recombination factor protein RarA; Reviewed
Pssm-ID: 237355 [Multi-domain] Cd Length: 413 Bit Score: 41.99 E-value: 1.06e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2021509219 189 LIGRDKELERAIQvlcRRRKNNPLLVGESGVGKTAIAEGLAwrivqgdvpeVMADCTIYSLDigSLLAGTKyrgDFEKRF 268
Cdd:PRK13342 20 LLGPGKPLRRMIE---AGRLSSMILWGPPGTGKTTLARIIA----------GATDAPFEALS--AVTSGVK---DLREVI 81
|
90 100
....*....|....*....|.
gi 2021509219 269 KALLKQLEQDTNSILFIDEIH 289
Cdd:PRK13342 82 EEARQRRSAGRRTILFIDEIH 102
|
|
| RecA-like_HslU |
cd19498 |
ATP-dependent protease ATPase subunit HslU; HslU is a component of the ATP-dependent protease ... |
209-312 |
1.36e-03 |
|
ATP-dependent protease ATPase subunit HslU; HslU is a component of the ATP-dependent protease HslVU. In HslVU, HslU ATPase serves to unfold and translocate protein substrate, and the HslV protease degrades the unfolded proteins. This RecA-like_HslU subfamily belongs to the RecA-like NTPase family which includes the NTP binding domain of F1 and V1 H(+)ATPases, DnaB and related helicases as well as bacterial RecA and related eukaryotic and archaeal recombinases. The RecA-like NTPase family also includes bacterial conjugation proteins and related DNA transfer proteins involved in type II and type IV secretion.
Pssm-ID: 410906 [Multi-domain] Cd Length: 183 Bit Score: 40.44 E-value: 1.36e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2021509219 209 NNPLLVGESGVGKTAIAEGLAwRIVqgDVPEVMADCTIYSlDIGsllagtkYRG-DFEKRFKALlkqleqdTNSILFIDE 287
Cdd:cd19498 47 KNILMIGPTGVGKTEIARRLA-KLA--GAPFIKVEATKFT-EVG-------YVGrDVESIIRDL-------VEGIVFIDE 108
|
90 100
....*....|....*....|....*
gi 2021509219 288 IHTIIGAGAASGGQVDAANLIKPLL 312
Cdd:cd19498 109 IDKIAKRGGSSGPDVSREGVQRDLL 133
|
|
| clpX |
PRK05342 |
ATP-dependent Clp protease ATP-binding subunit ClpX; |
208-245 |
1.42e-03 |
|
ATP-dependent Clp protease ATP-binding subunit ClpX;
Pssm-ID: 235422 [Multi-domain] Cd Length: 412 Bit Score: 41.68 E-value: 1.42e-03
10 20 30
....*....|....*....|....*....|....*...
gi 2021509219 208 KNNPLLVGESGVGKTAIAEGLAwRIVqgDVPEVMADCT 245
Cdd:PRK05342 108 KSNILLIGPTGSGKTLLAQTLA-RIL--DVPFAIADAT 142
|
|
| RecA-like_ClpB_Hsp104-like |
cd19499 |
Chaperone protein ClpB/Hsp104 subfamily; Bacterial Caseinolytic peptidase B (ClpB) and ... |
182-288 |
1.70e-03 |
|
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: 40.24 E-value: 1.70e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2021509219 182 RVGGIDPLIgrdKELERAIQvLCR---RRKNNP----LLVGESGVGKTAIAEGLAWRIVQGDVPEVMADCTIYS-LDIGS 253
Cdd:cd19499 12 RVVGQDEAV---KAVSDAIR-RARaglSDPNRPigsfLFLGPTGVGKTELAKALAELLFGDEDNLIRIDMSEYMeKHSVS 87
|
90 100 110
....*....|....*....|....*....|....*..
gi 2021509219 254 LLAGT--KYRGdFEKRFKaLLKQLEQDTNSILFIDEI 288
Cdd:cd19499 88 RLIGAppGYVG-YTEGGQ-LTEAVRRKPYSVVLLDEI 122
|
|
| PRK14969 |
PRK14969 |
DNA polymerase III subunits gamma and tau; Provisional |
463-516 |
1.88e-03 |
|
DNA polymerase III subunits gamma and tau; Provisional
Pssm-ID: 237873 [Multi-domain] Cd Length: 527 Bit Score: 41.66 E-value: 1.88e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 2021509219 463 GQDKAIEALTEAIKMARagLGHehkpvgSFLFAGPTGVGKTEVTVQLAKALGIE 516
Cdd:PRK14969 20 GQEHVVRALTNALEQQR--LHH------AYLFTGTRGVGKTTLARILAKSLNCE 65
|
|
| AAA_22 |
pfam13401 |
AAA domain; |
205-289 |
2.49e-03 |
|
AAA domain;
Pssm-ID: 379165 [Multi-domain] Cd Length: 129 Bit Score: 38.86 E-value: 2.49e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2021509219 205 RRRKNNPLLVGESGVGKTAIAEGLAWRIVQGDVP----EVMADCTIYSLdIGSLLAGTKYRGDFEKRFKALLKQLEQ--- 277
Cdd:pfam13401 2 RFGAGILVLTGESGTGKTTLLRRLLEQLPEVRDSvvfvDLPSGTSPKDL-LRALLRALGLPLSGRLSKEELLAALQQlll 80
|
90
....*....|....
gi 2021509219 278 --DTNSILFIDEIH 289
Cdd:pfam13401 81 alAVAVVLIIDEAQ 94
|
|
| RecA-like_ATAD1 |
cd19520 |
ATPase domain of ATPase family AAA domain-containing protein 1 and similar ATPase domains; ... |
212-344 |
3.40e-03 |
|
ATPase domain of ATPase family AAA domain-containing protein 1 and similar ATPase domains; ATPase family AAA domain-containing protein 1 (ATAD1, also known as Thorase) is an ATPase that plays a critical role in regulating the surface expression of alpha-amino-3-hydroxy-5-methyl-4-isoxazolepropionic acid (AMPA) receptors, thereby regulating synaptic plasticity, learning and memory. 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: 410928 [Multi-domain] Cd Length: 166 Bit Score: 38.94 E-value: 3.40e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2021509219 212 LLVGESGVGKTAIAEGLAWRivqgdvpevmADCTIYSLDIGSLLagTKYRGDFEKRFKALLKQLEQDTNSILFIDEIHTI 291
Cdd:cd19520 39 LLYGPPGCGKTMLAKATAKE----------AGARFINLQVSSLT--DKWYGESQKLVAAVFSLASKLQPSIIFIDEIDSF 106
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2021509219 292 IGAGAASGGQVDAA------NLIKPLLSGGKIRVI--GSTtyqefSNIFEKDRALARRFQK 344
Cdd:cd19520 107 LRQRSSTDHEATAMmkaefmSLWDGLSTDGNCRVIvmGAT-----NRPQDLDEAILRRMPK 162
|
|
| PRK12323 |
PRK12323 |
DNA polymerase III subunit gamma/tau; |
463-513 |
3.48e-03 |
|
DNA polymerase III subunit gamma/tau;
Pssm-ID: 237057 [Multi-domain] Cd Length: 700 Bit Score: 40.63 E-value: 3.48e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 2021509219 463 GQDKAIEALTEAIKMARagLGHehkpvgSFLFAGPTGVGKTEVTVQLAKAL 513
Cdd:PRK12323 20 GQEHVVRALTHALEQQR--LHH------AYLFTGTRGVGKTTLSRILAKSL 62
|
|
| AAA_22 |
pfam13401 |
AAA domain; |
490-586 |
3.79e-03 |
|
AAA domain;
Pssm-ID: 379165 [Multi-domain] Cd Length: 129 Bit Score: 38.09 E-value: 3.79e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2021509219 490 GSFLFAGPTGVGKTEVTVQLAKAL---GIELLRFDMSEYME----RHTVSRLIGAPPgyVGFDQGGLLTDAVIKH----- 557
Cdd:pfam13401 6 GILVLTGESGTGKTTLLRRLLEQLpevRDSVVFVDLPSGTSpkdlLRALLRALGLPL--SGRLSKEELLAALQQLllala 83
|
90 100
....*....|....*....|....*....
gi 2021509219 558 PHAVLLLDEIEKAHPDVFNILLQVMDNGT 586
Cdd:pfam13401 84 VAVVLIIDEAQHLSLEALEELRDLLNLSS 112
|
|
| RecA-like_NVL_r1-like |
cd19518 |
first of two ATPase domains of NVL (nuclear VCP-like protein) and similar ATPase domains; NVL ... |
212-324 |
3.89e-03 |
|
first of two ATPase domains of NVL (nuclear VCP-like protein) and similar ATPase domains; NVL exists in two forms with N-terminal extensions of different lengths in mammalian cells. NVL has two alternatively spliced isoforms, a short form, NVL1, and a long form, NVL2. NVL2, the major species, is mainly present in the nucleolus, whereas NVL1 is nucleoplasmic. Each has an N-terminal domain, followed by two tandem ATPase domains; this subfamily includes the first of the two ATPase domains. NVL2 is involved in the biogenesis of the 60S ribosome subunit by associating specifically with ribosome protein L5 and modulating the function of DOB1. NVL2 is also required for telomerase assembly and the regulation of telomerase activity, and is involved in pre-rRNA processing. The role of NVL1 is unclear. This RecA-like_NVL_r1-like subfamily belongs to the RecA-like NTPase family which includes the NTP binding domain of F1 and V1 H(+)ATPases, DnaB and related helicases as well as bacterial RecA and related eukaryotic and archaeal recombinases. The RecA-like NTPase family also includes bacterial conjugation proteins and related DNA transfer proteins involved in type II and type IV secretion.
Pssm-ID: 410926 [Multi-domain] Cd Length: 169 Bit Score: 38.92 E-value: 3.89e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2021509219 212 LLVGESGVGKTAIAEGLAWRIvqgDVPevmadctIYSLDIGSLLAGTKyrGDFEKRFKALLKQLEQDTNSILFIDEIHTI 291
Cdd:cd19518 38 LLHGPPGCGKTMLANAIAGEL---KVP-------FLKISATEIVSGVS--GESEEKIRELFDQAISNAPCIVFIDEIDAI 105
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 2021509219 292 igAGAASGGQVDAA------------NLIKPLLSGGKIRVIGSTT 324
Cdd:cd19518 106 --TPKRESAQREMErrivsqlltcmdELNNEKTAGGPVLVIGATN 148
|
|
| TIGR02928 |
TIGR02928 |
orc1/cdc6 family replication initiation protein; Members of this protein family are found ... |
187-328 |
5.54e-03 |
|
orc1/cdc6 family replication initiation protein; Members of this protein family are found exclusively in the archaea. This set of DNA binding proteins shows homology to the origin recognition complex subunit 1/cell division control protein 6 family in eukaryotes. Several members may be found in genome and interact with each other. [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 274354 [Multi-domain] Cd Length: 365 Bit Score: 39.92 E-value: 5.54e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2021509219 187 DPLIGRDKELE---RAIQVLCR-RRKNNPLLVGESGVGKTAIAEGLAwRIVQGDVPE-------VMADCTIYS------L 249
Cdd:TIGR02928 15 DRIVHRDEQIEelaKALRPILRgSRPSNVFIYGKTGTGKTAVTKYVM-KELEEAAEDrdvrvvtVYVNCQILDtlyqvlV 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2021509219 250 DIGSLLAGTK----YRG-DFEKRFKALLKQLEQDTNSILFI-DEIHTIIGAG---------AASGGQVDaanlikpllsG 314
Cdd:TIGR02928 94 ELANQLRGSGeevpTTGlSTSEVFRRLYKELNERGDSLIIVlDEIDYLVGDDddllyqlsrARSNGDLD----------N 163
|
170
....*....|....
gi 2021509219 315 GKIRVIGSTTYQEF 328
Cdd:TIGR02928 164 AKVGVIGISNDLKF 177
|
|
| PRK14965 |
PRK14965 |
DNA polymerase III subunits gamma and tau; Provisional |
463-516 |
6.44e-03 |
|
DNA polymerase III subunits gamma and tau; Provisional
Pssm-ID: 237871 [Multi-domain] Cd Length: 576 Bit Score: 39.72 E-value: 6.44e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 2021509219 463 GQDKAIEALTEAIKMARagLGHehkpvgSFLFAGPTGVGKTEVTVQLAKALGIE 516
Cdd:PRK14965 20 GQEHVSRTLQNAIDTGR--VAH------AFLFTGARGVGKTSTARILAKALNCE 65
|
|
| COG3899 |
COG3899 |
Predicted ATPase [General function prediction only]; |
5-237 |
7.35e-03 |
|
Predicted ATPase [General function prediction only];
Pssm-ID: 443106 [Multi-domain] Cd Length: 1244 Bit Score: 39.84 E-value: 7.35e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2021509219 5 ELELSLNMAFARAREHRHEFMTVEHLLLALLSNPSAREALEACSVDLVALRQELEAFIEQTTPVLPATEEERDTQPTLSF 84
Cdd:COG3899 105 LLLLLALALLLLALLALALLALLLALLLAAGVLGLLLGGLLLAALAALLALAALAAAAAAAAAAAAARAARLRRARAARL 184
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2021509219 85 QRVLQRAVFHVQSSGRSEVTGANVLVAIFSEQESQAAYLLRKHEVSRLDVVNFISHGTRKDEPSQPSENNASQPGNEEQA 164
Cdd:COG3899 185 AALALRALLLLVLLLLLLLLLLGLLLAAAAALAAAAAAAAAAAPAAPVVLVAALLLALAALLALLLLAARLLGLAGAAAL 264
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2021509219 165 GGEDRMENFTTNLNQLARVGGIDPLIGRDKELERAIQVL--CRRRKNNPLLV-GESGVGKTAIAEGLAWRIVQGDV 237
Cdd:COG3899 265 LLLGLLAAAAAGRRLLARRLIPQPLVGREAELAALLAALerARAGRGELVLVsGEAGIGKSRLVRELARRARARGG 340
|
|
| PRK14953 |
PRK14953 |
DNA polymerase III subunits gamma and tau; Provisional |
461-513 |
7.44e-03 |
|
DNA polymerase III subunits gamma and tau; Provisional
Pssm-ID: 237867 [Multi-domain] Cd Length: 486 Bit Score: 39.42 E-value: 7.44e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 2021509219 461 VFGQDKAIEALTEAIKMARagLGHehkpvgSFLFAGPTGVGKTEVTVQLAKAL 513
Cdd:PRK14953 18 VIGQEIVVRILKNAVKLQR--VSH------AYIFAGPRGTGKTTIARILAKVL 62
|
|
| |
