|
Name |
Accession |
Description |
Interval |
E-value |
| ClpA |
COG0542 |
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ... |
62-697 |
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: 1012.69 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2026840261 62 ATSQERPKQKGLLDELGRNLTDGAHAGLIDPVIGRDEEVTRVIEILNRRNKNNPVLIGEPGVGKTAIAEGLALKIANGDV 141
Cdd:COG0542 150 VTSQNPESKTPALDKYGRDLTELAREGKLDPVIGRDEEIRRVIQILSRRTKNNPVLIGEPGVGKTAIVEGLAQRIVNGDV 229
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2026840261 142 PNKLKNKQVYLLDVSSLVANTGVRGQFEERMKQLIKEL-QSRKNIILFVDEIHLLVGAGSAEGSMDAGNILKPALARGEL 220
Cdd:COG0542 230 PESLKDKRVLSLDLGALVAGAKYRGEFEERLKAVLDEVkKSEGNIILFIDELHTLVGAGGAEGAMDAANLLKPALARGEL 309
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2026840261 221 QLVGATTLKEYRQ-IEKDAALERRFQPVIVDEPTQDEAFEILKGIQDKYEAYHGVTYSDEAIKACVQLSSRYIQDRHLPD 299
Cdd:COG0542 310 RCIGATTLDEYRKyIEKDAALERRFQPVLVEEPSVEDTISILRGLKERYEAHHGVRITDEALVAAVRLSDRYITDRFLPD 389
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2026840261 300 KAIDLMDEAGSKANLSIDAASE--DELTNRLAQIAAEKQAALNEER---YEKAAKLRDEEEAIEARLQNKT----NDKEH 370
Cdd:COG0542 390 KAIDLIDEAAARVRMEIDSKPEelDELERRLEQLEIEKEALKKEQDeasFERLAELRDELAELEEELEALKarweAEKEL 469
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2026840261 371 V-----------------------------------------VTAEDIQSIVEQKTGIPVGKLQADEQTKMKEIDVRLKA 409
Cdd:COG0542 470 IeeiqelkeeleqrygkipelekelaeleeelaelapllreeVTEEDIAEVVSRWTGIPVGKLLEGEREKLLNLEEELHE 549
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2026840261 410 RVIGQEHAVEKVAKAVKRSRAGLKSKHRPTGSFLFVGPTGVGKTELSKTLAEELFGSKEAIIRLDMSEYMEKHSVSKIIG 489
Cdd:COG0542 550 RVIGQDEAVEAVADAIRRSRAGLKDPNRPIGSFLFLGPTGVGKTELAKALAEFLFGDEDALIRIDMSEYMEKHSVSRLIG 629
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2026840261 490 SPPGYVGHDEAGQLTEKVRRKPYSIILLDEIEKAHPDVQHMFLQIMEDGRLTDSQGRTVSFKDTVIIMTSNAGStdKKAV 569
Cdd:COG0542 630 APPGYVGYEEGGQLTEAVRRRPYSVVLLDEIEKAHPDVFNILLQVLDDGRLTDGQGRTVDFRNTIIIMTSNIGS--ELIL 707
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2026840261 570 KVGFQSEQEEAIEEQsLIDSLSAYFKPEFLNRFDSIIQFDSLDKDDLVKIVDLLLKDLSEQLKEQNLTVHVTNEAKEKIA 649
Cdd:COG0542 708 DLAEDEPDYEEMKEA-VMEELKKHFRPEFLNRIDEIIVFHPLSKEELRKIVDLQLKRLRKRLAERGITLELTDAAKDFLA 786
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|
gi 2026840261 650 ELGYHPAFGARPLRRTIQEHVEDQMTDMLLEEEQLTGFT--VDVEHDEIV 697
Cdd:COG0542 787 EKGYDPEYGARPLKRAIQRELEDPLAEEILAGEIKEGDTitVDVDDGELV 836
|
|
| chaperone_ClpB |
TIGR03346 |
ATP-dependent chaperone ClpB; Members of this protein family are the bacterial ATP-dependent ... |
62-697 |
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: 818.04 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2026840261 62 ATSQERPKQKGLLDELGRNLTDGAHAGLIDPVIGRDEEVTRVIEILNRRNKNNPVLIGEPGVGKTAIAEGLALKIANGDV 141
Cdd:TIGR03346 144 VTDANAEDQYEALEKYARDLTERAREGKLDPVIGRDEEIRRTIQVLSRRTKNNPVLIGEPGVGKTAIVEGLAQRIVNGDV 223
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2026840261 142 PNKLKNKQVYLLDVSSLVANTGVRGQFEERMKQLIKEL-QSRKNIILFVDEIHLLVGAGSAEGSMDAGNILKPALARGEL 220
Cdd:TIGR03346 224 PEGLKNKRLLALDMGALIAGAKYRGEFEERLKAVLNEVtKSEGQIILFIDELHTLVGAGKAEGAMDAGNMLKPALARGEL 303
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2026840261 221 QLVGATTLKEYRQ-IEKDAALERRFQPVIVDEPTQDEAFEILKGIQDKYEAYHGVTYSDEAIKACVQLSSRYIQDRHLPD 299
Cdd:TIGR03346 304 HCIGATTLDEYRKyIEKDAALERRFQPVFVDEPSVEDTISILRGLKERYEVHHGVRITDPAIVAAATLSHRYITDRFLPD 383
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2026840261 300 KAIDLMDEAGSKANLSIDAASE--DELTNRLAQIAAEKQA---------------------ALNEERYE----------- 345
Cdd:TIGR03346 384 KAIDLIDEAAARIRMEIDSKPEelDELDRRIIQLEIEREAlkkekdeaskkrledlekelaDLEEEYAEleeqwkaekas 463
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2026840261 346 --KAAKLRDEEE---------------------------AIEARLQNKTNDKEH--------VVTAEDIQSIVEQKTGIP 388
Cdd:TIGR03346 464 iqGIQQIKEEIEqvrleleqaeregdlakaaelqygklpELEKQLQAAEQKLGEeqnrllreEVTAEEIAEVVSRWTGIP 543
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2026840261 389 VGKLQADEQTKMKEIDVRLKARVIGQEHAVEKVAKAVKRSRAGLKSKHRPTGSFLFVGPTGVGKTELSKTLAEELFGSKE 468
Cdd:TIGR03346 544 VSKMLEGEREKLLHMEEELHERVVGQDEAVEAVSDAIRRSRAGLSDPNRPIGSFLFLGPTGVGKTELAKALAEFLFDSED 623
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2026840261 469 AIIRLDMSEYMEKHSVSKIIGSPPGYVGHDEAGQLTEKVRRKPYSIILLDEIEKAHPDVQHMFLQIMEDGRLTDSQGRTV 548
Cdd:TIGR03346 624 AMVRIDMSEYMEKHSVARLIGAPPGYVGYEEGGQLTEAVRRRPYSVVLFDEVEKAHPDVFNVLLQVLDDGRLTDGQGRTV 703
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2026840261 549 SFKDTVIIMTSNAGSTdkkAVKVGFQSEQEEAIEEQSLiDSLSAYFKPEFLNRFDSIIQFDSLDKDDLVKIVDLLLKDLS 628
Cdd:TIGR03346 704 DFRNTVIIMTSNLGSD---FIQELAGGDDYEEMREAVM-EVLRAHFRPEFLNRIDEIVVFHPLGREQIARIVEIQLGRLR 779
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2026840261 629 EQLKEQNLTVHVTNEAKEKIAELGYHPAFGARPLRRTIQEHVEDQMTDMLLEEEQLTG--FTVDVEHDEIV 697
Cdd:TIGR03346 780 KRLAERKITLELSDAALDFLAEAGYDPVYGARPLKRAIQREIENPLAKKILAGEVAPGdtIRVDVEGGRLV 850
|
|
| clpC |
CHL00095 |
Clp protease ATP binding subunit |
74-681 |
0e+00 |
|
Clp protease ATP binding subunit
Pssm-ID: 214361 [Multi-domain] Cd Length: 821 Bit Score: 806.59 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2026840261 74 LDELGRNLTDGAHAGLIDPVIGRDEEVTRVIEILNRRNKNNPVLIGEPGVGKTAIAEGLALKIANGDVPNKLKNKQVYLL 153
Cdd:CHL00095 162 LEEFGTNLTKEAIDGNLDPVIGREKEIERVIQILGRRTKNNPILIGEPGVGKTAIAEGLAQRIVNRDVPDILEDKLVITL 241
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2026840261 154 DVSSLVANTGVRGQFEERMKQLIKELQSRKNIILFVDEIHLLVGAGSAEGSMDAGNILKPALARGELQLVGATTLKEYRQ 233
Cdd:CHL00095 242 DIGLLLAGTKYRGEFEERLKRIFDEIQENNNIILVIDEVHTLIGAGAAEGAIDAANILKPALARGELQCIGATTLDEYRK 321
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2026840261 234 -IEKDAALERRFQPVIVDEPTQDEAFEILKGIQDKYEAYHGVTYSDEAIKACVQLSSRYIQDRHLPDKAIDLMDEAGSKA 312
Cdd:CHL00095 322 hIEKDPALERRFQPVYVGEPSVEETIEILFGLRSRYEKHHNLSISDKALEAAAKLSDQYIADRFLPDKAIDLLDEAGSRV 401
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2026840261 313 NL--SIDAASEDELTNRLAQIAAEKQAALNEERYEKAAKLRDEEEAIEARL----QNKTNDKEH-----VVTAEDIQSIV 381
Cdd:CHL00095 402 RLinSRLPPAARELDKELREILKDKDEAIREQDFETAKQLRDREMEVRAQIaaiiQSKKTEEEKrlevpVVTEEDIAEIV 481
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2026840261 382 EQKTGIPVGKLQADEQTKMKEIDVRLKARVIGQEHAVEKVAKAVKRSRAGLKSKHRPTGSFLFVGPTGVGKTELSKTLAE 461
Cdd:CHL00095 482 SAWTGIPVNKLTKSESEKLLHMEETLHKRIIGQDEAVVAVSKAIRRARVGLKNPNRPIASFLFSGPTGVGKTELTKALAS 561
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2026840261 462 ELFGSKEAIIRLDMSEYMEKHSVSKIIGSPPGYVGHDEAGQLTEKVRRKPYSIILLDEIEKAHPDVQHMFLQIMEDGRLT 541
Cdd:CHL00095 562 YFFGSEDAMIRLDMSEYMEKHTVSKLIGSPPGYVGYNEGGQLTEAVRKKPYTVVLFDEIEKAHPDIFNLLLQILDDGRLT 641
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2026840261 542 DSQGRTVSFKDTVIIMTSNAGS--TDKKAVKVGFQSEQEEAIEEQ-----SLIDS-LSAYFKPEFLNRFDSIIQFDSLDK 613
Cdd:CHL00095 642 DSKGRTIDFKNTLIIMTSNLGSkvIETNSGGLGFELSENQLSEKQykrlsNLVNEeLKQFFRPEFLNRLDEIIVFRQLTK 721
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2026840261 614 DDLVKIVDLLLKDLSEQLKEQNLTVHVTNEAKEKIAELGYHPAFGARPLRRTIQEHVEDQMTDMLLEE 681
Cdd:CHL00095 722 NDVWEIAEIMLKNLFKRLNEQGIQLEVTERIKTLLIEEGYNPLYGARPLRRAIMRLLEDPLAEEVLSF 789
|
|
| ClpA |
TIGR02639 |
ATP-dependent Clp protease ATP-binding subunit clpA; [Protein fate, Degradation of proteins, ... |
56-679 |
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: 694.85 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2026840261 56 SEQAGHATSQERPKQKGLLDELGRNLTDGAHAGLIDPVIGRDEEVTRVIEILNRRNKNNPVLIGEPGVGKTAIAEGLALK 135
Cdd:TIGR02639 146 KDQLGEEAGKEEEKGQDALEKYTVDLTEKAKNGKIDPLIGREDELERTIQVLCRRKKNNPLLVGEPGVGKTAIVEGLALR 225
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2026840261 136 IANGDVPNKLKNKQVYLLDVSSLVANTGVRGQFEERMKQLIKELQSRKNIILFVDEIHLLVGAGS-AEGSMDAGNILKPA 214
Cdd:TIGR02639 226 IAEGKVPERLKNAKIYSLDMGTLLAGTKYRGDFEERLKAVVSEIEKEPNAILFIDEIHTIVGAGAtSGGSMDASNLLKPA 305
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2026840261 215 LARGELQLVGATTLKEYRQI-EKDAALERRFQPVIVDEPTQDEAFEILKGIQDKYEAYHGVTYSDEAIKACVQLSSRYIQ 293
Cdd:TIGR02639 306 LSSGKIRCIGSTTYEEYKNHfEKDRALSRRFQKIDVGEPSIEETVKILKGLKEQYEEFHHVKYSDEALEAAVELSARYIN 385
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2026840261 294 DRHLPDKAIDLMDEAGSkanlsidaasedeltnrlaqiaaekqaalneeryekAAKLRDEEEaiearlqnktndKEHVVT 373
Cdd:TIGR02639 386 DRFLPDKAIDVIDEAGA------------------------------------AFRLRPKAK------------KKANVN 417
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2026840261 374 AEDIQSIVEQKTGIPVGKLQADEQTKMKEIDVRLKARVIGQEHAVEKVAKAVKRSRAGLKSKHRPTGSFLFVGPTGVGKT 453
Cdd:TIGR02639 418 VKDIENVVAKMAKIPVKTVSSDDREQLKNLEKNLKAKIFGQDEAIDQLVSAIKRSRAGLGDPNKPVGSFLFVGPTGVGKT 497
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2026840261 454 ELSKTLAEELfgsKEAIIRLDMSEYMEKHSVSKIIGSPPGYVGHDEAGQLTEKVRRKPYSIILLDEIEKAHPDVQHMFLQ 533
Cdd:TIGR02639 498 ELAKQLAEEL---GVHLLRFDMSEYMEKHTVSRLIGSPPGYVGFEQGGLLTDAVRKHPHCVLLLDEIEKAHPDIYNILLQ 574
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2026840261 534 IMEDGRLTDSQGRTVSFKDTVIIMTSNAGSTDKKAVKVGFQSEQEEAIEEqsliDSLSAYFKPEFLNRFDSIIQFDSLDK 613
Cdd:TIGR02639 575 VMDYATLTDNNGRKADFRNVILIMTSNAGASEMSKPPIGFGGENRESKSL----KAIKKLFSPEFRNRLDAIIHFNDLSE 650
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2026840261 614 DDLVKIVDLLLKDLSEQLKEQNLTVHVTNEAKEKIAELGYHPAFGARPLRRTIQEHVEDQMTDMLL 679
Cdd:TIGR02639 651 EMAEKIVKKFLDELQDQLNEKNIELELTDDAKKYLAEKGYDEEFGARPLARVIQEEIKKPLSDEIL 716
|
|
| PRK10865 |
PRK10865 |
ATP-dependent chaperone ClpB; |
70-700 |
0e+00 |
|
ATP-dependent chaperone ClpB;
Pssm-ID: 182791 [Multi-domain] Cd Length: 857 Bit Score: 633.04 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2026840261 70 QKGLLDELGRNLTDGAHAGLIDPVIGRDEEVTRVIEILNRRNKNNPVLIGEPGVGKTAIAEGLALKIANGDVPNKLKNKQ 149
Cdd:PRK10865 157 QRQALKKYTIDLTERAEQGKLDPVIGRDEEIRRTIQVLQRRTKNNPVLIGEPGVGKTAIVEGLAQRIINGEVPEGLKGRR 236
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2026840261 150 VYLLDVSSLVANTGVRGQFEERMKQLIKELQSRK-NIILFVDEIHLLVGAGSAEGSMDAGNILKPALARGELQLVGATTL 228
Cdd:PRK10865 237 VLALDMGALVAGAKYRGEFEERLKGVLNDLAKQEgNVILFIDELHTMVGAGKADGAMDAGNMLKPALARGELHCVGATTL 316
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2026840261 229 KEYRQ-IEKDAALERRFQPVIVDEPTQDEAFEILKGIQDKYEAYHGVTYSDEAIKACVQLSSRYIQDRHLPDKAIDLMDE 307
Cdd:PRK10865 317 DEYRQyIEKDAALERRFQKVFVAEPSVEDTIAILRGLKERYELHHHVQITDPAIVAAATLSHRYIADRQLPDKAIDLIDE 396
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2026840261 308 AGSKANLSIDAASE--DELTNRLAQIAAEKQA--------------ALNEERYEKA---AKLRDEEEAIEARLQNKTNDK 368
Cdd:PRK10865 397 AASSIRMQIDSKPEelDRLDRRIIQLKLEQQAlmkesdeaskkrldMLNEELSDKErqySELEEEWKAEKASLSGTQTIK 476
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2026840261 369 EHV---------------------------------------------------VTAEDIQSIVEQKTGIPVGKLQADEQ 397
Cdd:PRK10865 477 AELeqakiaieqarrvgdlarmselqygkipelekqlaaatqlegktmrllrnkVTDAEIAEVLARWTGIPVSRMLESER 556
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2026840261 398 TKMKEIDVRLKARVIGQEHAVEKVAKAVKRSRAGLKSKHRPTGSFLFVGPTGVGKTELSKTLAEELFGSKEAIIRLDMSE 477
Cdd:PRK10865 557 EKLLRMEQELHHRVIGQNEAVEAVSNAIRRSRAGLSDPNRPIGSFLFLGPTGVGKTELCKALANFMFDSDDAMVRIDMSE 636
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2026840261 478 YMEKHSVSKIIGSPPGYVGHDEAGQLTEKVRRKPYSIILLDEIEKAHPDVQHMFLQIMEDGRLTDSQGRTVSFKDTVIIM 557
Cdd:PRK10865 637 FMEKHSVSRLVGAPPGYVGYEEGGYLTEAVRRRPYSVILLDEVEKAHPDVFNILLQVLDDGRLTDGQGRTVDFRNTVVIM 716
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2026840261 558 TSNAGStDKKAVKVGFQSEQEeaiEEQSLIDSLSAYFKPEFLNRFDSIIQFDSLDKDDLVKIVDLLLKDLSEQLKEQNLT 637
Cdd:PRK10865 717 TSNLGS-DLIQERFGELDYAH---MKELVLGVVSHNFRPEFINRIDEVVVFHPLGEQHIASIAQIQLQRLYKRLEERGYE 792
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2026840261 638 VHVTNEAKEKIAELGYHPAFGARPLRRTIQEHVEDQMTDMLLEEEQLTG--FTVDVEHDEIVVKK 700
Cdd:PRK10865 793 IHISDEALKLLSENGYDPVYGARPLKRAIQQQIENPLAQQILSGELVPGkvIRLEVNDDRIVAVQ 857
|
|
| VI_ClpV1 |
TIGR03345 |
type VI secretion ATPase, ClpV1 family; Members of this protein family are homologs of ClpB, ... |
59-680 |
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: 629.67 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2026840261 59 AGHATSQERPKQKGLLDELGRNLTDGAHAGLIDPVIGRDEEVTRVIEILNRRNKNNPVLIGEPGVGKTAIAEGLALKIAN 138
Cdd:TIGR03345 155 AAPAGAAAGAAGTSALDQYTTDLTAQAREGKIDPVLGRDDEIRQMIDILLRRRQNNPILTGEAGVGKTAVVEGLALRIAA 234
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2026840261 139 GDVPNKLKNKQVYLLDVSSLVANTGVRGQFEERMKQLIKELQ-SRKNIILFVDEIHLLVGAGSAEGSMDAGNILKPALAR 217
Cdd:TIGR03345 235 GDVPPALRNVRLLSLDLGLLQAGASVKGEFENRLKSVIDEVKaSPQPIILFIDEAHTLIGAGGQAGQGDAANLLKPALAR 314
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2026840261 218 GELQLVGATTLKEYRQ-IEKDAALERRFQPVIVDEPTQDEAFEILKGIQDKYEAYHGVTYSDEAIKACVQLSSRYIQDRH 296
Cdd:TIGR03345 315 GELRTIAATTWAEYKKyFEKDPALTRRFQVVKVEEPDEETAIRMLRGLAPVLEKHHGVLILDEAVVAAVELSHRYIPGRQ 394
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2026840261 297 LPDKAIDLMDEAGSKANLSIDA--ASEDELTNRLAQIAAE-----KQAALNEERYEKAAKLRDEEEAIEARLQNKT---- 365
Cdd:TIGR03345 395 LPDKAVSLLDTACARVALSQNAtpAALEDLRRRIAALELEldaleREAALGADHDERLAELRAELAALEAELAALEarwq 474
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2026840261 366 -----------------------NDKEH-------------------------VVTAEDIQSIVEQKTGIPVGKLQADEQ 397
Cdd:TIGR03345 475 qekelveailalraeleadadapADDDDalraqlaeleaalasaqgeeplvfpEVDAQAVAEVVADWTGIPVGRMVRDEI 554
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2026840261 398 TKMKEIDVRLKARVIGQEHAVEKVAKAVKRSRAGLKSKHRPTGSFLFVGPTGVGKTELSKTLAEELFGSKEAIIRLDMSE 477
Cdd:TIGR03345 555 EAVLSLPDRLAERVIGQDHALEAIAERIRTARAGLEDPRKPLGVFLLVGPSGVGKTETALALAELLYGGEQNLITINMSE 634
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2026840261 478 YMEKHSVSKIIGSPPGYVGHDEAGQLTEKVRRKPYSIILLDEIEKAHPDVQHMFLQIMEDGRLTDSQGRTVSFKDTVIIM 557
Cdd:TIGR03345 635 FQEAHTVSRLKGSPPGYVGYGEGGVLTEAVRRKPYSVVLLDEVEKAHPDVLELFYQVFDKGVMEDGEGREIDFKNTVILL 714
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2026840261 558 TSNAGStdkKAVKVGFQSEQE----EAIEEqSLIDSLSAYFKPEFLNRFdSIIQFDSLDKDDLVKIVDLLLKDLSEQLKE 633
Cdd:TIGR03345 715 TSNAGS---DLIMALCADPETapdpEALLE-ALRPELLKVFKPAFLGRM-TVIPYLPLDDDVLAAIVRLKLDRIARRLKE 789
|
650 660 670 680
....*....|....*....|....*....|....*....|....*...
gi 2026840261 634 Q-NLTVHVTNEAKEKIAELGYHPAFGARPLRRTIQEHVEDQMTDMLLE 680
Cdd:TIGR03345 790 NhGAELVYSEALVEHIVARCTEVESGARNIDAILNQTLLPELSRQILE 837
|
|
| clpA |
PRK11034 |
ATP-dependent Clp protease ATP-binding subunit; Provisional |
50-695 |
0e+00 |
|
ATP-dependent Clp protease ATP-binding subunit; Provisional
Pssm-ID: 236828 [Multi-domain] Cd Length: 758 Bit Score: 545.59 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2026840261 50 GGGSFFSEQAGhatSQERpkqkglLDELGRNLTDGAHAGLIDPVIGRDEEVTRVIEILNRRNKNNPVLIGEPGVGKTAIA 129
Cdd:PRK11034 154 GSQPNSEEQAG---GEER------MENFTTNLNQLARVGGIDPLIGREKELERAIQVLCRRRKNNPLLVGESGVGKTAIA 224
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2026840261 130 EGLALKIANGDVPNKLKNKQVYLLDVSSLVANTGVRGQFEERMKQLIKELQSRKNIILFVDEIHLLVGAGSAEG-SMDAG 208
Cdd:PRK11034 225 EGLAWRIVQGDVPEVMADCTIYSLDIGSLLAGTKYRGDFEKRFKALLKQLEQDTNSILFIDEIHTIIGAGAASGgQVDAA 304
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2026840261 209 NILKPALARGELQLVGATTLKEYRQI-EKDAALERRFQPVIVDEPTQDEAFEILKGIQDKYEAYHGVTYSDEAIKACVQL 287
Cdd:PRK11034 305 NLIKPLLSSGKIRVIGSTTYQEFSNIfEKDRALARRFQKIDITEPSIEETVQIINGLKPKYEAHHDVRYTAKAVRAAVEL 384
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2026840261 288 SSRYIQDRHLPDKAIDLMDEAGSKAnlsidaasedeltnRLAQIAAEKqaalneeryekaaklrdeeeaiearlqnKTnd 367
Cdd:PRK11034 385 AVKYINDRHLPDKAIDVIDEAGARA--------------RLMPVSKRK----------------------------KT-- 420
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2026840261 368 kehvVTAEDIQSIVEQKTGIPVGKLQADEQTKMKEIDVRLKARVIGQEHAVEKVAKAVKRSRAGLKSKHRPTGSFLFVGP 447
Cdd:PRK11034 421 ----VNVADIESVVARIARIPEKSVSQSDRDTLKNLGDRLKMLVFGQDKAIEALTEAIKMSRAGLGHEHKPVGSFLFAGP 496
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2026840261 448 TGVGKTE----LSKTLAEELfgskeaiIRLDMSEYMEKHSVSKIIGSPPGYVGHDEAGQLTEKVRRKPYSIILLDEIEKA 523
Cdd:PRK11034 497 TGVGKTEvtvqLSKALGIEL-------LRFDMSEYMERHTVSRLIGAPPGYVGFDQGGLLTDAVIKHPHAVLLLDEIEKA 569
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2026840261 524 HPDVQHMFLQIMEDGRLTDSQGRTVSFKDTVIIMTSNAG--STDKKAVKVGFQSEQEEAIEEqslidsLSAYFKPEFLNR 601
Cdd:PRK11034 570 HPDVFNLLLQVMDNGTLTDNNGRKADFRNVVLVMTTNAGvrETERKSIGLIHQDNSTDAMEE------IKKIFTPEFRNR 643
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2026840261 602 FDSIIQFDSLDKDDLVKIVDLLLKDLSEQLKEQNLTVHVTNEAKEKIAELGYHPAFGARPLRRTIQEHVEDQMTDMLLEE 681
Cdd:PRK11034 644 LDNIIWFDHLSTDVIHQVVDKFIVELQAQLDQKGVSLEVSQEARDWLAEKGYDRAMGARPMARVIQDNLKKPLANELLFG 723
|
650
....*....|....
gi 2026840261 682 EQLTGFTVDVEHDE 695
Cdd:PRK11034 724 SLVDGGQVTVALDK 737
|
|
| RecA-like_ClpB_Hsp104-like |
cd19499 |
Chaperone protein ClpB/Hsp104 subfamily; Bacterial Caseinolytic peptidase B (ClpB) and ... |
399-608 |
5.92e-97 |
|
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: 296.40 E-value: 5.92e-97
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2026840261 399 KMKEIDVRLKARVIGQEHAVEKVAKAVKRSRAGLKSKHRPTGSFLFVGPTGVGKTELSKTLAEELFGSKEAIIRLDMSEY 478
Cdd:cd19499 1 KLLNLEERLHERVVGQDEAVKAVSDAIRRARAGLSDPNRPIGSFLFLGPTGVGKTELAKALAELLFGDEDNLIRIDMSEY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2026840261 479 MEKHSVSKIIGSPPGYVGHDEAGQLTEKVRRKPYSIILLDEIEKAHPDVQHMFLQIMEDGRLTDSQGRTVSFKDTVIIMT 558
Cdd:cd19499 81 MEKHSVSRLIGAPPGYVGYTEGGQLTEAVRRKPYSVVLLDEIEKAHPDVQNLLLQVLDDGRLTDSHGRTVDFKNTIIIMT 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 2026840261 559 SNagstdkkavkvgfqseqeeaieeqslidslsaYFKPEFLNRFDSIIQF 608
Cdd:cd19499 161 SN--------------------------------HFRPEFLNRIDEIVVF 178
|
|
| AAA_2 |
pfam07724 |
AAA domain (Cdc48 subfamily); This Pfam entry includes some of the AAA proteins not detected ... |
437-605 |
3.32e-87 |
|
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: 270.61 E-value: 3.32e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2026840261 437 RPTGSFLFVGPTGVGKTELSKTLAEELFGSKEAIIRLDMSEYMEKHSVSKIIGSPPGYVGHDEAGQLTEKVRRKPYSIIL 516
Cdd:pfam07724 1 RPIGSFLFLGPTGVGKTELAKALAELLFGDERALIRIDMSEYMEEHSVSRLIGAPPGYVGYEEGGQLTEAVRRKPYSIVL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2026840261 517 LDEIEKAHPDVQHMFLQIMEDGRLTDSQGRTVSFKDTVIIMTSNAGSTDKKAVKVGFQSEQEEAIEEQsLIDSLSAYFKP 596
Cdd:pfam07724 81 IDEIEKAHPGVQNDLLQILEGGTLTDKQGRTVDFKNTLFIMTGNFGSEKISDASRLGDSPDYELLKEE-VMDLLKKGFIP 159
|
....*....
gi 2026840261 597 EFLNRFDSI 605
Cdd:pfam07724 160 EFLGRLPII 168
|
|
| AAA_lid_9 |
pfam17871 |
AAA lid domain; This entry represents the alpha helical AAA+ lid domain that is found to the ... |
253-354 |
1.06e-40 |
|
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: 144.17 E-value: 1.06e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2026840261 253 TQDEAFEILKGIQDKYEAYHGVTYSDEAIKACVQLSSRYIQDRHLPDKAIDLMDEAGSKANLSIDAASE--DELTNRLAQ 330
Cdd:pfam17871 1 SVEEAIEILRGLKPKYEKHHGVRISDEALEAAVKLSKRYITDRFLPDKAIDLLDEACARVRLSQESKPEelEDLERELAK 80
|
90 100
....*....|....*....|....
gi 2026840261 331 IAAEKQAALNEERYEKAAKLRDEE 354
Cdd:pfam17871 81 LEIEKEALEREQDFEKAERLAKLE 104
|
|
| ClpB_D2-small |
pfam10431 |
C-terminal, D2-small domain, of ClpB protein; This is the C-terminal domain of ClpB protein, ... |
611-691 |
7.18e-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: 104.02 E-value: 7.18e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2026840261 611 LDKDDLVKIVDLLLKDLSEQLKEQNLTVHVTNEAKEKIAELGYHPAFGARPLRRTIQEHVEDQMTDMLLEEEQLTGFTVD 690
Cdd:pfam10431 1 LSKEELRKIVDLQLKELQKRLAERGITLELTDAAKDWLAEKGYDPEYGARPLRRAIQREIEDPLAEEILSGELKEGDTVR 80
|
.
gi 2026840261 691 V 691
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, ... |
611-698 |
9.08e-27 |
|
C-terminal, D2-small domain, of ClpB protein; This is the C-terminal domain of ClpB protein, referred to as the D2-small domain, and is a mixed alpha-beta structure. Compared with the D1-small domain (included in AAA) it lacks the long coiled-coil insertion, and instead of helix C4 contains a beta-strand (e3) that is part of a three stranded beta-pleated sheet. In Thermophilus the whole protein forms a hexamer with the D1-small and D2-small domains located on the outside of the hexamer, with the long coiled-coil being exposed on the surface. The D2-small domain is essential for oligomerisation, forming a tight interface with the D2-large domain of a neighbouring subunit and thereby providing enough binding energy to stabilise the functional assembly. The domain is associated with two Clp_N at the N-terminus as well as AAA and AAA_2.
Pssm-ID: 198154 [Multi-domain] Cd Length: 90 Bit Score: 104.06 E-value: 9.08e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2026840261 611 LDKDDLVKIVDLLLKDLSEQLKEQNLTVHVTNEAKEKIAELGYHPAFGARPLRRTIQEHVEDQMTDMLLEEEQLTG--FT 688
Cdd:smart01086 1 LDKEDLVRIVDLPLNALQKRLAEKGITLEFTDEALDWLAEKGYDPKYGARPLRRIIQRELEDPLAELILSGELKDGdtVV 80
|
90
....*....|
gi 2026840261 689 VDVEHDEIVV 698
Cdd:smart01086 81 VDVDDGELVF 90
|
|
| AAA |
cd00009 |
The AAA+ (ATPases Associated with a wide variety of cellular Activities) superfamily ... |
412-560 |
1.30e-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: 91.82 E-value: 1.30e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2026840261 412 IGQEHAVEKVAKAVKRsraglkskhRPTGSFLFVGPTGVGKTELSKTLAEELFGSKEAIIRLDMSEYMEKHSVSkiigsp 491
Cdd:cd00009 1 VGQEEAIEALREALEL---------PPPKNLLLYGPPGTGKTTLARAIANELFRPGAPFLYLNASDLLEGLVVA------ 65
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2026840261 492 pGYVGHDEAGQLTEKVRRKPYSIILLDEIEKAHPDVQHMFLQIMEDGRLTdsqgrTVSFKDTVIIMTSN 560
Cdd:cd00009 66 -ELFGHFLVRLLFELAEKAKPGVLFIDEIDSLSRGAQNALLRVLETLNDL-----RIDRENVRVIGATN 128
|
|
| AAA |
cd00009 |
The AAA+ (ATPases Associated with a wide variety of cellular Activities) superfamily ... |
94-252 |
3.85e-18 |
|
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: 81.81 E-value: 3.85e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2026840261 94 IGRDEEVTRVIEILNRRNKNNPVLIGEPGVGKTAIAEGLALKIANGDVPnklknkqVYLLDVSSLVANTGVRGQFEERM- 172
Cdd:cd00009 1 VGQEEAIEALREALELPPPKNLLLYGPPGTGKTTLARAIANELFRPGAP-------FLYLNASDLLEGLVVAELFGHFLv 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2026840261 173 KQLIKELQSRKNIILFVDEIHLLvGAGSAEGSMDAGNILKPALA-RGELQLVGATTLKEYRQIekDAALERRFQPVIVDE 251
Cdd:cd00009 74 RLLFELAEKAKPGVLFIDEIDSL-SRGAQNALLRVLETLNDLRIdRENVRVIGATNRPLLGDL--DRALYDRLDIRIVIP 150
|
.
gi 2026840261 252 P 252
Cdd:cd00009 151 L 151
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
443-564 |
2.60e-14 |
|
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: 70.87 E-value: 2.60e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2026840261 443 LFVGPTGVGKTELSKTLAEELFGSKEAIIRLDMSEYMEKHSVSK----IIGSPPGYVGHDEAGQLTEKVRRKPYSIILLD 518
Cdd:smart00382 6 LIVGPPGSGKTTLARALARELGPPGGGVIYIDGEDILEEVLDQLlliiVGGKKASGSGELRLRLALALARKLKPDVLILD 85
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 2026840261 519 EIEKAHPDVQHMFLQIMEDGRLTDsqgRTVSFKDTVIIMTSNAGST 564
Cdd:smart00382 86 EITSLLDAEQEALLLLLEELRLLL---LLKSEKNLTVILTTNDEKD 128
|
|
| SpoVK |
COG0464 |
AAA+-type ATPase, SpoVK/Ycf46/Vps4 family [Cell wall/membrane/envelope biogenesis, Cell cycle ... |
247-626 |
3.74e-12 |
|
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: 68.78 E-value: 3.74e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2026840261 247 VIVDEPTQDEAFEILKGIQDKYEAYHGVTYSDEAIKACVQLSSRYIQDRHLPDKAIDLMDEAGSKANLSIDAASEDELTN 326
Cdd:COG0464 1 LAELLALAVALALALLLLDDAALRLLLLLLLALAAALLLLLLLLLLLLLALLLVELLLLLLSGALAALLLLALLLLALLA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2026840261 327 RLAQIAAEKQAALNEERYEKAAKLRDEEEAIEARLQNKTNDKEHVVTAEDIQSIVEQKTGIPVGKLQADEQTKMkeidvr 406
Cdd:COG0464 81 LLAALLSALELLLLGELLLLLLLLLLLLLLLLDLERALLELLRESAEALALAAPLVTYEDIGGLEEELLELREA------ 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2026840261 407 LKARVIGQEHAVEKVAKAV----KRSRAGLKSKHRPTGSFLFVGPTGVGKTELSKTLAEELFGSkeaIIRLDMSEymekh 482
Cdd:COG0464 155 ILDDLGGLEEVKEELRELValplKRPELREEYGLPPPRGLLLYGPPGTGKTLLARALAGELGLP---LIEVDLSD----- 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2026840261 483 svskIIGsppGYVGHDEAG--QLTEKVRRKPYSIILLDEIEKAHPD-----------VQHMFLQIMEDGRltdsqgrtvs 549
Cdd:COG0464 227 ----LVS---KYVGETEKNlrEVFDKARGLAPCVLFIDEADALAGKrgevgdgvgrrVVNTLLTEMEELR---------- 289
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2026840261 550 fKDTVIIMTSNagstdkkavkvgfqseqeeaieeqsLIDSLSayfkPEFLNRFDSIIQFDSLDKDDLVKIVDLLLKD 626
Cdd:COG0464 290 -SDVVVIAATN-------------------------RPDLLD----PALLRRFDEIIFFPLPDAEERLEIFRIHLRK 336
|
|
| AAA_5 |
pfam07728 |
AAA domain (dynein-related subfamily); This Pfam entry includes some of the AAA proteins not ... |
441-560 |
6.92e-12 |
|
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: 63.47 E-value: 6.92e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2026840261 441 SFLFVGPTGVGKTELSKTLAEELFGSKEAIIRldMSEYMEKhsvSKIIGS----PPGYVGHDeaGQLTEKVRRKpySIIL 516
Cdd:pfam07728 1 GVLLVGPPGTGKTELAERLAAALSNRPVFYVQ--LTRDTTE---EDLFGRrnidPGGASWVD--GPLVRAAREG--EIAV 71
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 2026840261 517 LDEIEKAHPDVQHMFLQIMEDGRLTDSQGRT---VSFKDTVIIMTSN 560
Cdd:pfam07728 72 LDEINRANPDVLNSLLSLLDERRLLLPDGGElvkAAPDGFRLIATMN 118
|
|
| AAA |
pfam00004 |
ATPase family associated with various cellular activities (AAA); AAA family proteins often ... |
117-248 |
2.18e-11 |
|
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: 61.84 E-value: 2.18e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2026840261 117 LIGEPGVGKTAIAEGLAlkiangdvpNKLkNKQVYLLDVSSLVANTgvRGQFEERMKQLIKELQSRKNIILFVDEIHLLV 196
Cdd:pfam00004 3 LYGPPGTGKTTLAKAVA---------KEL-GAPFIEISGSELVSKY--VGESEKRLRELFEAAKKLAPCVIFIDEIDALA 70
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2026840261 197 GAGSAEGSMDAG---NILKPAL-----ARGELQLVGATTlkEYRQIekDAALERRFQPVI 248
Cdd:pfam00004 71 GSRGSGGDSESRrvvNQLLTELdgftsSNSKVIVIAATN--RPDKL--DPALLGRFDRII 126
|
|
| RPT1 |
COG1222 |
ATP-dependent 26S proteasome regulatory subunit [Posttranslational modification, protein ... |
329-627 |
3.44e-10 |
|
ATP-dependent 26S proteasome regulatory subunit [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440835 [Multi-domain] Cd Length: 326 Bit Score: 61.95 E-value: 3.44e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2026840261 329 AQIAAEKQAALNEERYEKAAKLRDEEEAIEARLQNKTNDKEHVVTAEDIQSIVEQKTGIPVGKLQADEQTkmkeiDVRLK 408
Cdd:COG1222 4 LLTIDENIKALLALIDALQERLGVELALLLQPVKALELLEEAPALLLNDANLTQKRLGTPRGTAVPAESP-----DVTFD 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2026840261 409 ArVIGQEHAVEKVAKAV--KRSRAGLKSKH--RPTGSFLFVGPTGVGKTELSKTLAEELfgsKEAIIRLDMSEymekhSV 484
Cdd:COG1222 79 D-IGGLDEQIEEIREAVelPLKNPELFRKYgiEPPKGVLLYGPPGTGKTLLAKAVAGEL---GAPFIRVRGSE-----LV 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2026840261 485 SKIIGsppgyvghdEAGQLTEKV----RRKPYSIILLDEIE---------KAHPDVQHM---FLQIMeDGrlTDSQGrtv 548
Cdd:COG1222 150 SKYIG---------EGARNVREVfelaREKAPSIIFIDEIDaiaarrtddGTSGEVQRTvnqLLAEL-DG--FESRG--- 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2026840261 549 sfkDTVIIMTSNAgstdkkavkvgfqseqeeaieeqslIDSL-SAYFKPeflNRFDSIIQFDSLDKDDLVKIVDLLLKDL 627
Cdd:COG1222 215 ---DVLIIAATNR-------------------------PDLLdPALLRP---GRFDRVIEVPLPDEEAREEILKIHLRDM 263
|
|
| SpoVK |
COG0464 |
AAA+-type ATPase, SpoVK/Ycf46/Vps4 family [Cell wall/membrane/envelope biogenesis, Cell cycle ... |
116-262 |
4.10e-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: 62.24 E-value: 4.10e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2026840261 116 VLIGEPGVGKTAIAEGLAlKIANGDVpnklknkqvYLLDVSSLVAntGVRGQFEERMKQLIKELQSRKNIILFVDEIHLL 195
Cdd:COG0464 195 LLYGPPGTGKTLLARALA-GELGLPL---------IEVDLSDLVS--KYVGETEKNLREVFDKARGLAPCVLFIDEADAL 262
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2026840261 196 VGAGSAEGSMDAG---NILKPALA--RGELQLVGATtlkeYRQIEKDAALERRFQPVI-VDEPTQDEAFEILK 262
Cdd:COG0464 263 AGKRGEVGDGVGRrvvNTLLTEMEelRSDVVVIAAT----NRPDLLDPALLRRFDEIIfFPLPDAEERLEIFR 331
|
|
| RecA-like_protease |
cd19481 |
proteases similar to RecA; RecA-like NTPases. This family includes the NTP binding domain of ... |
418-523 |
7.89e-10 |
|
proteases similar to RecA; RecA-like NTPases. This family includes the NTP binding domain of F1 and V1 H(+)ATPases, DnaB and related helicases as well as bacterial RecA and related eukaryotic and archaeal recombinases. This group also includes bacterial conjugation proteins and related DNA transfer proteins involved in type II and type IV secretion.
Pssm-ID: 410889 [Multi-domain] Cd Length: 158 Bit Score: 58.06 E-value: 7.89e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2026840261 418 VEKVAKAVKRSRAGLKSKHRPTGSFLFVGPTGVGKTELSKTLAEELfGSKEaiIRLDMSEYMEKHSvskiigsppgYVGH 497
Cdd:cd19481 5 LREAVEAPRRGSRLRRYGLGLPKGILLYGPPGTGKTLLAKALAGEL-GLPL--IVVKLSSLLSKYV----------GESE 71
|
90 100
....*....|....*....|....*.
gi 2026840261 498 DEAGQLTEKVRRKPYSIILLDEIEKA 523
Cdd:cd19481 72 KNLRKIFERARRLAPCILFIDEIDAI 97
|
|
| clpX |
PRK05342 |
ATP-dependent Clp protease ATP-binding subunit ClpX; |
401-680 |
8.34e-10 |
|
ATP-dependent Clp protease ATP-binding subunit ClpX;
Pssm-ID: 235422 [Multi-domain] Cd Length: 412 Bit Score: 61.33 E-value: 8.34e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2026840261 401 KEIDVRLKARVIGQEHAVEKVAKAV----KRSRAGL---------KSkhrptgSFLFVGPTGVGKTELSKTLAEEL---F 464
Cdd:PRK05342 63 KEIKAHLDQYVIGQERAKKVLSVAVynhyKRLRHGDkkdddvelqKS------NILLIGPTGSGKTLLAQTLARILdvpF 136
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2026840261 465 gskeAIIrlDMSEYMEKhsvskiigsppGYVGHD-EA--GQLTEK----VRRKPYSIILLDEIEK-----AHP----D-- 526
Cdd:PRK05342 137 ----AIA--DATTLTEA-----------GYVGEDvENilLKLLQAadydVEKAQRGIVYIDEIDKiarksENPsitrDvs 199
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2026840261 527 ---VQHMFLQIMEdgrltdsqGRTVSFK----------DTVIIMTSN----------------AGSTDKKAvkVGFQSEQ 577
Cdd:PRK05342 200 gegVQQALLKILE--------GTVASVPpqggrkhpqqEFIQVDTTNilficggafdglekiiKQRLGKKG--IGFGAEV 269
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2026840261 578 EEAIEEQSLIDSLSA-----YFK----PEFLNRFDSIIQFDSLDKDDLVKIV----DLLLKDLSEQLKEQNLTVHVTNEA 644
Cdd:PRK05342 270 KSKKEKRTEGELLKQvepedLIKfgliPEFIGRLPVVATLEELDEEALVRILtepkNALVKQYQKLFEMDGVELEFTDEA 349
|
330 340 350
....*....|....*....|....*....|....*.
gi 2026840261 645 KEKIAELGYHPAFGARPLrRTIQEHVedqMTDMLLE 680
Cdd:PRK05342 350 LEAIAKKAIERKTGARGL-RSILEEI---LLDVMFE 381
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
112-249 |
2.52e-09 |
|
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: 56.23 E-value: 2.52e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2026840261 112 KNNPVLIGEPGVGKTAIAEGLALKIANGDVPNKLKN-----KQVYLLDVSSLVANTGVRGQFEERMKQLIKELQSRKNII 186
Cdd:smart00382 2 GEVILIVGPPGSGKTTLARALARELGPPGGGVIYIDgedilEEVLDQLLLIIVGGKKASGSGELRLRLALALARKLKPDV 81
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2026840261 187 LFVDEIHLLVGAGSAEGSMDA--GNILKPALARGELQLVGATTLkeyRQIEKDAALERRFQPVIV 249
Cdd:smart00382 82 LILDEITSLLDAEQEALLLLLeeLRLLLLLKSEKNLTVILTTND---EKDLGPALLRRRFDRRIV 143
|
|
| COG1223 |
COG1223 |
Predicted ATPase, AAA+ superfamily [General function prediction only]; |
411-633 |
9.09e-09 |
|
Predicted ATPase, AAA+ superfamily [General function prediction only];
Pssm-ID: 440836 [Multi-domain] Cd Length: 246 Bit Score: 56.82 E-value: 9.09e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2026840261 411 VIGQEHAVEKVAKAVK-RSRAGLKSKHR--PTGSFLFVGPTGVGKTELSKTLAEELfGSKEAIIRLDmseymekhsvsKI 487
Cdd:COG1223 4 VVGQEEAKKKLKLIIKeLRRRENLRKFGlwPPRKILFYGPPGTGKTMLAEALAGEL-KLPLLTVRLD-----------SL 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2026840261 488 IGSppgYVGHDEA--GQLTEKVRRKPySIILLDEIE---------KAHPDVQ---HMFLQIMEDGRltdsqgrtvsfKDT 553
Cdd:COG1223 72 IGS---YLGETARnlRKLFDFARRAP-CVIFFDEFDaiakdrgdqNDVGEVKrvvNALLQELDGLP-----------SGS 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2026840261 554 VIIMTSNagstdkkavkvgfqseQEEaieeqsLIDslsayfkPEFLNRFDSIIQFDSLDKDDLVKIVDLLLKDLSEQLKE 633
Cdd:COG1223 137 VVIAATN----------------HPE------LLD-------SALWRRFDEVIEFPLPDKEERKEILELNLKKFPLPFEL 187
|
|
| AAA |
pfam00004 |
ATPase family associated with various cellular activities (AAA); AAA family proteins often ... |
443-609 |
8.02e-08 |
|
ATPase family associated with various cellular activities (AAA); AAA family proteins often perform chaperone-like functions that assist in the assembly, operation, or disassembly of protein complexes.
Pssm-ID: 459627 [Multi-domain] Cd Length: 130 Bit Score: 51.44 E-value: 8.02e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2026840261 443 LFVGPTGVGKTELSKTLAEELFGSkeaIIRLDMSEYMEKhsvskiigsppgYVGHDEAG--QLTEKVRRKPYSIILLDEI 520
Cdd:pfam00004 2 LLYGPPGTGKTTLAKAVAKELGAP---FIEISGSELVSK------------YVGESEKRlrELFEAAKKLAPCVIFIDEI 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2026840261 521 EKAHP-----------DVQHMFLQIMEdgrltdsqGRTVSFKDTVIIMTSNagstdkkavkvgfqseqeeaieeqsLIDS 589
Cdd:pfam00004 67 DALAGsrgsggdsesrRVVNQLLTELD--------GFTSSNSKVIVIAATN-------------------------RPDK 113
|
170 180
....*....|....*....|
gi 2026840261 590 LSayfkPEFLNRFDSIIQFD 609
Cdd:pfam00004 114 LD----PALLGRFDRIIEFP 129
|
|
| MoxR |
COG0714 |
MoxR-like ATPase [General function prediction only]; MoxR-like ATPase is part of the Pathway ... |
400-560 |
1.59e-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: 53.63 E-value: 1.59e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2026840261 400 MKEIDVR--LKARVIGQEHAVEKVAKAVkrsRAGlksKHrptgsFLFVGPTGVGKTELSKTLAEELFGSkeaIIRL---- 473
Cdd:COG0714 1 MTEARLRaeIGKVYVGQEELIELVLIAL---LAG---GH-----LLLEGVPGVGKTTLAKALARALGLP---FIRIqftp 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2026840261 474 DMseyMEkhsvSKIIGSppgYVGHDEAGQltEKVRRKPY--SIILLDEIEKAHPDVQHMFLQIMEDGRLTdSQGRTVSFK 551
Cdd:COG0714 67 DL---LP----SDILGT---YIYDQQTGE--FEFRPGPLfaNVLLADEINRAPPKTQSALLEAMEERQVT-IPGGTYKLP 133
|
170
....*....|
gi 2026840261 552 DT-VIIMTSN 560
Cdd:COG0714 134 EPfLVIATQN 143
|
|
| RecA-like_ClpX |
cd19497 |
ATP-dependent Clp protease ATP-binding subunit ClpX; ClpX is a component of the ATP-dependent ... |
401-608 |
2.94e-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: 49.14 E-value: 2.94e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2026840261 401 KEIDVRLKARVIGQEHAVEKVAKAV----KRSRAGLKSKHRPT----GSFLFVGPTGVGKTELSKTLAEEL---FgskeA 469
Cdd:cd19497 4 KEIKEHLDKYVIGQERAKKVLSVAVynhyKRIRNNLKQKDDDVelekSNILLIGPTGSGKTLLAQTLAKILdvpF----A 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2026840261 470 IIrlDMSEYMEKhsvskiigsppGYVGHDEAGQLTE-------KVRRKPYSIILLDEIEK-----AHPD---------VQ 528
Cdd:cd19497 80 IA--DATTLTEA-----------GYVGEDVENILLKllqaadyDVERAQRGIVYIDEIDKiarksENPSitrdvsgegVQ 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2026840261 529 HMFLQIMEDG--RLTDSQGRTVSFKDTVIIMTSN-----AGS-----------TDKKAvkVGFQSEQEEAIEEQSLIDSL 590
Cdd:cd19497 147 QALLKILEGTvaNVPPQGGRKHPQQEFIQVDTTNilficGGAfvglekiiarrLGKKS--LGFGAETSSEKDEKERDELL 224
|
250 260
....*....|....*....|....*..
gi 2026840261 591 S--------AY-FKPEFLNRFDSIIQF 608
Cdd:cd19497 225 SkvepedliKFgLIPEFVGRLPVIVTL 251
|
|
| PRK13342 |
PRK13342 |
recombination factor protein RarA; Reviewed |
119-288 |
3.49e-06 |
|
recombination factor protein RarA; Reviewed
Pssm-ID: 237355 [Multi-domain] Cd Length: 413 Bit Score: 50.08 E-value: 3.49e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2026840261 119 GEPGVGKTAIAEGLAlkiangdvpNKLKNKQVYLLDVSSlvantGVrgqfeERMKQLIKE----LQSRKNIILFVDEIH- 193
Cdd:PRK13342 43 GPPGTGKTTLARIIA---------GATDAPFEALSAVTS-----GV-----KDLREVIEEarqrRSAGRRTILFIDEIHr 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2026840261 194 --------LLvgagsaegsmdagnilkPALARGELQLVGATTlkEYRQIEKDAALERRFQpVIVDEP-TQDEAFEIL-KG 263
Cdd:PRK13342 104 fnkaqqdaLL-----------------PHVEDGTITLIGATT--ENPSFEVNPALLSRAQ-VFELKPlSEEDIEQLLkRA 163
|
170 180
....*....|....*....|....*
gi 2026840261 264 IQDKYEAYhgVTYSDEAIKACVQLS 288
Cdd:PRK13342 164 LEDKERGL--VELDDEALDALARLA 186
|
|
| RecA-like_protease |
cd19481 |
proteases similar to RecA; RecA-like NTPases. This family includes the NTP binding domain of ... |
117-248 |
5.64e-06 |
|
proteases similar to RecA; RecA-like NTPases. This family includes the NTP binding domain of F1 and V1 H(+)ATPases, DnaB and related helicases as well as bacterial RecA and related eukaryotic and archaeal recombinases. This group also includes bacterial conjugation proteins and related DNA transfer proteins involved in type II and type IV secretion.
Pssm-ID: 410889 [Multi-domain] Cd Length: 158 Bit Score: 46.89 E-value: 5.64e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2026840261 117 LIGEPGVGKTAIAEGLAlkiangdvpNKLKNKqVYLLDVSSLVanTGVRGQFEERMKQLIKELQSRKNIILFVDEIHLLV 196
Cdd:cd19481 31 LYGPPGTGKTLLAKALA---------GELGLP-LIVVKLSSLL--SKYVGESEKNLRKIFERARRLAPCILFIDEIDAIG 98
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2026840261 197 GAGSAEGSMDAGNILKPAL--------ARGELQLVGATTLKEyrqiEKDAALER--RFQPVI 248
Cdd:cd19481 99 RKRDSSGESGELRRVLNQLlteldgvnSRSKVLVIAATNRPD----LLDPALLRpgRFDEVI 156
|
|
| TIGR02928 |
TIGR02928 |
orc1/cdc6 family replication initiation protein; Members of this protein family are found ... |
89-313 |
5.75e-06 |
|
orc1/cdc6 family replication initiation protein; Members of this protein family are found exclusively in the archaea. This set of DNA binding proteins shows homology to the origin recognition complex subunit 1/cell division control protein 6 family in eukaryotes. Several members may be found in genome and interact with each other. [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 274354 [Multi-domain] Cd Length: 365 Bit Score: 49.17 E-value: 5.75e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2026840261 89 LIDPVIGRDEEVTRVI----EILNRRNKNNPVLIGEPGVGKTAIAEGLaLKIANGDVPNKLK-------NKQVY------ 151
Cdd:TIGR02928 13 VPDRIVHRDEQIEELAkalrPILRGSRPSNVFIYGKTGTGKTAVTKYV-MKELEEAAEDRDVrvvtvyvNCQILdtlyqv 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2026840261 152 -------LLDVSSLVANTGVrgQFEERMKQLIKELQSRKNIILFV-DEIHLLVGAGS----------AEGSMDAGNIlkp 213
Cdd:TIGR02928 92 lvelanqLRGSGEEVPTTGL--STSEVFRRLYKELNERGDSLIIVlDEIDYLVGDDDdllyqlsrarSNGDLDNAKV--- 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2026840261 214 alarGELQLVGATTLKEyrqiEKDAALERRFQP-VIVDEP-TQDEAFEILKGIQDKyeAYH-GVTySDEAIKACVQLSSr 290
Cdd:TIGR02928 167 ----GVIGISNDLKFRE----NLDPRVKSSLCEeEIIFPPyDAEELRDILENRAEK--AFYdGVL-DDGVIPLCAALAA- 234
|
250 260
....*....|....*....|...
gi 2026840261 291 yiQDRHLPDKAIDLMDEAGSKAN 313
Cdd:TIGR02928 235 --QEHGDARKAIDLLRVAGEIAE 255
|
|
| RecA-like_HslU |
cd19498 |
ATP-dependent protease ATPase subunit HslU; HslU is a component of the ATP-dependent protease ... |
401-522 |
7.51e-06 |
|
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: 46.99 E-value: 7.51e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2026840261 401 KEIDVRLKARVIGQEHAVEKVAKAVK----RSRAGLKSKHRPT-GSFLFVGPTGVGKTELSKTLAEElfgSKEAIIRLDM 475
Cdd:cd19498 3 REIVSELDKYIIGQDEAKRAVAIALRnrwrRMQLPEELRDEVTpKNILMIGPTGVGKTEIARRLAKL---AGAPFIKVEA 79
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 2026840261 476 SEYMEKhsvskiigsppGYVGHDeagqLTEKVRRKPYSIILLDEIEK 522
Cdd:cd19498 80 TKFTEV-----------GYVGRD----VESIIRDLVEGIVFIDEIDK 111
|
|
| PRK13341 |
PRK13341 |
AAA family ATPase; |
114-289 |
8.34e-06 |
|
AAA family ATPase;
Pssm-ID: 237354 [Multi-domain] Cd Length: 725 Bit Score: 49.28 E-value: 8.34e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2026840261 114 NPVLIGEPGVGKTAiaegLALKIANgdvpnklkNKQVYLLDVSSLVAntGVRgqfeeRMKQLIKELQSR-----KNIILF 188
Cdd:PRK13341 54 SLILYGPPGVGKTT----LARIIAN--------HTRAHFSSLNAVLA--GVK-----DLRAEVDRAKERlerhgKRTILF 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2026840261 189 VDEIHLLVGAgsaegSMDAgniLKPALARGELQLVGATTLKEYRQIEKdAALER----RFQPVivdepTQDEAFEIL-KG 263
Cdd:PRK13341 115 IDEVHRFNKA-----QQDA---LLPWVENGTITLIGATTENPYFEVNK-ALVSRsrlfRLKSL-----SDEDLHQLLkRA 180
|
170 180
....*....|....*....|....*...
gi 2026840261 264 IQDKYEAYH--GVTYSDEAIKACVQLSS 289
Cdd:PRK13341 181 LQDKERGYGdrKVDLEPEAEKHLVDVAN 208
|
|
| RuvB_N |
pfam05496 |
Holliday junction DNA helicase RuvB P-loop domain; The RuvB protein makes up part of the ... |
412-540 |
2.02e-05 |
|
Holliday junction DNA helicase RuvB P-loop domain; The RuvB protein makes up part of the RuvABC revolvasome which catalyzes the resolution of Holliday junctions that arise during genetic recombination and DNA repair. Branch migration is catalyzed by the RuvB protein that is targeted to the Holliday junction by the structure specific RuvA protein. This family contains the N-terminal region of the protein.
Pssm-ID: 398900 [Multi-domain] Cd Length: 159 Bit Score: 45.18 E-value: 2.02e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2026840261 412 IGQEHAVEKVAKAVKRSRaglkSKHRPTGSFLFVGPTGVGKTELSKTLAEELfgskEAIIRLDMSEYMEKhsvskiigsp 491
Cdd:pfam05496 10 IGQEKVKENLKIFIEAAK----QRGEALDHVLLYGPPGLGKTTLANIIANEM----GVNIRITSGPAIER---------- 71
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 2026840261 492 PGyvghDEAGQLTEkvrRKPYSIILLDEIEKAHPDVQHMFLQIMEDGRL 540
Cdd:pfam05496 72 PG----DLAAILTN---LEPGDVLFIDEIHRLNRAVEEILYPAMEDFRL 113
|
|
| ClpX |
COG1219 |
ATP-dependent protease Clp, ATPase subunit ClpX [Posttranslational modification, protein ... |
375-676 |
5.61e-05 |
|
ATP-dependent protease Clp, ATPase subunit ClpX [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440832 [Multi-domain] Cd Length: 409 Bit Score: 46.19 E-value: 5.61e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2026840261 375 EDIQSIVEQKTGIPVGKLQADEQTKMKEIDVRLKARVIGQEHAVEKVAKAV----KRsragLKSKHRPTGS-------FL 443
Cdd:COG1219 38 ELCNEIIEEELKEEEAEEELKKLPKPKEIKAFLDEYVIGQERAKKVLSVAVynhyKR----LNSGSKDDDDveleksnIL 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2026840261 444 FVGPTGVGKTELSKTLAeelfgskeaiirldmseymekhsvsKIIGSP-----------PGYVGHD-E---------AGQ 502
Cdd:COG1219 114 LIGPTGSGKTLLAQTLA-------------------------RILDVPfaiadattlteAGYVGEDvEnillkllqaADY 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2026840261 503 LTEKVRRkpySIILLDEIEK-----AHP----D-----VQHMFLQIMEdgrltdsqGRTVSF----------KDTVIIMT 558
Cdd:COG1219 169 DVEKAER---GIIYIDEIDKiarksENPsitrDvsgegVQQALLKILE--------GTVANVppqggrkhpqQEFIQIDT 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2026840261 559 SN-----AGS-----------TDKKAvkVGFQSEQEEAIEEqslidSLSAYFK-------------PEFLNRFDSIIQFD 609
Cdd:COG1219 238 TNilficGGAfdglekiierrLGKKS--IGFGAEVKSKKEK-----DEGELLKqvepedlikfgliPEFIGRLPVIATLE 310
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2026840261 610 SLDKDDLVKIvdL------LLKDLSEQLKEQNLTVHVTNEAKEKIAELGYHPAFGARPLrRTIQEHVedqMTD 676
Cdd:COG1219 311 ELDEEALVRI--LtepknaLVKQYQKLFEMDGVELEFTDEALEAIAKKAIERKTGARGL-RSILEEI---LLD 377
|
|
| CDC48 |
TIGR01243 |
AAA family ATPase, CDC48 subfamily; This subfamily of the AAA family ATPases includes two ... |
116-525 |
6.41e-05 |
|
AAA family ATPase, CDC48 subfamily; This subfamily of the AAA family ATPases includes two members each from three archaeal species. It also includes yeast CDC48 (cell division control protein 48) and the human ortholog, transitional endoplasmic reticulum ATPase (valosin-containing protein). These proteins in eukaryotes are involved in the budding and transfer of membrane from the transitional endoplasmic reticulum to the Golgi apparatus.
Pssm-ID: 273521 [Multi-domain] Cd Length: 733 Bit Score: 46.44 E-value: 6.41e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2026840261 116 VLIGEPGVGKTAIAEGLALKIAngdvpnklknkqVYLLDVSSLVANTGVRGQFEERMKQLIKELQSRKNIILFVDEIHLL 195
Cdd:TIGR01243 216 LLYGPPGTGKTLLAKAVANEAG------------AYFISINGPEIMSKYYGESEERLREIFKEAEENAPSIIFIDEIDAI 283
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2026840261 196 V-----GAGSAEGSMDAG--NILKPALARGELQLVGATTlkeyRQIEKDAALER--RF-QPVIVDEPTQDEAFEILKgiq 265
Cdd:TIGR01243 284 ApkreeVTGEVEKRVVAQllTLMDGLKGRGRVIVIGATN----RPDALDPALRRpgRFdREIVIRVPDKRARKEILK--- 356
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2026840261 266 dkyeayhgvtysdeaikacvqlssryIQDRHLPDKAIDLMDEAGSKANLSIDAasedeltnRLAQIAaeKQAALNE-ERY 344
Cdd:TIGR01243 357 --------------------------VHTRNMPLAEDVDLDKLAEVTHGFVGA--------DLAALA--KEAAMAAlRRF 400
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2026840261 345 EKAAKLRDEEEAIEARLQnktndKEHVVTAEDIQSiveqktgipvgKLQADEQTKMKEIDVRLK----ARVIGQEHAVEK 420
Cdd:TIGR01243 401 IREGKINFEAEEIPAEVL-----KELKVTMKDFME-----------ALKMVEPSAIREVLVEVPnvrwSDIGGLEEVKQE 464
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2026840261 421 VAKAV----KRSRAGLKSKHRPTGSFLFVGPTGVGKTELSKTLAEElfgSKEAIIRLDMSEYMEKhsvskiigsppgYVG 496
Cdd:TIGR01243 465 LREAVewplKHPEIFEKMGIRPPKGVLLFGPPGTGKTLLAKAVATE---SGANFIAVRGPEILSK------------WVG 529
|
410 420 430
....*....|....*....|....*....|.
gi 2026840261 497 HDEAG--QLTEKVRRKPYSIILLDEIEKAHP 525
Cdd:TIGR01243 530 ESEKAirEIFRKARQAAPAIIFFDEIDAIAP 560
|
|
| McsA |
COG3880 |
Protein-arginine kinase activator protein McsA [Posttranslational modification, protein ... |
1-71 |
7.74e-05 |
|
Protein-arginine kinase activator protein McsA [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 443088 [Multi-domain] Cd Length: 173 Bit Score: 43.73 E-value: 7.74e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2026840261 1 MRCQHCQVNEATIRLNMQVNSSRSQMVLCEDCYTSLMEQSKMKMGP----NLFGGgsFFSEQAGHATSQERPKQK 71
Cdd:COG3880 1 MLCERCKKRPATVHLTQIINGEKTEVHLCEECAKEKGEFSFGFDEPfslhDLLSG--LLNFDSGQSSEKAPEDEL 73
|
|
| UVR |
pfam02151 |
UvrB/uvrC motif; |
325-359 |
7.80e-05 |
|
UvrB/uvrC motif;
Pssm-ID: 308001 [Multi-domain] Cd Length: 36 Bit Score: 40.07 E-value: 7.80e-05
10 20 30
....*....|....*....|....*....|....*
gi 2026840261 325 TNRLAQIAAEKQAALNEERYEKAAKLRDEEEAIEA 359
Cdd:pfam02151 1 KKLIKELEEEMEEAAENEDFEKAAKLRDQINALKK 35
|
|
| HolB |
COG0470 |
DNA polymerase III, delta prime subunit [Replication, recombination and repair]; |
414-561 |
1.46e-04 |
|
DNA polymerase III, delta prime subunit [Replication, recombination and repair];
Pssm-ID: 440238 [Multi-domain] Cd Length: 289 Bit Score: 44.20 E-value: 1.46e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2026840261 414 QEHAVEKVAKAVKRSRaglkSKHrptgSFLFVGPTGVGKTELSKTLAEELFGSKEAiirlDMSEYMEKHSVSKIIGSPPG 493
Cdd:COG0470 1 QEEAWEQLLAAAESGR----LPH----ALLLHGPPGIGKTTLALALARDLLCENPE----GGKACGQCHSRLMAAGNHPD 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2026840261 494 YV-----------GHDEAGQLTEKVRRKPYS----IILLDEIEKAHPDVQHMFLQIMEDGRltdsqgrtvsfKDTVIIMT 558
Cdd:COG0470 69 LLelnpeeksdqiGIDQIRELGEFLSLTPLEggrkVVIIDEADAMNEAAANALLKTLEEPP-----------KNTPFILI 137
|
...
gi 2026840261 559 SNA 561
Cdd:COG0470 138 AND 140
|
|
| AAA_16 |
pfam13191 |
AAA ATPase domain; This family of domains contain a P-loop motif that is characteriztic of the ... |
92-133 |
4.14e-04 |
|
AAA ATPase domain; This family of domains contain a P-loop motif that is characteriztic of the AAA superfamily.
Pssm-ID: 433025 [Multi-domain] Cd Length: 167 Bit Score: 41.72 E-value: 4.14e-04
10 20 30 40
....*....|....*....|....*....|....*....|....*
gi 2026840261 92 PVIGRDEEVTRVIEILNRRNKNNP---VLIGEPGVGKTAIAEGLA 133
Cdd:pfam13191 1 RLVGREEELEQLLDALDRVRSGRPpsvLLTGEAGTGKTTLLRELL 45
|
|
| rfc |
PRK00440 |
replication factor C small subunit; Reviewed |
411-536 |
4.25e-04 |
|
replication factor C small subunit; Reviewed
Pssm-ID: 234763 [Multi-domain] Cd Length: 319 Bit Score: 42.94 E-value: 4.25e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2026840261 411 VIGQEHAVEKVAKAVKRsraglksKHRPtgSFLFVGPTGVGKTELSKTLAEELFGS--KEAIIRLDMSeymekhsvskii 488
Cdd:PRK00440 19 IVGQEEIVERLKSYVKE-------KNMP--HLLFAGPPGTGKTTAALALARELYGEdwRENFLELNAS------------ 77
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2026840261 489 gsppgyvghDEAGqlTEKVRRK-------------PYSIILLDEIEKAHPDVQHMFLQIME 536
Cdd:PRK00440 78 ---------DERG--IDVIRNKikefartapvggaPFKIIFLDEADNLTSDAQQALRRTME 127
|
|
| DnaX |
COG2812 |
DNA polymerase III, gamma/tau subunits [Replication, recombination and repair]; |
409-460 |
4.73e-04 |
|
DNA polymerase III, gamma/tau subunits [Replication, recombination and repair];
Pssm-ID: 442061 [Multi-domain] Cd Length: 340 Bit Score: 42.87 E-value: 4.73e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 2026840261 409 ARVIGQEHAVEKVAKAVKRSRAGlkskHrptgSFLFVGPTGVGKTELSKTLA 460
Cdd:COG2812 10 DDVVGQEHVVRTLKNALASGRLA----H----AYLFTGPRGVGKTTLARILA 53
|
|
| McsA |
COG3880 |
Protein-arginine kinase activator protein McsA [Posttranslational modification, protein ... |
323-366 |
6.12e-04 |
|
Protein-arginine kinase activator protein McsA [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 443088 [Multi-domain] Cd Length: 173 Bit Score: 41.03 E-value: 6.12e-04
10 20 30 40
....*....|....*....|....*....|....*....|....
gi 2026840261 323 ELTNRLAQIAAEKQAALNEERYEKAAKLRDEEEAIEARLQNKTN 366
Cdd:COG3880 130 RIKREIEELKEELQEAVEKEEYEEAAELRDEIRELEKELGEEGE 173
|
|
| RecA-like_Yta7-like |
cd19517 |
ATPase domain of Saccharomyces cerevisiae Yta7 and similar ATPase domains; Saccharomyces ... |
116-244 |
6.37e-04 |
|
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: 40.96 E-value: 6.37e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2026840261 116 VLIGEPGVGKTAIAEGLALKIANGDvpnklkNKQVYLLDVSSLVANTGVrGQFEERMKQLIKELQSRKNIILFVDEIHLL 195
Cdd:cd19517 38 LFHGPPGTGKTLMARALAAECSKGG------QKVSFFMRKGADCLSKWV-GEAERQLRLLFEEAYRMQPSIIFFDEIDGL 110
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 2026840261 196 VGAGSAEGSMDAGNILKPALA-------RGELQLVGATTlkeyRQIEKDAALER--RF 244
Cdd:cd19517 111 APVRSSKQEQIHASIVSTLLAlmdgldnRGQVVVIGATN----RPDALDPALRRpgRF 164
|
|
| MoxR |
COG0714 |
MoxR-like ATPase [General function prediction only]; MoxR-like ATPase is part of the Pathway ... |
93-133 |
1.31e-03 |
|
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: 41.31 E-value: 1.31e-03
10 20 30 40
....*....|....*....|....*....|....*....|...
gi 2026840261 93 VIGRDEEVTRV-IEILNRRnknnPVLI-GEPGVGKTAIAEGLA 133
Cdd:COG0714 14 YVGQEELIELVlIALLAGG----HLLLeGVPGVGKTTLAKALA 52
|
|
| RecA-like_NVL_r1-like |
cd19518 |
first of two ATPase domains of NVL (nuclear VCP-like protein) and similar ATPase domains; NVL ... |
116-192 |
1.54e-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: 40.08 E-value: 1.54e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2026840261 116 VLIGEPGVGKTAIAEGLAlkiangdvpNKLKnkqVYLLDVSSLVANTGVRGQFEERMKQLIKELQSRKNIILFVDEI 192
Cdd:cd19518 38 LLHGPPGCGKTMLANAIA---------GELK---VPFLKISATEIVSGVSGESEEKIRELFDQAISNAPCIVFIDEI 102
|
|
| RecA-like_CDC48_r2-like |
cd19511 |
second of two ATPase domains of CDC48/p97, PEX1 and -6, VAT and NVL, and similar ATPase ... |
428-521 |
1.65e-03 |
|
second of two ATPase domains of CDC48/p97, PEX1 and -6, VAT and NVL, and similar ATPase domains; This subfamily includes the second of two ATPase domains of the molecular chaperone CDC48 in yeast and p97 or VCP in metazoans, Peroxisomal biogenesis factor 1 (PEX1) and -6 (PEX6), Valosin-containing protein-like ATPase (VAT), and nuclear VCP-like protein (NVL). 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: 410919 [Multi-domain] Cd Length: 159 Bit Score: 39.57 E-value: 1.65e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2026840261 428 SRAGLKskhRPTGsFLFVGPTGVGKTELSKTLAEElfgSKEAIIRLDMSEYMEKhsvskiigsppgYVGHDEAG--QLTE 505
Cdd:cd19511 20 KRLGIR---PPKG-VLLYGPPGCGKTLLAKALASE---AGLNFISVKGPELFSK------------YVGESERAvrEIFQ 80
|
90
....*....|....*.
gi 2026840261 506 KVRRKPYSIILLDEIE 521
Cdd:cd19511 81 KARQAAPCIIFFDEID 96
|
|
| RecA-like_FtsH |
cd19501 |
ATP-dependent zinc metalloprotease FtsH; FtsH ATPase is a processive, ATP-dependent zinc ... |
411-521 |
2.01e-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: 39.52 E-value: 2.01e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2026840261 411 VIGQEHAVEKVAKAV-------KRSRAGLKSkhrPTGsFLFVGPTGVGKTELSKTLAEElfgSKEAIIRLDMSEYMEkhs 483
Cdd:cd19501 6 VAGCEEAKEELKEVVeflknpeKFTKLGAKI---PKG-VLLVGPPGTGKTLLAKAVAGE---AGVPFFSISGSDFVE--- 75
|
90 100 110
....*....|....*....|....*....|....*...
gi 2026840261 484 vsKIIGsppgyVGHDEAGQLTEKVRRKPYSIILLDEIE 521
Cdd:cd19501 76 --MFVG-----VGASRVRDLFEQAKKNAPCIVFIDEID 106
|
|
| AAA_22 |
pfam13401 |
AAA domain; |
109-195 |
2.30e-03 |
|
AAA domain;
Pssm-ID: 379165 [Multi-domain] Cd Length: 129 Bit Score: 38.86 E-value: 2.30e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2026840261 109 RRNKNNPVLIGEPGVGKTAIAEGLALKIANG-------DVPNKLKNKQVYLLDVSSLVANTGVRGQFEERMKQLIKELQS 181
Cdd:pfam13401 2 RFGAGILVLTGESGTGKTTLLRRLLEQLPEVrdsvvfvDLPSGTSPKDLLRALLRALGLPLSGRLSKEELLAALQQLLLA 81
|
90
....*....|....*
gi 2026840261 182 RKN-IILFVDEIHLL 195
Cdd:pfam13401 82 LAVaVVLIIDEAQHL 96
|
|
| RecA-like_VPS4 |
cd19521 |
ATPase domain of vacuolar protein sorting-associated protein 4; Vacuolar protein ... |
108-248 |
2.82e-03 |
|
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: 39.07 E-value: 2.82e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2026840261 108 NRRNKNNPVLIGEPGVGKTAIAEGLALKIangdvpnklkNKQVYLLDVSSLVANTgvRGQFEERMKQLIKELQSRKNIIL 187
Cdd:cd19521 36 NRKPWSGILLYGPPGTGKSYLAKAVATEA----------NSTFFSVSSSDLVSKW--MGESEKLVKQLFAMARENKPSII 103
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2026840261 188 FVDEIHLLVGAGSaEGSMDAGNILKPAL----------ARGELQLvGATTLKeyrqIEKDAALERRFQPVI 248
Cdd:cd19521 104 FIDEVDSLCGTRG-EGESEASRRIKTELlvqmngvgndSQGVLVL-GATNIP----WQLDSAIRRRFEKRI 168
|
|
| ruvB |
TIGR00635 |
Holliday junction DNA helicase, RuvB subunit; All proteins in this family for which functions ... |
412-540 |
3.07e-03 |
|
Holliday junction DNA helicase, RuvB subunit; All proteins in this family for which functions are known are 5'-3' DNA helicases that, as part of a complex with RuvA homologs serve as a 5'-3' Holliday junction helicase. RuvA specifically binds Holliday junctions as a sandwich of two tetramers and maintains the configuration of the junction. It forms a complex with two hexameric rings of RuvB, the subunit that contains helicase activity. The complex drives ATP-dependent branch migration of the Holliday junction recombination intermediate. The endonuclease RuvC resolves junctions. [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129721 [Multi-domain] Cd Length: 305 Bit Score: 40.36 E-value: 3.07e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2026840261 412 IGQEHAVEKVAKAVKRSRAglksKHRPTGSFLFVGPTGVGKTELSKTLAEELfGSKeaiIRLDMSEYMEKhsvskiigsp 491
Cdd:TIGR00635 7 IGQEKVKEQLQLFIEAAKM----RQEALDHLLLYGPPGLGKTTLAHIIANEM-GVN---LKITSGPALEK---------- 68
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 2026840261 492 PGyvghDEAGQLTEkvrRKPYSIILLDEIEKAHPDVQHMFLQIMEDGRL 540
Cdd:TIGR00635 69 PG----DLAAILTN---LEEGDVLFIDEIHRLSPAVEELLYPAMEDFRL 110
|
|
| PRK14951 |
PRK14951 |
DNA polymerase III subunits gamma and tau; Provisional |
412-463 |
3.82e-03 |
|
DNA polymerase III subunits gamma and tau; Provisional
Pssm-ID: 237865 [Multi-domain] Cd Length: 618 Bit Score: 40.47 E-value: 3.82e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 2026840261 412 IGQEHAVEKVAKAVKRSRAglkskHRptgSFLFVGPTGVGKTELSKTLAEEL 463
Cdd:PRK14951 19 VGQEHVVQALTNALTQQRL-----HH---AYLFTGTRGVGKTTVSRILAKSL 62
|
|
| RecA-like_VPS4 |
cd19521 |
ATPase domain of vacuolar protein sorting-associated protein 4; Vacuolar protein ... |
433-521 |
3.84e-03 |
|
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: 38.69 E-value: 3.84e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2026840261 433 KSKHRPTGSFLFVGPTGVGKTELSKTLAEELFGSKEAIIRLDMseymekhsVSKIIGSPPGYVGhdeagQLTEKVRRKPY 512
Cdd:cd19521 34 TGNRKPWSGILLYGPPGTGKSYLAKAVATEANSTFFSVSSSDL--------VSKWMGESEKLVK-----QLFAMARENKP 100
|
....*....
gi 2026840261 513 SIILLDEIE 521
Cdd:cd19521 101 SIIFIDEVD 109
|
|
| RAD55 |
COG0467 |
RecA-superfamily ATPase, KaiC/GvpD/RAD55 family [Signal transduction mechanisms]; |
438-568 |
4.42e-03 |
|
RecA-superfamily ATPase, KaiC/GvpD/RAD55 family [Signal transduction mechanisms];
Pssm-ID: 440235 [Multi-domain] Cd Length: 221 Bit Score: 39.13 E-value: 4.42e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2026840261 438 PTGSF-LFVGPTGVGKTELSKTLAEE------------LFGSKEAIIR------LDMSEYMEKHSVsKIIGSPPGYVGHD 498
Cdd:COG0467 18 PRGSStLLSGPPGTGKTTLALQFLAEglrrgekglyvsFEESPEQLLRraeslgLDLEEYIESGLL-RIIDLSPEELGLD 96
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2026840261 499 ---EAGQLTEKVRRKPYSIILLD---EIEKAHPDVQHMFLQIMedgRLTdsqgRTVSFKDTVIIMTSNAGSTDKKA 568
Cdd:COG0467 97 leeLLARLREAVEEFGAKRVVIDslsGLLLALPDPERLREFLH---RLL----RYLKKRGVTTLLTSETGGLEDEA 165
|
|
| PRK14950 |
PRK14950 |
DNA polymerase III subunits gamma and tau; Provisional |
409-460 |
5.45e-03 |
|
DNA polymerase III subunits gamma and tau; Provisional
Pssm-ID: 237864 [Multi-domain] Cd Length: 585 Bit Score: 39.79 E-value: 5.45e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 2026840261 409 ARVIGQEHAVEKVAKAVKRSRAGlkskHrptgSFLFVGPTGVGKTELSKTLA 460
Cdd:PRK14950 16 AELVGQEHVVQTLRNAIAEGRVA----H----AYLFTGPRGVGKTSTARILA 59
|
|
| Zeta_toxin |
pfam06414 |
Zeta toxin; This family consists of several bacterial zeta toxin proteins. Zeta toxin is ... |
433-548 |
6.91e-03 |
|
Zeta toxin; This family consists of several bacterial zeta toxin proteins. Zeta toxin is thought to be part of a postregulational killing system in bacteria. It relies on antitoxin/toxin systems that secure stable inheritance of low and medium copy number plasmids during cell division and kill cells that have lost the plasmid.
Pssm-ID: 428926 Cd Length: 192 Bit Score: 38.50 E-value: 6.91e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2026840261 433 KSKHRPTGSFLfVGPTGVGKTELSKTLAEELfGSKEAIIRLDMSEYMEKH-SVSKIIGSPP---GYVGHDEAGQLTEKVR 508
Cdd:pfam06414 6 TSQERPKAILL-GGQPGAGKTELARALLDEL-GRQGNVVRIDPDDFRELHpHYRELQAADPktaSEYTQPDASRWVEKLL 83
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 2026840261 509 RKP----YSIILldEIEKAHPDVqhmFLQIMEDGRltdSQGRTV 548
Cdd:pfam06414 84 QHAiengYNIIL--EGTLRSPDV---AKKIARALK---AAGYRV 119
|
|
| PRK14965 |
PRK14965 |
DNA polymerase III subunits gamma and tau; Provisional |
412-463 |
9.84e-03 |
|
DNA polymerase III subunits gamma and tau; Provisional
Pssm-ID: 237871 [Multi-domain] Cd Length: 576 Bit Score: 38.95 E-value: 9.84e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 2026840261 412 IGQEHAVEKVAKAVKRSRAGlkskHrptgSFLFVGPTGVGKTELSKTLAEEL 463
Cdd:PRK14965 19 TGQEHVSRTLQNAIDTGRVA----H----AFLFTGARGVGKTSTARILAKAL 62
|
|
| DNA_pol3_delta2 |
pfam13177 |
DNA polymerase III, delta subunit; DNA polymerase III, delta subunit (EC 2.7.7.7) is required ... |
413-536 |
9.86e-03 |
|
DNA polymerase III, delta subunit; DNA polymerase III, delta subunit (EC 2.7.7.7) is required for, along with delta' subunit, the assembly of the processivity factor beta(2) onto primed DNA in the DNA polymerase III holoenzyme-catalyzed reaction. The delta subunit is also known as HolA.
Pssm-ID: 433013 [Multi-domain] Cd Length: 161 Bit Score: 37.57 E-value: 9.86e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2026840261 413 GQEHAVEKVAKAVKrsraglksKHRPTGSFLFVGPTGVGKTELSKTLAEELFGSKEAI---------IRLDMSeymEKHS 483
Cdd:pfam13177 1 GQPEAIQLLQNSLE--------NGRLSHAYLFSGPEGVGKLELALAFAKALFCEEPGDdlpcgqcrsCRRIES---GNHP 69
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 2026840261 484 VSKIIGSPPGYVGHDEAGQLTEKVRRKPY----SIILLDEIEKAHPDVQHMFLQIME 536
Cdd:pfam13177 70 DLVIIEPEGQSIKIDQIRELQKEFSKSPYegkkKVYIIEDAEKMTASAANSLLKFLE 126
|
|
| |
