|
Name |
Accession |
Description |
Interval |
E-value |
| ClpA |
TIGR02639 |
ATP-dependent Clp protease ATP-binding subunit clpA; [Protein fate, Degradation of proteins, ... |
4-749 |
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: 1187.90 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733551948 4 FSPHLEQTLHRALAEANKRRHEYATLEHLLLGLLDDSDAAAVLKACNVDDDVLRVNLTGYLDKELDSLKVDDDgVEATPT 83
Cdd:TIGR02639 1 ISEELERILSDALEEAKERRHEFVTLEHLLLALLDDNEAIEILEECGGDVELLRKRLEDYLEENLPVIPEDID-EEPEQT 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733551948 84 AGFQRVVQRAILHVQSSGREEMTGANVLVALFSERESHAVYFLQQQDMTRLDAVSYISHGIAKSPQQserrplrgssdde 163
Cdd:TIGR02639 80 VGVQRVIQRALLHVKSAGKKEIDIGDLLVALFDEEDSHASYFLKSQGITRLDILNYISHGISKDDGK------------- 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733551948 164 hgHDSEQAARADTKKGDSALENYCVDLNQRARDGKIDPLIGRQSEIDRTIQILCRRSKNNPLFVGDPGVGKTAIAEGLAR 243
Cdd:TIGR02639 147 --DQLGEEAGKEEEKGQDALEKYTVDLTEKAKNGKIDPLIGREDELERTIQVLCRRKKNNPLLVGEPGVGKTAIVEGLAL 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733551948 244 KIVEGDVPEVLLDATIFSLDMGSLLAGTRYRGDFEERLKAVVKELEDHDGAILFIDEIHTVIGAGATSGGAMDASNLLKP 323
Cdd:TIGR02639 225 RIAEGKVPERLKNAKIYSLDMGTLLAGTKYRGDFEERLKAVVSEIEKEPNAILFIDEIHTIVGAGATSGGSMDASNLLKP 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733551948 324 ALASGAIRCIGSTTYKEFRGHFEKDRALLRRFQKIDIAEPTLPDTIKIMQGLKPYFEKHHRVRYTADAIKAAVELSARYI 403
Cdd:TIGR02639 305 ALSSGKIRCIGSTTYEEYKNHFEKDRALSRRFQKIDVGEPSIEETVKILKGLKEQYEEFHHVKYSDEALEAAVELSARYI 384
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733551948 404 TDRKLPDKAIDVIDETGAAQMLLPISRRKKTVGVKDVEAVVAKIARIPPKSVSKDDTKVMANIERDLKRVVFGQNRAITA 483
Cdd:TIGR02639 385 NDRFLPDKAIDVIDEAGAAFRLRPKAKKKANVNVKDIENVVAKMAKIPVKTVSSDDREQLKNLEKNLKAKIFGQDEAIDQ 464
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733551948 484 LAASIKLSRAGLREPNKPIGSYLFSGPTGVGKTEVARQLALLLGVELTRFDMSEYMERHTVSRLIGAPPGYVGFDQGGLL 563
Cdd:TIGR02639 465 LVSAIKRSRAGLGDPNKPVGSFLFVGPTGVGKTELAKQLAEELGVHLLRFDMSEYMEKHTVSRLIGSPPGYVGFEQGGLL 544
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733551948 564 TDAVDQHPHSVLLLDEIEKAHPDLFNLLLQVMDAGTLTDHNGKKIDFRNVILIMTTNAGATELAKSAIGFARDSREGEDE 643
Cdd:TIGR02639 545 TDAVRKHPHCVLLLDEIEKAHPDIYNILLQVMDYATLTDNNGRKADFRNVILIMTSNAGASEMSKPPIGFGGENRESKSL 624
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733551948 644 EAIKKLFTPEFRNRLDAIVPFDYLPTEVVSRVVEKFILELEVQLAERDVMISVTDGAKKWMAEKGYDRKFGARPLSRVIQ 723
Cdd:TIGR02639 625 KAIKKLFSPEFRNRLDAIIHFNDLSEEMAEKIVKKFLDELQDQLNEKNIELELTDDAKKYLAEKGYDEEFGARPLARVIQ 704
|
730 740
....*....|....*....|....*.
gi 1733551948 724 ENVKKPLADELLFGRLQKGGEVVVRL 749
Cdd:TIGR02639 705 EEIKKPLSDEILFGKLKKGGSVKISL 730
|
|
| clpA |
PRK11034 |
ATP-dependent Clp protease ATP-binding subunit; Provisional |
8-757 |
0e+00 |
|
ATP-dependent Clp protease ATP-binding subunit; Provisional
Pssm-ID: 236828 [Multi-domain] Cd Length: 758 Bit Score: 1037.49 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733551948 8 LEQTLHRALAEANKRRHEYATLEHLLLGLLDDSDAAAVLKACNVDDDVLRVNLTGYLDKELDSLKVDDDGVEATPTAGFQ 87
Cdd:PRK11034 6 LELSLNMAFARAREHRHEFMTVEHLLLALLSNPSAREALEACSVDLVALRQELEAFIEQTTPVLPASEEERDTQPTLSFQ 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733551948 88 RVVQRAILHVQSSGREEMTGANVLVALFSERESHAVYFLQQQDMTRLDAVSYISHGIAKSpqqserrplrgsSDDEHGHD 167
Cdd:PRK11034 86 RVLQRAVFHVQSSGRSEVTGANVLVAIFSEQESQAAYLLRKHEVSRLDVVNFISHGTRKD------------EPSQSSDP 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733551948 168 SEQAARADTKKGDSALENYCVDLNQRARDGKIDPLIGRQSEIDRTIQILCRRSKNNPLFVGDPGVGKTAIAEGLARKIVE 247
Cdd:PRK11034 154 GSQPNSEEQAGGEERMENFTTNLNQLARVGGIDPLIGREKELERAIQVLCRRRKNNPLLVGESGVGKTAIAEGLAWRIVQ 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733551948 248 GDVPEVLLDATIFSLDMGSLLAGTRYRGDFEERLKAVVKELEDHDGAILFIDEIHTVIGAGATSGGAMDASNLLKPALAS 327
Cdd:PRK11034 234 GDVPEVMADCTIYSLDIGSLLAGTKYRGDFEKRFKALLKQLEQDTNSILFIDEIHTIIGAGAASGGQVDAANLIKPLLSS 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733551948 328 GAIRCIGSTTYKEFRGHFEKDRALLRRFQKIDIAEPTLPDTIKIMQGLKPYFEKHHRVRYTADAIKAAVELSARYITDRK 407
Cdd:PRK11034 314 GKIRVIGSTTYQEFSNIFEKDRALARRFQKIDITEPSIEETVQIINGLKPKYEAHHDVRYTAKAVRAAVELAVKYINDRH 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733551948 408 LPDKAIDVIDETGAAQMLLPISRRKKTVGVKDVEAVVAKIARIPPKSVSKDDTKVMANIERDLKRVVFGQNRAITALAAS 487
Cdd:PRK11034 394 LPDKAIDVIDEAGARARLMPVSKRKKTVNVADIESVVARIARIPEKSVSQSDRDTLKNLGDRLKMLVFGQDKAIEALTEA 473
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733551948 488 IKLSRAGLREPNKPIGSYLFSGPTGVGKTEVARQLALLLGVELTRFDMSEYMERHTVSRLIGAPPGYVGFDQGGLLTDAV 567
Cdd:PRK11034 474 IKMSRAGLGHEHKPVGSFLFAGPTGVGKTEVTVQLSKALGIELLRFDMSEYMERHTVSRLIGAPPGYVGFDQGGLLTDAV 553
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733551948 568 DQHPHSVLLLDEIEKAHPDLFNLLLQVMDAGTLTDHNGKKIDFRNVILIMTTNAGATELAKSAIGFARDSREGEDEEAIK 647
Cdd:PRK11034 554 IKHPHAVLLLDEIEKAHPDVFNLLLQVMDNGTLTDNNGRKADFRNVVLVMTTNAGVRETERKSIGLIHQDNSTDAMEEIK 633
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733551948 648 KLFTPEFRNRLDAIVPFDYLPTEVVSRVVEKFILELEVQLAERDVMISVTDGAKKWMAEKGYDRKFGARPLSRVIQENVK 727
Cdd:PRK11034 634 KIFTPEFRNRLDNIIWFDHLSTDVIHQVVDKFIVELQAQLDQKGVSLEVSQEARDWLAEKGYDRAMGARPMARVIQDNLK 713
|
730 740 750
....*....|....*....|....*....|
gi 1733551948 728 KPLADELLFGRLQKGGEVVVRLRDGKIDFE 757
Cdd:PRK11034 714 KPLANELLFGSLVDGGQVTVALDKEKNELT 743
|
|
| ClpA |
COG0542 |
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ... |
4-754 |
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: 846.67 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733551948 4 FSPHLEQTLHRALAEANKRRHEYATLE--HLLLGLLDDSDAAAVLKACNVDDDVLRvnltGYLDKELDSL-KVDDDGVEA 80
Cdd:COG0542 6 FTEKAQEALEAAQELARRLGHQEVEPEhlLLALLEQGEGLAAKLLRKLGVDLDALR----EELEEALGRLpKVSGSSGQP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733551948 81 TPTAGFQRVVQRAILHVQSSGREEMTGANVLVALFSERESHAVYFLQQQDMTRlDAVsyishgiakspqQSERRPLRGSS 160
Cdd:COG0542 82 YLSPRLKRVLELAELEARKLGDEYISTEHLLLALLREGEGVAARILKKLGITL-EAL------------REALEELRGGS 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733551948 161 ddehgHDSEQAARADTkkgdSALENYCVDLNQRARDGKIDPLIGRQSEIDRTIQILCRRSKNNPLFVGDPGVGKTAIAEG 240
Cdd:COG0542 149 -----RVTSQNPESKT----PALDKYGRDLTELAREGKLDPVIGRDEEIRRVIQILSRRTKNNPVLIGEPGVGKTAIVEG 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733551948 241 LARKIVEGDVPEVLLDATIFSLDMGSLLAGTRYRGDFEERLKAVVKELEDHDG-AILFIDEIHTVIGAGATSgGAMDASN 319
Cdd:COG0542 220 LAQRIVNGDVPESLKDKRVLSLDLGALVAGAKYRGEFEERLKAVLDEVKKSEGnIILFIDELHTLVGAGGAE-GAMDAAN 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733551948 320 LLKPALASGAIRCIGSTTYKEFRGHFEKDRALLRRFQKIDIAEPTLPDTIKIMQGLKPYFEKHHRVRYTADAIKAAVELS 399
Cdd:COG0542 299 LLKPALARGELRCIGATTLDEYRKYIEKDAALERRFQPVLVEEPSVEDTISILRGLKERYEAHHGVRITDEALVAAVRLS 378
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733551948 400 ARYITDRKLPDKAIDVIDETGA----AQMLLP-----ISRR--------------------------------------- 431
Cdd:COG0542 379 DRYITDRFLPDKAIDLIDEAAArvrmEIDSKPeeldeLERRleqleiekealkkeqdeasferlaelrdelaeleeelea 458
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733551948 432 --------------------------------------------------KKTVGVKDVEAVVAKIARIPPKSVSKDDTK 461
Cdd:COG0542 459 lkarweaekelieeiqelkeeleqrygkipelekelaeleeelaelapllREEVTEEDIAEVVSRWTGIPVGKLLEGERE 538
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733551948 462 VMANIERDLKRVVFGQNRAITALAASIKLSRAGLREPNKPIGSYLFSGPTGVGKTEVARQLA-LLLGVE--LTRFDMSEY 538
Cdd:COG0542 539 KLLNLEEELHERVIGQDEAVEAVADAIRRSRAGLKDPNRPIGSFLFLGPTGVGKTELAKALAeFLFGDEdaLIRIDMSEY 618
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733551948 539 MERHTVSRLIGAPPGYVGFDQGGLLTDAVDQHPHSVLLLDEIEKAHPDLFNLLLQVMDAGTLTDHNGKKIDFRNVILIMT 618
Cdd:COG0542 619 MEKHSVSRLIGAPPGYVGYEEGGQLTEAVRRRPYSVVLLDEIEKAHPDVFNILLQVLDDGRLTDGQGRTVDFRNTIIIMT 698
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733551948 619 TNAGATELAKSAIGFARDSREGED-EEAIKKLFTPEFRNRLDAIVPFDYLPTEVVSRVVEKFILELEVQLAERDVMISVT 697
Cdd:COG0542 699 SNIGSELILDLAEDEPDYEEMKEAvMEELKKHFRPEFLNRIDEIIVFHPLSKEELRKIVDLQLKRLRKRLAERGITLELT 778
|
810 820 830 840 850
....*....|....*....|....*....|....*....|....*....|....*..
gi 1733551948 698 DGAKKWMAEKGYDRKFGARPLSRVIQENVKKPLADELLFGRLQKGGEVVVRLRDGKI 754
Cdd:COG0542 779 DAAKDFLAEKGYDPEYGARPLKRAIQRELEDPLAEEILAGEIKEGDTITVDVDDGEL 835
|
|
| chaperone_ClpB |
TIGR03346 |
ATP-dependent chaperone ClpB; Members of this protein family are the bacterial ATP-dependent ... |
4-754 |
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: 689.00 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733551948 4 FSPHLEQTLHRALAEANKRRHEYATLEHLLLGLLDDSD--AAAVLKACNVDDDVLRvnltGYLDKELDSL-KVDDDGVEA 80
Cdd:TIGR03346 1 LTEKFQEALQAAQSLALGRDHQQIEPEHLLKALLDQEGglARPLLQKAGVNVGALR----QALEKELERLpKVSGPGGQV 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733551948 81 TPTAGFQRVVQRAILHVQSSGREEMTGANVLVALFSERESHAVYFLQQqdmtrldavsyishGIAKSPQQSERRPLRGSS 160
Cdd:TIGR03346 77 YLSPDLNRLLNLAEKLAQKRGDEFISSEHLLLALLDDKGTLGKLLKEA--------------GATADALEAAINAVRGGQ 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733551948 161 --DDEHGHDSEQAaradtkkgdsaLENYCVDLNQRARDGKIDPLIGRQSEIDRTIQILCRRSKNNPLFVGDPGVGKTAIA 238
Cdd:TIGR03346 143 kvTDANAEDQYEA-----------LEKYARDLTERAREGKLDPVIGRDEEIRRTIQVLSRRTKNNPVLIGEPGVGKTAIV 211
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733551948 239 EGLARKIVEGDVPEVLLDATIFSLDMGSLLAGTRYRGDFEERLKAVVKELEDHDGA-ILFIDEIHTVIGAGATsGGAMDA 317
Cdd:TIGR03346 212 EGLAQRIVNGDVPEGLKNKRLLALDMGALIAGAKYRGEFEERLKAVLNEVTKSEGQiILFIDELHTLVGAGKA-EGAMDA 290
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733551948 318 SNLLKPALASGAIRCIGSTTYKEFRGHFEKDRALLRRFQKIDIAEPTLPDTIKIMQGLKPYFEKHHRVRYTADAIKAAVE 397
Cdd:TIGR03346 291 GNMLKPALARGELHCIGATTLDEYRKYIEKDAALERRFQPVFVDEPSVEDTISILRGLKERYEVHHGVRITDPAIVAAAT 370
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733551948 398 LSARYITDRKLPDKAIDVIDEtgAAQML------LP-----ISRR----------------------------------- 431
Cdd:TIGR03346 371 LSHRYITDRFLPDKAIDLIDE--AAARIrmeidsKPeeldeLDRRiiqleierealkkekdeaskkrledlekeladlee 448
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733551948 432 ---------------------------------------------------------------------------KKTVG 436
Cdd:TIGR03346 449 eyaeleeqwkaekasiqgiqqikeeieqvrleleqaeregdlakaaelqygklpelekqlqaaeqklgeeqnrllREEVT 528
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733551948 437 VKDVEAVVAKIARIPpksVSKddtkvMANIERD--------LKRVVFGQNRAITALAASIKLSRAGLREPNKPIGSYLFS 508
Cdd:TIGR03346 529 AEEIAEVVSRWTGIP---VSK-----MLEGEREkllhmeeeLHERVVGQDEAVEAVSDAIRRSRAGLSDPNRPIGSFLFL 600
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733551948 509 GPTGVGKTEVARQLA-LLLGVE--LTRFDMSEYMERHTVSRLIGAPPGYVGFDQGGLLTDAVDQHPHSVLLLDEIEKAHP 585
Cdd:TIGR03346 601 GPTGVGKTELAKALAeFLFDSEdaMVRIDMSEYMEKHSVARLIGAPPGYVGYEEGGQLTEAVRRRPYSVVLFDEVEKAHP 680
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733551948 586 DLFNLLLQVMDAGTLTDHNGKKIDFRNVILIMTTNAGATELAKSAIGFARDSREGEDEEAIKKLFTPEFRNRLDAIVPFD 665
Cdd:TIGR03346 681 DVFNVLLQVLDDGRLTDGQGRTVDFRNTVIIMTSNLGSDFIQELAGGDDYEEMREAVMEVLRAHFRPEFLNRIDEIVVFH 760
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733551948 666 YLPTEVVSRVVEKFILELEVQLAERDVMISVTDGAKKWMAEKGYDRKFGARPLSRVIQENVKKPLADELLFGRLQKGGEV 745
Cdd:TIGR03346 761 PLGREQIARIVEIQLGRLRKRLAERKITLELSDAALDFLAEAGYDPVYGARPLKRAIQREIENPLAKKILAGEVAPGDTI 840
|
....*....
gi 1733551948 746 VVRLRDGKI 754
Cdd:TIGR03346 841 RVDVEGGRL 849
|
|
| clpC |
CHL00095 |
Clp protease ATP binding subunit |
165-753 |
0e+00 |
|
Clp protease ATP binding subunit
Pssm-ID: 214361 [Multi-domain] Cd Length: 821 Bit Score: 665.60 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733551948 165 GHDSEQAARADTKKGD-SALENYCVDLNQRARDGKIDPLIGRQSEIDRTIQILCRRSKNNPLFVGDPGVGKTAIAEGLAR 243
Cdd:CHL00095 143 GEIIEAILGAEQSRSKtPTLEEFGTNLTKEAIDGNLDPVIGREKEIERVIQILGRRTKNNPILIGEPGVGKTAIAEGLAQ 222
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733551948 244 KIVEGDVPEVLLDATIFSLDMGSLLAGTRYRGDFEERLKAVVKELEDHDGAILFIDEIHTVIGAGATSGgAMDASNLLKP 323
Cdd:CHL00095 223 RIVNRDVPDILEDKLVITLDIGLLLAGTKYRGEFEERLKRIFDEIQENNNIILVIDEVHTLIGAGAAEG-AIDAANILKP 301
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733551948 324 ALASGAIRCIGSTTYKEFRGHFEKDRALLRRFQKIDIAEPTLPDTIKIMQGLKPYFEKHHRVRYTADAIKAAVELSARYI 403
Cdd:CHL00095 302 ALARGELQCIGATTLDEYRKHIEKDPALERRFQPVYVGEPSVEETIEILFGLRSRYEKHHNLSISDKALEAAAKLSDQYI 381
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733551948 404 TDRKLPDKAIDVIDETGAA----QMLLPISRRK----------------------------------------------- 432
Cdd:CHL00095 382 ADRFLPDKAIDLLDEAGSRvrliNSRLPPAAREldkelreilkdkdeaireqdfetakqlrdremevraqiaaiiqskkt 461
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733551948 433 --------KTVGVKDVEAVVAKIARIPPKSVSKDDTKVMANIERDLKRVVFGQNRAITALAASIKLSRAGLREPNKPIGS 504
Cdd:CHL00095 462 eeekrlevPVVTEEDIAEIVSAWTGIPVNKLTKSESEKLLHMEETLHKRIIGQDEAVVAVSKAIRRARVGLKNPNRPIAS 541
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733551948 505 YLFSGPTGVGKTEVARQLALLL-GVE--LTRFDMSEYMERHTVSRLIGAPPGYVGFDQGGLLTDAVDQHPHSVLLLDEIE 581
Cdd:CHL00095 542 FLFSGPTGVGKTELTKALASYFfGSEdaMIRLDMSEYMEKHTVSKLIGSPPGYVGYNEGGQLTEAVRKKPYTVVLFDEIE 621
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733551948 582 KAHPDLFNLLLQVMDAGTLTDHNGKKIDFRNVILIMTTNAGATELAKSAIGFARDSRE-GEDE-----------EAIKKL 649
Cdd:CHL00095 622 KAHPDIFNLLLQILDDGRLTDSKGRTIDFKNTLIIMTSNLGSKVIETNSGGLGFELSEnQLSEkqykrlsnlvnEELKQF 701
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733551948 650 FTPEFRNRLDAIVPFDYLPTEVVSRVVEKFILELEVQLAERDVMISVTDGAKKWMAEKGYDRKFGARPLSRVIQENVKKP 729
Cdd:CHL00095 702 FRPEFLNRLDEIIVFRQLTKNDVWEIAEIMLKNLFKRLNEQGIQLEVTERIKTLLIEEGYNPLYGARPLRRAIMRLLEDP 781
|
650 660
....*....|....*....|....
gi 1733551948 730 LADELLFGRLQKGGEVVVRLRDGK 753
Cdd:CHL00095 782 LAEEVLSFKIKPGDIIIVDVNDEK 805
|
|
| PRK10865 |
PRK10865 |
ATP-dependent chaperone ClpB; |
182-754 |
0e+00 |
|
ATP-dependent chaperone ClpB;
Pssm-ID: 182791 [Multi-domain] Cd Length: 857 Bit Score: 553.68 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733551948 182 ALENYCVDLNQRARDGKIDPLIGRQSEIDRTIQILCRRSKNNPLFVGDPGVGKTAIAEGLARKIVEGDVPEVLLDATIFS 261
Cdd:PRK10865 160 ALKKYTIDLTERAEQGKLDPVIGRDEEIRRTIQVLQRRTKNNPVLIGEPGVGKTAIVEGLAQRIINGEVPEGLKGRRVLA 239
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733551948 262 LDMGSLLAGTRYRGDFEERLKAVVKELEDHDGA-ILFIDEIHTVIGAGaTSGGAMDASNLLKPALASGAIRCIGSTTYKE 340
Cdd:PRK10865 240 LDMGALVAGAKYRGEFEERLKGVLNDLAKQEGNvILFIDELHTMVGAG-KADGAMDAGNMLKPALARGELHCVGATTLDE 318
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733551948 341 FRGHFEKDRALLRRFQKIDIAEPTLPDTIKIMQGLKPYFEKHHRVRYTADAIKAAVELSARYITDRKLPDKAIDVIDETG 420
Cdd:PRK10865 319 YRQYIEKDAALERRFQKVFVAEPSVEDTIAILRGLKERYELHHHVQITDPAIVAAATLSHRYIADRQLPDKAIDLIDEAA 398
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733551948 421 A------------------------------------------------------------------------------- 421
Cdd:PRK10865 399 Ssirmqidskpeeldrldrriiqlkleqqalmkesdeaskkrldmlneelsdkerqyseleeewkaekaslsgtqtikae 478
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733551948 422 ---AQMLLPISRRKKTVG----------------------------------VKDVE--AVVAKIARIPPKSVSKDDTKV 462
Cdd:PRK10865 479 leqAKIAIEQARRVGDLArmselqygkipelekqlaaatqlegktmrllrnkVTDAEiaEVLARWTGIPVSRMLESEREK 558
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733551948 463 MANIERDLKRVVFGQNRAITALAASIKLSRAGLREPNKPIGSYLFSGPTGVGKTEVARQLALLL---GVELTRFDMSEYM 539
Cdd:PRK10865 559 LLRMEQELHHRVIGQNEAVEAVSNAIRRSRAGLSDPNRPIGSFLFLGPTGVGKTELCKALANFMfdsDDAMVRIDMSEFM 638
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733551948 540 ERHTVSRLIGAPPGYVGFDQGGLLTDAVDQHPHSVLLLDEIEKAHPDLFNLLLQVMDAGTLTDHNGKKIDFRNVILIMTT 619
Cdd:PRK10865 639 EKHSVSRLVGAPPGYVGYEEGGYLTEAVRRRPYSVILLDEVEKAHPDVFNILLQVLDDGRLTDGQGRTVDFRNTVVIMTS 718
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733551948 620 NAGaTELAKSAIGfARDSREGEDE--EAIKKLFTPEFRNRLDAIVPFDYLPTEVVSRVVEKFILELEVQLAERDVMISVT 697
Cdd:PRK10865 719 NLG-SDLIQERFG-ELDYAHMKELvlGVVSHNFRPEFINRIDEVVVFHPLGEQHIASIAQIQLQRLYKRLEERGYEIHIS 796
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....*..
gi 1733551948 698 DGAKKWMAEKGYDRKFGARPLSRVIQENVKKPLADELLFGRLQKGGEVVVRLRDGKI 754
Cdd:PRK10865 797 DEALKLLSENGYDPVYGARPLKRAIQQQIENPLAQQILSGELVPGKVIRLEVNDDRI 853
|
|
| VI_ClpV1 |
TIGR03345 |
type VI secretion ATPase, ClpV1 family; Members of this protein family are homologs of ClpB, ... |
38-735 |
2.01e-180 |
|
type VI secretion ATPase, ClpV1 family; Members of this protein family are homologs of ClpB, an ATPase associated with chaperone-related functions. These ClpB homologs, designated ClpV1, are a key component of the bacterial pathogenicity-associated type VI secretion system. [Protein fate, Protein and peptide secretion and trafficking, Cellular processes, Pathogenesis]
Pssm-ID: 274528 [Multi-domain] Cd Length: 852 Bit Score: 538.37 E-value: 2.01e-180
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733551948 38 DDSDAAAVLKACNVDDDVLRVNLtgylDKELDSLKVDDDGVEATPTAgFQRVVQRA-ILHVQSSGREEMTGANVLVALFS 116
Cdd:TIGR03345 37 PDSDLAAILRHFGVDLGRLKADL----ARALDKLPRGNTRTPVFSPH-LVELLQEAwLLASLELGDGRIRSGHLLLALLT 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733551948 117 ERESHAVYFLQQQDMTRLDaVSYISHGIAkspqqserRPLRGSSDDEHGHDSEQAARADTKKGD-SALENYCVDLNQRAR 195
Cdd:TIGR03345 112 DPELRRLLGSISPELAKID-REALREALP--------ALVEGSAEASAAAADAAPAGAAAGAAGtSALDQYTTDLTAQAR 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733551948 196 DGKIDPLIGRQSEIDRTIQILCRRSKNNPLFVGDPGVGKTAIAEGLARKIVEGDVPEVLLDATIFSLDMGSLLAGTRYRG 275
Cdd:TIGR03345 183 EGKIDPVLGRDDEIRQMIDILLRRRQNNPILTGEAGVGKTAVVEGLALRIAAGDVPPALRNVRLLSLDLGLLQAGASVKG 262
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733551948 276 DFEERLKAVVKELEDHDGA-ILFIDEIHTVIGAGATSGGAmDASNLLKPALASGAIRCIGSTTYKEFRGHFEKDRALLRR 354
Cdd:TIGR03345 263 EFENRLKSVIDEVKASPQPiILFIDEAHTLIGAGGQAGQG-DAANLLKPALARGELRTIAATTWAEYKKYFEKDPALTRR 341
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733551948 355 FQKIDIAEPTLPDTIKIMQGLKPYFEKHHRVRYTADAIKAAVELSARYITDRKLPDKAIDVID----------------- 417
Cdd:TIGR03345 342 FQVVKVEEPDEETAIRMLRGLAPVLEKHHGVLILDEAVVAAVELSHRYIPGRQLPDKAVSLLDtacarvalsqnatpaal 421
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733551948 418 ------------------------------------------------------ETGAAQMLLPISRRKKTVGVKD---- 439
Cdd:TIGR03345 422 edlrrriaaleleldalereaalgadhderlaelraelaaleaelaalearwqqEKELVEAILALRAELEADADAPaddd 501
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733551948 440 --------------------------------VEAVVAKIARIPPKSVSKDDTKVMANIERDLKRVVFGQNRAITALAAS 487
Cdd:TIGR03345 502 dalraqlaeleaalasaqgeeplvfpevdaqaVAEVVADWTGIPVGRMVRDEIEAVLSLPDRLAERVIGQDHALEAIAER 581
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733551948 488 IKLSRAGLREPNKPIGSYLFSGPTGVGKTEVARQLA-LLLGVE--LTRFDMSEYMERHTVSRLIGAPPGYVGFDQGGLLT 564
Cdd:TIGR03345 582 IRTARAGLEDPRKPLGVFLLVGPSGVGKTETALALAeLLYGGEqnLITINMSEFQEAHTVSRLKGSPPGYVGYGEGGVLT 661
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733551948 565 DAVDQHPHSVLLLDEIEKAHPDLFNLLLQVMDAGTLTDHNGKKIDFRNVILIMTTNAGATELAKSAIGFARDSREGEDEE 644
Cdd:TIGR03345 662 EAVRRKPYSVVLLDEVEKAHPDVLELFYQVFDKGVMEDGEGREIDFKNTVILLTSNAGSDLIMALCADPETAPDPEALLE 741
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733551948 645 AIK----KLFTPEFRNRLdAIVPFDYLPTEVVSRVVEKFILELEVQLAER-DVMISVTDGAKKWMAEKGYDRKFGARPLS 719
Cdd:TIGR03345 742 ALRpellKVFKPAFLGRM-TVIPYLPLDDDVLAAIVRLKLDRIARRLKENhGAELVYSEALVEHIVARCTEVESGARNID 820
|
810
....*....|....*.
gi 1733551948 720 RVIQENVKKPLADELL 735
Cdd:TIGR03345 821 AILNQTLLPELSRQIL 836
|
|
| RecA-like_ClpB_Hsp104-like |
cd19499 |
Chaperone protein ClpB/Hsp104 subfamily; Bacterial Caseinolytic peptidase B (ClpB) and ... |
465-664 |
7.18e-84 |
|
Chaperone protein ClpB/Hsp104 subfamily; Bacterial Caseinolytic peptidase B (ClpB) and eukaryotic Heat shock protein 104 (Hsp104) are ATP-dependent molecular chaperones and essential proteins of the heat-shock response. ClpB/Hsp104 ATPases, in concert with the DnaK/Hsp70 chaperone system, disaggregate and reactivate aggregated proteins. This RecA-like_ClpB_Hsp104_like subfamily belongs to the RecA-like NTPase family which includes the NTP binding domain of F1 and V1 H(+)ATPases, DnaB and related helicases as well as bacterial RecA and related eukaryotic and archaeal recombinases. The RecA-like NTPase family also includes bacterial conjugation proteins and related DNA transfer proteins involved in type II and type IV secretion.
Pssm-ID: 410907 [Multi-domain] Cd Length: 178 Bit Score: 264.04 E-value: 7.18e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733551948 465 NIERDLKRVVFGQNRAITALAASIKLSRAGLREPNKPIGSYLFSGPTGVGKTEVARQLALLL---GVELTRFDMSEYMER 541
Cdd:cd19499 4 NLEERLHERVVGQDEAVKAVSDAIRRARAGLSDPNRPIGSFLFLGPTGVGKTELAKALAELLfgdEDNLIRIDMSEYMEK 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733551948 542 HTVSRLIGAPPGYVGFDQGGLLTDAVDQHPHSVLLLDEIEKAHPDLFNLLLQVMDAGTLTDHNGKKIDFRNVILIMTTNA 621
Cdd:cd19499 84 HSVSRLIGAPPGYVGYTEGGQLTEAVRRKPYSVVLLDEIEKAHPDVQNLLLQVLDDGRLTDSHGRTVDFKNTIIIMTSNH 163
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1733551948 622 gatelaksaigfardsregedeeaikklFTPEFRNRLDAIVPF 664
Cdd:cd19499 164 ----------------------------FRPEFLNRIDEIVVF 178
|
|
| AAA_2 |
pfam07724 |
AAA domain (Cdc48 subfamily); This Pfam entry includes some of the AAA proteins not detected ... |
500-661 |
2.43e-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: 246.72 E-value: 2.43e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733551948 500 KPIGSYLFSGPTGVGKTEVARQLALLLGV---ELTRFDMSEYMERHTVSRLIGAPPGYVGFDQGGLLTDAVDQHPHSVLL 576
Cdd:pfam07724 1 RPIGSFLFLGPTGVGKTELAKALAELLFGderALIRIDMSEYMEEHSVSRLIGAPPGYVGYEEGGQLTEAVRRKPYSIVL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733551948 577 LDEIEKAHPDLFNLLLQVMDAGTLTDHNGKKIDFRNVILIMTTNAGATELAKSAIGFARDSRE---GEDEEAIKKLFTPE 653
Cdd:pfam07724 81 IDEIEKAHPGVQNDLLQILEGGTLTDKQGRTVDFKNTLFIMTGNFGSEKISDASRLGDSPDYEllkEEVMDLLKKGFIPE 160
|
....*...
gi 1733551948 654 FRNRLDAI 661
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 ... |
364-468 |
1.41e-33 |
|
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: 124.14 E-value: 1.41e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733551948 364 TLPDTIKIMQGLKPYFEKHHRVRYTADAIKAAVELSARYITDRKLPDKAIDVIDETGAAqmlLPISRRKKTVGVKDVEAV 443
Cdd:pfam17871 1 SVEEAIEILRGLKPKYEKHHGVRISDEALEAAVKLSKRYITDRFLPDKAIDLLDEACAR---VRLSQESKPEELEDLERE 77
|
90 100
....*....|....*....|....*
gi 1733551948 444 VAKIARIPPKSVSKDDTKVMANIER 468
Cdd:pfam17871 78 LAKLEIEKEALEREQDFEKAERLAK 102
|
|
| ClpB_D2-small |
pfam10431 |
C-terminal, D2-small domain, of ClpB protein; This is the C-terminal domain of ClpB protein, ... |
667-747 |
7.10e-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, 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: 104.41 E-value: 7.10e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733551948 667 LPTEVVSRVVEKFILELEVQLAERDVMISVTDGAKKWMAEKGYDRKFGARPLSRVIQENVKKPLADELLFGRLQKGGEVV 746
Cdd:pfam10431 1 LSKEELRKIVDLQLKELQKRLAERGITLELTDAAKDWLAEKGYDPEYGARPLRRAIQREIEDPLAEEILSGELKEGDTVR 80
|
.
gi 1733551948 747 V 747
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, ... |
667-756 |
1.31e-26 |
|
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: 104.06 E-value: 1.31e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733551948 667 LPTEVVSRVVEKFILELEVQLAERDVMISVTDGAKKWMAEKGYDRKFGARPLSRVIQENVKKPLADELLFGRLQKGGEVV 746
Cdd:smart01086 1 LDKEDLVRIVDLPLNALQKRLAEKGITLEFTDEALDWLAEKGYDPKYGARPLRRIIQRELEDPLAELILSGELKDGDTVV 80
|
90
....*....|
gi 1733551948 747 VRLRDGKIDF 756
Cdd:smart01086 81 VDVDDGELVF 90
|
|
| AAA |
cd00009 |
The AAA+ (ATPases Associated with a wide variety of cellular Activities) superfamily ... |
203-358 |
2.35e-21 |
|
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: 91.05 E-value: 2.35e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733551948 203 IGRQSEIDRTIQILCRRSKNNPLFVGDPGVGKTAIAEGLARKIVEGDVPevlldatIFSLDMGSLLAGTRYRGDFEERLK 282
Cdd:cd00009 1 VGQEEAIEALREALELPPPKNLLLYGPPGTGKTTLARAIANELFRPGAP-------FLYLNASDLLEGLVVAELFGHFLV 73
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1733551948 283 AVVKEL-EDHDGAILFIDEIHTVigAGATSGGAMDASNLLKPALAS-GAIRCIGSTTYKEFRghfEKDRALLRRFQKI 358
Cdd:cd00009 74 RLLFELaEKAKPGVLFIDEIDSL--SRGAQNALLRVLETLNDLRIDrENVRVIGATNRPLLG---DLDRALYDRLDIR 146
|
|
| AAA |
pfam00004 |
ATPase family associated with various cellular activities (AAA); AAA family proteins often ... |
225-358 |
3.76e-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: 75.32 E-value: 3.76e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733551948 225 LFVGDPGVGKTAIAEGLARKivegdvpevlLDATIFSLDMGSLLAGtrYRGDFEERLKAVVKELEDHDGAILFIDEIHTV 304
Cdd:pfam00004 2 LLYGPPGTGKTTLAKAVAKE----------LGAPFIEISGSELVSK--YVGESEKRLRELFEAAKKLAPCVIFIDEIDAL 69
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1733551948 305 IGAGATSGG--AMDASNLLKPAL-----ASGAIRCIGSTTYKEfrghfEKDRALLRRFQKI 358
Cdd:pfam00004 70 AGSRGSGGDseSRRVVNQLLTELdgftsSNSKVIVIAATNRPD-----KLDPALLGRFDRI 125
|
|
| AAA |
cd00009 |
The AAA+ (ATPases Associated with a wide variety of cellular Activities) superfamily ... |
475-620 |
1.11e-15 |
|
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: 74.88 E-value: 1.11e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733551948 475 FGQNRAITALAASIKLsraglrepnKPIGSYLFSGPTGVGKTEVARQLALLL---GVELTRFDMSEYMERHTVSRLIgap 551
Cdd:cd00009 1 VGQEEAIEALREALEL---------PPPKNLLLYGPPGTGKTTLARAIANELfrpGAPFLYLNASDLLEGLVVAELF--- 68
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1733551948 552 pgyvGFDQGGLLTDAVDQHPHSVLLLDEIEKAHPDLFNLLLQVMDagtltDHNGKKIDFRNVILIMTTN 620
Cdd:cd00009 69 ----GHFLVRLLFELAEKAKPGVLFIDEIDSLSRGAQNALLRVLE-----TLNDLRIDRENVRVIGATN 128
|
|
| RecA-like_protease |
cd19481 |
proteases similar to RecA; RecA-like NTPases. This family includes the NTP binding domain of ... |
466-620 |
1.20e-12 |
|
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: 66.15 E-value: 1.20e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733551948 466 IERDLKRVVFGQNRAITALAASIKLSRaglrepnkpigSYLFSGPTGVGKTEVARQLALLLGVELTRFDMSEYMERHTvs 545
Cdd:cd19481 1 LKASLREAVEAPRRGSRLRRYGLGLPK-----------GILLYGPPGTGKTLLAKALAGELGLPLIVVKLSSLLSKYV-- 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733551948 546 rligappGYVGfDQGGLLTDAVDQHPHSVLLLDEIEKAHPD------------LFNLLLQVMDAGTLTDhngkkidfrNV 613
Cdd:cd19481 68 -------GESE-KNLRKIFERARRLAPCILFIDEIDAIGRKrdssgesgelrrVLNQLLTELDGVNSRS---------KV 130
|
....*..
gi 1733551948 614 ILIMTTN 620
Cdd:cd19481 131 LVIAATN 137
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
503-636 |
2.43e-10 |
|
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a variety of cellular activities. This profile/alignment only detects a fraction of this vast family. The poorly conserved N-terminal helix is missing from the alignment.
Pssm-ID: 214640 [Multi-domain] Cd Length: 148 Bit Score: 59.31 E-value: 2.43e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733551948 503 GSYLFSGPTGVGKTEVARQLALLLGVELTRF---DMSEYMERHTVSRLIGAPPGYVGFDQGG----LLTDAVDQHPHSVL 575
Cdd:smart00382 3 EVILIVGPPGSGKTTLARALARELGPPGGGViyiDGEDILEEVLDQLLLIIVGGKKASGSGElrlrLALALARKLKPDVL 82
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1733551948 576 LLDEIEKAHPDLFNLLLQVMDagtLTDHNGKKIDFRNVILIMTTNAGATELAKSAIGFARD 636
Cdd:smart00382 83 ILDEITSLLDAEQEALLLLLE---ELRLLLLLKSEKNLTVILTTNDEKDLGPALLRRRFDR 140
|
|
| AAA |
pfam00004 |
ATPase family associated with various cellular activities (AAA); AAA family proteins often ... |
505-620 |
3.06e-10 |
|
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: 58.76 E-value: 3.06e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733551948 505 YLFSGPTGVGKTEVARQLALLLGVELTRFDMSEymerhTVSRLIGAPPGYVgfdqGGLLTDAVDQHPhSVLLLDEIEKAH 584
Cdd:pfam00004 1 LLLYGPPGTGKTTLAKAVAKELGAPFIEISGSE-----LVSKYVGESEKRL----RELFEAAKKLAP-CVIFIDEIDALA 70
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 1733551948 585 P-----------DLFNLLLQVMDagtltdhnGKKIDFRNVILIMTTN 620
Cdd:pfam00004 71 GsrgsggdsesrRVVNQLLTELD--------GFTSSNSKVIVIAATN 109
|
|
| AAA_5 |
pfam07728 |
AAA domain (dynein-related subfamily); This Pfam entry includes some of the AAA proteins not ... |
509-620 |
3.31e-10 |
|
AAA domain (dynein-related subfamily); This Pfam entry includes some of the AAA proteins not detected by the pfam00004 model.
Pssm-ID: 400191 [Multi-domain] Cd Length: 135 Bit Score: 58.46 E-value: 3.31e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733551948 509 GPTGVGKTEVARQLA-LLLGVELTRFDMSEYMerhTVSRLIGappGYVGFDQGGLLTDAV----DQHPHsVLLLDEIEKA 583
Cdd:pfam07728 6 GPPGTGKTELAERLAaALSNRPVFYVQLTRDT---TEEDLFG---RRNIDPGGASWVDGPlvraAREGE-IAVLDEINRA 78
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 1733551948 584 HPDLFNLLLQVMDAGTL-TDHNGKKIDFR--NVILIMTTN 620
Cdd:pfam07728 79 NPDVLNSLLSLLDERRLlLPDGGELVKAApdGFRLIATMN 118
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
220-358 |
4.82e-10 |
|
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a variety of cellular activities. This profile/alignment only detects a fraction of this vast family. The poorly conserved N-terminal helix is missing from the alignment.
Pssm-ID: 214640 [Multi-domain] Cd Length: 148 Bit Score: 58.54 E-value: 4.82e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733551948 220 SKNNPLFVGDPGVGKTAIAEGLARKIVEGDVPEVLLDATIFSLDMGSLLAGTR-----YRGDFEERLKAVVKELEDHDGA 294
Cdd:smart00382 1 PGEVILIVGPPGSGKTTLARALARELGPPGGGVIYIDGEDILEEVLDQLLLIIvggkkASGSGELRLRLALALARKLKPD 80
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1733551948 295 ILFIDEIHTVIGAGATSGG-AMDASNLLKPALASGAIRCIGSTTykefRGHFEKDRALLRRFQKI 358
Cdd:smart00382 81 VLILDEITSLLDAEQEALLlLLEELRLLLLLKSEKNLTVILTTN----DEKDLGPALLRRRFDRR 141
|
|
| SpoVK |
COG0464 |
AAA+-type ATPase, SpoVK/Ycf46/Vps4 family [Cell wall/membrane/envelope biogenesis, Cell cycle ... |
225-358 |
6.09e-10 |
|
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: 61.85 E-value: 6.09e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733551948 225 LFVGDPGVGKTAIAEGLARkivegdvpevLLDATIFSLDMGSLLAGtrYRGDFEERLKAVVKELEDHDGAILFIDEIHTV 304
Cdd:COG0464 195 LLYGPPGTGKTLLARALAG----------ELGLPLIEVDLSDLVSK--YVGETEKNLREVFDKARGLAPCVLFIDEADAL 262
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733551948 305 IGA-GATSGGAMDA--SNLLK--PALASGAIrCIGsTTYkefrgHFEK-DRALLRRFQKI 358
Cdd:COG0464 263 AGKrGEVGDGVGRRvvNTLLTemEELRSDVV-VIA-ATN-----RPDLlDPALLRRFDEI 315
|
|
| RecA-like_protease |
cd19481 |
proteases similar to RecA; RecA-like NTPases. This family includes the NTP binding domain of ... |
225-358 |
1.33e-09 |
|
proteases similar to RecA; RecA-like NTPases. This family includes the NTP binding domain of F1 and V1 H(+)ATPases, DnaB and related helicases as well as bacterial RecA and related eukaryotic and archaeal recombinases. This group also includes bacterial conjugation proteins and related DNA transfer proteins involved in type II and type IV secretion.
Pssm-ID: 410889 [Multi-domain] Cd Length: 158 Bit Score: 57.68 E-value: 1.33e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733551948 225 LFVGDPGVGKTAIAEGLARkivegdvpevLLDATIFSLDMGSLLagTRYRGDFEERLKAVVKELEDHDGAILFIDEIHTV 304
Cdd:cd19481 30 LLYGPPGTGKTLLAKALAG----------ELGLPLIVVKLSSLL--SKYVGESEKNLRKIFERARRLAPCILFIDEIDAI 97
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1733551948 305 IGAGATSGGAMDAS-------NLLKPALASGAIRCIGSTTYKEfrghfEKDRALLR--RFQKI 358
Cdd:cd19481 98 GRKRDSSGESGELRrvlnqllTELDGVNSRSKVLVIAATNRPD-----LLDPALLRpgRFDEV 155
|
|
| RecA-like_CDC48_NLV2_r1-like |
cd19503 |
first of two ATPase domains of CDC48 and NLV2, and similar ATPase domains; CDC48 in yeast and ... |
225-318 |
1.95e-07 |
|
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: 51.52 E-value: 1.95e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733551948 225 LFVGDPGVGKTAIAEGLARKivegdvpevlLDATIFSLDMGSLLAGtrYRGDFEERLKAVVKELEDHDGAILFIDEIHTV 304
Cdd:cd19503 38 LLHGPPGTGKTLLARAVANE----------AGANFLSISGPSIVSK--YLGESEKNLREIFEEARSHAPSIIFIDEIDAL 105
|
90
....*....|....
gi 1733551948 305 IGAGATSGGAMDAS 318
Cdd:cd19503 106 APKREEDQREVERR 119
|
|
| RecA-like_HslU |
cd19498 |
ATP-dependent protease ATPase subunit HslU; HslU is a component of the ATP-dependent protease ... |
466-582 |
2.82e-07 |
|
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: 51.23 E-value: 2.82e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733551948 466 IERDLKRVVFGQNRAITALAASIK------LSRAGLREPNKPiGSYLFSGPTGVGKTEVARQLALLLGVELTRFDMSEYM 539
Cdd:cd19498 5 IVSELDKYIIGQDEAKRAVAIALRnrwrrmQLPEELRDEVTP-KNILMIGPTGVGKTEIARRLAKLAGAPFIKVEATKFT 83
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 1733551948 540 ErhtvsrligapPGYVGFDQGGLLTDAVDqhphSVLLLDEIEK 582
Cdd:cd19498 84 E-----------VGYVGRDVESIIRDLVE----GIVFIDEIDK 111
|
|
| COG1223 |
COG1223 |
Predicted ATPase, AAA+ superfamily [General function prediction only]; |
222-418 |
3.72e-07 |
|
Predicted ATPase, AAA+ superfamily [General function prediction only];
Pssm-ID: 440836 [Multi-domain] Cd Length: 246 Bit Score: 52.19 E-value: 3.72e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733551948 222 NNPLFVGDPGVGKTAIAEGLARKIvegDVPevlldatIFSLDMGSLLagTRYRGDFEERLKAVVKELEDHDGaILFIDEI 301
Cdd:COG1223 36 RKILFYGPPGTGKTMLAEALAGEL---KLP-------LLTVRLDSLI--GSYLGETARNLRKLFDFARRAPC-VIFFDEF 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733551948 302 HTvIGA--GATSGGA------------MDasnllkpALASGAIrCIGSTTYKEFRghfekDRALLRRFQ-KIDIAEPTLP 366
Cdd:COG1223 103 DA-IAKdrGDQNDVGevkrvvnallqeLD-------GLPSGSV-VIAATNHPELL-----DSALWRRFDeVIEFPLPDKE 168
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733551948 367 DTIKIMQ----GLKPYFEKH------------HR--VRYTADAIKAAVELSARYITDRKLpDKAIDVIDE 418
Cdd:COG1223 169 ERKEILElnlkKFPLPFELDlkklakkleglsGAdiEKVLKTALKKAILEDREKVTKEDL-EEALKQRKE 237
|
|
| MoxR |
COG0714 |
MoxR-like ATPase [General function prediction only]; MoxR-like ATPase is part of the Pathway ... |
464-596 |
4.56e-07 |
|
MoxR-like ATPase [General function prediction only]; MoxR-like ATPase is part of the Pathway/BioSystem: Cobalamine/B12 biosynthesis
Pssm-ID: 440478 [Multi-domain] Cd Length: 292 Bit Score: 52.09 E-value: 4.56e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733551948 464 ANIERDLKRVVFGQNRAITALAASIKLsraglrepNKPIgsyLFSGPTGVGKTEVARQLALLLGVELTRF----DMseym 539
Cdd:COG0714 4 ARLRAEIGKVYVGQEELIELVLIALLA--------GGHL---LLEGVPGVGKTTLAKALARALGLPFIRIqftpDL---- 68
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1733551948 540 erhTVSRLIG---APPGYVGF--DQGGLLTdavdqhphSVLLLDEIEKAHPDLFNLLLQVMD 596
Cdd:COG0714 69 ---LPSDILGtyiYDQQTGEFefRPGPLFA--------NVLLADEINRAPPKTQSALLEAME 119
|
|
| RPT1 |
COG1222 |
ATP-dependent 26S proteasome regulatory subunit [Posttranslational modification, protein ... |
225-449 |
4.96e-07 |
|
ATP-dependent 26S proteasome regulatory subunit [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440835 [Multi-domain] Cd Length: 326 Bit Score: 52.32 E-value: 4.96e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733551948 225 LFVGDPGVGKTAIAEGLARKivegdvpevlLDATIFSLDMGSLLagTRYRGDFEERLKAVVKELEDHDGAILFIDEIHTv 304
Cdd:COG1222 116 LLYGPPGTGKTLLAKAVAGE----------LGAPFIRVRGSELV--SKYIGEGARNVREVFELAREKAPSIIFIDEIDA- 182
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733551948 305 IGAGATSGGAMDASNLLKPAL--------ASGAIRCIGSTTYKEfrghfEKDRALLR--RF-QKIDIAEPTLPDTIKImq 373
Cdd:COG1222 183 IAARRTDDGTSGEVQRTVNQLlaeldgfeSRGDVLIIAATNRPD-----LLDPALLRpgRFdRVIEVPLPDEEAREEI-- 255
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733551948 374 glkpyFEKHHRVRYTADAI------KAAVELSARYItdrklpdKAIdvIDEtgaAQMLLpISRRKKTVGVKDVEAVVAKI 447
Cdd:COG1222 256 -----LKIHLRDMPLADDVdldklaKLTEGFSGADL-------KAI--VTE---AGMFA-IREGRDTVTMEDLEKAIEKV 317
|
..
gi 1733551948 448 AR 449
Cdd:COG1222 318 KK 319
|
|
| SpoVK |
COG0464 |
AAA+-type ATPase, SpoVK/Ycf46/Vps4 family [Cell wall/membrane/envelope biogenesis, Cell cycle ... |
348-620 |
1.42e-06 |
|
AAA+-type ATPase, SpoVK/Ycf46/Vps4 family [Cell wall/membrane/envelope biogenesis, Cell cycle control, cell division, chromosome partitioning, Signal transduction mechanisms];
Pssm-ID: 440232 [Multi-domain] Cd Length: 397 Bit Score: 51.45 E-value: 1.42e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733551948 348 DRALLRRFQKIDIAEPTLPDTIKIMQGLKPYFEKHHRVRYTADAIKAAVELSARYITDRKLPDKAIDVIDETGAAQMLLP 427
Cdd:COG0464 44 LLLLLLALLLVELLLLLLSGALAALLLLALLLLALLALLAALLSALELLLLGELLLLLLLLLLLLLLLLDLERALLELLR 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733551948 428 ISRRKKTVGVKDVEAVVAKIARIPPKSVSK---DDTKVMANIERDLKRVVFGQNRAITALAasiklsRAGLRepnkPIGS 504
Cdd:COG0464 124 ESAEALALAAPLVTYEDIGGLEEELLELREailDDLGGLEEVKEELRELVALPLKRPELRE------EYGLP----PPRG 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733551948 505 YLFSGPTGVGKTEVARQLALLLGVELTRFDMSEymerhtvsrLIGappGYVG---------FDQgglltdaVDQHPHSVL 575
Cdd:COG0464 194 LLLYGPPGTGKTLLARALAGELGLPLIEVDLSD---------LVS---KYVGeteknlrevFDK-------ARGLAPCVL 254
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 1733551948 576 LLDEIEKAHPD-----------LFNLLLQVMDagtltDHNGkkidfrNVILIMTTN 620
Cdd:COG0464 255 FIDEADALAGKrgevgdgvgrrVVNTLLTEME-----ELRS------DVVVIAATN 299
|
|
| RecA-like_VPS4-like |
cd19509 |
ATPase domain of VPS4, ATAD1, K, KTNA1, Spastin, FIGL-1 and similar ATPase domains; This ... |
225-357 |
2.88e-06 |
|
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: 48.12 E-value: 2.88e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733551948 225 LFVGDPGVGKTAIAEGLARKIvegdvpevllDATIFSLDMGSLLAgtRYRGDFEERLKAVVKELEDHDGAILFIDEIHTV 304
Cdd:cd19509 36 LLYGPPGTGKTLLARAVASES----------GSTFFSISASSLVS--KWVGESEKIVRALFALARELQPSIIFIDEIDSL 103
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1733551948 305 I---GAGATSGGAMDASNLLK-----PALASGAIRCIGSTTYKEfrghfEKDRALLRRFQK 357
Cdd:cd19509 104 LserGSGEHEASRRVKTEFLVqmdgvLNKPEDRVLVLGATNRPW-----ELDEAFLRRFEK 159
|
|
| AAA_22 |
pfam13401 |
AAA domain; |
503-621 |
2.89e-06 |
|
AAA domain;
Pssm-ID: 379165 [Multi-domain] Cd Length: 129 Bit Score: 47.34 E-value: 2.89e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733551948 503 GSYLFSGPTGVGKTEVARQLALLL---GVELTRFDMSEYME----RHTVSRLIGAPPGYvGFDQGGLLT----DAVDQHP 571
Cdd:pfam13401 6 GILVLTGESGTGKTTLLRRLLEQLpevRDSVVFVDLPSGTSpkdlLRALLRALGLPLSG-RLSKEELLAalqqLLLALAV 84
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 1733551948 572 HSVLLLDEIEKAHPDLFNLLLqvmdagTLTDHNGKKIdfrNVILIMTTNA 621
Cdd:pfam13401 85 AVVLIIDEAQHLSLEALEELR------DLLNLSSKLL---QLILVGTPEL 125
|
|
| CDC48 |
TIGR01243 |
AAA family ATPase, CDC48 subfamily; This subfamily of the AAA family ATPases includes two ... |
225-523 |
1.57e-05 |
|
AAA family ATPase, CDC48 subfamily; This subfamily of the AAA family ATPases includes two members each from three archaeal species. It also includes yeast CDC48 (cell division control protein 48) and the human ortholog, transitional endoplasmic reticulum ATPase (valosin-containing protein). These proteins in eukaryotes are involved in the budding and transfer of membrane from the transitional endoplasmic reticulum to the Golgi apparatus.
Pssm-ID: 273521 [Multi-domain] Cd Length: 733 Bit Score: 48.36 E-value: 1.57e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733551948 225 LFVGDPGVGKTAIAEGLARKIvegdvpevllDATIFSLDMGSLLagTRYRGDFEERLKAVVKELEDHDGAILFIDEIHTV 304
Cdd:TIGR01243 216 LLYGPPGTGKTLLAKAVANEA----------GAYFISINGPEIM--SKYYGESEERLREIFKEAEENAPSIIFIDEIDAI 283
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733551948 305 IGAGATSGGAMDAS------NLLKPALASGAIRCIGSTTYKEfrghfEKDRALLR--RFQK-IDIAEPTLPDTIKIMQ-- 373
Cdd:TIGR01243 284 APKREEVTGEVEKRvvaqllTLMDGLKGRGRVIVIGATNRPD-----ALDPALRRpgRFDReIVIRVPDKRARKEILKvh 358
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733551948 374 ----------GLKPYFEKHHrvRYTADAIKAAVELSARYITDRKLPDKAIDVIDETGAAQML--LPISRRKKTVGVKDVE 441
Cdd:TIGR01243 359 trnmplaedvDLDKLAEVTH--GFVGADLAALAKEAAMAALRRFIREGKINFEAEEIPAEVLkeLKVTMKDFMEALKMVE 436
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733551948 442 AVVAKIARIPPKSVSKDDTKVMANIERDLKRVVfgqnraITALAASIKLSRAGLREPNkpiGSYLFsGPTGVGKTEVARQ 521
Cdd:TIGR01243 437 PSAIREVLVEVPNVRWSDIGGLEEVKQELREAV------EWPLKHPEIFEKMGIRPPK---GVLLF-GPPGTGKTLLAKA 506
|
..
gi 1733551948 522 LA 523
Cdd:TIGR01243 507 VA 508
|
|
| DnaX |
COG2812 |
DNA polymerase III, gamma/tau subunits [Replication, recombination and repair]; |
474-523 |
1.93e-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: 1.93e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 1733551948 474 VFGQNRAITALAASIKLSRaglrepnkpIG-SYLFSGPTGVGKTEVARQLA 523
Cdd:COG2812 12 VVGQEHVVRTLKNALASGR---------LAhAYLFTGPRGVGKTTLARILA 53
|
|
| AAA_5 |
pfam07728 |
AAA domain (dynein-related subfamily); This Pfam entry includes some of the AAA proteins not ... |
225-302 |
6.16e-05 |
|
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: 43.44 E-value: 6.16e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733551948 225 LFVGDPGVGKTAIAEGLARKIVEGDVPEVLLDAtifslDMGS--LLAGTRYRGDFEERLKAVVKElEDHDGAILFIDEIH 302
Cdd:pfam07728 3 LLVGPPGTGKTELAERLAAALSNRPVFYVQLTR-----DTTEedLFGRRNIDPGGASWVDGPLVR-AAREGEIAVLDEIN 76
|
|
| RecA-like_Lon |
cd19500 |
lon protease homolog 2 peroxisomal; Lon protease (also known as Lon peptidase) is an ... |
506-620 |
8.75e-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: 44.09 E-value: 8.75e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733551948 506 LFSGPTGVGKTEVARQLALLLGVELTRF------DMSEYM-ERHTvsrLIGAPPGYVgfDQGglLTDAVDQHPhsVLLLD 578
Cdd:cd19500 41 CLVGPPGVGKTSLGKSIARALGRKFVRIslggvrDEAEIRgHRRT---YVGAMPGRI--IQA--LKKAGTNNP--VFLLD 111
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 1733551948 579 EIEK----AHPDLFNLLLQVMDA---GTLTDHN-GKKIDFRNVILIMTTN 620
Cdd:cd19500 112 EIDKigssFRGDPASALLEVLDPeqnSTFSDHYlDVPFDLSKVLFIATAN 161
|
|
| dnaX_nterm |
TIGR02397 |
DNA polymerase III, subunit gamma and tau; This model represents the well-conserved first ~ ... |
474-523 |
1.16e-04 |
|
DNA polymerase III, subunit gamma and tau; This model represents the well-conserved first ~ 365 amino acids of the translation of the dnaX gene. The full-length product of the dnaX gene in the model bacterium E. coli is the DNA polymerase III tau subunit. A translational frameshift leads to early termination and a truncated protein subunit gamma, about 1/3 shorter than tau and present in roughly equal amounts. This frameshift mechanism is not necessarily universal for species with DNA polymerase III but appears conserved in the exterme thermophile Thermus thermophilis. [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 274111 [Multi-domain] Cd Length: 355 Bit Score: 45.25 E-value: 1.16e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 1733551948 474 VFGQNRAITALAASIKLSRAGLrepnkpigSYLFSGPTGVGKTEVARQLA 523
Cdd:TIGR02397 16 VIGQEHIVQTLKNAIKNGRIAH--------AYLFSGPRGTGKTSIARIFA 57
|
|
| RecA-like_CDC48_r1-like |
cd19519 |
first of two ATPase domains of CDC48 and similar ATPase domains; CDC48 in yeast and p97 or VCP ... |
225-304 |
2.35e-04 |
|
first of two ATPase domains of CDC48 and similar ATPase domains; CDC48 in yeast and p97 or VCP metazoans is an ATP-dependent molecular chaperone which plays an essential role in many cellular processes, by segregating polyubiquitinated proteins from complexes or membranes. Cdc48/p97 consists of an N-terminal domain and two ATPase domains; this subfamily represents the first of the two ATPase domains. CDC48's roles include in the fragmentation of Golgi stacks during mitosis and for their reassembly after mitosis, and in the formation of the nuclear envelope, and of the transitional endoplasmic reticulum (tER). This RecA-like_cdc48_r1-like subfamily belongs to the RecA-like family which includes the NTP binding domain of F1 and V1 H(+)ATPases, DnaB and related helicases as well as bacterial RecA and related eukaryotic and archaeal recombinases. The RecA-like NTPase family also includes bacterial conjugation proteins and related DNA transfer proteins involved in type II and type IV secretion.
Pssm-ID: 410927 [Multi-domain] Cd Length: 166 Bit Score: 42.42 E-value: 2.35e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733551948 225 LFVGDPGVGKTAIAEGLARKIvegdvpevllDATIFSLDMGSLLagTRYRGDFEERLKAVVKELEDHDGAILFIDEIHTV 304
Cdd:cd19519 38 LLYGPPGTGKTLIARAVANET----------GAFFFLINGPEIM--SKLAGESESNLRKAFEEAEKNAPAIIFIDEIDAI 105
|
|
| hslU |
PRK05201 |
ATP-dependent protease ATPase subunit HslU; |
509-533 |
2.92e-04 |
|
ATP-dependent protease ATPase subunit HslU;
Pssm-ID: 235364 [Multi-domain] Cd Length: 443 Bit Score: 43.91 E-value: 2.92e-04
10 20 30
....*....|....*....|....*....|
gi 1733551948 509 GPTGVGKTEVARQLALLLG-----VELTRF 533
Cdd:PRK05201 57 GPTGVGKTEIARRLAKLANapfikVEATKF 86
|
|
| PRK13342 |
PRK13342 |
recombination factor protein RarA; Reviewed |
225-402 |
3.08e-04 |
|
recombination factor protein RarA; Reviewed
Pssm-ID: 237355 [Multi-domain] Cd Length: 413 Bit Score: 43.92 E-value: 3.08e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733551948 225 LFVGDPGVGKTAIAEGLARkivEGDVPEVLLDATIFSLdmgsllagtryrgdfeERLKAVVKELEDHDGA----ILFIDE 300
Cdd:PRK13342 40 ILWGPPGTGKTTLARIIAG---ATDAPFEALSAVTSGV----------------KDLREVIEEARQRRSAgrrtILFIDE 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733551948 301 IHtvigagatsggamDAsnLLkPALASGAIRCIGSTTYKEFrghFEKDRALLRR-----FQKIDIAEptlpdtikIMQGL 375
Cdd:PRK13342 101 IHrfnk------aqqDA--LL-PHVEDGTITLIGATTENPS---FEVNPALLSRaqvfeLKPLSEED--------IEQLL 160
|
170 180 190
....*....|....*....|....*....|..
gi 1733551948 376 KPYFEKHHR--VRYTADAIKAAVELS---ARY 402
Cdd:PRK13342 161 KRALEDKERglVELDDEALDALARLAngdARR 192
|
|
| HslU |
COG1220 |
ATP-dependent protease HslVU (ClpYQ), ATPase subunit HslU [Posttranslational modification, ... |
509-533 |
4.02e-04 |
|
ATP-dependent protease HslVU (ClpYQ), ATPase subunit HslU [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440833 [Multi-domain] Cd Length: 454 Bit Score: 43.50 E-value: 4.02e-04
10 20 30
....*....|....*....|....*....|
gi 1733551948 509 GPTGVGKTEVARQLALLLG-----VELTRF 533
Cdd:COG1220 57 GPTGVGKTEIARRLAKLANapfikVEATKF 86
|
|
| PRK06647 |
PRK06647 |
DNA polymerase III subunits gamma and tau; Validated |
468-526 |
5.18e-04 |
|
DNA polymerase III subunits gamma and tau; Validated
Pssm-ID: 235845 [Multi-domain] Cd Length: 563 Bit Score: 43.61 E-value: 5.18e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 1733551948 468 RDLKRVVfGQNRAITALAASIklsraglrEPNKPIGSYLFSGPTGVGKTEVARQLALLL 526
Cdd:PRK06647 13 RDFNSLE-GQDFVVETLKHSI--------ESNKIANAYIFSGPRGVGKTSSARAFARCL 62
|
|
| RecA-like_VPS4 |
cd19521 |
ATPase domain of vacuolar protein sorting-associated protein 4; Vacuolar protein ... |
218-357 |
6.39e-04 |
|
ATPase domain of vacuolar protein sorting-associated protein 4; Vacuolar protein sorting-associated protein 4 (Vps4) is believed to be involved in intracellular protein transport out of a prevacuolar endosomal compartment. This subfamily belongs to the RecA-like NTPase family which includes the NTP binding domain of F1 and V1 H(+)ATPases, DnaB and related helicases as well as bacterial RecA and related eukaryotic and archaeal recombinases. The RecA-like NTPase family also includes bacterial conjugation proteins and related DNA transfer proteins involved in type II and type IV secretion.
Pssm-ID: 410929 [Multi-domain] Cd Length: 170 Bit Score: 41.39 E-value: 6.39e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733551948 218 RRSKNNPLFVGDPGVGKTAIAEGLARKIvegdvpevllDATIFSLDMGSLLagTRYRGDFEERLKAVVKELEDHDGAILF 297
Cdd:cd19521 37 RKPWSGILLYGPPGTGKSYLAKAVATEA----------NSTFFSVSSSDLV--SKWMGESEKLVKQLFAMARENKPSIIF 104
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1733551948 298 IDEIHTVigAGATSGGAMDASNLLKPALA---------SGAIRCIGSTTYKefrghFEKDRALLRRFQK 357
Cdd:cd19521 105 IDEVDSL--CGTRGEGESEASRRIKTELLvqmngvgndSQGVLVLGATNIP-----WQLDSAIRRRFEK 166
|
|
| RecA-like_ClpX |
cd19497 |
ATP-dependent Clp protease ATP-binding subunit ClpX; ClpX is a component of the ATP-dependent ... |
474-664 |
6.51e-04 |
|
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: 42.20 E-value: 6.51e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733551948 474 VFGQNRAITALAASI----KLSRAGLREPNKPI----GSYLFSGPTGVGKTEVARQLALLLGVELTRFDMSEYMErhtvs 545
Cdd:cd19497 14 VIGQERAKKVLSVAVynhyKRIRNNLKQKDDDVelekSNILLIGPTGSGKTLLAQTLAKILDVPFAIADATTLTE----- 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733551948 546 rligapPGYVGFDQGG----LLTDA---VDQHPHSVLLLDEIEK-----AHPDLF---------NLLLQVMDaGTL---T 601
Cdd:cd19497 89 ------AGYVGEDVENillkLLQAAdydVERAQRGIVYIDEIDKiarksENPSITrdvsgegvqQALLKILE-GTVanvP 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733551948 602 DHNGKKIDFRNVILIMTTN-----AGATE---------LAKSAIGFARDSREGEDEEAIKKLFT-------------PEF 654
Cdd:cd19497 162 PQGGRKHPQQEFIQVDTTNilficGGAFVglekiiarrLGKKSLGFGAETSSEKDEKERDELLSkvepedlikfgliPEF 241
|
250
....*....|
gi 1733551948 655 RNRLDAIVPF 664
Cdd:cd19497 242 VGRLPVIVTL 251
|
|
| RecA-like_KTNA1 |
cd19522 |
Katanin p60 ATPase-containing subunit A1; Katanin p60 ATPase-containing subunit A1 (KTNA1) is ... |
218-357 |
1.00e-03 |
|
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: 40.74 E-value: 1.00e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733551948 218 RRSKNNPLFVGDPGVGKTAIAEGLARKIvegdvpevllDATIFSLDMGSLlaGTRYRGDFEERLKAVVKELEDHDGAILF 297
Cdd:cd19522 30 RRPWKGVLMVGPPGTGKTLLAKAVATEC----------GTTFFNVSSSTL--TSKYRGESEKLVRLLFEMARFYAPTTIF 97
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1733551948 298 IDEIHTVIGAGATSgGAMDASNLLKPAL---------------ASGAIRCIGSTTYKefrghFEKDRALLRRFQK 357
Cdd:cd19522 98 IDEIDSICSRRGTS-EEHEASRRVKSELlvqmdgvggasenddPSKMVMVLAATNFP-----WDIDEALRRRLEK 166
|
|
| RecA-like_FtsH |
cd19501 |
ATP-dependent zinc metalloprotease FtsH; FtsH ATPase is a processive, ATP-dependent zinc ... |
225-316 |
1.22e-03 |
|
ATP-dependent zinc metalloprotease FtsH; FtsH ATPase is a processive, ATP-dependent zinc metallopeptidase for both cytoplasmic and membrane proteins. It is anchored to the cytoplasmic membrane such that the amino- and carboxy-termini are exposed to the cytoplasm. It presents a membrane-bound hexameric structure that is able to unfold and degrade protein substrates. It is comprised of an N-terminal transmembrane region and the larger C-terminal cytoplasmic region, which consists of an ATPase domain and a protease domain. This RecA-Like FTsH subfamily represents the ATPase domain, and 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: 410909 [Multi-domain] Cd Length: 171 Bit Score: 40.29 E-value: 1.22e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733551948 225 LFVGDPGVGKTAIAEGLARkivEGDVPevlldatIFSLDmGSllagtryrgDFEE--------RLKAVVKELEDHDGAIL 296
Cdd:cd19501 41 LLVGPPGTGKTLLAKAVAG---EAGVP-------FFSIS-GS---------DFVEmfvgvgasRVRDLFEQAKKNAPCIV 100
|
90 100
....*....|....*....|.
gi 1733551948 297 FIDEIHTVIGA-GATSGGAMD 316
Cdd:cd19501 101 FIDEIDAVGRKrGAGLGGGHD 121
|
|
| RecA-like_Ycf46-like |
cd19507 |
ATPase domain of Ycf46 and similar ATPase domains; Ycf46 may play a role in the regulation of ... |
225-313 |
1.34e-03 |
|
ATPase domain of Ycf46 and similar ATPase domains; Ycf46 may play a role in the regulation of photosynthesis in cyanobacteria, especially in CO2 uptake and utilization. This subfamily belongs to the RecA-like NTPase family which includes the NTP binding domain of F1 and V1 H(+)ATPases, DnaB and related helicases as well as bacterial RecA and related eukaryotic and archaeal recombinases. The RecA-like NTPase family also includes bacterial conjugation proteins and related DNA transfer proteins involved in type II and type IV secretion.
Pssm-ID: 410915 [Multi-domain] Cd Length: 161 Bit Score: 40.04 E-value: 1.34e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733551948 225 LFVGDPGVGKTAIAEGLARKivegdvpevlLDATIFSLDMGSLLAGtrYRGDFEERLKAVVKELEDHDGAILFIDEIHTV 304
Cdd:cd19507 35 LLVGIQGTGKSLTAKAIAGV----------WQLPLLRLDMGRLFGG--LVGESESRLRQMIQTAEAIAPCVLWIDEIEKG 102
|
....*....
gi 1733551948 305 IGaGATSGG 313
Cdd:cd19507 103 FS-NADSKG 110
|
|
| RecA-like_PEX6_r2 |
cd19527 |
second of two ATPase domains of Peroxisomal biogenesis factor 6 (PEX6); PEX6(also known as ... |
219-358 |
1.51e-03 |
|
second of two ATPase domains of Peroxisomal biogenesis factor 6 (PEX6); PEX6(also known as Peroxin61)/PEX1 is a protein unfoldase; PEX6 and PEX1 form a heterohexameric Type-2 AAA-ATPase complex and are essential for peroxisome biogenesis as they are required for the import of folded proteins into the peroxisomal matrix. This subfamily represents the second ATPase domain of PEX6. 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: 410935 [Multi-domain] Cd Length: 160 Bit Score: 39.80 E-value: 1.51e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733551948 219 RSKNNPLFVGDPGVGKTAIAEGLARKivegdvpevlLDATIFSLDMGSLLagTRYRGDFEERLKAVVKELEDHDGAILFI 298
Cdd:cd19527 24 RKRSGILLYGPPGTGKTLLAKAIATE----------CSLNFLSVKGPELI--NMYIGESEANVREVFQKARDAKPCVIFF 91
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1733551948 299 DEIHTVI---GAGATSGGAMD--ASNLLKP----ALASGAIRCIGSTTYKEFRghfekDRALLR--RFQKI 358
Cdd:cd19527 92 DELDSLApsrGNSGDSGGVMDrvVSQLLAEldgmSSSGQDVFVIGATNRPDLL-----DPALLRpgRFDKL 157
|
|
| DNA_pol3_delta2 |
pfam13177 |
DNA polymerase III, delta subunit; DNA polymerase III, delta subunit (EC 2.7.7.7) is required ... |
476-526 |
1.55e-03 |
|
DNA polymerase III, delta subunit; DNA polymerase III, delta subunit (EC 2.7.7.7) is required for, along with delta' subunit, the assembly of the processivity factor beta(2) onto primed DNA in the DNA polymerase III holoenzyme-catalyzed reaction. The delta subunit is also known as HolA.
Pssm-ID: 433013 [Multi-domain] Cd Length: 161 Bit Score: 39.89 E-value: 1.55e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 1733551948 476 GQNRAITALAASIklsraglrEPNKPIGSYLFSGPTGVGKTEVARQLALLL 526
Cdd:pfam13177 1 GQPEAIQLLQNSL--------ENGRLSHAYLFSGPEGVGKLELALAFAKAL 43
|
|
| RecA-like_spastin |
cd19524 |
ATPase domain of spastin; Spastin is an ATP-dependent microtubule-severing protein involved in ... |
218-357 |
2.13e-03 |
|
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: 39.45 E-value: 2.13e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733551948 218 RRSKNNPLFVGDPGVGKTAIAEGLARKIvegdvpevllDATIFSLDMGSLLagTRYRGDFEERLKAVVKELEDHDGAILF 297
Cdd:cd19524 30 RAPARGLLLFGPPGNGKTMLAKAVAAES----------NATFFNISAASLT--SKYVGEGEKLVRALFAVARELQPSIIF 97
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733551948 298 IDEIHTVIgaGATSGGAMDASNLLKP-------ALASGA---IRCIGSTTYKEfrghfEKDRALLRRFQK 357
Cdd:cd19524 98 IDEVDSLL--SERSEGEHEASRRLKTefliefdGVQSNGddrVLVMGATNRPQ-----ELDDAVLRRFTK 160
|
|
| PRK11331 |
PRK11331 |
5-methylcytosine-specific restriction enzyme subunit McrB; Provisional |
506-658 |
2.42e-03 |
|
5-methylcytosine-specific restriction enzyme subunit McrB; Provisional
Pssm-ID: 183088 [Multi-domain] Cd Length: 459 Bit Score: 41.22 E-value: 2.42e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733551948 506 LFSGPTGVGKTEVARQLALLLGVELT--RFDMSEYMERHTVSRLI-GAPPGYVGF-DQGGLLTDAVDQ---HPHS--VLL 576
Cdd:PRK11331 198 ILQGPPGVGKTFVARRLAYLLTGEKApqRVNMVQFHQSYSYEDFIqGYRPNGVGFrRKDGIFYNFCQQakeQPEKkyVFI 277
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733551948 577 LDEIEKAH-PDLFNLLLQVMD--------AGTLTDHNGKKIDF---RNVILIMTTNAGATELAKSAIGFAR-----DSRE 639
Cdd:PRK11331 278 IDEINRANlSKVFGEVMMLMEhdkrgenwSVPLTYSENDEERFyvpENVYIIGLMNTADRSLAVVDYALRRrfsfiDIEP 357
|
170
....*....|....*....
gi 1733551948 640 GEDeeaikklfTPEFRNRL 658
Cdd:PRK11331 358 GFD--------TPQFRNFL 368
|
|
| PRK07399 |
PRK07399 |
DNA polymerase III subunit delta'; Validated |
469-526 |
2.42e-03 |
|
DNA polymerase III subunit delta'; Validated
Pssm-ID: 236011 [Multi-domain] Cd Length: 314 Bit Score: 40.65 E-value: 2.42e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 1733551948 469 DLKRVVFGQNRAITALAASIKlsraglrepNKPIG-SYLFSGPTGVGKTEVARQLALLL 526
Cdd:PRK07399 1 NLFANLIGQPLAIELLTAAIK---------QNRIApAYLFAGPEGVGRKLAALCFIEGL 50
|
|
| RAD55 |
COG0467 |
RecA-superfamily ATPase, KaiC/GvpD/RAD55 family [Signal transduction mechanisms]; |
501-629 |
3.06e-03 |
|
RecA-superfamily ATPase, KaiC/GvpD/RAD55 family [Signal transduction mechanisms];
Pssm-ID: 440235 [Multi-domain] Cd Length: 221 Bit Score: 39.90 E-value: 3.06e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733551948 501 PIGS-YLFSGPTGVGKTEVARQLA----------LLLGVELTR-----------FDMSEYMERHTVsRLIGAPPGYVGFD 558
Cdd:COG0467 18 PRGSsTLLSGPPGTGKTTLALQFLaeglrrgekgLYVSFEESPeqllrraeslgLDLEEYIESGLL-RIIDLSPEELGLD 96
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1733551948 559 QGGL---LTDAVDQHPHSVLLLD---EIEKAHPDLFNLLLQVMDagtLTDHNGKkidfRNVILIMTTNAGATELAKS 629
Cdd:COG0467 97 LEELlarLREAVEEFGAKRVVIDslsGLLLALPDPERLREFLHR---LLRYLKK----RGVTTLLTSETGGLEDEAT 166
|
|
| TIP49 |
COG1224 |
DNA helicase TIP49, TBP-interacting protein [Transcription]; |
225-264 |
3.67e-03 |
|
DNA helicase TIP49, TBP-interacting protein [Transcription];
Pssm-ID: 440837 [Multi-domain] Cd Length: 452 Bit Score: 40.72 E-value: 3.67e-03
10 20 30 40
....*....|....*....|....*....|....*....|.
gi 1733551948 225 LFVGDPGVGKTAIAEGLARKIVEgDVPEVLLDAT-IFSLDM 264
Cdd:COG1224 68 LIVGPPGTGKTALAVAIARELGE-DTPFVAISGSeIYSAEL 107
|
|
| AAA_16 |
pfam13191 |
AAA ATPase domain; This family of domains contain a P-loop motif that is characteriztic of the ... |
201-250 |
4.31e-03 |
|
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: 38.64 E-value: 4.31e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 1733551948 201 PLIGRQSEIDRTIQILCRRSKNNP---LFVGDPGVGKTAIAEGLARKIVEGDV 250
Cdd:pfam13191 1 RLVGREEELEQLLDALDRVRSGRPpsvLLTGEAGTGKTTLLRELLRALERDGG 53
|
|
| TIP49 |
pfam06068 |
TIP49 P-loop domain; This family consists of the C-terminal region of several eukaryotic and ... |
225-265 |
4.76e-03 |
|
TIP49 P-loop domain; This family consists of the C-terminal region of several eukaryotic and archaeal RuvB-like 1 (Pontin or TIP49a) and RuvB-like 2 (Reptin or TIP49b) proteins. The N-terminal domain contains the pfam00004 domain. In zebrafish, the liebeskummer (lik) mutation, causes development of hyperplastic embryonic hearts. lik encodes Reptin, a component of a DNA-stimulated ATPase complex. Beta-catenin and Pontin, a DNA-stimulated ATPase that is often part of complexes with Reptin, are in the same genetic pathways. The Reptin/Pontin ratio serves to regulate heart growth during development, at least in part via the beta-catenin pathway. TBP-interacting protein 49 (TIP49) was originally identified as a TBP-binding protein, and two related proteins are encoded by individual genes, tip49a and b. Although the function of this gene family has not been elucidated, they are supposed to play a critical role in nuclear events because they interact with various kinds of nuclear factors and have DNA helicase activities.TIP49a has been suggested to act as an autoantigen in some patients with autoimmune diseases.
Pssm-ID: 399217 [Multi-domain] Cd Length: 347 Bit Score: 39.99 E-value: 4.76e-03
10 20 30 40
....*....|....*....|....*....|....*....|..
gi 1733551948 225 LFVGDPGVGKTAIAEGLARKIVEgDVPEVLLDAT-IFSLDMG 265
Cdd:pfam06068 54 LIAGPPGTGKTALAIAISKELGE-DTPFTSISGSeVYSLEMK 94
|
|
| RecA-like_HslU |
cd19498 |
ATP-dependent protease ATPase subunit HslU; HslU is a component of the ATP-dependent protease ... |
222-313 |
6.02e-03 |
|
ATP-dependent protease ATPase subunit HslU; HslU is a component of the ATP-dependent protease HslVU. In HslVU, HslU ATPase serves to unfold and translocate protein substrate, and the HslV protease degrades the unfolded proteins. This RecA-like_HslU subfamily belongs to the RecA-like NTPase family which includes the NTP binding domain of F1 and V1 H(+)ATPases, DnaB and related helicases as well as bacterial RecA and related eukaryotic and archaeal recombinases. The RecA-like NTPase family also includes bacterial conjugation proteins and related DNA transfer proteins involved in type II and type IV secretion.
Pssm-ID: 410906 [Multi-domain] Cd Length: 183 Bit Score: 38.51 E-value: 6.02e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733551948 222 NNPLFVGDPGVGKTAIAEGLARKIvegDVPEVLLDATIFSlDMGsllagtrYRG-DFEerlkAVVKELEDhdgAILFIDE 300
Cdd:cd19498 47 KNILMIGPTGVGKTEIARRLAKLA---GAPFIKVEATKFT-EVG-------YVGrDVE----SIIRDLVE---GIVFIDE 108
|
90
....*....|...
gi 1733551948 301 IHTVIGAGATSGG 313
Cdd:cd19498 109 IDKIAKRGGSSGP 121
|
|
| RecA-like_ClpX |
cd19497 |
ATP-dependent Clp protease ATP-binding subunit ClpX; ClpX is a component of the ATP-dependent ... |
220-301 |
6.29e-03 |
|
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: 39.12 E-value: 6.29e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733551948 220 SKNNPLFVGDPGVGKTAIAEGLARKIvegDVPEVLLDATifsldmgSLL-AGtrYRGDFEERLkaVVKELEDHDG----- 293
Cdd:cd19497 49 EKSNILLIGPTGSGKTLLAQTLAKIL---DVPFAIADAT-------TLTeAG--YVGEDVENI--LLKLLQAADYdvera 114
|
90
....*....|
gi 1733551948 294 --AILFIDEI 301
Cdd:cd19497 115 qrGIVYIDEI 124
|
|
| PRK13341 |
PRK13341 |
AAA family ATPase; |
223-354 |
6.85e-03 |
|
AAA family ATPase;
Pssm-ID: 237354 [Multi-domain] Cd Length: 725 Bit Score: 40.04 E-value: 6.85e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733551948 223 NPLFVGDPGVGKTAIAEGLARKIvegdvpevllDATIFSLDmgSLLAGTRyrgDFEERLKAVVKELEDHD-GAILFIDEI 301
Cdd:PRK13341 54 SLILYGPPGVGKTTLARIIANHT----------RAHFSSLN--AVLAGVK---DLRAEVDRAKERLERHGkRTILFIDEV 118
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 1733551948 302 HTVIGAgatsggAMDAsnlLKPALASGAIRCIGSTTYKEFrghFEKDRALLRR 354
Cdd:PRK13341 119 HRFNKA------QQDA---LLPWVENGTITLIGATTENPY---FEVNKALVSR 159
|
|
| RAD55 |
COG0467 |
RecA-superfamily ATPase, KaiC/GvpD/RAD55 family [Signal transduction mechanisms]; |
225-299 |
7.79e-03 |
|
RecA-superfamily ATPase, KaiC/GvpD/RAD55 family [Signal transduction mechanisms];
Pssm-ID: 440235 [Multi-domain] Cd Length: 221 Bit Score: 38.74 E-value: 7.79e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733551948 225 LFVGDPGVGKTA-----IAEGLAR--KIV----EGDVPEVLLDATIFSLDMGSL----------LAGTRYRGDFEERLKA 283
Cdd:COG0467 24 LLSGPPGTGKTTlalqfLAEGLRRgeKGLyvsfEESPEQLLRRAESLGLDLEEYiesgllriidLSPEELGLDLEELLAR 103
|
90
....*....|....*.
gi 1733551948 284 VVKELEDHDGAILFID 299
Cdd:COG0467 104 LREAVEEFGAKRVVID 119
|
|
| |
