|
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: 1604.12 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2298857976 1 MLNQELELSLNMAFARAREHRHEFMTVEHLLLALLSNPAAREALEACTVDLAALRQELEAFIEQTTPTLPASEEERDTQP 80
Cdd:PRK11034 1 MLNQELELSLNMAFARAREHRHEFMTVEHLLLALLSNPSAREALEACSVDLVALRQELEAFIEQTTPVLPASEEERDTQP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2298857976 81 TLSFQRVLQRAVFHVQSSGRSEVSGANVLVAIFSEQESQAAYLLRKHDVSRLDVVNFISHGTRKDEPGQ-APNAENPVNE 159
Cdd:PRK11034 81 TLSFQRVLQRAVFHVQSSGRSEVTGANVLVAIFSEQESQAAYLLRKHEVSRLDVVNFISHGTRKDEPSQsSDPGSQPNSE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2298857976 160 EQSGGEDRMENFTTNLNQLARVGGIDPLIGRDPELERAIQVLCRRRKNNPLLVGESGVGKTAIAEGLAWRIVQGDVPEVM 239
Cdd:PRK11034 161 EQAGGEERMENFTTNLNQLARVGGIDPLIGREKELERAIQVLCRRRKNNPLLVGESGVGKTAIAEGLAWRIVQGDVPEVM 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2298857976 240 ADCTLYSLDIGSLLAGTKYRGDFEKRFKALLKQLEQDQNSILFIDEIHTIIGAGAASGGQVDAANLIKPLLSSGKIRVIG 319
Cdd:PRK11034 241 ADCTIYSLDIGSLLAGTKYRGDFEKRFKALLKQLEQDTNSILFIDEIHTIIGAGAASGGQVDAANLIKPLLSSGKIRVIG 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2298857976 320 STTYQEFSNIFEKDRALARRFQKIDITEPTPEETVQIINGLKTKYEAHHDVRYTAKAIRAAVELSVKYINDRHLPDKAID 399
Cdd:PRK11034 321 STTYQEFSNIFEKDRALARRFQKIDITEPSIEETVQIINGLKPKYEAHHDVRYTAKAVRAAVELAVKYINDRHLPDKAID 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2298857976 400 VIDEAGARSRLMPVSKRKKTVNVADIESVVARIARIPEKTVSASDRDVLRSLGDRLKMLVFGQDQAIEALTEAIKMSRAG 479
Cdd:PRK11034 401 VIDEAGARARLMPVSKRKKTVNVADIESVVARIARIPEKSVSQSDRDTLKNLGDRLKMLVFGQDKAIEALTEAIKMSRAG 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2298857976 480 LGHDRKPVGSFLFAGPTGVGKTEVTVQLAKAMDIELLRFDMSEYMERHTVSRLIGAPPGYVGYDQGGLLTDAVIKHPHSV 559
Cdd:PRK11034 481 LGHEHKPVGSFLFAGPTGVGKTEVTVQLSKALGIELLRFDMSEYMERHTVSRLIGAPPGYVGFDQGGLLTDAVIKHPHAV 560
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2298857976 560 VLLDEIEKAHPDVFNLLLQVMDNGTLTDNNGRKADFRNVILVMTTNAGVRETERKSIGLVQQDNSTDAMEEIKKVFTPEF 639
Cdd:PRK11034 561 LLLDEIEKAHPDVFNLLLQVMDNGTLTDNNGRKADFRNVVLVMTTNAGVRETERKSIGLIHQDNSTDAMEEIKKIFTPEF 640
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2298857976 640 RNRLDNIIWFNHLSTEVIQQVVDKFIVELQAQLDAKGVSLEVSDEARDWLSVKGYDRAMGARPMARVMQENLKKPLANEL 719
Cdd:PRK11034 641 RNRLDNIIWFDHLSTDVIHQVVDKFIVELQAQLDQKGVSLEVSQEARDWLAEKGYDRAMGARPMARVIQDNLKKPLANEL 720
|
730 740 750 760
....*....|....*....|....*....|....*....|
gi 2298857976 720 LFGSLVDGGSVKVELDKDKKQLTYHFLSAQKRKADegAVH 759
Cdd:PRK11034 721 LFGSLVDGGQVTVALDKEKNELTYGFQSAQKHKAE--AAH 758
|
|
| ClpA |
TIGR02639 |
ATP-dependent Clp protease ATP-binding subunit clpA; [Protein fate, Degradation of proteins, ... |
2-734 |
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: 1118.95 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2298857976 2 LNQELELSLNMAFARAREHRHEFMTVEHLLLALLSNPAAREALEACTVDLAALRQELEAFIEQTTPTLPaSEEERDTQPT 81
Cdd:TIGR02639 1 ISEELERILSDALEEAKERRHEFVTLEHLLLALLDDNEAIEILEECGGDVELLRKRLEDYLEENLPVIP-EDIDEEPEQT 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2298857976 82 LSFQRVLQRAVFHVQSSGRSEVSGANVLVAIFSEQESQAAYLLRKHDVSRLDVVNFISHGTRKDePGQAPNAENPVNEEQ 161
Cdd:TIGR02639 80 VGVQRVIQRALLHVKSAGKKEIDIGDLLVALFDEEDSHASYFLKSQGITRLDILNYISHGISKD-DGKDQLGEEAGKEEE 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2298857976 162 SGgEDRMENFTTNLNQLARVGGIDPLIGRDPELERAIQVLCRRRKNNPLLVGESGVGKTAIAEGLAWRIVQGDVPEVMAD 241
Cdd:TIGR02639 159 KG-QDALEKYTVDLTEKAKNGKIDPLIGREDELERTIQVLCRRKKNNPLLVGEPGVGKTAIVEGLALRIAEGKVPERLKN 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2298857976 242 CTLYSLDIGSLLAGTKYRGDFEKRFKALLKQLEQDQNSILFIDEIHTIIGAGAASGGQVDAANLIKPLLSSGKIRVIGST 321
Cdd:TIGR02639 238 AKIYSLDMGTLLAGTKYRGDFEERLKAVVSEIEKEPNAILFIDEIHTIVGAGATSGGSMDASNLLKPALSSGKIRCIGST 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2298857976 322 TYQEFSNIFEKDRALARRFQKIDITEPTPEETVQIINGLKTKYEAHHDVRYTAKAIRAAVELSVKYINDRHLPDKAIDVI 401
Cdd:TIGR02639 318 TYEEYKNHFEKDRALSRRFQKIDVGEPSIEETVKILKGLKEQYEEFHHVKYSDEALEAAVELSARYINDRFLPDKAIDVI 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2298857976 402 DEAGARSRLMPVSKRKKTVNVADIESVVARIARIPEKTVSASDRDVLRSLGDRLKMLVFGQDQAIEALTEAIKMSRAGLG 481
Cdd:TIGR02639 398 DEAGAAFRLRPKAKKKANVNVKDIENVVAKMAKIPVKTVSSDDREQLKNLEKNLKAKIFGQDEAIDQLVSAIKRSRAGLG 477
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2298857976 482 HDRKPVGSFLFAGPTGVGKTEVTVQLAKAMDIELLRFDMSEYMERHTVSRLIGAPPGYVGYDQGGLLTDAVIKHPHSVVL 561
Cdd:TIGR02639 478 DPNKPVGSFLFVGPTGVGKTELAKQLAEELGVHLLRFDMSEYMEKHTVSRLIGSPPGYVGFEQGGLLTDAVRKHPHCVLL 557
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2298857976 562 LDEIEKAHPDVFNLLLQVMDNGTLTDNNGRKADFRNVILVMTTNAGVRETERKSIGLVqQDNSTDAMEE-IKKVFTPEFR 640
Cdd:TIGR02639 558 LDEIEKAHPDIYNILLQVMDYATLTDNNGRKADFRNVILIMTSNAGASEMSKPPIGFG-GENRESKSLKaIKKLFSPEFR 636
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2298857976 641 NRLDNIIWFNHLSTEVIQQVVDKFIVELQAQLDAKGVSLEVSDEARDWLSVKGYDRAMGARPMARVMQENLKKPLANELL 720
Cdd:TIGR02639 637 NRLDAIIHFNDLSEEMAEKIVKKFLDELQDQLNEKNIELELTDDAKKYLAEKGYDEEFGARPLARVIQEEIKKPLSDEIL 716
|
730
....*....|....
gi 2298857976 721 FGSLVDGGSVKVEL 734
Cdd:TIGR02639 717 FGKLKKGGSVKISL 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: 859.00 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2298857976 2 LNQELELSLNMAFARAREHRHEFMTVEHLLLALLSNP--AAREALEACTVDLAALRQELEAFIEQTTPTLPASEeerdtQ 79
Cdd:COG0542 6 FTEKAQEALEAAQELARRLGHQEVEPEHLLLALLEQGegLAAKLLRKLGVDLDALREELEEALGRLPKVSGSSG-----Q 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2298857976 80 PTLS--FQRVLQRAVFHVQSSGRSEVSGANVLVAIFSEQESQAAYLLRKHDVSRLDVVNFIShGTRKDEPGQAPNAEnpv 157
Cdd:COG0542 81 PYLSprLKRVLELAELEARKLGDEYISTEHLLLALLREGEGVAARILKKLGITLEALREALE-ELRGGSRVTSQNPE--- 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2298857976 158 neeqsGGEDRMENFTTNLNQLARVGGIDPLIGRDPELERAIQVLCRRRKNNPLLVGESGVGKTAIAEGLAWRIVQGDVPE 237
Cdd:COG0542 157 -----SKTPALDKYGRDLTELAREGKLDPVIGRDEEIRRVIQILSRRTKNNPVLIGEPGVGKTAIVEGLAQRIVNGDVPE 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2298857976 238 VMADCTLYSLDIGSLLAGTKYRGDFEKRFKALLKQLEQ-DQNSILFIDEIHTIIGAGAASgGQVDAANLIKPLLSSGKIR 316
Cdd:COG0542 232 SLKDKRVLSLDLGALVAGAKYRGEFEERLKAVLDEVKKsEGNIILFIDELHTLVGAGGAE-GAMDAANLLKPALARGELR 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2298857976 317 VIGSTTYQEFSNIFEKDRALARRFQKIDITEPTPEETVQIINGLKTKYEAHHDVRYTAKAIRAAVELSVKYINDRHLPDK 396
Cdd:COG0542 311 CIGATTLDEYRKYIEKDAALERRFQPVLVEEPSVEDTISILRGLKERYEAHHGVRITDEALVAAVRLSDRYITDRFLPDK 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2298857976 397 AIDVIDEAGARSRLMPVSK------------------------------------------------------------- 415
Cdd:COG0542 391 AIDLIDEAAARVRMEIDSKpeeldelerrleqleiekealkkeqdeasferlaelrdelaeleeelealkarweaekeli 470
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2298857976 416 -------------------------------------RKKTVNVADIESVVARIARIPEKTVSASDRDVLRSLGDRLKML 458
Cdd:COG0542 471 eeiqelkeeleqrygkipelekelaeleeelaelaplLREEVTEEDIAEVVSRWTGIPVGKLLEGEREKLLNLEEELHER 550
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2298857976 459 VFGQDQAIEALTEAIKMSRAGLGHDRKPVGSFLFAGPTGVGKTEVTVQLAKAM-DIE--LLRFDMSEYMERHTVSRLIGA 535
Cdd:COG0542 551 VIGQDEAVEAVADAIRRSRAGLKDPNRPIGSFLFLGPTGVGKTELAKALAEFLfGDEdaLIRIDMSEYMEKHSVSRLIGA 630
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2298857976 536 PPGYVGYDQGGLLTDAVIKHPHSVVLLDEIEKAHPDVFNLLLQVMDNGTLTDNNGRKADFRNVILVMTTNAGVRE-TERK 614
Cdd:COG0542 631 PPGYVGYEEGGQLTEAVRRRPYSVVLLDEIEKAHPDVFNILLQVLDDGRLTDGQGRTVDFRNTIIIMTSNIGSELiLDLA 710
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2298857976 615 SIGLVQQDNSTDAMEEIKKVFTPEFRNRLDNIIWFNHLSTEVIQQVVDKFIVELQAQLDAKGVSLEVSDEARDWLSVKGY 694
Cdd:COG0542 711 EDEPDYEEMKEAVMEELKKHFRPEFLNRIDEIIVFHPLSKEELRKIVDLQLKRLRKRLAERGITLELTDAAKDFLAEKGY 790
|
810 820 830 840
....*....|....*....|....*....|....*....|....
gi 2298857976 695 DRAMGARPMARVMQENLKKPLANELLFGSLVDGGSVKVELDKDK 738
Cdd:COG0542 791 DPEYGARPLKRAIQRELEDPLAEEILAGEIKEGDTITVDVDDGE 834
|
|
| chaperone_ClpB |
TIGR03346 |
ATP-dependent chaperone ClpB; Members of this protein family are the bacterial ATP-dependent ... |
17-738 |
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: 686.69 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2298857976 17 AREHRHEFMTVEHLLLALL--SNPAAREALEACTVDLAALRQELEAFIEQttptLPA-SEEERDTQPTLSFQRVLQRAVF 93
Cdd:TIGR03346 16 ALGRDHQQIEPEHLLKALLdqEGGLARPLLQKAGVNVGALRQALEKELER----LPKvSGPGGQVYLSPDLNRLLNLAEK 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2298857976 94 HVQSSGRSEVSGANVLVAIfSEQESQAAYLLRKHDVSRLDVVNFIsHGTRKDEPGQAPNAENpvneeqsgGEDRMENFTT 173
Cdd:TIGR03346 92 LAQKRGDEFISSEHLLLAL-LDDKGTLGKLLKEAGATADALEAAI-NAVRGGQKVTDANAED--------QYEALEKYAR 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2298857976 174 NLNQLARVGGIDPLIGRDPELERAIQVLCRRRKNNPLLVGESGVGKTAIAEGLAWRIVQGDVPEVMADCTLYSLDIGSLL 253
Cdd:TIGR03346 162 DLTERAREGKLDPVIGRDEEIRRTIQVLSRRTKNNPVLIGEPGVGKTAIVEGLAQRIVNGDVPEGLKNKRLLALDMGALI 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2298857976 254 AGTKYRGDFEKRFKALLKQLE-QDQNSILFIDEIHTIIGAGAASGGqVDAANLIKPLLSSGKIRVIGSTTYQEFSNIFEK 332
Cdd:TIGR03346 242 AGAKYRGEFEERLKAVLNEVTkSEGQIILFIDELHTLVGAGKAEGA-MDAGNMLKPALARGELHCIGATTLDEYRKYIEK 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2298857976 333 DRALARRFQKIDITEPTPEETVQIINGLKTKYEAHHDVRYTAKAIRAAVELSVKYINDRHLPDKAIDVIDEAGARSRL-- 410
Cdd:TIGR03346 321 DAALERRFQPVFVDEPSVEDTISILRGLKERYEVHHGVRITDPAIVAAATLSHRYITDRFLPDKAIDLIDEAAARIRMei 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2298857976 411 --MP---------------------------------------------------------------------------- 412
Cdd:TIGR03346 401 dsKPeeldeldrriiqleierealkkekdeaskkrledlekeladleeeyaeleeqwkaekasiqgiqqikeeieqvrle 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2298857976 413 --VSKR-------------------------------------KKTVNVADIESVVARIARIPEKTVSASDRDVLRSLGD 453
Cdd:TIGR03346 481 leQAERegdlakaaelqygklpelekqlqaaeqklgeeqnrllREEVTAEEIAEVVSRWTGIPVSKMLEGEREKLLHMEE 560
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2298857976 454 RLKMLVFGQDQAIEALTEAIKMSRAGLGHDRKPVGSFLFAGPTGVGKTEVTVQLAKAM-DIE--LLRFDMSEYMERHTVS 530
Cdd:TIGR03346 561 ELHERVVGQDEAVEAVSDAIRRSRAGLSDPNRPIGSFLFLGPTGVGKTELAKALAEFLfDSEdaMVRIDMSEYMEKHSVA 640
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2298857976 531 RLIGAPPGYVGYDQGGLLTDAVIKHPHSVVLLDEIEKAHPDVFNLLLQVMDNGTLTDNNGRKADFRNVILVMTTNAGVRE 610
Cdd:TIGR03346 641 RLIGAPPGYVGYEEGGQLTEAVRRRPYSVVLFDEVEKAHPDVFNVLLQVLDDGRLTDGQGRTVDFRNTVIIMTSNLGSDF 720
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2298857976 611 TERKSIGLVQQDNSTDAMEEIKKVFTPEFRNRLDNIIWFNHLSTEVIQQVVDKFIVELQAQLDAKGVSLEVSDEARDWLS 690
Cdd:TIGR03346 721 IQELAGGDDYEEMREAVMEVLRAHFRPEFLNRIDEIVVFHPLGREQIARIVEIQLGRLRKRLAERKITLELSDAALDFLA 800
|
810 820 830 840
....*....|....*....|....*....|....*....|....*...
gi 2298857976 691 VKGYDRAMGARPMARVMQENLKKPLANELLFGSLVDGGSVKVELDKDK 738
Cdd:TIGR03346 801 EAGYDPVYGARPLKRAIQREIENPLAKKILAGEVAPGDTIRVDVEGGR 848
|
|
| clpC |
CHL00095 |
Clp protease ATP binding subunit |
1-739 |
0e+00 |
|
Clp protease ATP binding subunit
Pssm-ID: 214361 [Multi-domain] Cd Length: 821 Bit Score: 671.77 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2298857976 1 MLNQELelslnmafarAREHRHEFMTVEHLLLALL--SNPAAREALEACTVDLAALRQELEAFIEQTTpTLPASEeerdT 78
Cdd:CHL00095 14 MLSQEE----------ARRLGHNFVGTEQILLGLIgeGTGIAARALKSMGVTLKDARIEVEKIIGRGT-GFVAVE----I 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2298857976 79 QPTLSFQRVLQRAVFHVQSSGRSEVSGANVLVAIFSEQESQAAYLLRKHDVS----RLDVVNFISHGTRKDEPGQAPNAE 154
Cdd:CHL00095 79 PFTPRAKRVLEMSLEEARDLGHNYIGTEHLLLALLEEGEGVAARVLENLGVDlskiRSLILNLIGEIIEAILGAEQSRSK 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2298857976 155 NPVNEEqsggedrmenFTTNLNQLARVGGIDPLIGRDPELERAIQVLCRRRKNNPLLVGESGVGKTAIAEGLAWRIVQGD 234
Cdd:CHL00095 159 TPTLEE----------FGTNLTKEAIDGNLDPVIGREKEIERVIQILGRRTKNNPILIGEPGVGKTAIAEGLAQRIVNRD 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2298857976 235 VPEVMADCTLYSLDIGSLLAGTKYRGDFEKRFKALLKQLEQDQNSILFIDEIHTIIGAGAASGGqVDAANLIKPLLSSGK 314
Cdd:CHL00095 229 VPDILEDKLVITLDIGLLLAGTKYRGEFEERLKRIFDEIQENNNIILVIDEVHTLIGAGAAEGA-IDAANILKPALARGE 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2298857976 315 IRVIGSTTYQEFSNIFEKDRALARRFQKIDITEPTPEETVQIINGLKTKYEAHHDVRYTAKAIRAAVELSVKYINDRHLP 394
Cdd:CHL00095 308 LQCIGATTLDEYRKHIEKDPALERRFQPVYVGEPSVEETIEILFGLRSRYEKHHNLSISDKALEAAAKLSDQYIADRFLP 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2298857976 395 DKAIDVIDEAGARSRLM-----------------------------------------------------------PVSK 415
Cdd:CHL00095 388 DKAIDLLDEAGSRVRLInsrlppaareldkelreilkdkdeaireqdfetakqlrdremevraqiaaiiqskkteeEKRL 467
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2298857976 416 RKKTVNVADIESVVARIARIPEKTVSASDRDVLRSLGDRLKMLVFGQDQAIEALTEAIKMSRAGLGHDRKPVGSFLFAGP 495
Cdd:CHL00095 468 EVPVVTEEDIAEIVSAWTGIPVNKLTKSESEKLLHMEETLHKRIIGQDEAVVAVSKAIRRARVGLKNPNRPIASFLFSGP 547
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2298857976 496 TGVGKTEVTVQLAKAM---DIELLRFDMSEYMERHTVSRLIGAPPGYVGYDQGGLLTDAVIKHPHSVVLLDEIEKAHPDV 572
Cdd:CHL00095 548 TGVGKTELTKALASYFfgsEDAMIRLDMSEYMEKHTVSKLIGSPPGYVGYNEGGQLTEAVRKKPYTVVLFDEIEKAHPDI 627
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2298857976 573 FNLLLQVMDNGTLTDNNGRKADFRNVILVMTTNAGVRETERKSIGL------VQQDNSTDAM------EEIKKVFTPEFR 640
Cdd:CHL00095 628 FNLLLQILDDGRLTDSKGRTIDFKNTLIIMTSNLGSKVIETNSGGLgfelseNQLSEKQYKRlsnlvnEELKQFFRPEFL 707
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2298857976 641 NRLDNIIWFNHLSTEVIQQVVDKFIVELQAQLDAKGVSLEVSDEARDWLSVKGYDRAMGARPMARVMQENLKKPLANELL 720
Cdd:CHL00095 708 NRLDEIIVFRQLTKNDVWEIAEIMLKNLFKRLNEQGIQLEVTERIKTLLIEEGYNPLYGARPLRRAIMRLLEDPLAEEVL 787
|
810
....*....|....*....
gi 2298857976 721 FGSLVDGGSVKVELDKDKK 739
Cdd:CHL00095 788 SFKIKPGDIIIVDVNDEKE 806
|
|
| VI_ClpV1 |
TIGR03345 |
type VI secretion ATPase, ClpV1 family; Members of this protein family are homologs of ClpB, ... |
2-720 |
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: 556.48 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2298857976 2 LNQELELSLNMAFARAREHRHEFMTVEHLLLALLSNPA--AREALEACTVDLAALRQELEAFIEQttptLPASEEERdtq 79
Cdd:TIGR03345 1 LNPTSRRALEQAAALCVARGHPEVELEHWLLALLDQPDsdLAAILRHFGVDLGRLKADLARALDK----LPRGNTRT--- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2298857976 80 PTLS--FQRVLQRAvFHVQSS--GRSEVSGANVLVAIFSEQE-----SQAAYLLRKHDVSRLD-VVNFISHGTRkdEPGQ 149
Cdd:TIGR03345 74 PVFSphLVELLQEA-WLLASLelGDGRIRSGHLLLALLTDPElrrllGSISPELAKIDREALReALPALVEGSA--EASA 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2298857976 150 APNAENPVNEEQS-GGEDRMENFTTNLNQLARVGGIDPLIGRDPELERAIQVLCRRRKNNPLLVGESGVGKTAIAEGLAW 228
Cdd:TIGR03345 151 AAADAAPAGAAAGaAGTSALDQYTTDLTAQAREGKIDPVLGRDDEIRQMIDILLRRRQNNPILTGEAGVGKTAVVEGLAL 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2298857976 229 RIVQGDVPEVMADCTLYSLDIGSLLAGTKYRGDFEKRFKALLKQLEQ-DQNSILFIDEIHTIIGAGAASgGQVDAANLIK 307
Cdd:TIGR03345 231 RIAAGDVPPALRNVRLLSLDLGLLQAGASVKGEFENRLKSVIDEVKAsPQPIILFIDEAHTLIGAGGQA-GQGDAANLLK 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2298857976 308 PLLSSGKIRVIGSTTYQEFSNIFEKDRALARRFQKIDITEPTPEETVQIINGLKTKYEAHHDVRYTAKAIRAAVELSVKY 387
Cdd:TIGR03345 310 PALARGELRTIAATTWAEYKKYFEKDPALTRRFQVVKVEEPDEETAIRMLRGLAPVLEKHHGVLILDEAVVAAVELSHRY 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2298857976 388 INDRHLPDKAIDVIDEAGARSRL--------------------------------------------------------- 410
Cdd:TIGR03345 390 IPGRQLPDKAVSLLDTACARVALsqnatpaaledlrrriaaleleldalereaalgadhderlaelraelaaleaelaal 469
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2298857976 411 --------------------------MPVSKRKKT------------------------VNVADIESVVARIARIPEKTV 440
Cdd:TIGR03345 470 earwqqekelveailalraeleadadAPADDDDALraqlaeleaalasaqgeeplvfpeVDAQAVAEVVADWTGIPVGRM 549
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2298857976 441 SASDRDVLRSLGDRLKMLVFGQDQAIEALTEAIKMSRAGLGHDRKPVGSFLFAGPTGVGKTEVTVQLAKAM---DIELLR 517
Cdd:TIGR03345 550 VRDEIEAVLSLPDRLAERVIGQDHALEAIAERIRTARAGLEDPRKPLGVFLLVGPSGVGKTETALALAELLyggEQNLIT 629
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2298857976 518 FDMSEYMERHTVSRLIGAPPGYVGYDQGGLLTDAVIKHPHSVVLLDEIEKAHPDVFNLLLQVMDNGTLTDNNGRKADFRN 597
Cdd:TIGR03345 630 INMSEFQEAHTVSRLKGSPPGYVGYGEGGVLTEAVRRKPYSVVLLDEVEKAHPDVLELFYQVFDKGVMEDGEGREIDFKN 709
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2298857976 598 VILVMTTNAGvreTERKSIGLVQQDNSTDA-------MEEIKKVFTPEFRNRLdNIIWFNHLSTEVIQQVVDKFIVELQA 670
Cdd:TIGR03345 710 TVILLTSNAG---SDLIMALCADPETAPDPeallealRPELLKVFKPAFLGRM-TVIPYLPLDDDVLAAIVRLKLDRIAR 785
|
810 820 830 840 850
....*....|....*....|....*....|....*....|....*....|.
gi 2298857976 671 QLDAK-GVSLEVSDEARDWLSVKGYDRAMGARPMARVMQENLKKPLANELL 720
Cdd:TIGR03345 786 RLKENhGAELVYSEALVEHIVARCTEVESGARNIDAILNQTLLPELSRQIL 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: 545.60 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2298857976 2 LNQELELSLNMAFARAREHRHEFMTVEHLLLALLSNPAA--REALEACTVDLAALRQEleafIEQTTPTLPASE-EERDT 78
Cdd:PRK10865 6 LTNKFQLALADAQSLALGHDNQFIEPLHLMSALLNQEGGsvRPLLTSAGINAGQLRTD----INQALSRLPQVEgTGGDV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2298857976 79 QPTLSFQRVLQRAVFHVQSSGRSEVSGANVLVAIFsEQESQAAYLLRKHDVSRLDVVNFIShgtrkdepgQAPNAENpVN 158
Cdd:PRK10865 82 QPSQDLVRVLNLCDKLAQKRGDNFISSELFVLAAL-ESRGTLADILKAAGATTANITQAIE---------QMRGGES-VN 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2298857976 159 EEqsGGEDR---MENFTTNLNQLARVGGIDPLIGRDPELERAIQVLCRRRKNNPLLVGESGVGKTAIAEGLAWRIVQGDV 235
Cdd:PRK10865 151 DQ--GAEDQrqaLKKYTIDLTERAEQGKLDPVIGRDEEIRRTIQVLQRRTKNNPVLIGEPGVGKTAIVEGLAQRIINGEV 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2298857976 236 PEVMADCTLYSLDIGSLLAGTKYRGDFEKRFKALLKQL-EQDQNSILFIDEIHTIIGAGAASGGqVDAANLIKPLLSSGK 314
Cdd:PRK10865 229 PEGLKGRRVLALDMGALVAGAKYRGEFEERLKGVLNDLaKQEGNVILFIDELHTMVGAGKADGA-MDAGNMLKPALARGE 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2298857976 315 IRVIGSTTYQEFSNIFEKDRALARRFQKIDITEPTPEETVQIINGLKTKYEAHHDVRYTAKAIRAAVELSVKYINDRHLP 394
Cdd:PRK10865 308 LHCVGATTLDEYRQYIEKDAALERRFQKVFVAEPSVEDTIAILRGLKERYELHHHVQITDPAIVAAATLSHRYIADRQLP 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2298857976 395 DKAIDVIDEAGARSRLMPVSK---------------------RKKT---------------------------------- 419
Cdd:PRK10865 388 DKAIDLIDEAASSIRMQIDSKpeeldrldrriiqlkleqqalMKESdeaskkrldmlneelsdkerqyseleeewkaeka 467
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2298857976 420 ---------------------------------------------------------------VNVADIESVVARIARIP 436
Cdd:PRK10865 468 slsgtqtikaeleqakiaieqarrvgdlarmselqygkipelekqlaaatqlegktmrllrnkVTDAEIAEVLARWTGIP 547
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2298857976 437 EKTVSASDRDVLRSLGDRLKMLVFGQDQAIEALTEAIKMSRAGLGHDRKPVGSFLFAGPTGVGKTEVTVQLAKAM---DI 513
Cdd:PRK10865 548 VSRMLESEREKLLRMEQELHHRVIGQNEAVEAVSNAIRRSRAGLSDPNRPIGSFLFLGPTGVGKTELCKALANFMfdsDD 627
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2298857976 514 ELLRFDMSEYMERHTVSRLIGAPPGYVGYDQGGLLTDAVIKHPHSVVLLDEIEKAHPDVFNLLLQVMDNGTLTDNNGRKA 593
Cdd:PRK10865 628 AMVRIDMSEFMEKHSVSRLVGAPPGYVGYEEGGYLTEAVRRRPYSVILLDEVEKAHPDVFNILLQVLDDGRLTDGQGRTV 707
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2298857976 594 DFRNVILVMTTNAGVRETERKSIGLVQQDNSTDAMEEIKKVFTPEFRNRLDNIIWFNHLSTEVIQQVVDKFIVELQAQLD 673
Cdd:PRK10865 708 DFRNTVVIMTSNLGSDLIQERFGELDYAHMKELVLGVVSHNFRPEFINRIDEVVVFHPLGEQHIASIAQIQLQRLYKRLE 787
|
810 820 830 840 850 860
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2298857976 674 AKGVSLEVSDEARDWLSVKGYDRAMGARPMARVMQENLKKPLANELLFGSLVDGGSVKVELDKD 737
Cdd:PRK10865 788 ERGYEIHISDEALKLLSENGYDPVYGARPLKRAIQQQIENPLAQQILSGELVPGKVIRLEVNDD 851
|
|
| RecA-like_ClpB_Hsp104-like |
cd19499 |
Chaperone protein ClpB/Hsp104 subfamily; Bacterial Caseinolytic peptidase B (ClpB) and ... |
448-649 |
6.33e-88 |
|
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: 274.44 E-value: 6.33e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2298857976 448 LRSLGDRLKMLVFGQDQAIEALTEAIKMSRAGLGHDRKPVGSFLFAGPTGVGKTEVTVQLAKAM---DIELLRFDMSEYM 524
Cdd:cd19499 2 LLNLEERLHERVVGQDEAVKAVSDAIRRARAGLSDPNRPIGSFLFLGPTGVGKTELAKALAELLfgdEDNLIRIDMSEYM 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2298857976 525 ERHTVSRLIGAPPGYVGYDQGGLLTDAVIKHPHSVVLLDEIEKAHPDVFNLLLQVMDNGTLTDNNGRKADFRNVILVMTT 604
Cdd:cd19499 82 EKHSVSRLIGAPPGYVGYTEGGQLTEAVRRKPYSVVLLDEIEKAHPDVQNLLLQVLDDGRLTDSHGRTVDFKNTIIIMTS 161
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 2298857976 605 NAgvreterksiglvqqdnstdameeikkvFTPEFRNRLDNIIWF 649
Cdd:cd19499 162 NH----------------------------FRPEFLNRIDEIVVF 178
|
|
| AAA_2 |
pfam07724 |
AAA domain (Cdc48 subfamily); This Pfam entry includes some of the AAA proteins not detected ... |
485-646 |
7.92e-79 |
|
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: 250.19 E-value: 7.92e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2298857976 485 KPVGSFLFAGPTGVGKTEVTVQLAKAMDI---ELLRFDMSEYMERHTVSRLIGAPPGYVGYDQGGLLTDAVIKHPHSVVL 561
Cdd:pfam07724 1 RPIGSFLFLGPTGVGKTELAKALAELLFGderALIRIDMSEYMEEHSVSRLIGAPPGYVGYEEGGQLTEAVRRKPYSIVL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2298857976 562 LDEIEKAHPDVFNLLLQVMDNGTLTDNNGRKADFRNVILVMTTNAGVRETERKSIGLVQQDNST---DAMEEIKKVFTPE 638
Cdd:pfam07724 81 IDEIEKAHPGVQNDLLQILEGGTLTDKQGRTVDFKNTLFIMTGNFGSEKISDASRLGDSPDYELlkeEVMDLLKKGFIPE 160
|
....*...
gi 2298857976 639 FRNRLDNI 646
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 ... |
349-451 |
1.17e-35 |
|
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: 130.30 E-value: 1.17e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2298857976 349 TPEETVQIINGLKTKYEAHHDVRYTAKAIRAAVELSVKYINDRHLPDKAIDVIDEAGARSRLmpvSKRKKTVNVADIESV 428
Cdd:pfam17871 1 SVEEAIEILRGLKPKYEKHHGVRISDEALEAAVKLSKRYITDRFLPDKAIDLLDEACARVRL---SQESKPEELEDLERE 77
|
90 100
....*....|....*....|...
gi 2298857976 429 VARIARIPEKTVSASDRDVLRSL 451
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, ... |
652-732 |
2.93e-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: 108.26 E-value: 2.93e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2298857976 652 LSTEVIQQVVDKFIVELQAQLDAKGVSLEVSDEARDWLSVKGYDRAMGARPMARVMQENLKKPLANELLFGSLVDGGSVK 731
Cdd:pfam10431 1 LSKEELRKIVDLQLKELQKRLAERGITLELTDAAKDWLAEKGYDPEYGARPLRRAIQREIEDPLAEEILSGELKEGDTVR 80
|
.
gi 2298857976 732 V 732
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, ... |
652-741 |
5.12e-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: 105.22 E-value: 5.12e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2298857976 652 LSTEVIQQVVDKFIVELQAQLDAKGVSLEVSDEARDWLSVKGYDRAMGARPMARVMQENLKKPLANELLFGSLVDGGSVK 731
Cdd:smart01086 1 LDKEDLVRIVDLPLNALQKRLAEKGITLEFTDEALDWLAEKGYDPKYGARPLRRIIQRELEDPLAELILSGELKDGDTVV 80
|
90
....*....|
gi 2298857976 732 VELDKDKKQL 741
Cdd:smart01086 81 VDVDDGELVF 90
|
|
| AAA |
cd00009 |
The AAA+ (ATPases Associated with a wide variety of cellular Activities) superfamily ... |
188-343 |
6.00e-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: 92.98 E-value: 6.00e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2298857976 188 IGRDPELERAIQVLCRRRKNNPLLVGESGVGKTAIAEGLAWRIVQGDVPevmadctLYSLDIGSLLAGTKYRGDFE-KRF 266
Cdd:cd00009 1 VGQEEAIEALREALELPPPKNLLLYGPPGTGKTTLARAIANELFRPGAP-------FLYLNASDLLEGLVVAELFGhFLV 73
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2298857976 267 KALLKQLEQDQNSILFIDEIHTIigAGAASGGQVDAAN-LIKPLLSSGKIRVIGSTTYqefSNIFEKDRALARRFQKI 343
Cdd:cd00009 74 RLLFELAEKAKPGVLFIDEIDSL--SRGAQNALLRVLEtLNDLRIDRENVRVIGATNR---PLLGDLDRALYDRLDIR 146
|
|
| AAA |
pfam00004 |
ATPase family associated with various cellular activities (AAA); AAA family proteins often ... |
210-343 |
9.80e-17 |
|
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: 77.25 E-value: 9.80e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2298857976 210 LLVGESGVGKTAIAEGLAWrivqgdvpevMADCTLYSLDIGSLLAgtKYRGDFEKRFKALLKQLEQDQNSILFIDEIHTI 289
Cdd:pfam00004 2 LLYGPPGTGKTTLAKAVAK----------ELGAPFIEISGSELVS--KYVGESEKRLRELFEAAKKLAPCVIFIDEIDAL 69
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2298857976 290 IGAGAASGGQV--DAANLIKPLL-----SSGKIRVIGSTTYqefsnIFEKDRALARRFQKI 343
Cdd:pfam00004 70 AGSRGSGGDSEsrRVVNQLLTELdgftsSNSKVIVIAATNR-----PDKLDPALLGRFDRI 125
|
|
| SpoVK |
COG0464 |
AAA+-type ATPase, SpoVK/Ycf46/Vps4 family [Cell wall/membrane/envelope biogenesis, Cell cycle ... |
26-402 |
2.85e-16 |
|
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: 81.50 E-value: 2.85e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2298857976 26 TVEHLLLALLSNPAAREALEACTVDLAALRQELEAFIEQTTPTLPASEEERDTQPTLSFQRVLQRAVFHVQSSGRSEVSG 105
Cdd:COG0464 5 LALAVALALALLLLDDAALRLLLLLLLALAAALLLLLLLLLLLLLALLLVELLLLLLSGALAALLLLALLLLALLALLAA 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2298857976 106 ANVLVAIFSEQESQAAYLLRKHDVSRLDVVNFISHGTRKDEPGQAPNAENPVNEEQSGGEDRmENFTTNLNQLARVGGID 185
Cdd:COG0464 85 LLSALELLLLGELLLLLLLLLLLLLLLLDLERALLELLRESAEALALAAPLVTYEDIGGLEE-ELLELREAILDDLGGLE 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2298857976 186 PLIGRDPELERAIQVLCRRRKNNP-------LLVGESGVGKTAIAEGLAwRIVQGDvpevmadctLYSLDIGSLLAgtKY 258
Cdd:COG0464 164 EVKEELRELVALPLKRPELREEYGlppprglLLYGPPGTGKTLLARALA-GELGLP---------LIEVDLSDLVS--KY 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2298857976 259 RGDFEKRFKALLKQLEQDQNSILFIDEIHTIIGAGAASGGQVDA----------ANLIKPLLssgkirVIGsTTYQeFSN 328
Cdd:COG0464 232 VGETEKNLREVFDKARGLAPCVLFIDEADALAGKRGEVGDGVGRrvvntlltemEELRSDVV------VIA-ATNR-PDL 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2298857976 329 IfekDRALARRFQ-KIDITEPTPEETVQIINGLKTKYEAHHDVRYTA------------------KAIRAAVELSVKYIN 389
Cdd:COG0464 304 L---DPALLRRFDeIIFFPLPDAEERLEIFRIHLRKRPLDEDVDLEElaeateglsgadirnvvrRAALQALRLGREPVT 380
|
410
....*....|...
gi 2298857976 390 DRHLpDKAIDVID 402
Cdd:COG0464 381 TEDL-LEALERED 392
|
|
| AAA |
cd00009 |
The AAA+ (ATPases Associated with a wide variety of cellular Activities) superfamily ... |
460-616 |
1.06e-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: 69.10 E-value: 1.06e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2298857976 460 FGQDQAIEALTEAIKmsraglghdRKPVGSFLFAGPTGVGKTEVTVQLAKA---MDIELLRFDMSEYMERHTVSRLIgap 536
Cdd:cd00009 1 VGQEEAIEALREALE---------LPPPKNLLLYGPPGTGKTTLARAIANElfrPGAPFLYLNASDLLEGLVVAELF--- 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2298857976 537 pgyvGYDQGGLLTDAVIKHPHSVVLLDEIEKAHPDVFNLLLQVMDNGtltdnNGRKADFRNVILVMTTNAGVRETERKSI 616
Cdd:cd00009 69 ----GHFLVRLLFELAEKAKPGVLFIDEIDSLSRGAQNALLRVLETL-----NDLRIDRENVRVIGATNRPLLGDLDRAL 139
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
205-343 |
1.33e-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: 65.86 E-value: 1.33e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2298857976 205 RKNNPLLVGESGVGKTAIAEGLAWRIVQGDVPEVMADCT-----LYSLDIGSLLAGTKYRGDFEKRFKALLKQLEQDQNS 279
Cdd:smart00382 1 PGEVILIVGPPGSGKTTLARALARELGPPGGGVIYIDGEdileeVLDQLLLIIVGGKKASGSGELRLRLALALARKLKPD 80
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2298857976 280 ILFIDEIHTIIGAGAASGGQVDA-ANLIKPLLSSGKIRVIGSTTYQEFSnifeKDRALARRFQKI 343
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 |
6.20e-12 |
|
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: 61.00 E-value: 6.20e-12
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 2298857976 13 AFARAREHRHEFMTVEHLLLALLSNP--AAREALEACTVDLAALRQELEAFIE 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 ... |
210-343 |
1.14e-11 |
|
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: 63.46 E-value: 1.14e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2298857976 210 LLVGESGVGKTAIAEGLAwrivqgdvpeVMADCTLYSLDIGSLLagTKYRGDFEKRFKALLKQLEQDQNSILFIDEIHTI 289
Cdd:cd19481 30 LLYGPPGTGKTLLAKALA----------GELGLPLIVVKLSSLL--SKYVGESEKNLRKIFERARRLAPCILFIDEIDAI 97
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2298857976 290 IGAGAASGGQVDAA-------NLIKPLLSSGKIRVIGSTtyqefSNIFEKDRALAR--RFQKI 343
Cdd:cd19481 98 GRKRDSSGESGELRrvlnqllTELDGVNSRSKVLVIAAT-----NRPDLLDPALLRpgRFDEV 155
|
|
| AAA_5 |
pfam07728 |
AAA domain (dynein-related subfamily); This Pfam entry includes some of the AAA proteins not ... |
489-605 |
1.27e-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: 62.70 E-value: 1.27e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2298857976 489 SFLFAGPTGVGKTEVTVQLAKAMD-----IELLRFDMSEymerhtvSRLIGappGYVGYDQGGLLTDAVI----KHPHsV 559
Cdd:pfam07728 1 GVLLVGPPGTGKTELAERLAAALSnrpvfYVQLTRDTTE-------EDLFG---RRNIDPGGASWVDGPLvraaREGE-I 69
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 2298857976 560 VLLDEIEKAHPDVFNLLLQVMDNGTLTDNNGR---KADFRNVILVMTTN 605
Cdd:pfam07728 70 AVLDEINRANPDVLNSLLSLLDERRLLLPDGGelvKAAPDGFRLIATMN 118
|
|
| COG1223 |
COG1223 |
Predicted ATPase, AAA+ superfamily [General function prediction only]; |
207-403 |
8.85e-11 |
|
Predicted ATPase, AAA+ superfamily [General function prediction only];
Pssm-ID: 440836 [Multi-domain] Cd Length: 246 Bit Score: 62.98 E-value: 8.85e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2298857976 207 NNPLLVGESGVGKTAIAEGLAWRIvqgDVPevmadctLYSLDIGSLLagTKYRGDFEKRFKALLKQLEQDQnSILFIDEI 286
Cdd:COG1223 36 RKILFYGPPGTGKTMLAEALAGEL---KLP-------LLTVRLDSLI--GSYLGETARNLRKLFDFARRAP-CVIFFDEF 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2298857976 287 HTIigagaasGGQVDAANL---IKPLLSS---------GKIRVIGSTTYQEFSnifekDRALARRFQ-KIDITEPTPEET 353
Cdd:COG1223 103 DAI-------AKDRGDQNDvgeVKRVVNAllqeldglpSGSVVIAATNHPELL-----DSALWRRFDeVIEFPLPDKEER 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2298857976 354 VQI----INGLKTKYEAHHD--------------VRYTAKAIRAAVELSVKYINDRHLpDKAIDVIDE 403
Cdd:COG1223 171 KEIlelnLKKFPLPFELDLKklakkleglsgadiEKVLKTALKKAILEDREKVTKEDL-EEALKQRKE 237
|
|
| RecA-like_protease |
cd19481 |
proteases similar to RecA; RecA-like NTPases. This family includes the NTP binding domain of ... |
464-605 |
1.45e-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: 60.37 E-value: 1.45e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2298857976 464 QAIEALTEAIKMSRAGLGHDRkpvgSFLFAGPTGVGKTEVTVQLAKAMDIELLRFDMSEYMERHtvsrligappGYVGYD 543
Cdd:cd19481 7 EAVEAPRRGSRLRRYGLGLPK----GILLYGPPGTGKTLLAKALAGELGLPLIVVKLSSLLSKY----------VGESEK 72
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2298857976 544 QGGLLTDAVIKHPHSVVLLDEIEKAHPD------------VFNLLLQVMDNGTLTDnngrkadfrNVILVMTTN 605
Cdd:cd19481 73 NLRKIFERARRLAPCILFIDEIDAIGRKrdssgesgelrrVLNQLLTELDGVNSRS---------KVLVIAATN 137
|
|
| RPT1 |
COG1222 |
ATP-dependent 26S proteasome regulatory subunit [Posttranslational modification, protein ... |
184-438 |
5.20e-09 |
|
ATP-dependent 26S proteasome regulatory subunit [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440835 [Multi-domain] Cd Length: 326 Bit Score: 58.48 E-value: 5.20e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2298857976 184 IDPLigRDPELERAIQVLCRRRKnnpLLVGESGVGKTAIAEGLAWRivqgdvpevmADCTLYSLDIGSLLagTKYRGDFE 263
Cdd:COG1222 95 ELPL--KNPELFRKYGIEPPKGV---LLYGPPGTGKTLLAKAVAGE----------LGAPFIRVRGSELV--SKYIGEGA 157
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2298857976 264 KRFKALLKQLEQDQNSILFIDEIHTIIGA--GAASGGQVDaaNLIKPLL-------SSGKIRVIGSTTYQEfsnifEKDR 334
Cdd:COG1222 158 RNVREVFELAREKAPSIIFIDEIDAIAARrtDDGTSGEVQ--RTVNQLLaeldgfeSRGDVLIIAATNRPD-----LLDP 230
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2298857976 335 ALAR--RF-QKIDITEPTPEETVQIINGLKTKYEAHHDVRYTAKAIRAAvELSVKYIndrhlpdKAIdvIDEAGARSrlm 411
Cdd:COG1222 231 ALLRpgRFdRVIEVPLPDEEAREEILKIHLRDMPLADDVDLDKLAKLTE-GFSGADL-------KAI--VTEAGMFA--- 297
|
250 260
....*....|....*....|....*..
gi 2298857976 412 pVSKRKKTVNVADIESVVARIARIPEK 438
Cdd:COG1222 298 -IREGRDTVTMEDLEKAIEKVKKKTET 323
|
|
| AAA |
pfam00004 |
ATPase family associated with various cellular activities (AAA); AAA family proteins often ... |
491-605 |
5.52e-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: 54.91 E-value: 5.52e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2298857976 491 LFAGPTGVGKTEVTVQLAKAMDIELLRFDMSEymerhTVSRLIGAPPGYVgydqGGLLTDAVIKHPhSVVLLDEIEKAHP 570
Cdd:pfam00004 2 LLYGPPGTGKTTLAKAVAKELGAPFIEISGSE-----LVSKYVGESEKRL----RELFEAAKKLAP-CVIFIDEIDALAG 71
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 2298857976 571 -----------DVFNLLLQVMDngtltdnnGRKADFRNVILVMTTN 605
Cdd:pfam00004 72 srgsggdsesrRVVNQLLTELD--------GFTSSNSKVIVIAATN 109
|
|
| RecA-like_VPS4-like |
cd19509 |
ATPase domain of VPS4, ATAD1, K, KTNA1, Spastin, FIGL-1 and similar ATPase domains; This ... |
210-342 |
2.45e-08 |
|
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: 53.90 E-value: 2.45e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2298857976 210 LLVGESGVGKTAIAEGLAWRIvqgdvpevmaDCTLYSLDIGSLLAgtKYRGDFEKRFKALLKQLEQDQNSILFIDEIHTI 289
Cdd:cd19509 36 LLYGPPGTGKTLLARAVASES----------GSTFFSISASSLVS--KWVGESEKIVRALFALARELQPSIIFIDEIDSL 103
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2298857976 290 IgaGAASGGQVDAANLIKPLL----------SSGKIRVIGSTtyqefSNIFEKDRALARRFQK 342
Cdd:cd19509 104 L--SERGSGEHEASRRVKTEFlvqmdgvlnkPEDRVLVLGAT-----NRPWELDEAFLRRFEK 159
|
|
| RecA-like_VPS4 |
cd19521 |
ATPase domain of vacuolar protein sorting-associated protein 4; Vacuolar protein ... |
210-342 |
5.89e-08 |
|
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: 52.94 E-value: 5.89e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2298857976 210 LLVGESGVGKTAIAEGLAwrivqgdvpeVMADCTLYSLDIGSLLagTKYRGDFEKRFKALLKQLEQDQNSILFIDEIHTI 289
Cdd:cd19521 44 LLYGPPGTGKSYLAKAVA----------TEANSTFFSVSSSDLV--SKWMGESEKLVKQLFAMARENKPSIIFIDEVDSL 111
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2298857976 290 igAGAASGGQVDAANLIKPLL---------SSGKIRVIGSTtyqefsNI-FEKDRALARRFQK 342
Cdd:cd19521 112 --CGTRGEGESEASRRIKTELlvqmngvgnDSQGVLVLGAT------NIpWQLDSAIRRRFEK 166
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
491-605 |
8.18e-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: 51.99 E-value: 8.18e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2298857976 491 LFAGPTGVGKTEVTVQLAKAMDIE---LLRFDMSEYMERHTVSRLIGAPPGYVGYDQGG----LLTDAVIKHPHSVVLLD 563
Cdd:smart00382 6 LIVGPPGSGKTTLARALARELGPPgggVIYIDGEDILEEVLDQLLLIIVGGKKASGSGElrlrLALALARKLKPDVLILD 85
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 2298857976 564 EIEKAHPDVFNLLLQVMDNGTLTDnngRKADFRNVILVMTTN 605
Cdd:smart00382 86 EITSLLDAEQEALLLLLEELRLLL---LLKSEKNLTVILTTN 124
|
|
| CDC48 |
TIGR01243 |
AAA family ATPase, CDC48 subfamily; This subfamily of the AAA family ATPases includes two ... |
210-514 |
5.21e-07 |
|
AAA family ATPase, CDC48 subfamily; This subfamily of the AAA family ATPases includes two members each from three archaeal species. It also includes yeast CDC48 (cell division control protein 48) and the human ortholog, transitional endoplasmic reticulum ATPase (valosin-containing protein). These proteins in eukaryotes are involved in the budding and transfer of membrane from the transitional endoplasmic reticulum to the Golgi apparatus.
Pssm-ID: 273521 [Multi-domain] Cd Length: 733 Bit Score: 53.37 E-value: 5.21e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2298857976 210 LLVGESGVGKTAIAEGLAWRI----VQGDVPEVMadctlysldigsllagTKYRGDFEKRFKALLKQLEQDQNSILFIDE 285
Cdd:TIGR01243 216 LLYGPPGTGKTLLAKAVANEAgayfISINGPEIM----------------SKYYGESEERLREIFKEAEENAPSIIFIDE 279
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2298857976 286 IHTIIGAGAASGGQVDAA------NLIKPLLSSGKIRVIGSTTYQEfsnifEKDRALAR--RFQK-IDITEPTPEETVQI 356
Cdd:TIGR01243 280 IDAIAPKREEVTGEVEKRvvaqllTLMDGLKGRGRVIVIGATNRPD-----ALDPALRRpgRFDReIVIRVPDKRARKEI 354
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2298857976 357 INGLKTKYEAHHDVR----------YTAKAIRAAVELSVKYINDRHLPDKAIDVIDEAGARSRL--MPVSKRKKTVNVAD 424
Cdd:TIGR01243 355 LKVHTRNMPLAEDVDldklaevthgFVGADLAALAKEAAMAALRRFIREGKINFEAEEIPAEVLkeLKVTMKDFMEALKM 434
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2298857976 425 IESVVARIARIPEKTVSASDrdvlrslgdrlkmlVFGQDQAIEALTEAIK--------MSRAGLghdRKPVGSFLFaGPT 496
Cdd:TIGR01243 435 VEPSAIREVLVEVPNVRWSD--------------IGGLEEVKQELREAVEwplkhpeiFEKMGI---RPPKGVLLF-GPP 496
|
330
....*....|....*...
gi 2298857976 497 GVGKTevtvQLAKAMDIE 514
Cdd:TIGR01243 497 GTGKT----LLAKAVATE 510
|
|
| RecA-like_CDC48_NLV2_r1-like |
cd19503 |
first of two ATPase domains of CDC48 and NLV2, and similar ATPase domains; CDC48 in yeast and ... |
190-321 |
1.08e-06 |
|
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: 49.21 E-value: 1.08e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2298857976 190 RDPELERAIQVLCRRrknNPLLVGESGVGKTAIAEGLAWRivqgdvpevmADCTLYSLDIGSLLAgtKYRGDFEKRFKAL 269
Cdd:cd19503 21 KYPELFRALGLKPPR---GVLLHGPPGTGKTLLARAVANE----------AGANFLSISGPSIVS--KYLGESEKNLREI 85
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 2298857976 270 LKQLEQDQNSILFIDEIHTIIGAGAASGGQVDAA------NLIKPLLSSGKIRVIGST 321
Cdd:cd19503 86 FEEARSHAPSIIFIDEIDALAPKREEDQREVERRvvaqllTLMDGMSSRGKVVVIAAT 143
|
|
| RecA-like_ClpX |
cd19497 |
ATP-dependent Clp protease ATP-binding subunit ClpX; ClpX is a component of the ATP-dependent ... |
206-289 |
5.82e-06 |
|
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: 48.37 E-value: 5.82e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2298857976 206 KNNPLLVGESGVGKTAIAEGLAwRIVqgDVPEVMADCTlysldigSLL-AGtkYRG-DFEKRFKALLK----QLEQDQNS 279
Cdd:cd19497 50 KSNILLIGPTGSGKTLLAQTLA-KIL--DVPFAIADAT-------TLTeAG--YVGeDVENILLKLLQaadyDVERAQRG 117
|
90
....*....|
gi 2298857976 280 ILFIDEIHTI 289
Cdd:cd19497 118 IVYIDEIDKI 127
|
|
| RecA-like_KTNA1 |
cd19522 |
Katanin p60 ATPase-containing subunit A1; Katanin p60 ATPase-containing subunit A1 (KTNA1) is ... |
192-342 |
8.05e-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: 46.90 E-value: 8.05e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2298857976 192 PELERAIqvlcRRRKNNPLLVGESGVGKTAIAEGLAwrivqgdvpevmADCTLYSLDIGSLLAGTKYRGDFEKRFKALLK 271
Cdd:cd19522 23 PEFFKGI----RRPWKGVLMVGPPGTGKTLLAKAVA------------TECGTTFFNVSSSTLTSKYRGESEKLVRLLFE 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2298857976 272 QLEQDQNSILFIDEIHTIIGAgAASGGQVDAANLIKPLLSSGKIRVIGSTTYQEFSNI----------FEKDRALARRFQ 341
Cdd:cd19522 87 MARFYAPTTIFIDEIDSICSR-RGTSEEHEASRRVKSELLVQMDGVGGASENDDPSKMvmvlaatnfpWDIDEALRRRLE 165
|
.
gi 2298857976 342 K 342
Cdd:cd19522 166 K 166
|
|
| RecA-like_CDC48_r1-like |
cd19519 |
first of two ATPase domains of CDC48 and similar ATPase domains; CDC48 in yeast and p97 or VCP ... |
176-344 |
8.84e-06 |
|
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: 46.66 E-value: 8.84e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2298857976 176 NQLARVGGIDPLIGRDPELERAIQVlcrRRKNNPLLVGESGVGKTAIAEGLA------WRIVQGdvPEVMadctlysldi 249
Cdd:cd19519 7 KQLAQIREMVELPLRHPELFKAIGI---KPPRGILLYGPPGTGKTLIARAVAnetgafFFLING--PEIM---------- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2298857976 250 gsllagTKYRGDFEKRFKALLKQLEQDQNSILFIDEIHTIIGAGAASGGQVDAA------NLIKPLLSSGKIRVIGSTty 323
Cdd:cd19519 72 ------SKLAGESESNLRKAFEEAEKNAPAIIFIDEIDAIAPKREKTHGEVERRivsqllTLMDGLKQRAHVIVMAAT-- 143
|
170 180
....*....|....*....|.
gi 2298857976 324 qefSNIFEKDRALaRRFQKID 344
Cdd:cd19519 144 ---NRPNSIDPAL-RRFGRFD 160
|
|
| RecA-like_Lon |
cd19500 |
lon protease homolog 2 peroxisomal; Lon protease (also known as Lon peptidase) is an ... |
491-605 |
1.46e-05 |
|
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: 46.40 E-value: 1.46e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2298857976 491 LFAGPTGVGKTEVTVQLAKAMDIELLRF------DMSEYM-ERHTvsrLIGAPPGYVgyDQGglLTDAVIKHPhsVVLLD 563
Cdd:cd19500 41 CLVGPPGVGKTSLGKSIARALGRKFVRIslggvrDEAEIRgHRRT---YVGAMPGRI--IQA--LKKAGTNNP--VFLLD 111
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 2298857976 564 EIEK----AHPDVFNLLLQVMD---NGTLTDNN-GRKADFRNVILVMTTN 605
Cdd:cd19500 112 EIDKigssFRGDPASALLEVLDpeqNSTFSDHYlDVPFDLSKVLFIATAN 161
|
|
| DnaX |
COG2812 |
DNA polymerase III, gamma/tau subunits [Replication, recombination and repair]; |
459-511 |
1.73e-05 |
|
DNA polymerase III, gamma/tau subunits [Replication, recombination and repair];
Pssm-ID: 442061 [Multi-domain] Cd Length: 340 Bit Score: 47.49 E-value: 1.73e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 2298857976 459 VFGQDQAIEALTEAIKMSRagLGHdrkpvgSFLFAGPTGVGKTEVTVQLAKAM 511
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 ... |
186-245 |
3.72e-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: 3.72e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2298857976 186 PLIGRDPELERAIQVLCRRRKNNP---LLVGESGVGKTAIAEGLAWRIVQGDVPEVMADCTLY 245
Cdd:pfam13191 1 RLVGREEELEQLLDALDRVRSGRPpsvLLTGEAGTGKTTLLRELLRALERDGGYFLRGKCDEN 63
|
|
| RecA-like_Ycf46-like |
cd19507 |
ATPase domain of Ycf46 and similar ATPase domains; Ycf46 may play a role in the regulation of ... |
210-298 |
4.54e-05 |
|
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: 44.28 E-value: 4.54e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2298857976 210 LLVGESGVGKTAIAEGLA--WRIvqgdvpevmadcTLYSLDIGSLLAGtkYRGDFEKRFKALLKQLEQDQNSILFIDEIH 287
Cdd:cd19507 35 LLVGIQGTGKSLTAKAIAgvWQL------------PLLRLDMGRLFGG--LVGESESRLRQMIQTAEAIAPCVLWIDEIE 100
|
90
....*....|.
gi 2298857976 288 TIIGaGAASGG 298
Cdd:cd19507 101 KGFS-NADSKG 110
|
|
| SpoVK |
COG0464 |
AAA+-type ATPase, SpoVK/Ycf46/Vps4 family [Cell wall/membrane/envelope biogenesis, Cell cycle ... |
333-605 |
4.74e-05 |
|
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: 46.44 E-value: 4.74e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2298857976 333 DRALARRFQKIDITEPTPEETVQIINGLKTKYEAHHDVRYTAKAIRAAVELSVKYINDRHLPDKAIDVIDEAGARSRLMP 412
Cdd:COG0464 34 AAALLLLLLLLLLLLLALLLVELLLLLLSGALAALLLLALLLLALLALLAALLSALELLLLGELLLLLLLLLLLLLLLLD 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2298857976 413 VSKRKKTVNVADIESVVARIARIPEKTVSASDRDVLRSLGDRLKMLVfGQDQAIEALTEAI----KMSRAGLGHDRKPVG 488
Cdd:COG0464 114 LERALLELLRESAEALALAAPLVTYEDIGGLEEELLELREAILDDLG-GLEEVKEELRELValplKRPELREEYGLPPPR 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2298857976 489 SFLFAGPTGVGKTEVTVQLAKAMDIELLRFDMSEymerhtvsrLIGappGYVGydQGGLLTDAVIK----HPHSVVLLDE 564
Cdd:COG0464 193 GLLLYGPPGTGKTLLARALAGELGLPLIEVDLSD---------LVS---KYVG--ETEKNLREVFDkargLAPCVLFIDE 258
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 2298857976 565 IEKAHPD-----------VFNLLLQVMDNGTltdnngrkadfRNVILVMTTN 605
Cdd:COG0464 259 ADALAGKrgevgdgvgrrVVNTLLTEMEELR-----------SDVVVIAATN 299
|
|
| RecA-like_HslU |
cd19498 |
ATP-dependent protease ATPase subunit HslU; HslU is a component of the ATP-dependent protease ... |
491-567 |
4.81e-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: 4.81e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2298857976 491 LFAGPTGVGKTEVTVQLAKAMDIELLRFDMSEYMErhtvsrligapPGYVGYDQGGLLTDAVikhpHSVVLLDEIEK 567
Cdd:cd19498 50 LMIGPTGVGKTEIARRLAKLAGAPFIKVEATKFTE-----------VGYVGRDVESIIRDLV----EGIVFIDEIDK 111
|
|
| RecA-like_Figl-1 |
cd19525 |
ATPase domain of Fidgetin-Like 1 (FIGL-1); FIGL-1 may participate in DNA repair in the nucleus; ... |
210-342 |
7.25e-05 |
|
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: 44.21 E-value: 7.25e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2298857976 210 LLVGESGVGKTAIAEGLAWRivqgdvpevmADCTLYSLDIGSLLagTKYRGDFEKRFKALLKQLEQDQNSILFIDEIHTI 289
Cdd:cd19525 59 LLFGPPGTGKTLIGKCIASQ----------SGATFFSISASSLT--SKWVGEGEKMVRALFSVARCKQPAVIFIDEIDSL 126
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2298857976 290 IgaGAASGGQVDAANLIKPLL----------SSGKIRVIGSTTYQEfsnifEKDRALARRFQK 342
Cdd:cd19525 127 L--SQRGEGEHESSRRIKTEFlvqldgattsSEDRILVVGATNRPQ-----EIDEAARRRLVK 182
|
|
| clpX |
PRK05342 |
ATP-dependent Clp protease ATP-binding subunit ClpX; |
206-286 |
1.61e-04 |
|
ATP-dependent Clp protease ATP-binding subunit ClpX;
Pssm-ID: 235422 [Multi-domain] Cd Length: 412 Bit Score: 44.76 E-value: 1.61e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2298857976 206 KNNPLLVGESGVGKTAIAEGLAwRIVqgDVPEVMADCTlysldigSLL-AGtkYRG-DFEkrfKALLKQL-------EQD 276
Cdd:PRK05342 108 KSNILLIGPTGSGKTLLAQTLA-RIL--DVPFAIADAT-------TLTeAG--YVGeDVE---NILLKLLqaadydvEKA 172
|
90
....*....|
gi 2298857976 277 QNSILFIDEI 286
Cdd:PRK05342 173 QRGIVYIDEI 182
|
|
| RecA-like_spastin |
cd19524 |
ATPase domain of spastin; Spastin is an ATP-dependent microtubule-severing protein involved in ... |
210-342 |
1.76e-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: 42.91 E-value: 1.76e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2298857976 210 LLVGESGVGKTAIAEGLAWRivqgdvpevmADCTLYSLDIGSLLagTKYRGDFEKRFKALLKQLEQDQNSILFIDEIHTI 289
Cdd:cd19524 37 LLFGPPGNGKTMLAKAVAAE----------SNATFFNISAASLT--SKYVGEGEKLVRALFAVARELQPSIIFIDEVDSL 104
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2298857976 290 IgaGAASGGQVDAANLIKP--------LLSSG--KIRVIGSTTYQEfsnifEKDRALARRFQK 342
Cdd:cd19524 105 L--SERSEGEHEASRRLKTefliefdgVQSNGddRVLVMGATNRPQ-----ELDDAVLRRFTK 160
|
|
| TniB |
pfam05621 |
Bacterial TniB protein; This family consists of several bacterial TniB NTP-binding proteins. ... |
193-343 |
2.38e-04 |
|
Bacterial TniB protein; This family consists of several bacterial TniB NTP-binding proteins. TniB is a probable ATP-binding protein which is involved in Tn5053 mercury resistance transposition. This entry represents a P-loop domain.
Pssm-ID: 428547 Cd Length: 189 Bit Score: 42.96 E-value: 2.38e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2298857976 193 ELERAIQVLCRRRKNNPLLVGESGVGKTAIAEGLAWR---IVQGD---VPEVMADC-------TLYSLDIGSLLAGTKYR 259
Cdd:pfam05621 22 RLEDLLDYPKRLRMPNLLLVGDSNNGKTMIVERFARLhppTDDEDaeiVPVVVVQMppkpdekRLYVAILEALGAPFRPR 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2298857976 260 GDFEKRFKALLKQLEQDQNSILFIDEIHTIIgAGAASgGQVDAANLIKPLLSSGKIRVIGSTTyQEFSNIFEKDRALARR 339
Cdd:pfam05621 102 DRLSKLEQQVLRLLRAVGVRMLIIDEFHNLL-AGSAR-KQREFLNVLKSLGNELRIPIVGVGT-REAVRAIRTDPQLASR 178
|
....
gi 2298857976 340 FQKI 343
Cdd:pfam05621 179 FEPI 182
|
|
| PRK13341 |
PRK13341 |
AAA family ATPase; |
183-339 |
2.91e-04 |
|
AAA family ATPase;
Pssm-ID: 237354 [Multi-domain] Cd Length: 725 Bit Score: 44.28 E-value: 2.91e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2298857976 183 GIDPLIGRDPELERAIQVlcrRRKNNPLLVGESGVGKTAIAEGLAwRIVQGDVpevmadctlysLDIGSLLAGTKyrgDF 262
Cdd:PRK13341 32 GQDHILGEGRLLRRAIKA---DRVGSLILYGPPGVGKTTLARIIA-NHTRAHF-----------SSLNAVLAGVK---DL 93
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2298857976 263 EKRFKALLKQLEQ-DQNSILFIDEIHTIIGAgaasggQVDAanlIKPLLSSGKIRVIGSTTYQEFsniFEKDRALARR 339
Cdd:PRK13341 94 RAEVDRAKERLERhGKRTILFIDEVHRFNKA------QQDA---LLPWVENGTITLIGATTENPY---FEVNKALVSR 159
|
|
| RecA-like_ATAD1 |
cd19520 |
ATPase domain of ATPase family AAA domain-containing protein 1 and similar ATPase domains; ... |
210-342 |
3.87e-04 |
|
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: 41.64 E-value: 3.87e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2298857976 210 LLVGESGVGKTAIAEGLAWRivqgdvpevmADCTLYSLDIGSLLagTKYRGDFEKRFKALLKQLEQDQNSILFIDEIHTI 289
Cdd:cd19520 39 LLYGPPGCGKTMLAKATAKE----------AGARFINLQVSSLT--DKWYGESQKLVAAVFSLASKLQPSIIFIDEIDSF 106
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2298857976 290 IGAGAASGGQVDAA------NLIKPLLSSGKIRVI--GSTtyqefSNIFEKDRALARRFQK 342
Cdd:cd19520 107 LRQRSSTDHEATAMmkaefmSLWDGLSTDGNCRVIvmGAT-----NRPQDLDEAILRRMPK 162
|
|
| DNA_pol3_delta2 |
pfam13177 |
DNA polymerase III, delta subunit; DNA polymerase III, delta subunit (EC 2.7.7.7) is required ... |
461-511 |
5.20e-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: 41.43 E-value: 5.20e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 2298857976 461 GQDQAIEALTEAIKMSRagLGHdrkpvgSFLFAGPTGVGKTEVTVQLAKAM 511
Cdd:pfam13177 1 GQPEAIQLLQNSLENGR--LSH------AYLFSGPEGVGKLELALAFAKAL 43
|
|
| PRK13342 |
PRK13342 |
recombination factor protein RarA; Reviewed |
187-322 |
8.10e-04 |
|
recombination factor protein RarA; Reviewed
Pssm-ID: 237355 [Multi-domain] Cd Length: 413 Bit Score: 42.38 E-value: 8.10e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2298857976 187 LIGRDPELERAIQvlcRRRKNNPLLVGESGVGKTAIAEGLAwrivqgdvpeVMADCTLYSLDigSLLAGTKyrgDFEKRF 266
Cdd:PRK13342 20 LLGPGKPLRRMIE---AGRLSSMILWGPPGTGKTTLARIIA----------GATDAPFEALS--AVTSGVK---DLREVI 81
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 2298857976 267 KALLKQLEQDQNSILFIDEIHTIigagaaSGGQVDAanLIkPLLSSGKIRVIGSTT 322
Cdd:PRK13342 82 EEARQRRSAGRRTILFIDEIHRF------NKAQQDA--LL-PHVEDGTITLIGATT 128
|
|
| RecA-like_ClpB_Hsp104-like |
cd19499 |
Chaperone protein ClpB/Hsp104 subfamily; Bacterial Caseinolytic peptidase B (ClpB) and ... |
187-286 |
1.55e-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: 1.55e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2298857976 187 LIGRDPELERAIQVLCR-----RRKNNP----LLVGESGVGKTAIAEGLAWRIVQGDVPEVMADCTLYS-LDIGSLLAGT 256
Cdd:cd19499 13 VVGQDEAVKAVSDAIRRaraglSDPNRPigsfLFLGPTGVGKTELAKALAELLFGDEDNLIRIDMSEYMeKHSVSRLIGA 92
|
90 100 110
....*....|....*....|....*....|..
gi 2298857976 257 --KYRGdFEKRFKaLLKQLEQDQNSILFIDEI 286
Cdd:cd19499 93 ppGYVG-YTEGGQ-LTEAVRRKPYSVVLLDEI 122
|
|
| PRK14969 |
PRK14969 |
DNA polymerase III subunits gamma and tau; Provisional |
461-514 |
1.90e-03 |
|
DNA polymerase III subunits gamma and tau; Provisional
Pssm-ID: 237873 [Multi-domain] Cd Length: 527 Bit Score: 41.66 E-value: 1.90e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 2298857976 461 GQDQAIEALTEAIKMSRagLGHdrkpvgSFLFAGPTGVGKTEVTVQLAKAMDIE 514
Cdd:PRK14969 20 GQEHVVRALTNALEQQR--LHH------AYLFTGTRGVGKTTLARILAKSLNCE 65
|
|
| AAA_22 |
pfam13401 |
AAA domain; |
203-287 |
2.46e-03 |
|
AAA domain;
Pssm-ID: 379165 [Multi-domain] Cd Length: 129 Bit Score: 38.86 E-value: 2.46e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2298857976 203 RRRKNNPLLVGESGVGKTAIAEGLAWRIVQGDVP----EVMADCTLYSL--DIGSLLAGTKYRGDFEKRFKALLKQLEQD 276
Cdd:pfam13401 2 RFGAGILVLTGESGTGKTTLLRRLLEQLPEVRDSvvfvDLPSGTSPKDLlrALLRALGLPLSGRLSKEELLAALQQLLLA 81
|
90
....*....|...
gi 2298857976 277 QNS--ILFIDEIH 287
Cdd:pfam13401 82 LAVavVLIIDEAQ 94
|
|
| RecA-like_HslU |
cd19498 |
ATP-dependent protease ATPase subunit HslU; HslU is a component of the ATP-dependent protease ... |
207-310 |
2.54e-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: 39.67 E-value: 2.54e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2298857976 207 NNPLLVGESGVGKTAIAEGLAwRIVqgDVPEVMADCTLYSlDIGsllagtkYRG-DFEKRFKALLkqleqdqNSILFIDE 285
Cdd:cd19498 47 KNILMIGPTGVGKTEIARRLA-KLA--GAPFIKVEATKFT-EVG-------YVGrDVESIIRDLV-------EGIVFIDE 108
|
90 100
....*....|....*....|....*
gi 2298857976 286 IHTIIGAGAASGGQVDAANLIKPLL 310
Cdd:cd19498 109 IDKIAKRGGSSGPDVSREGVQRDLL 133
|
|
| PRK07399 |
PRK07399 |
DNA polymerase III subunit delta'; Validated |
459-510 |
3.87e-03 |
|
DNA polymerase III subunit delta'; Validated
Pssm-ID: 236011 [Multi-domain] Cd Length: 314 Bit Score: 40.27 E-value: 3.87e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 2298857976 459 VFGQDQAIEALTEAIKMSRAGLGhdrkpvgsFLFAGPTGVGKTEVTVQLAKA 510
Cdd:PRK07399 6 LIGQPLAIELLTAAIKQNRIAPA--------YLFAGPEGVGRKLAALCFIEG 49
|
|
| RecA-like_Yta7-like |
cd19517 |
ATPase domain of Saccharomyces cerevisiae Yta7 and similar ATPase domains; Saccharomyces ... |
210-321 |
3.87e-03 |
|
ATPase domain of Saccharomyces cerevisiae Yta7 and similar ATPase domains; Saccharomyces cerevisiae Yta7 is a chromatin-associated AAA-ATPase involved in regulation of chromatin dynamics. Its human ortholog ANCCA/ATAD2 transcriptionally activates pathways of malignancy in a broad range of cancers. The RecA-like_Yta7 subfamily belongs to the RecA-like NTPase family which includes the NTP binding domain of F1 and V1 H(+)ATPases, DnaB and related helicases as well as bacterial RecA and related eukaryotic and archaeal recombinases. The RecA-like NTPase family also includes bacterial conjugation proteins and related DNA transfer proteins involved in type II and type IV secretion.
Pssm-ID: 410925 [Multi-domain] Cd Length: 170 Bit Score: 39.03 E-value: 3.87e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2298857976 210 LLVGESGVGKTAIAEGLAWRIVQGD--VPEVM---ADCTlysldigsllagTKYRGDFEKRFKALLKQLEQDQNSILFID 284
Cdd:cd19517 38 LFHGPPGTGKTLMARALAAECSKGGqkVSFFMrkgADCL------------SKWVGEAERQLRLLFEEAYRMQPSIIFFD 105
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 2298857976 285 EIHTIIGAGAASGGQVDAA------NLIKPLLSSGKIRVIGST 321
Cdd:cd19517 106 EIDGLAPVRSSKQEQIHASivstllALMDGLDNRGQVVVIGAT 148
|
|
| AcoR |
COG3284 |
Transcriptional regulator DhaR of acetoin/glycerol metabolism [Transcription]; |
185-286 |
4.32e-03 |
|
Transcriptional regulator DhaR of acetoin/glycerol metabolism [Transcription];
Pssm-ID: 442514 [Multi-domain] Cd Length: 625 Bit Score: 40.27 E-value: 4.32e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2298857976 185 DPLIGRDPELERAIQVLCR-RRKNNPLLV-GESGVGKTAIAEGLAWRIVQGDVPEVMADCTLYSLD-IGSLLAGTKyRGD 261
Cdd:COG3284 321 AALAGGDPAMRRALRRARRlADRDIPVLIlGETGTGKELFARAIHAASPRADGPFVAVNCAAIPEElIESELFGYE-PGA 399
|
90 100
....*....|....*....|....*..
gi 2298857976 262 F--EKRFKALLKqLEQDQNSILFIDEI 286
Cdd:COG3284 400 FtgARRKGRPGK-IEQADGGTLFLDEI 425
|
|
| PRK12723 |
PRK12723 |
flagellar biosynthesis regulator FlhF; Provisional |
462-610 |
5.83e-03 |
|
flagellar biosynthesis regulator FlhF; Provisional
Pssm-ID: 183702 [Multi-domain] Cd Length: 388 Bit Score: 39.88 E-value: 5.83e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2298857976 462 QDQAIEALTEAIKMSRAGLGHDRKPVgsFLFAGPTGVGKTEVTVQLA---------KAMDIELLRFD---MSEYMERHTV 529
Cdd:PRK12723 151 RDSVIIYIAKTIKCSGSIIDNLKKRV--FILVGPTGVGKTTTIAKLAaiyginsddKSLNIKIITIDnyrIGAKKQIQTY 228
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2298857976 530 SRLIGAPPGYVGYDQgGLLTDAVIKHPHSVVLLDEIEKAHPDVFNLllqvMDNGTLTDNNGRKADFRNVILVMTTNAGVR 609
Cdd:PRK12723 229 GDIMGIPVKAIESFK-DLKEEITQSKDFDLVLVDTIGKSPKDFMKL----AEMKELLNACGRDAEFHLAVSSTTKTSDVK 303
|
.
gi 2298857976 610 E 610
Cdd:PRK12723 304 E 304
|
|
| RecA-like_PAN_like |
cd19502 |
proteasome activating nucleotidase PAN and related proteasome subunits; This subfamily ... |
210-321 |
6.72e-03 |
|
proteasome activating nucleotidase PAN and related proteasome subunits; This subfamily contains ATPase subunits of the eukaryotic 26S proteasome, and of the archaeal proteasome which carry out ATP-dependent degradation of substrates of the ubiquitin-proteasome pathway. The eukaryotic 26S proteasome consists of a proteolytic 20S core particle (CP), and a 19S regulatory particle (RP) which provides the ATP-dependence and the specificity for ubiquitinated proteins. In the archaea the RP is a homohexameric complex of proteasome-activating nucleotidase (PAN). This subfamily also includes various eukaryotic 26S subunits including, proteasome 26S subunit, ATPase 2 (PSMC2, also known as S7 and MSS1) which is a member of the 19S RP and has a chaperone like activity; and proteasome 20S subunit alpha 6 (PSMA6, also known as IOTA, p27K, and PROS27) which is a member of the 20S CP. This RecA-like_PAN 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: 410910 [Multi-domain] Cd Length: 171 Bit Score: 38.09 E-value: 6.72e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2298857976 210 LLVGESGVGKTAIAEGLAWRivqgdvpevmADCTLYSLdIGSLLAgTKYRGDFEKRFKALLKQLEQDQNSILFIDEIHTI 289
Cdd:cd19502 41 LLYGPPGTGKTLLAKAVANH----------TDATFIRV-VGSELV-QKYIGEGARLVRELFEMAREKAPSIIFIDEIDAI 108
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 2298857976 290 IGA--GAASGGQVDAANLIKPLL-------SSGKIRVIGST 321
Cdd:cd19502 109 GAKrfDSGTGGDREVQRTMLELLnqldgfdPRGNIKVIMAT 149
|
|
| AAA_22 |
pfam13401 |
AAA domain; |
488-584 |
8.73e-03 |
|
AAA domain;
Pssm-ID: 379165 [Multi-domain] Cd Length: 129 Bit Score: 36.94 E-value: 8.73e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2298857976 488 GSFLFAGPTGVGKTEVTVQLAK---AMDIELLRFDMSEYME----RHTVSRLIGAPPgyVGYDQGGLLTDAVIKH----- 555
Cdd:pfam13401 6 GILVLTGESGTGKTTLLRRLLEqlpEVRDSVVFVDLPSGTSpkdlLRALLRALGLPL--SGRLSKEELLAALQQLllala 83
|
90 100
....*....|....*....|....*....
gi 2298857976 556 PHSVVLLDEIEKAHPDVFNLLLQVMDNGT 584
Cdd:pfam13401 84 VAVVLIIDEAQHLSLEALEELRDLLNLSS 112
|
|
| COG3899 |
COG3899 |
Predicted ATPase [General function prediction only]; |
4-235 |
9.01e-03 |
|
Predicted ATPase [General function prediction only];
Pssm-ID: 443106 [Multi-domain] Cd Length: 1244 Bit Score: 39.46 E-value: 9.01e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2298857976 4 QELELSLNMAFARAREHRHEFMTVEHLLLALLSNPAAREALEACTVDLAALRQELEAFIEQTTPTLPASEEERDTQPTLS 83
Cdd:COG3899 112 ALLLLALLALALLALLLALLLAAGVLGLLLGGLLLAALAALLALAALAAAAAAAAAAAAARAARLRRARAARLAALALRA 191
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2298857976 84 FQRVLQRAVFHVQSSGRSEVSGANVLVAIFSEQESQAAYLLRKHDVSRLDVVNFISHGTRKDEPGQAPNAEnpvneeQSG 163
Cdd:COG3899 192 LLLLVLLLLLLLLLLGLLLAAAAALAAAAAAAAAAAPAAPVVLVAALLLALAALLALLLLAARLLGLAGAA------ALL 265
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2298857976 164 GEDRMENFTTNLNQLARVGGIDPLIGRDPELERAIQVL--CRRRKNNPLLV-GESGVGKTAIAEGLAWRIVQGDV 235
Cdd:COG3899 266 LLGLLAAAAAGRRLLARRLIPQPLVGREAELAALLAALerARAGRGELVLVsGEAGIGKSRLVRELARRARARGG 340
|
|
| RecA-like_NVL_r1-like |
cd19518 |
first of two ATPase domains of NVL (nuclear VCP-like protein) and similar ATPase domains; NVL ... |
210-289 |
9.37e-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: 37.77 E-value: 9.37e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2298857976 210 LLVGESGVGKTAIAEGLAWRIvqgDVPevmadctLYSLDIGSLLAGTKyrGDFEKRFKALLKQLEQDQNSILFIDEIHTI 289
Cdd:cd19518 38 LLHGPPGCGKTMLANAIAGEL---KVP-------FLKISATEIVSGVS--GESEEKIRELFDQAISNAPCIVFIDEIDAI 105
|
|
| |
