|
Name |
Accession |
Description |
Interval |
E-value |
| ClpA |
COG0542 |
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ... |
72-697 |
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: 820.48 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 997579501 72 GQQSGNGNYLEQIGRNLTQEARDGLLDPVIGRDKEIQETAEVLSRRTKNNPILVGEAGVGKTAIVEGLAQAIVEGNVPAA 151
Cdd:COG0542 153 QNPESKTPALDKYGRDLTELAREGKLDPVIGRDEEIRRVIQILSRRTKNNPVLIGEPGVGKTAIVEGLAQRIVNGDVPES 232
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 997579501 152 IKDKEIISIDISSLEAGTQYRGAFEENIQKLVEGVKSSQ-NAVLFFDEIHQIIGSGATgsdSGSKGLSDILKPALSRGEI 230
Cdd:COG0542 233 LKDKRVLSLDLGALVAGAKYRGEFEERLKAVLDEVKKSEgNIILFIDELHTLVGAGGA---EGAMDAANLLKPALARGEL 309
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 997579501 231 SIIGATTQDEYRNNIMKDAALTRRFNEVLVNEPSAKDTVEILKGIREKFETHHQVKLPDDVLKACVDLSIQYIPQRLLPD 310
Cdd:COG0542 310 RCIGATTLDEYRKYIEKDAALERRFQPVLVEEPSVEDTISILRGLKERYEAHHGVRITDEALVAAVRLSDRYITDRFLPD 389
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 997579501 311 KAIDVLDITAAHL----SAQSPAIDKVttEKRISELEHDKRKAVSAEE---YKKADDIQKEIKSLQDKLE----NSNGEH 379
Cdd:COG0542 390 KAIDLIDEAAARVrmeiDSKPEELDEL--ERRLEQLEIEKEALKKEQDeasFERLAELRDELAELEEELEalkaRWEAEK 467
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 997579501 380 TAVA-----------------------------------------TVHDISDTIQRLTGIPVSQMDANDIERLKNISSRL 418
Cdd:COG0542 468 ELIEeiqelkeeleqrygkipelekelaeleeelaelapllreevTEEDIAEVVSRWTGIPVGKLLEGEREKLLNLEEEL 547
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 997579501 419 RSKIIGQDKAVEMVSRAIRRNRAGFDDGNRPIGSFLFVGPTGVGKTELAKQLAIDLFGNKEALIRLDMSEYSDTTAVSKM 498
Cdd:COG0542 548 HERVIGQDEAVEAVADAIRRSRAGLKDPNRPIGSFLFLGPTGVGKTELAKALAEFLFGDEDALIRIDMSEYMEKHSVSRL 627
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 997579501 499 IGTTAGYVGYDDNsNTLTEKVRRNPYSVILFDEIEKANPQILTLLLQVMDDGNLTDGQGNVINFKNTIIICTSNAG---- 574
Cdd:COG0542 628 IGAPPGYVGYEEG-GQLTEAVRRRPYSVVLLDEIEKAHPDVFNILLQVLDDGRLTDGQGRTVDFRNTIIIMTSNIGseli 706
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 997579501 575 ---FGNGNDTEE--KDIMHEMKKFFRPEFLNRFNGIVEFLHLDKDALQDIVNLLLDDVQVTLDKKGITMDVSQDAKDWLI 649
Cdd:COG0542 707 ldlAEDEPDYEEmkEAVMEELKKHFRPEFLNRIDEIIVFHPLSKEELRKIVDLQLKRLRKRLAERGITLELTDAAKDFLA 786
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|
gi 997579501 650 EEGYDEELGARPLRRIVEQQVRDKITDYYLDH--TDVKHVDIDVEDNELV 697
Cdd:COG0542 787 EKGYDPEYGARPLKRAIQRELEDPLAEEILAGeiKEGDTITVDVDDGELV 836
|
|
| chaperone_ClpB |
TIGR03346 |
ATP-dependent chaperone ClpB; Members of this protein family are the bacterial ATP-dependent ... |
81-697 |
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: 664.73 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 997579501 81 LEQIGRNLTQEARDGLLDPVIGRDKEIQETAEVLSRRTKNNPILVGEAGVGKTAIVEGLAQAIVEGNVPAAIKDKEIISI 160
Cdd:TIGR03346 156 LEKYARDLTERAREGKLDPVIGRDEEIRRTIQVLSRRTKNNPVLIGEPGVGKTAIVEGLAQRIVNGDVPEGLKNKRLLAL 235
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 997579501 161 DISSLEAGTQYRGAFEENIQKLVEGVKSSQ-NAVLFFDEIHQIIGSGATGsdsGSKGLSDILKPALSRGEISIIGATTQD 239
Cdd:TIGR03346 236 DMGALIAGAKYRGEFEERLKAVLNEVTKSEgQIILFIDELHTLVGAGKAE---GAMDAGNMLKPALARGELHCIGATTLD 312
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 997579501 240 EYRNNIMKDAALTRRFNEVLVNEPSAKDTVEILKGIREKFETHHQVKLPDDVLKACVDLSIQYIPQRLLPDKAIDVLDIT 319
Cdd:TIGR03346 313 EYRKYIEKDAALERRFQPVFVDEPSVEDTISILRGLKERYEVHHGVRITDPAIVAAATLSHRYITDRFLPDKAIDLIDEA 392
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 997579501 320 AAHLSAQ---SP-AIDKVttEKRISELEHDkRKAVSAEE----YKKADDIQKEI------------------------KS 367
Cdd:TIGR03346 393 AARIRMEidsKPeELDEL--DRRIIQLEIE-REALKKEKdeasKKRLEDLEKELadleeeyaeleeqwkaekasiqgiQQ 469
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 997579501 368 LQDKLENSNGE------------------------------------HTAVA------TVHDISDTIQRLTGIPVSQMDA 405
Cdd:TIGR03346 470 IKEEIEQVRLEleqaeregdlakaaelqygklpelekqlqaaeqklgEEQNRllreevTAEEIAEVVSRWTGIPVSKMLE 549
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 997579501 406 NDIERLKNISSRLRSKIIGQDKAVEMVSRAIRRNRAGFDDGNRPIGSFLFVGPTGVGKTELAKQLAIDLFGNKEALIRLD 485
Cdd:TIGR03346 550 GEREKLLHMEEELHERVVGQDEAVEAVSDAIRRSRAGLSDPNRPIGSFLFLGPTGVGKTELAKALAEFLFDSEDAMVRID 629
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 997579501 486 MSEYSDTTAVSKMIGTTAGYVGYDDnSNTLTEKVRRNPYSVILFDEIEKANPQILTLLLQVMDDGNLTDGQGNVINFKNT 565
Cdd:TIGR03346 630 MSEYMEKHSVARLIGAPPGYVGYEE-GGQLTEAVRRRPYSVVLFDEVEKAHPDVFNVLLQVLDDGRLTDGQGRTVDFRNT 708
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 997579501 566 IIICTSNAG------FGNGNDTEE--KDIMHEMKKFFRPEFLNRFNGIVEFLHLDKDALQDIVNLLLDDVQVTLDKKGIT 637
Cdd:TIGR03346 709 VIIMTSNLGsdfiqeLAGGDDYEEmrEAVMEVLRAHFRPEFLNRIDEIVVFHPLGREQIARIVEIQLGRLRKRLAERKIT 788
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 997579501 638 MDVSQDAKDWLIEEGYDEELGARPLRRIVEQQVRDKITDYYL--DHTDVKHVDIDVEDNELV 697
Cdd:TIGR03346 789 LELSDAALDFLAEAGYDPVYGARPLKRAIQREIENPLAKKILagEVAPGDTIRVDVEGGRLV 850
|
|
| clpC |
CHL00095 |
Clp protease ATP binding subunit |
72-694 |
0e+00 |
|
Clp protease ATP binding subunit
Pssm-ID: 214361 [Multi-domain] Cd Length: 821 Bit Score: 636.71 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 997579501 72 GQQSGNGNYLEQIGRNLTQEARDGLLDPVIGRDKEIQETAEVLSRRTKNNPILVGEAGVGKTAIVEGLAQAIVEGNVPAA 151
Cdd:CHL00095 153 EQSRSKTPTLEEFGTNLTKEAIDGNLDPVIGREKEIERVIQILGRRTKNNPILIGEPGVGKTAIAEGLAQRIVNRDVPDI 232
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 997579501 152 IKDKEIISIDISSLEAGTQYRGAFEENIQKLVEGVKSSQNAVLFFDEIHQIIGSGATgsdSGSKGLSDILKPALSRGEIS 231
Cdd:CHL00095 233 LEDKLVITLDIGLLLAGTKYRGEFEERLKRIFDEIQENNNIILVIDEVHTLIGAGAA---EGAIDAANILKPALARGELQ 309
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 997579501 232 IIGATTQDEYRNNIMKDAALTRRFNEVLVNEPSAKDTVEILKGIREKFETHHQVKLPDDVLKACVDLSIQYIPQRLLPDK 311
Cdd:CHL00095 310 CIGATTLDEYRKHIEKDPALERRFQPVYVGEPSVEETIEILFGLRSRYEKHHNLSISDKALEAAAKLSDQYIADRFLPDK 389
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 997579501 312 AIDVLDITAAHL----SAQSPAIDKVTTEKRisELEHDKRKAVSAEEYKKADD-------IQKEIKSLQDKLENSNGEHT 380
Cdd:CHL00095 390 AIDLLDEAGSRVrlinSRLPPAARELDKELR--EILKDKDEAIREQDFETAKQlrdremeVRAQIAAIIQSKKTEEEKRL 467
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 997579501 381 AVATVH--DISDTIQRLTGIPVSQMDANDIERLKNISSRLRSKIIGQDKAVEMVSRAIRRNRAGFDDGNRPIGSFLFVGP 458
Cdd:CHL00095 468 EVPVVTeeDIAEIVSAWTGIPVNKLTKSESEKLLHMEETLHKRIIGQDEAVVAVSKAIRRARVGLKNPNRPIASFLFSGP 547
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 997579501 459 TGVGKTELAKQLAIDLFGNKEALIRLDMSEYSDTTAVSKMIGTTAGYVGYDDnSNTLTEKVRRNPYSVILFDEIEKANPQ 538
Cdd:CHL00095 548 TGVGKTELTKALASYFFGSEDAMIRLDMSEYMEKHTVSKLIGSPPGYVGYNE-GGQLTEAVRKKPYTVVLFDEIEKAHPD 626
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 997579501 539 ILTLLLQVMDDGNLTDGQGNVINFKNTIIICTSNAGF-------------GNGNDTEEKD-------IMHEMKKFFRPEF 598
Cdd:CHL00095 627 IFNLLLQILDDGRLTDSKGRTIDFKNTLIIMTSNLGSkvietnsgglgfeLSENQLSEKQykrlsnlVNEELKQFFRPEF 706
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 997579501 599 LNRFNGIVEFLHLDKDALQDIVNLLLDDVQVTLDKKGITMDVSQDAKDWLIEEGYDEELGARPLRRIVEQQVRDKITDYY 678
Cdd:CHL00095 707 LNRLDEIIVFRQLTKNDVWEIAEIMLKNLFKRLNEQGIQLEVTERIKTLLIEEGYNPLYGARPLRRAIMRLLEDPLAEEV 786
|
650
....*....|....*...
gi 997579501 679 LDHT--DVKHVDIDVEDN 694
Cdd:CHL00095 787 LSFKikPGDIIIVDVNDE 804
|
|
| VI_ClpV1 |
TIGR03345 |
type VI secretion ATPase, ClpV1 family; Members of this protein family are homologs of ClpB, ... |
72-691 |
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: 543.77 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 997579501 72 GQQSGNGNYLEQIGRNLTQEARDGLLDPVIGRDKEIQETAEVLSRRTKNNPILVGEAGVGKTAIVEGLAQAIVEGNVPAA 151
Cdd:TIGR03345 161 AAGAAGTSALDQYTTDLTAQAREGKIDPVLGRDDEIRQMIDILLRRRQNNPILTGEAGVGKTAVVEGLALRIAAGDVPPA 240
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 997579501 152 IKDKEIISIDISSLEAGTQYRGAFEENIQKLVEGVKSS-QNAVLFFDEIHQIIGSGatgsdsGSKGLSD---ILKPALSR 227
Cdd:TIGR03345 241 LRNVRLLSLDLGLLQAGASVKGEFENRLKSVIDEVKASpQPIILFIDEAHTLIGAG------GQAGQGDaanLLKPALAR 314
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 997579501 228 GEISIIGATTQDEYRNNIMKDAALTRRFNEVLVNEPSAKDTVEILKGIREKFETHHQVKLPDDVLKACVDLSIQYIPQRL 307
Cdd:TIGR03345 315 GELRTIAATTWAEYKKYFEKDPALTRRFQVVKVEEPDEETAIRMLRGLAPVLEKHHGVLILDEAVVAAVELSHRYIPGRQ 394
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 997579501 308 LPDKAIDVLDITAAH----LSAQSPAIDKVTTEKRISELE-------------HDKRKAVSAEEY--------------- 355
Cdd:TIGR03345 395 LPDKAVSLLDTACARvalsQNATPAALEDLRRRIAALELEldalereaalgadHDERLAELRAELaaleaelaalearwq 474
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 997579501 356 ---------------------KKADDI---QKEIKSLQDKLENSNGEHTAVATVHD---ISDTIQRLTGIPVSQMDANDI 408
Cdd:TIGR03345 475 qekelveailalraeleadadAPADDDdalRAQLAELEAALASAQGEEPLVFPEVDaqaVAEVVADWTGIPVGRMVRDEI 554
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 997579501 409 ERLKNISSRLRSKIIGQDKAVEMVSRAIRRNRAGFDDGNRPIGSFLFVGPTGVGKTELAKQLAIDLFGNKEALIRLDMSE 488
Cdd:TIGR03345 555 EAVLSLPDRLAERVIGQDHALEAIAERIRTARAGLEDPRKPLGVFLLVGPSGVGKTETALALAELLYGGEQNLITINMSE 634
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 997579501 489 YSDTTAVSKMIGTTAGYVGYDDnSNTLTEKVRRNPYSVILFDEIEKANPQILTLLLQVMDDGNLTDGQGNVINFKNTIII 568
Cdd:TIGR03345 635 FQEAHTVSRLKGSPPGYVGYGE-GGVLTEAVRRKPYSVVLLDEVEKAHPDVLELFYQVFDKGVMEDGEGREIDFKNTVIL 713
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 997579501 569 CTSNAGF----GNGNDTEEKD--------IMHEMKKFFRPEFLNRFNgIVEFLHLDKDALQDIVNLLLDDVQVTLDKK-G 635
Cdd:TIGR03345 714 LTSNAGSdlimALCADPETAPdpealleaLRPELLKVFKPAFLGRMT-VIPYLPLDDDVLAAIVRLKLDRIARRLKENhG 792
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|
gi 997579501 636 ITMDVSQDAKDWLIEEGYDEELGARPLRRIVEQQVRDKITDYYLDH----TDVKHVDIDV 691
Cdd:TIGR03345 793 AELVYSEALVEHIVARCTEVESGARNIDAILNQTLLPELSRQILERlaagEPIERIHLDV 852
|
|
| PRK10865 |
PRK10865 |
ATP-dependent chaperone ClpB; |
87-699 |
9.35e-180 |
|
ATP-dependent chaperone ClpB;
Pssm-ID: 182791 [Multi-domain] Cd Length: 857 Bit Score: 534.04 E-value: 9.35e-180
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 997579501 87 NLTQEARDGLLDPVIGRDKEIQETAEVLSRRTKNNPILVGEAGVGKTAIVEGLAQAIVEGNVPAAIKDKEIISIDISSLE 166
Cdd:PRK10865 167 DLTERAEQGKLDPVIGRDEEIRRTIQVLQRRTKNNPVLIGEPGVGKTAIVEGLAQRIINGEVPEGLKGRRVLALDMGALV 246
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 997579501 167 AGTQYRGAFEENIQKLVEGV-KSSQNAVLFFDEIHQIIGSGATgsdSGSKGLSDILKPALSRGEISIIGATTQDEYRNNI 245
Cdd:PRK10865 247 AGAKYRGEFEERLKGVLNDLaKQEGNVILFIDELHTMVGAGKA---DGAMDAGNMLKPALARGELHCVGATTLDEYRQYI 323
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 997579501 246 MKDAALTRRFNEVLVNEPSAKDTVEILKGIREKFETHHQVKLPDDVLKACVDLSIQYIPQRLLPDKAIDVLDITAAHLSA 325
Cdd:PRK10865 324 EKDAALERRFQKVFVAEPSVEDTIAILRGLKERYELHHHVQITDPAIVAAATLSHRYIADRQLPDKAIDLIDEAASSIRM 403
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 997579501 326 Q----SPAIDKVttEKRI--------------------------SELEHDKRKAVSAEEYKKAD--------DIQKEIKS 367
Cdd:PRK10865 404 QidskPEELDRL--DRRIiqlkleqqalmkesdeaskkrldmlnEELSDKERQYSELEEEWKAEkaslsgtqTIKAELEQ 481
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 997579501 368 LQDKLEN------------------------------SNGEHTAV----ATVHDISDTIQRLTGIPVSQMDANDIERLKN 413
Cdd:PRK10865 482 AKIAIEQarrvgdlarmselqygkipelekqlaaatqLEGKTMRLlrnkVTDAEIAEVLARWTGIPVSRMLESEREKLLR 561
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 997579501 414 ISSRLRSKIIGQDKAVEMVSRAIRRNRAGFDDGNRPIGSFLFVGPTGVGKTELAKQLAIDLFGNKEALIRLDMSEYSDTT 493
Cdd:PRK10865 562 MEQELHHRVIGQNEAVEAVSNAIRRSRAGLSDPNRPIGSFLFLGPTGVGKTELCKALANFMFDSDDAMVRIDMSEFMEKH 641
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 997579501 494 AVSKMIGTTAGYVGYDDnSNTLTEKVRRNPYSVILFDEIEKANPQILTLLLQVMDDGNLTDGQGNVINFKNTIIICTSNA 573
Cdd:PRK10865 642 SVSRLVGAPPGYVGYEE-GGYLTEAVRRRPYSVILLDEVEKAHPDVFNILLQVLDDGRLTDGQGRTVDFRNTVVIMTSNL 720
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 997579501 574 G-------FGNGNDTEEKD-IMHEMKKFFRPEFLNRFNGIVEFLHLDKDALQDIVNLLLDDVQVTLDKKGITMDVSQDAK 645
Cdd:PRK10865 721 GsdliqerFGELDYAHMKElVLGVVSHNFRPEFINRIDEVVVFHPLGEQHIASIAQIQLQRLYKRLEERGYEIHISDEAL 800
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....*.
gi 997579501 646 DWLIEEGYDEELGARPLRRIVEQQVRDKITDYYLDHTDV--KHVDIDVEDNELVVK 699
Cdd:PRK10865 801 KLLSENGYDPVYGARPLKRAIQQQIENPLAQQILSGELVpgKVIRLEVNDDRIVAV 856
|
|
| clpA |
PRK11034 |
ATP-dependent Clp protease ATP-binding subunit; Provisional |
24-697 |
1.36e-178 |
|
ATP-dependent Clp protease ATP-binding subunit; Provisional
Pssm-ID: 236828 [Multi-domain] Cd Length: 758 Bit Score: 527.87 E-value: 1.36e-178
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 997579501 24 SNQTSNKKYYINGKEVSPEELAQFTQQGGnhSAEQSAQAFQQAALRQQGQQSGNGNYLEQIGRNLTQEARDGLLDPVIGR 103
Cdd:PRK11034 114 SEQESQAAYLLRKHEVSRLDVVNFISHGT--RKDEPSQSSDPGSQPNSEEQAGGEERMENFTTNLNQLARVGGIDPLIGR 191
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 997579501 104 DKEIQETAEVLSRRTKNNPILVGEAGVGKTAIVEGLAQAIVEGNVPAAIKDKEIISIDISSLEAGTQYRGAFEENIQKLV 183
Cdd:PRK11034 192 EKELERAIQVLCRRRKNNPLLVGESGVGKTAIAEGLAWRIVQGDVPEVMADCTIYSLDIGSLLAGTKYRGDFEKRFKALL 271
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 997579501 184 EGVKSSQNAVLFFDEIHQIIGSGAtgSDSGSKGLSDILKPALSRGEISIIGATTQDEYRNNIMKDAALTRRFNEVLVNEP 263
Cdd:PRK11034 272 KQLEQDTNSILFIDEIHTIIGAGA--ASGGQVDAANLIKPLLSSGKIRVIGSTTYQEFSNIFEKDRALARRFQKIDITEP 349
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 997579501 264 SAKDTVEILKGIREKFETHHQVKLPDDVLKACVDLSIQYIPQRLLPDKAIDVLDITAAHlSAQSPAidkvttekrisele 343
Cdd:PRK11034 350 SIEETVQIINGLKPKYEAHHDVRYTAKAVRAAVELAVKYINDRHLPDKAIDVIDEAGAR-ARLMPV-------------- 414
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 997579501 344 hDKRKavsaeeykkaddiqKEIkslqdklensngehtavaTVHDISDTIQRLTGIPVSQMDANDIERLKNISSRLRSKII 423
Cdd:PRK11034 415 -SKRK--------------KTV------------------NVADIESVVARIARIPEKSVSQSDRDTLKNLGDRLKMLVF 461
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 997579501 424 GQDKAVEMVSRAIRRNRAGFDDGNRPIGSFLFVGPTGVGKTELAKQLAiDLFGNKeaLIRLDMSEYSDTTAVSKMIGTTA 503
Cdd:PRK11034 462 GQDKAIEALTEAIKMSRAGLGHEHKPVGSFLFAGPTGVGKTEVTVQLS-KALGIE--LLRFDMSEYMERHTVSRLIGAPP 538
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 997579501 504 GYVGYDdNSNTLTEKVRRNPYSVILFDEIEKANPQILTLLLQVMDDGNLTDGQGNVINFKNTIIICTSNAGFgngNDTEE 583
Cdd:PRK11034 539 GYVGFD-QGGLLTDAVIKHPHAVLLLDEIEKAHPDVFNLLLQVMDNGTLTDNNGRKADFRNVVLVMTTNAGV---RETER 614
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 997579501 584 KDI-----------MHEMKKFFRPEFLNRFNGIVEFLHLDKDALQDIVNLLLDDVQVTLDKKGITMDVSQDAKDWLIEEG 652
Cdd:PRK11034 615 KSIglihqdnstdaMEEIKKIFTPEFRNRLDNIIWFDHLSTDVIHQVVDKFIVELQAQLDQKGVSLEVSQEARDWLAEKG 694
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|
gi 997579501 653 YDEELGARPLRRIVEQQVRDKITDYYL-----DHTDVKhVDIDVEDNELV 697
Cdd:PRK11034 695 YDRAMGARPMARVIQDNLKKPLANELLfgslvDGGQVT-VALDKEKNELT 743
|
|
| RecA-like_ClpB_Hsp104-like |
cd19499 |
Chaperone protein ClpB/Hsp104 subfamily; Bacterial Caseinolytic peptidase B (ClpB) and ... |
410-608 |
9.54e-82 |
|
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: 256.72 E-value: 9.54e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 997579501 410 RLKNISSRLRSKIIGQDKAVEMVSRAIRRNRAGFDDGNRPIGSFLFVGPTGVGKTELAKQLAIDLFGNKEALIRLDMSEY 489
Cdd:cd19499 1 KLLNLEERLHERVVGQDEAVKAVSDAIRRARAGLSDPNRPIGSFLFLGPTGVGKTELAKALAELLFGDEDNLIRIDMSEY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 997579501 490 SDTTAVSKMIGTTAGYVGYDDnSNTLTEKVRRNPYSVILFDEIEKANPQILTLLLQVMDDGNLTDGQGNVINFKNTIIIC 569
Cdd:cd19499 81 MEKHSVSRLIGAPPGYVGYTE-GGQLTEAVRRKPYSVVLLDEIEKAHPDVQNLLLQVLDDGRLTDSHGRTVDFKNTIIIM 159
|
170 180 190
....*....|....*....|....*....|....*....
gi 997579501 570 TSNagfgngndteekdimhemkkFFRPEFLNRFNGIVEF 608
Cdd:cd19499 160 TSN--------------------HFRPEFLNRIDEIVVF 178
|
|
| AAA_2 |
pfam07724 |
AAA domain (Cdc48 subfamily); This Pfam entry includes some of the AAA proteins not detected ... |
448-602 |
1.44e-66 |
|
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: 216.68 E-value: 1.44e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 997579501 448 RPIGSFLFVGPTGVGKTELAKQLAIDLFGNKEALIRLDMSEYSDTTAVSKMIGTTAGYVGYDDNSnTLTEKVRRNPYSVI 527
Cdd:pfam07724 1 RPIGSFLFLGPTGVGKTELAKALAELLFGDERALIRIDMSEYMEEHSVSRLIGAPPGYVGYEEGG-QLTEAVRRKPYSIV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 997579501 528 LFDEIEKANPQILTLLLQVMDDGNLTDGQGNVINFKNTIIICTSNAG-----------FGNGNDTEEKDIMHEMKKFFRP 596
Cdd:pfam07724 80 LIDEIEKAHPGVQNDLLQILEGGTLTDKQGRTVDFKNTLFIMTGNFGsekisdasrlgDSPDYELLKEEVMDLLKKGFIP 159
|
....*.
gi 997579501 597 EFLNRF 602
Cdd:pfam07724 160 EFLGRL 165
|
|
| AAA_lid_9 |
pfam17871 |
AAA lid domain; This entry represents the alpha helical AAA+ lid domain that is found to the ... |
264-364 |
4.56e-31 |
|
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: 116.82 E-value: 4.56e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 997579501 264 SAKDTVEILKGIREKFETHHQVKLPDDVLKACVDLSIQYIPQRLLPDKAIDVLDITAAHL----SAQSPAIDKVttEKRI 339
Cdd:pfam17871 1 SVEEAIEILRGLKPKYEKHHGVRISDEALEAAVKLSKRYITDRFLPDKAIDLLDEACARVrlsqESKPEELEDL--EREL 78
|
90 100
....*....|....*....|....*
gi 997579501 340 SELEHDKRKAVSAEEYKKADDIQKE 364
Cdd:pfam17871 79 AKLEIEKEALEREQDFEKAERLAKL 103
|
|
| ClpB_D2-small |
smart01086 |
C-terminal, D2-small domain, of ClpB protein; This is the C-terminal domain of ClpB protein, ... |
611-698 |
1.96e-23 |
|
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: 94.82 E-value: 1.96e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 997579501 611 LDKDALQDIVNLLLDDVQVTLDKKGITMDVSQDAKDWLIEEGYDEELGARPLRRIVEQQVRDKITDYYL--DHTDVKHVD 688
Cdd:smart01086 1 LDKEDLVRIVDLPLNALQKRLAEKGITLEFTDEALDWLAEKGYDPKYGARPLRRIIQRELEDPLAELILsgELKDGDTVV 80
|
90
....*....|
gi 997579501 689 IDVEDNELVV 698
Cdd:smart01086 81 VDVDDGELVF 90
|
|
| ClpB_D2-small |
pfam10431 |
C-terminal, D2-small domain, of ClpB protein; This is the C-terminal domain of ClpB protein, ... |
611-689 |
3.51e-21 |
|
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: 87.85 E-value: 3.51e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 997579501 611 LDKDALQDIVNLLLDDVQVTLDKKGITMDVSQDAKDWLIEEGYDEELGARPLRRIVEQQVRDKITDYYLDH--TDVKHVD 688
Cdd:pfam10431 1 LSKEELRKIVDLQLKELQKRLAERGITLELTDAAKDWLAEKGYDPEYGARPLRRAIQREIEDPLAEEILSGelKEGDTVR 80
|
.
gi 997579501 689 I 689
Cdd:pfam10431 81 V 81
|
|
| AAA |
cd00009 |
The AAA+ (ATPases Associated with a wide variety of cellular Activities) superfamily ... |
101-260 |
3.74e-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: 3.74e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 997579501 101 IGRDKEIQETAEVLSRRTKNNPILVGEAGVGKTAIVEGLAQAIVEGNVPaaikdkeIISIDISSLEAGTQYRGAFEENIQ 180
Cdd:cd00009 1 VGQEEAIEALREALELPPPKNLLLYGPPGTGKTTLARAIANELFRPGAP-------FLYLNASDLLEGLVVAELFGHFLV 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 997579501 181 KLVEG-VKSSQNAVLFFDEIHQIigsgATGSDSGSKGLSDILKPAL-SRGEISIIGATTQDEYrnnIMKDAALTRRFNEV 258
Cdd:cd00009 74 RLLFElAEKAKPGVLFIDEIDSL----SRGAQNALLRVLETLNDLRiDRENVRVIGATNRPLL---GDLDRALYDRLDIR 146
|
..
gi 997579501 259 LV 260
Cdd:cd00009 147 IV 148
|
|
| AAA |
cd00009 |
The AAA+ (ATPases Associated with a wide variety of cellular Activities) superfamily ... |
423-608 |
2.41e-17 |
|
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: 79.50 E-value: 2.41e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 997579501 423 IGQDKAVEMVSRAIRRNragfddgnrPIGSFLFVGPTGVGKTELAKQLAIDLFGNKEALIRLDMSEYSDTTAVSKMIGTT 502
Cdd:cd00009 1 VGQEEAIEALREALELP---------PPKNLLLYGPPGTGKTTLARAIANELFRPGAPFLYLNASDLLEGLVVAELFGHF 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 997579501 503 AGYVgyddnsntLTEKVRRNPYSVILFDEIEKANPQILTLLLQVMDDGNLTdgqgnVINFKNTIIICTSNAGFGNgndte 582
Cdd:cd00009 72 LVRL--------LFELAEKAKPGVLFIDEIDSLSRGAQNALLRVLETLNDL-----RIDRENVRVIGATNRPLLG----- 133
|
170 180
....*....|....*....|....*.
gi 997579501 583 ekdimhemkkFFRPEFLNRFNGIVEF 608
Cdd:cd00009 134 ----------DLDRALYDRLDIRIVI 149
|
|
| AAA |
pfam00004 |
ATPase family associated with various cellular activities (AAA); AAA family proteins often ... |
123-259 |
2.20e-15 |
|
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: 73.01 E-value: 2.20e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 997579501 123 ILVGEAGVGKTAIVEGLAQAIvegnvpaaikDKEIISIDISSLEAgtQYRGAFEENIQKLVEGVKSSQNAVLFFDEIHQI 202
Cdd:pfam00004 2 LLYGPPGTGKTTLAKAVAKEL----------GAPFIEISGSELVS--KYVGESEKRLRELFEAAKKLAPCVIFIDEIDAL 69
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 997579501 203 IGSGATGSDSGSKGLSDILKPALSRGEIS-----IIGATTQ-DEYrnnimkDAALTRRFNEVL 259
Cdd:pfam00004 70 AGSRGSGGDSESRRVVNQLLTELDGFTSSnskviVIAATNRpDKL------DPALLGRFDRII 126
|
|
| SpoVK |
COG0464 |
AAA+-type ATPase, SpoVK/Ycf46/Vps4 family [Cell wall/membrane/envelope biogenesis, Cell cycle ... |
90-299 |
2.77e-13 |
|
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: 72.25 E-value: 2.77e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 997579501 90 QEARDGLLDPVIGRD---KEIQETAEVLSRRTK-------NNP---ILVGEAGVGKTAIVEGLAQAIvegnvpaaikDKE 156
Cdd:COG0464 149 LELREAILDDLGGLEevkEELRELVALPLKRPElreeyglPPPrglLLYGPPGTGKTLLARALAGEL----------GLP 218
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 997579501 157 IISIDISSLEAgtQYRGAFEENIQKLVEGVKSSQNAVLFFDEIHQIIGSGATGSDSGSKGLSDILKPAL--SRGEISIIG 234
Cdd:COG0464 219 LIEVDLSDLVS--KYVGETEKNLREVFDKARGLAPCVLFIDEADALAGKRGEVGDGVGRRVVNTLLTEMeeLRSDVVVIA 296
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 997579501 235 ATtqdeyrNNIMK-DAALTRRFNEVL-VNEPSAKDTVEILKGIREKFETHHQVKLpDDVLKACVDLS 299
Cdd:COG0464 297 AT------NRPDLlDPALLRRFDEIIfFPLPDAEERLEIFRIHLRKRPLDEDVDL-EELAEATEGLS 356
|
|
| SpoVK |
COG0464 |
AAA+-type ATPase, SpoVK/Ycf46/Vps4 family [Cell wall/membrane/envelope biogenesis, Cell cycle ... |
430-632 |
1.05e-11 |
|
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: 67.24 E-value: 1.05e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 997579501 430 EMVSRAIRRNRAGFDDGNRPIGSFLFVGPTGVGKTELAKQLAIDLFGNkeaLIRLDMSEYsdttaVSKMIGTTAGyvgyd 509
Cdd:COG0464 171 ELVALPLKRPELREEYGLPPPRGLLLYGPPGTGKTLLARALAGELGLP---LIEVDLSDL-----VSKYVGETEK----- 237
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 997579501 510 dNSNTLTEKVRRNPYSVILFDEIEKANP-----------QILTLLLQVMDDGNltdgqgnvinfKNTIIICTSNAgFGNG 578
Cdd:COG0464 238 -NLREVFDKARGLAPCVLFIDEADALAGkrgevgdgvgrRVVNTLLTEMEELR-----------SDVVVIAATNR-PDLL 304
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 997579501 579 NdteekdimhemkkffrPEFLNRFNGIVEFLHLDKDALQDIVNLLLDDVQVTLD 632
Cdd:COG0464 305 D----------------PALLRRFDEIIFFPLPDAEERLEIFRIHLRKRPLDED 342
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
454-572 |
3.12e-11 |
|
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: 62.01 E-value: 3.12e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 997579501 454 LFVGPTGVGKTELAKQLAIDLFGNKEALIRLDMSEYSDTTAVSKMIGTTAGYVGYDDNSNT---LTEKVRRNPYSVILFD 530
Cdd:smart00382 6 LIVGPPGSGKTTLARALARELGPPGGGVIYIDGEDILEEVLDQLLLIIVGGKKASGSGELRlrlALALARKLKPDVLILD 85
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 997579501 531 EIEKANPQILTLLLQVMDDGNLTDgqgNVINFKNTIIICTSN 572
Cdd:smart00382 86 EITSLLDAEQEALLLLLEELRLLL---LLKSEKNLTVILTTN 124
|
|
| RecA-like_protease |
cd19481 |
proteases similar to RecA; RecA-like NTPases. This family includes the NTP binding domain of ... |
427-572 |
4.14e-11 |
|
proteases similar to RecA; RecA-like NTPases. This family includes the NTP binding domain of F1 and V1 H(+)ATPases, DnaB and related helicases as well as bacterial RecA and related eukaryotic and archaeal recombinases. This group also includes bacterial conjugation proteins and related DNA transfer proteins involved in type II and type IV secretion.
Pssm-ID: 410889 [Multi-domain] Cd Length: 158 Bit Score: 61.92 E-value: 4.14e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 997579501 427 KAVEMVSRAIRRNRAGFDDGNRPIGSFLFVGPTGVGKTELAKQLAIDLfGNKeaLIRLDMSEYsdttaVSKMIGTTAgyv 506
Cdd:cd19481 3 ASLREAVEAPRRGSRLRRYGLGLPKGILLYGPPGTGKTLLAKALAGEL-GLP--LIVVKLSSL-----LSKYVGESE--- 71
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 997579501 507 gydDNSNTLTEKVRRNPYSVILFDEIEKANP------------QILTLLLQVMDDGNLTDgqgnvinfkNTIIICTSN 572
Cdd:cd19481 72 ---KNLRKIFERARRLAPCILFIDEIDAIGRkrdssgesgelrRVLNQLLTELDGVNSRS---------KVLVIAATN 137
|
|
| RecA-like_protease |
cd19481 |
proteases similar to RecA; RecA-like NTPases. This family includes the NTP binding domain of ... |
123-259 |
1.68e-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: 59.99 E-value: 1.68e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 997579501 123 ILVGEAGVGKTAIVEGLAQaivEGNVPaaikdkeIISIDISSLEagTQYRGAFEENIQKLVEGVKSSQNAVLFFDEIHQI 202
Cdd:cd19481 30 LLYGPPGTGKTLLAKALAG---ELGLP-------LIVVKLSSLL--SKYVGESEKNLRKIFERARRLAPCILFIDEIDAI 97
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 997579501 203 IGSGATGSDSG--SKGLSDILK---PALSRGEISIIGATtqdeyrNNI-MKDAALTR--RFNEVL 259
Cdd:cd19481 98 GRKRDSSGESGelRRVLNQLLTeldGVNSRSKVLVIAAT------NRPdLLDPALLRpgRFDEVI 156
|
|
| RPT1 |
COG1222 |
ATP-dependent 26S proteasome regulatory subunit [Posttranslational modification, protein ... |
420-629 |
9.78e-10 |
|
ATP-dependent 26S proteasome regulatory subunit [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440835 [Multi-domain] Cd Length: 326 Bit Score: 60.79 E-value: 9.78e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 997579501 420 SKIIGQDKAVEMVSRAI---RRNRAGFDD-GNRPIGSFLFVGPTGVGKTELAKQLAidlfGNKEA-LIRLDMSEYsdtta 494
Cdd:COG1222 78 DDIGGLDEQIEEIREAVelpLKNPELFRKyGIEPPKGVLLYGPPGTGKTLLAKAVA----GELGApFIRVRGSEL----- 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 997579501 495 VSKMIGTTAgyvgydDNSNTLTEKVRRNPYSVILFDEIE------------KANPQILTLLLQVMDDgnlTDGQGNVinf 562
Cdd:COG1222 149 VSKYIGEGA------RNVREVFELAREKAPSIIFIDEIDaiaarrtddgtsGEVQRTVNQLLAELDG---FESRGDV--- 216
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 997579501 563 kntIIICTSNAgfgngndteeKDIMHEmkKFFRPeflNRFNGIVEFLHLDKDALQDIVNLLLDDVQV 629
Cdd:COG1222 217 ---LIIAATNR----------PDLLDP--ALLRP---GRFDRVIEVPLPDEEAREEILKIHLRDMPL 265
|
|
| RPT1 |
COG1222 |
ATP-dependent 26S proteasome regulatory subunit [Posttranslational modification, protein ... |
91-287 |
6.39e-09 |
|
ATP-dependent 26S proteasome regulatory subunit [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440835 [Multi-domain] Cd Length: 326 Bit Score: 58.09 E-value: 6.39e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 997579501 91 EARDGLLDPVIGRDKEIQETAEVLSRRTKNNPI-------------LVGEAGVGKTAivegLAQAIV-EGNVPaaikdke 156
Cdd:COG1222 71 ESPDVTFDDIGGLDEQIEEIREAVELPLKNPELfrkygieppkgvlLYGPPGTGKTL----LAKAVAgELGAP------- 139
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 997579501 157 IISIDISSLeagTQ-YRGAFEENIQKLVEGVKSSQNAVLFFDEIHQIigsGATGSDSGSKGLSDILKPAL--------SR 227
Cdd:COG1222 140 FIRVRGSEL---VSkYIGEGARNVREVFELAREKAPSIIFIDEIDAI---AARRTDDGTSGEVQRTVNQLlaeldgfeSR 213
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 997579501 228 GEISIIGATtqdeyrNNI-MKDAALTR--RFNEVL-VNEPSAKDTVEILKGIREKFETHHQVKL 287
Cdd:COG1222 214 GDVLIIAAT------NRPdLLDPALLRpgRFDRVIeVPLPDEEAREEILKIHLRDMPLADDVDL 271
|
|
| MoxR |
COG0714 |
MoxR-like ATPase [General function prediction only]; MoxR-like ATPase is part of the Pathway ... |
403-556 |
6.89e-09 |
|
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: 57.48 E-value: 6.89e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 997579501 403 MDANDIERLknissrLRSKIIGQDKAVEMVSRAIRrnragfddGNRPIgsfLFVGPTGVGKTELAKQLA--IDLfgnkeA 480
Cdd:COG0714 1 MTEARLRAE------IGKVYVGQEELIELVLIALL--------AGGHL---LLEGVPGVGKTTLAKALAraLGL-----P 58
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 997579501 481 LIRLDMseYSDTTAvSKMIGTtagyvgYDDNSNTLTEKVRRNPY--SVILFDEIEKANPQILTLLLQVMDDGNLT-DGQ 556
Cdd:COG0714 59 FIRIQF--TPDLLP-SDILGT------YIYDQQTGEFEFRPGPLfaNVLLADEINRAPPKTQSALLEAMEERQVTiPGG 128
|
|
| CDC48 |
TIGR01243 |
AAA family ATPase, CDC48 subfamily; This subfamily of the AAA family ATPases includes two ... |
123-537 |
1.89e-08 |
|
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: 57.61 E-value: 1.89e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 997579501 123 ILVGEAGVGKTAIVEGLAQAIveGNVPAAIKDKEIISidissleagtQYRGAFEENIQKLVEGVKSSQNAVLFFDEIHQI 202
Cdd:TIGR01243 216 LLYGPPGTGKTLLAKAVANEA--GAYFISINGPEIMS----------KYYGESEERLREIFKEAEENAPSIIFIDEIDAI 283
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 997579501 203 IGSGATGSDSGSK-------GLSDILKpalSRGEISIIGATTqdeyRNNIMkDAALTR--RFN-EVLVNEPSAKDTVEIL 272
Cdd:TIGR01243 284 APKREEVTGEVEKrvvaqllTLMDGLK---GRGRVIVIGATN----RPDAL-DPALRRpgRFDrEIVIRVPDKRARKEIL 355
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 997579501 273 KgirekFETHHQVKLPDDVLKACVDLSIQYIPQrllpdkaidvlDITAAHLSAQSPAIDKVTTEKRISelehdkrkaVSA 352
Cdd:TIGR01243 356 K-----VHTRNMPLAEDVDLDKLAEVTHGFVGA-----------DLAALAKEAAMAALRRFIREGKIN---------FEA 410
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 997579501 353 EEYKKadDIQKEIKSLQDKLENSngehtavatVHDISDTIQRLTGIPVSQMDANDIERLKNISSRLRSKIIGQDKAVEMV 432
Cdd:TIGR01243 411 EEIPA--EVLKELKVTMKDFMEA---------LKMVEPSAIREVLVEVPNVRWSDIGGLEEVKQELREAVEWPLKHPEIF 479
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 997579501 433 SRAirrnragfddGNRPIGSFLFVGPTGVGKTELAKQLAIDLFGNkeaLIRLDMSEysdttAVSKMIGTTAGYVgyddns 512
Cdd:TIGR01243 480 EKM----------GIRPPKGVLLFGPPGTGKTLLAKAVATESGAN---FIAVRGPE-----ILSKWVGESEKAI------ 535
|
410 420
....*....|....*....|....*
gi 997579501 513 NTLTEKVRRNPYSVILFDEIEKANP 537
Cdd:TIGR01243 536 REIFRKARQAAPAIIFFDEIDAIAP 560
|
|
| AAA |
pfam00004 |
ATPase family associated with various cellular activities (AAA); AAA family proteins often ... |
454-572 |
4.16e-08 |
|
ATPase family associated with various cellular activities (AAA); AAA family proteins often perform chaperone-like functions that assist in the assembly, operation, or disassembly of protein complexes.
Pssm-ID: 459627 [Multi-domain] Cd Length: 130 Bit Score: 52.21 E-value: 4.16e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 997579501 454 LFVGPTGVGKTELAKQLAIDLFGNkeaLIRLDMSEysdttAVSKMIGTTAGYVgyddnsNTLTEKVRRNPYSVILFDEIE 533
Cdd:pfam00004 2 LLYGPPGTGKTTLAKAVAKELGAP---FIEISGSE-----LVSKYVGESEKRL------RELFEAAKKLAPCVIFIDEID 67
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 997579501 534 KANP-----------QILTLLLQVMDDgnLTDGQGNVinfkntIIICTSN 572
Cdd:pfam00004 68 ALAGsrgsggdsesrRVVNQLLTELDG--FTSSNSKV------IVIAATN 109
|
|
| COG1223 |
COG1223 |
Predicted ATPase, AAA+ superfamily [General function prediction only]; |
420-633 |
4.61e-08 |
|
Predicted ATPase, AAA+ superfamily [General function prediction only];
Pssm-ID: 440836 [Multi-domain] Cd Length: 246 Bit Score: 54.50 E-value: 4.61e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 997579501 420 SKIIGQDKAVEMVSRAIR-----RNRAGFddGNRPIGSFLFVGPTGVGKTELAKQLAIDLfgNKEAL-IRLDmseysdtT 493
Cdd:COG1223 2 DDVVGQEEAKKKLKLIIKelrrrENLRKF--GLWPPRKILFYGPPGTGKTMLAEALAGEL--KLPLLtVRLD-------S 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 997579501 494 AVSKMIGTTAGyvgyddNSNTLTEKVRRNPySVILFDEI-----EKANPQ-------ILTLLLQVMDDGNltdgqgnvin 561
Cdd:COG1223 71 LIGSYLGETAR------NLRKLFDFARRAP-CVIFFDEFdaiakDRGDQNdvgevkrVVNALLQELDGLP---------- 133
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 997579501 562 fKNTIIICTSNagfgngndteekdimhemkkffRPEFLN-----RFNGIVEFLHLDKDALQDIVNLLLDDVQVTLDK 633
Cdd:COG1223 134 -SGSVVIAATN----------------------HPELLDsalwrRFDEVIEFPLPDKEERKEILELNLKKFPLPFEL 187
|
|
| AAA_5 |
pfam07728 |
AAA domain (dynein-related subfamily); This Pfam entry includes some of the AAA proteins not ... |
452-572 |
9.20e-08 |
|
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: 51.52 E-value: 9.20e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 997579501 452 SFLFVGPTGVGKTELAKQLAiDLFGNKEALIrldMSEYSDTTAvSKMIG---TTAGYVGYDDNSntLTEKVRRNpySVIL 528
Cdd:pfam07728 1 GVLLVGPPGTGKTELAERLA-AALSNRPVFY---VQLTRDTTE-EDLFGrrnIDPGGASWVDGP--LVRAAREG--EIAV 71
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 997579501 529 FDEIEKANPQILTLLLQVMDDGNLT--DGqGNVINFKNT--IIICTSN 572
Cdd:pfam07728 72 LDEINRANPDVLNSLLSLLDERRLLlpDG-GELVKAAPDgfRLIATMN 118
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
118-263 |
1.23e-07 |
|
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a variety of cellular activities. This profile/alignment only detects a fraction of this vast family. The poorly conserved N-terminal helix is missing from the alignment.
Pssm-ID: 214640 [Multi-domain] Cd Length: 148 Bit Score: 51.61 E-value: 1.23e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 997579501 118 TKNNPILVGEAGVGKTAIVEGLAQAIVEGNVPAAIKDKEIISIDISS-----LEAGTQYRGAFEENIQKLVEGVKSSQNA 192
Cdd:smart00382 1 PGEVILIVGPPGSGKTTLARALARELGPPGGGVIYIDGEDILEEVLDqllliIVGGKKASGSGELRLRLALALARKLKPD 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 997579501 193 VLFFDEIHQIIGSgATGSDSGSKGLSDILKPALSRGEISIIGATTqdeyRNNIMKDAALTRRFNEVLVNEP 263
Cdd:smart00382 81 VLILDEITSLLDA-EQEALLLLLEELRLLLLLKSEKNLTVILTTN----DEKDLGPALLRRRFDRRIVLLL 146
|
|
| DnaX |
COG2812 |
DNA polymerase III, gamma/tau subunits [Replication, recombination and repair]; |
420-471 |
1.60e-06 |
|
DNA polymerase III, gamma/tau subunits [Replication, recombination and repair];
Pssm-ID: 442061 [Multi-domain] Cd Length: 340 Bit Score: 50.58 E-value: 1.60e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 997579501 420 SKIIGQDKAVEMVSRAIRRNRagfddgnrpIG-SFLFVGPTGVGKTELAKQLA 471
Cdd:COG2812 10 DDVVGQEHVVRTLKNALASGR---------LAhAYLFTGPRGVGKTTLARILA 53
|
|
| RecA-like_HslU |
cd19498 |
ATP-dependent protease ATPase subunit HslU; HslU is a component of the ATP-dependent protease ... |
412-534 |
1.60e-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: 48.92 E-value: 1.60e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 997579501 412 KNISSRLRSKIIGQDKAVEMVSRAIRrNR-------AGFDDGNRPiGSFLFVGPTGVGKTELAKQLAiDLFGnkEALIRL 484
Cdd:cd19498 3 REIVSELDKYIIGQDEAKRAVAIALR-NRwrrmqlpEELRDEVTP-KNILMIGPTGVGKTEIARRLA-KLAG--APFIKV 77
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 997579501 485 DMSEYsdttavskmigTTAGYVGYDdnsntlTEKVRRNPYSVILF-DEIEK 534
Cdd:cd19498 78 EATKF-----------TEVGYVGRD------VESIIRDLVEGIVFiDEIDK 111
|
|
| COG1223 |
COG1223 |
Predicted ATPase, AAA+ superfamily [General function prediction only]; |
97-299 |
4.02e-06 |
|
Predicted ATPase, AAA+ superfamily [General function prediction only];
Pssm-ID: 440836 [Multi-domain] Cd Length: 246 Bit Score: 48.73 E-value: 4.02e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 997579501 97 LDPVIGRDKEIQETAEVLS--------RRTKNNP----ILVGEAGVGKTAIVEGLAQaivEGNVPaaikdkeIISIDISS 164
Cdd:COG1223 1 LDDVVGQEEAKKKLKLIIKelrrrenlRKFGLWPprkiLFYGPPGTGKTMLAEALAG---ELKLP-------LLTVRLDS 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 997579501 165 LEagTQYRGAFEENIQKLVEGVKSSQnAVLFFDEIHQIigsgatGSDSGSKGLSDILKPALS---------RGEISIIGA 235
Cdd:COG1223 71 LI--GSYLGETARNLRKLFDFARRAP-CVIFFDEFDAI------AKDRGDQNDVGEVKRVVNallqeldglPSGSVVIAA 141
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 997579501 236 TTQDEyrnniMKDAALTRRFNEVL-VNEPSAKDTVEILKGIREKFEthHQVKLPDDVL-KACVDLS 299
Cdd:COG1223 142 TNHPE-----LLDSALWRRFDEVIeFPLPDKEERKEILELNLKKFP--LPFELDLKKLaKKLEGLS 200
|
|
| CDC6 |
COG1474 |
Cdc6-related protein, AAA superfamily ATPase [Replication, recombination and repair]; |
100-362 |
9.51e-06 |
|
Cdc6-related protein, AAA superfamily ATPase [Replication, recombination and repair];
Pssm-ID: 441083 [Multi-domain] Cd Length: 389 Bit Score: 48.31 E-value: 9.51e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 997579501 100 VIGRDKEIQETAEVLSRRTKNNP----ILVGEAGVGKTAIVEGLAQAIVEGnvpAAIKDKEIISIDISSLEAGTQY---- 171
Cdd:COG1474 28 LPHREEEIEELASALRPALRGERpsnvLIYGPTGTGKTAVAKYVLEELEEE---AEERGVDVRVVYVNCRQASTRYrvls 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 997579501 172 --------------RG-AFEENIQKLVEGV-KSSQNAVLFFDEIHQIigsgatGSDSGSKGLSDILK--PALSRGEISII 233
Cdd:COG1474 105 rileelgsgedipsTGlSTDELFDRLYEALdERDGVLVVVLDEIDYL------VDDEGDDLLYQLLRanEELEGARVGVI 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 997579501 234 GATTQDEYRNNImkDAALTRRFNEVLVN-EP-SAKDTVEILK-----GIREKfethhqvKLPDDVLKACVDLSIQyipqr 306
Cdd:COG1474 179 GISNDLEFLENL--DPRVKSSLGEEEIVfPPyDADELRDILEdraelAFYDG-------VLSDEVIPLIAALAAQ----- 244
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 997579501 307 llpD-----KAIDVLD-------------ITAAHLSAQSPAIDKVTTEKRISEL-EHDKR--KAVSAEEYKKADDIQ 362
Cdd:COG1474 245 ---EhgdarKAIDLLRvageiaeregsdrVTEEHVREAREKIERDRLLEVLRGLpTHEKLvlLAIAELLKDGEDPVR 318
|
|
| PRK13342 |
PRK13342 |
recombination factor protein RarA; Reviewed |
123-237 |
1.20e-05 |
|
recombination factor protein RarA; Reviewed
Pssm-ID: 237355 [Multi-domain] Cd Length: 413 Bit Score: 48.16 E-value: 1.20e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 997579501 123 ILVGEAGVGKTAIVEGLAQAIvegnvpaaikDKEIISIdiSSLEAGT-QYRGAFEENIQKLVEGvkssQNAVLFFDEIHQ 201
Cdd:PRK13342 40 ILWGPPGTGKTTLARIIAGAT----------DAPFEAL--SAVTSGVkDLREVIEEARQRRSAG----RRTILFIDEIHR 103
|
90 100 110
....*....|....*....|....*....|....*.
gi 997579501 202 IigsgatgsdsgSKGLSDILKPALSRGEISIIGATT 237
Cdd:PRK13342 104 F-----------NKAQQDALLPHVEDGTITLIGATT 128
|
|
| FlhF |
COG1419 |
Flagellar biosynthesis GTPase FlhF [Cell motility]; |
329-485 |
1.38e-05 |
|
Flagellar biosynthesis GTPase FlhF [Cell motility];
Pssm-ID: 441029 [Multi-domain] Cd Length: 361 Bit Score: 47.94 E-value: 1.38e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 997579501 329 AIDKVTTEKRISELEHDKRKAVSAEEyKKADDIQKEIKSLQDKLEN-SNGEHTAVATVHDISDTIQRLtgipvsqMDAND 407
Cdd:COG1419 48 AVDEDEAEKAPAAAAAPAAASAAAEE-EELEELRRELAELKELLEEqLSGLAGESARLPPELAELLER-------LLEAG 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 997579501 408 IErlKNISSRLRSKI---IGQDKAVEMVSRAIRRNragFDDGNRPIGS----FLFVGPTGVGKT-ELAKqLAID--LFGN 477
Cdd:COG1419 120 VS--PELARELLEKLpedLSAEEAWRALLEALARR---LPVAEDPLLDeggvIALVGPTGVGKTtTIAK-LAARfvLRGK 193
|
....*....
gi 997579501 478 KE-ALIRLD 485
Cdd:COG1419 194 KKvALITTD 202
|
|
| FlhF |
TIGR03499 |
flagellar biosynthetic protein FlhF; [Cellular processes, Chemotaxis and motility] |
265-485 |
4.37e-05 |
|
flagellar biosynthetic protein FlhF; [Cellular processes, Chemotaxis and motility]
Pssm-ID: 274609 [Multi-domain] Cd Length: 282 Bit Score: 45.79 E-value: 4.37e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 997579501 265 AKDTVEILKGIREKfethhqvkLPDDVLKacvdLSIQYIPQRLLPDKAIDVL--------------DITAAHLSAQSPAI 330
Cdd:TIGR03499 8 APTMREALKKVKEE--------LGPDAVI----LSTRKVRKGLFGKKFVEVTaaideeeaaaasaeEEASKALEQADPKP 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 997579501 331 DKVTTEKRISEL---EHDKRKAVSAEEYKKADDIQKEIKSLQDKLENSNGEHTAVATVHDISDTIQRLtgipvsqmDAND 407
Cdd:TIGR03499 76 LSATAEPLELPApqeEPAAPAAQAAEPLLPEEELRKELEALRELLERLLAGLAWLQRPPERAKLYERL--------LEAG 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 997579501 408 IErlKNISSRLRSKIIGQ---DKAVEMVSRAIRRNRAgFDDGNRPIGS----FLFVGPTGVGKT----ELAKQLAIDLFG 476
Cdd:TIGR03499 148 VS--EELARELLEKLPEDadaEDAWRWLREALEGMLP-VKPEEDPILEqggvIALVGPTGVGKTttlaKLAARFALEHGK 224
|
....*....
gi 997579501 477 NKEALIRLD 485
Cdd:TIGR03499 225 KKVALITTD 233
|
|
| flhF |
PRK05703 |
flagellar biosynthesis protein FlhF; |
298-485 |
5.63e-05 |
|
flagellar biosynthesis protein FlhF;
Pssm-ID: 235570 [Multi-domain] Cd Length: 424 Bit Score: 46.04 E-value: 5.63e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 997579501 298 LSIQYIPQRLLPDKAIDVLDITAAHLSAQSPAIDKVTTEKRISELEHDKRKAVSAEEYkkaDDIQKEIKSLQDKLEnsng 377
Cdd:PRK05703 75 LSLQALLEKRPSRTNSQDALLQAENALPEWKKELEKPSEPKEEEPKAAAESKVVQKEL---DELRDELKELKNLLE---- 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 997579501 378 ehtavatvHDISDTIQRLTGIPVSqmdANDIERLKN--ISSRLRSKIIG---------QDKAVEMVSRAIRRN-RAGFDD 445
Cdd:PRK05703 148 --------DQLSGLRQVERIPPEF---AELYKRLKRsgLSPEIAEKLLKlllehmpprERTAWRYLLELLANMiPVRVED 216
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 997579501 446 GNRPIGSFLFVGPTGVGK-TELAKqLA---IDLFGNKE-ALIRLD 485
Cdd:PRK05703 217 ILKQGGVVALVGPTGVGKtTTLAK-LAaryALLYGKKKvALITLD 260
|
|
| AAA_16 |
pfam13191 |
AAA ATPase domain; This family of domains contain a P-loop motif that is characteriztic of the ... |
99-148 |
5.65e-05 |
|
AAA ATPase domain; This family of domains contain a P-loop motif that is characteriztic of the AAA superfamily.
Pssm-ID: 433025 [Multi-domain] Cd Length: 167 Bit Score: 44.03 E-value: 5.65e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 997579501 99 PVIGRDKEIQETAEVLSRRTKNNP---ILVGEAGVGKTAIVEGLAQAIVEGNV 148
Cdd:pfam13191 1 RLVGREEELEQLLDALDRVRSGRPpsvLLTGEAGTGKTTLLRELLRALERDGG 53
|
|
| RecA-like_CDC48_NLV2_r1-like |
cd19503 |
first of two ATPase domains of CDC48 and NLV2, and similar ATPase domains; CDC48 in yeast and ... |
123-255 |
5.89e-05 |
|
first of two ATPase domains of CDC48 and NLV2, and similar ATPase domains; CDC48 in yeast and p97 or VCP metazoans is an ATP-dependent molecular chaperone which plays an essential role in many cellular processes, by segregating polyubiquitinated proteins from complexes or membranes. Cdc48/p97 consists of an N-terminal domain and two ATPase domains; this subfamily represents the first of the two ATPase domains. This subfamily also includes the first of the two ATPase domains of NVL (nuclear VCP-like protein) 2, an isoform of NVL mainly present in the nucleolus, which is involved in ribosome biogenesis, in telomerase assembly and the regulation of telomerase activity, and in pre-rRNA processing. This subfamily belongs to the RecA-like NTPase family which includes the NTP binding domain of F1 and V1 H(+)ATPases, DnaB and related helicases as well as bacterial RecA and related eukaryotic and archaeal recombinases. The RecA-like NTPase family also includes bacterial conjugation proteins and related DNA transfer proteins involved in type II and type IV secretion.
Pssm-ID: 410911 [Multi-domain] Cd Length: 165 Bit Score: 44.20 E-value: 5.89e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 997579501 123 ILVGEAGVGKTAIVEGLAQaivEGNVPA-AIKDKEIISidissleagtQYRGAFEENIQKLVEGVKSSQNAVLFFDEIHQ 201
Cdd:cd19503 38 LLHGPPGTGKTLLARAVAN---EAGANFlSISGPSIVS----------KYLGESEKNLREIFEEARSHAPSIIFIDEIDA 104
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 997579501 202 IIGS-GATGSDSGSK------GLSDILKpalSRGEISIIGATTqdeyRNNIMkDAALTR--RF 255
Cdd:cd19503 105 LAPKrEEDQREVERRvvaqllTLMDGMS---SRGKVVVIAATN----RPDAI-DPALRRpgRF 159
|
|
| clpX |
PRK05342 |
ATP-dependent Clp protease ATP-binding subunit ClpX; |
412-701 |
1.14e-04 |
|
ATP-dependent Clp protease ATP-binding subunit ClpX;
Pssm-ID: 235422 [Multi-domain] Cd Length: 412 Bit Score: 45.15 E-value: 1.14e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 997579501 412 KNISSRLRSKIIGQDKAVEMVSRA-------IRRNRAGFDDG-----NrpIgsfLFVGPTGVGKTELAKQLAidlfgnke 479
Cdd:PRK05342 63 KEIKAHLDQYVIGQERAKKVLSVAvynhykrLRHGDKKDDDVelqksN--I---LLIGPTGSGKTLLAQTLA-------- 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 997579501 480 aliR-LD----MSeysDTTAVskmigTTAGYVGyDDNSNTLTEKVRRNPYSV------ILF-DEIEK-----ANPQI--- 539
Cdd:PRK05342 130 ---RiLDvpfaIA---DATTL-----TEAGYVG-EDVENILLKLLQAADYDVekaqrgIVYiDEIDKiarksENPSItrd 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 997579501 540 ----------LTLL----LQVMDDGnltdGQGNV------INFKNTIIIC----------------TSNAGFG-----NG 578
Cdd:PRK05342 198 vsgegvqqalLKILegtvASVPPQG----GRKHPqqefiqVDTTNILFICggafdglekiikqrlgKKGIGFGaevksKK 273
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 997579501 579 NDTEEKDIMHE-----MKKF-FRPEFLNRFNgIVEFLH-LDKDALQDIV----NLLLDDVQVTLDKKGITMDVSQDAKDW 647
Cdd:PRK05342 274 EKRTEGELLKQvepedLIKFgLIPEFIGRLP-VVATLEeLDEEALVRILtepkNALVKQYQKLFEMDGVELEFTDEALEA 352
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
gi 997579501 648 LIEEGYDEELGARPLRRIVEQQVRDkiTDYYL-DHTDVKHVDIDvednELVVKGK 701
Cdd:PRK05342 353 IAKKAIERKTGARGLRSILEEILLD--VMFELpSREDVEKVVIT----KEVVEGK 401
|
|
| RecA-like_VPS4-like |
cd19509 |
ATPase domain of VPS4, ATAD1, K, KTNA1, Spastin, FIGL-1 and similar ATPase domains; This ... |
123-255 |
3.34e-04 |
|
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: 41.95 E-value: 3.34e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 997579501 123 ILVGEAGVGKTAivegLAQAIvegnvpAAIKDKEIISIDISSLEAgtQYRGAFEENIQKLVEGVKSSQNAVLFFDEIHQI 202
Cdd:cd19509 36 LLYGPPGTGKTL----LARAV------ASESGSTFFSISASSLVS--KWVGESEKIVRALFALARELQPSIIFIDEIDSL 103
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 997579501 203 IGSGATGSDSGSKGL-SDILK-----PALSRGEISIIGATTqdeyRNNIMKDAALtRRF 255
Cdd:cd19509 104 LSERGSGEHEASRRVkTEFLVqmdgvLNKPEDRVLVLGATN----RPWELDEAFL-RRF 157
|
|
| RecA-like_NVL_r1-like |
cd19518 |
first of two ATPase domains of NVL (nuclear VCP-like protein) and similar ATPase domains; NVL ... |
430-560 |
4.22e-04 |
|
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: 41.62 E-value: 4.22e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 997579501 430 EMVSRAIRRNRAGFDDGNRPIGSFLFVGPTGVGKTELAKQLAIDLfgnkealiRLDMSEYSDTTAVSKMIGTTagyvgyD 509
Cdd:cd19518 14 ELLIHPILPPEYFQHLGVEPPRGVLLHGPPGCGKTMLANAIAGEL--------KVPFLKISATEIVSGVSGES------E 79
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 997579501 510 DNSNTLTEKVRRNPYSVILFDEIEKANPQ-----------ILTLLLQVMDDGNL--TDGQGNVI 560
Cdd:cd19518 80 EKIRELFDQAISNAPCIVFIDEIDAITPKresaqremerrIVSQLLTCMDELNNekTAGGPVLV 143
|
|
| COG3899 |
COG3899 |
Predicted ATPase [General function prediction only]; |
80-148 |
4.23e-04 |
|
Predicted ATPase [General function prediction only];
Pssm-ID: 443106 [Multi-domain] Cd Length: 1244 Bit Score: 43.69 E-value: 4.23e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 997579501 80 YLEQIGRNLTQEARDGLLDPVIGRDKEIQETAEVLSRRTKNNPILV---GEAGVGKTAIVEGLAQAIVEGNV 148
Cdd:COG3899 269 LLAAAAAGRRLLARRLIPQPLVGREAELAALLAALERARAGRGELVlvsGEAGIGKSRLVRELARRARARGG 340
|
|
| PRK07399 |
PRK07399 |
DNA polymerase III subunit delta'; Validated |
420-475 |
6.37e-04 |
|
DNA polymerase III subunit delta'; Validated
Pssm-ID: 236011 [Multi-domain] Cd Length: 314 Bit Score: 42.58 E-value: 6.37e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 997579501 420 SKIIGQDKAVEMVSRAIRRNRAGfddgnrPigSFLFVGPTGVGKTELAKQLAIDLF 475
Cdd:PRK07399 4 ANLIGQPLAIELLTAAIKQNRIA------P--AYLFAGPEGVGRKLAALCFIEGLL 51
|
|
| hslU |
PRK05201 |
ATP-dependent protease ATPase subunit HslU; |
412-471 |
1.19e-03 |
|
ATP-dependent protease ATPase subunit HslU;
Pssm-ID: 235364 [Multi-domain] Cd Length: 443 Bit Score: 41.99 E-value: 1.19e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 997579501 412 KNISSRLRSKIIGQDKAVEMVSRAIRrNR---AGFDDGNR----P--IgsfLFVGPTGVGKTELAKQLA 471
Cdd:PRK05201 7 REIVSELDKYIIGQDDAKRAVAIALR-NRwrrMQLPEELRdevtPknI---LMIGPTGVGKTEIARRLA 71
|
|
| RecA-like_CDC48_r2-like |
cd19511 |
second of two ATPase domains of CDC48/p97, PEX1 and -6, VAT and NVL, and similar ATPase ... |
123-259 |
1.31e-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: 39.96 E-value: 1.31e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 997579501 123 ILVGEAGVGKTAIVEGLAQaivEGNVP-AAIKDKEIISidissleagtQYRGAFEENIQKLVEGVKSSQNAVLFFDEIHQ 201
Cdd:cd19511 31 LLYGPPGCGKTLLAKALAS---EAGLNfISVKGPELFS----------KYVGESERAVREIFQKARQAAPCIIFFDEIDS 97
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 997579501 202 IIG--SGATGSDSGSKGLSDILKP---ALSRGEISIIGATTQDEyrnniMKDAALTR--RFNEVL 259
Cdd:cd19511 98 LAPrrGQSDSSGVTDRVVSQLLTEldgIESLKGVVVIAATNRPD-----MIDPALLRpgRLDKLI 157
|
|
| RecA-like_NVL_r1-like |
cd19518 |
first of two ATPase domains of NVL (nuclear VCP-like protein) and similar ATPase domains; NVL ... |
123-258 |
1.37e-03 |
|
first of two ATPase domains of NVL (nuclear VCP-like protein) and similar ATPase domains; NVL exists in two forms with N-terminal extensions of different lengths in mammalian cells. NVL has two alternatively spliced isoforms, a short form, NVL1, and a long form, NVL2. NVL2, the major species, is mainly present in the nucleolus, whereas NVL1 is nucleoplasmic. Each has an N-terminal domain, followed by two tandem ATPase domains; this subfamily includes the first of the two ATPase domains. NVL2 is involved in the biogenesis of the 60S ribosome subunit by associating specifically with ribosome protein L5 and modulating the function of DOB1. NVL2 is also required for telomerase assembly and the regulation of telomerase activity, and is involved in pre-rRNA processing. The role of NVL1 is unclear. This RecA-like_NVL_r1-like subfamily belongs to the RecA-like NTPase family which includes the NTP binding domain of F1 and V1 H(+)ATPases, DnaB and related helicases as well as bacterial RecA and related eukaryotic and archaeal recombinases. The RecA-like NTPase family also includes bacterial conjugation proteins and related DNA transfer proteins involved in type II and type IV secretion.
Pssm-ID: 410926 [Multi-domain] Cd Length: 169 Bit Score: 40.08 E-value: 1.37e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 997579501 123 ILVGEAGVGKTAivegLAQAIV-EGNVPaaikdkeIISIDISSLEAGTQyrGAFEENIQKLVEGVKSSQNAVLFFDEIHQ 201
Cdd:cd19518 38 LLHGPPGCGKTM----LANAIAgELKVP-------FLKISATEIVSGVS--GESEEKIRELFDQAISNAPCIVFIDEIDA 104
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 997579501 202 IIGSGATGSDSGSK--------GLSDILKPALSRGEISIIGATTQDEyrnniMKDAALTR--RF-NEV 258
Cdd:cd19518 105 ITPKRESAQREMERrivsqlltCMDELNNEKTAGGPVLVIGATNRPD-----SLDPALRRagRFdREI 167
|
|
| RecA-like_PEX6_r2 |
cd19527 |
second of two ATPase domains of Peroxisomal biogenesis factor 6 (PEX6); PEX6(also known as ... |
117-259 |
1.44e-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: 1.44e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 997579501 117 RTKNNPILVGEAGVGKTAIVEGLAQAIVEGNVpaAIKDKEIISIdissleagtqYRGAFEENIQKLVEGVKSSQNAVLFF 196
Cdd:cd19527 24 RKRSGILLYGPPGTGKTLLAKAIATECSLNFL--SVKGPELINM----------YIGESEANVREVFQKARDAKPCVIFF 91
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 997579501 197 DEIHQIIGSGATGSDSG-------SKGLSDILKPALSRGEISIIGATTQDEyrnniMKDAALTR--RFNEVL 259
Cdd:cd19527 92 DELDSLAPSRGNSGDSGgvmdrvvSQLLAELDGMSSSGQDVFVIGATNRPD-----LLDPALLRpgRFDKLL 158
|
|
| RecA-like_ClpB_Hsp104-like |
cd19499 |
Chaperone protein ClpB/Hsp104 subfamily; Bacterial Caseinolytic peptidase B (ClpB) and ... |
93-199 |
1.44e-03 |
|
Chaperone protein ClpB/Hsp104 subfamily; Bacterial Caseinolytic peptidase B (ClpB) and eukaryotic Heat shock protein 104 (Hsp104) are ATP-dependent molecular chaperones and essential proteins of the heat-shock response. ClpB/Hsp104 ATPases, in concert with the DnaK/Hsp70 chaperone system, disaggregate and reactivate aggregated proteins. This RecA-like_ClpB_Hsp104_like subfamily belongs to the RecA-like NTPase family which includes the NTP binding domain of F1 and V1 H(+)ATPases, DnaB and related helicases as well as bacterial RecA and related eukaryotic and archaeal recombinases. The RecA-like NTPase family also includes bacterial conjugation proteins and related DNA transfer proteins involved in type II and type IV secretion.
Pssm-ID: 410907 [Multi-domain] Cd Length: 178 Bit Score: 40.24 E-value: 1.44e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 997579501 93 RDGLLDPVIGRDKEIQETAEVLSR-----RTKNNPI----LVGEAGVGKTAIVEGLAQAIVEGNvpaaikdKEIISIDIS 163
Cdd:cd19499 6 EERLHERVVGQDEAVKAVSDAIRRaraglSDPNRPIgsflFLGPTGVGKTELAKALAELLFGDE-------DNLIRIDMS 78
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 997579501 164 SL-EAGTQ---------YRGafEENIQKLVEGVKSSQNAVLFFDEI 199
Cdd:cd19499 79 EYmEKHSVsrligappgYVG--YTEGGQLTEAVRRKPYSVVLLDEI 122
|
|
| RecA-like_Yta7-like |
cd19517 |
ATPase domain of Saccharomyces cerevisiae Yta7 and similar ATPase domains; Saccharomyces ... |
454-560 |
1.51e-03 |
|
ATPase domain of Saccharomyces cerevisiae Yta7 and similar ATPase domains; Saccharomyces cerevisiae Yta7 is a chromatin-associated AAA-ATPase involved in regulation of chromatin dynamics. Its human ortholog ANCCA/ATAD2 transcriptionally activates pathways of malignancy in a broad range of cancers. The RecA-like_Yta7 subfamily belongs to the RecA-like NTPase family which includes the NTP binding domain of F1 and V1 H(+)ATPases, DnaB and related helicases as well as bacterial RecA and related eukaryotic and archaeal recombinases. The RecA-like NTPase family also includes bacterial conjugation proteins and related DNA transfer proteins involved in type II and type IV secretion.
Pssm-ID: 410925 [Multi-domain] Cd Length: 170 Bit Score: 40.19 E-value: 1.51e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 997579501 454 LFVGPTGVGKTELAKQLAIDLfGNKEALIRLDMSEYSDttAVSKMIGTTagyvgyDDNSNTLTEKVRRNPYSVILFDEIE 533
Cdd:cd19517 38 LFHGPPGTGKTLMARALAAEC-SKGGQKVSFFMRKGAD--CLSKWVGEA------ERQLRLLFEEAYRMQPSIIFFDEID 108
|
90 100 110
....*....|....*....|....*....|....*...
gi 997579501 534 KANP-----------QILTLLLQVMDDgnlTDGQGNVI 560
Cdd:cd19517 109 GLAPvrsskqeqihaSIVSTLLALMDG---LDNRGQVV 143
|
|
| RecA-like_VCP_r2 |
cd19529 |
second of two ATPase domains of Valosin-containing protein-like ATPase (VAT) and similar ... |
123-259 |
1.96e-03 |
|
second of two ATPase domains of Valosin-containing protein-like ATPase (VAT) and similar ATPase domains; The Valosin-containing protein-like ATPase of Thermoplasma acidophilum (VAT), is an archaeal homolog of the ubiquitous Cdc48/p97. It is a protein unfoldase that functions in concert with the 20S proteasome by unfolding proteasome substrates and passing them on for degradation. VAT forms a homohexamer, each monomer contains two tandem ATPase domains, referred to as D1 and D2, and an N-terminal domain. 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: 410937 [Multi-domain] Cd Length: 159 Bit Score: 39.40 E-value: 1.96e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 997579501 123 ILVGEAGVGKTAIVEGLAQaivEGNVP-AAIKDKEIISidissleagtQYRGAFEENIQKLVEGVKSSQNAVLFFDEIHQ 201
Cdd:cd19529 31 LLYGPPGTGKTLLAKAVAT---ESNANfISVKGPELLS----------KWVGESEKAIREIFRKARQVAPCVIFFDEIDS 97
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 997579501 202 IIGSGATGSDSG------SKGLS--DILKPAlsrGEISIIGATTqdeyRNNIMkDAALTR--RFNEVL 259
Cdd:cd19529 98 IAPRRGTTGDSGvtervvNQLLTelDGLEEM---NGVVVIAATN----RPDII-DPALLRagRFDRLI 157
|
|
| PRK12723 |
PRK12723 |
flagellar biosynthesis regulator FlhF; Provisional |
340-479 |
2.09e-03 |
|
flagellar biosynthesis regulator FlhF; Provisional
Pssm-ID: 183702 [Multi-domain] Cd Length: 388 Bit Score: 41.04 E-value: 2.09e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 997579501 340 SELEHDKRK---AVSAEEYKKADDIQKEIKSLQDKLENS--NGEHTAVATVHD-----------ISDTIQRLTG-IPVSQ 402
Cdd:PRK12723 64 INVEDEKRKilqSIKKEENSSIEDVLKEVKSLKNELAHKkeEINHPTILKIEDilrendfsesyIKDINEFIKKeFSLSD 143
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 997579501 403 MDanDIERLknissrlrskiigQDKAVEMVSRAIRRNRAGFDDGNRPIgsFLFVGPTGVGK-TELAKQLAIDLFGNKE 479
Cdd:PRK12723 144 LD--DYDKV-------------RDSVIIYIAKTIKCSGSIIDNLKKRV--FILVGPTGVGKtTTIAKLAAIYGINSDD 204
|
|
| RecA-like_ClpX |
cd19497 |
ATP-dependent Clp protease ATP-binding subunit ClpX; ClpX is a component of the ATP-dependent ... |
412-539 |
2.09e-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: 40.28 E-value: 2.09e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 997579501 412 KNISSRLRSKIIGQDKAVEMVSRAI----RRNRAGFDDGNRPI----GSFLFVGPTGVGKTELAKQLAIDLfgNKEALIr 483
Cdd:cd19497 4 KEIKEHLDKYVIGQERAKKVLSVAVynhyKRIRNNLKQKDDDVelekSNILLIGPTGSGKTLLAQTLAKIL--DVPFAI- 80
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 997579501 484 ldmseySDTTAVskmigTTAGYVGyDDNSNTLTE-------KVRRNPYSVILFDEIEK-----ANPQI 539
Cdd:cd19497 81 ------ADATTL-----TEAGYVG-EDVENILLKllqaadyDVERAQRGIVYIDEIDKiarksENPSI 136
|
|
| DNA_pol3_delta2 |
pfam13177 |
DNA polymerase III, delta subunit; DNA polymerase III, delta subunit (EC 2.7.7.7) is required ... |
424-475 |
2.43e-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: 39.12 E-value: 2.43e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 997579501 424 GQDKAVEMVSRAIRRNRAGFddgnrpigSFLFVGPTGVGKTELAKQLAIDLF 475
Cdd:pfam13177 1 GQPEAIQLLQNSLENGRLSH--------AYLFSGPEGVGKLELALAFAKALF 44
|
|
| HslU |
COG1220 |
ATP-dependent protease HslVU (ClpYQ), ATPase subunit HslU [Posttranslational modification, ... |
422-471 |
2.93e-03 |
|
ATP-dependent protease HslVU (ClpYQ), ATPase subunit HslU [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440833 [Multi-domain] Cd Length: 454 Bit Score: 40.80 E-value: 2.93e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 997579501 422 IIGQDKAVEMVSRAIRrnragfddgNR---------------P--IgsfLFVGPTGVGKTELAKQLA 471
Cdd:COG1220 17 IIGQDEAKRAVAIALR---------NRwrrqqlpeelrdeitPknI---LMIGPTGVGKTEIARRLA 71
|
|
| RecA-like_CDC48_NLV2_r1-like |
cd19503 |
first of two ATPase domains of CDC48 and NLV2, and similar ATPase domains; CDC48 in yeast and ... |
421-560 |
3.18e-03 |
|
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: 38.81 E-value: 3.18e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 997579501 421 KIIGQDKAV----EMVSRAIRRNRAGFDDGNRPIGSFLFVGPTGVGKTELAKQLAidlfgnKEALIRLDMseYSDTTAVS 496
Cdd:cd19503 1 DIGGLDEQIaslkELIELPLKYPELFRALGLKPPRGVLLHGPPGTGKTLLARAVA------NEAGANFLS--ISGPSIVS 72
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 997579501 497 KMIGTTagyvgyDDNSNTLTEKVRRNPYSVILFDEIEKANP---------------QILTLLlqvmdDGNltDGQGNVI 560
Cdd:cd19503 73 KYLGES------EKNLREIFEEARSHAPSIIFIDEIDALAPkreedqreverrvvaQLLTLM-----DGM--SSRGKVV 138
|
|
| RarA |
COG2256 |
Replication-associated recombination protein RarA (DNA-dependent ATPase) [Replication, ... |
123-237 |
3.34e-03 |
|
Replication-associated recombination protein RarA (DNA-dependent ATPase) [Replication, recombination and repair];
Pssm-ID: 441857 [Multi-domain] Cd Length: 439 Bit Score: 40.42 E-value: 3.34e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 997579501 123 ILVGEAGVGKTAIVEGLAQAIvegnvpaaikDKEIISIdiSSLEAGT-QYRGAFEENIQKLVEGvkssQNAVLFFDEIHQ 201
Cdd:COG2256 53 ILWGPPGTGKTTLARLIANAT----------DAEFVAL--SAVTSGVkDIREVIEEARERRAYG----RRTILFVDEIHR 116
|
90 100 110
....*....|....*....|....*....|....*.
gi 997579501 202 IigsgatgsdsgSKGLSDILKPALSRGEISIIGATT 237
Cdd:COG2256 117 F-----------NKAQQDALLPHVEDGTITLIGATT 141
|
|
| RecA-like_ClpX |
cd19497 |
ATP-dependent Clp protease ATP-binding subunit ClpX; ClpX is a component of the ATP-dependent ... |
119-202 |
4.06e-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: 39.51 E-value: 4.06e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 997579501 119 KNNPILVGEAGVGKTAIVEGLAQAIvegNVPAAIkdkeiisIDISSL-EAGtqYRGAFEENI-QKLVEG----VKSSQNA 192
Cdd:cd19497 50 KSNILLIGPTGSGKTLLAQTLAKIL---DVPFAI-------ADATTLtEAG--YVGEDVENIlLKLLQAadydVERAQRG 117
|
90
....*....|
gi 997579501 193 VLFFDEIHQI 202
Cdd:cd19497 118 IVYIDEIDKI 127
|
|
| HolB |
COG0470 |
DNA polymerase III, delta prime subunit [Replication, recombination and repair]; |
425-476 |
8.01e-03 |
|
DNA polymerase III, delta prime subunit [Replication, recombination and repair];
Pssm-ID: 440238 [Multi-domain] Cd Length: 289 Bit Score: 38.80 E-value: 8.01e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 997579501 425 QDKAVEMVSRAIRRNRAGfddgnrpiGSFLFVGPTGVGKTELAKQLAIDLFG 476
Cdd:COG0470 1 QEEAWEQLLAAAESGRLP--------HALLLHGPPGIGKTTLALALARDLLC 44
|
|
| TIGR02928 |
TIGR02928 |
orc1/cdc6 family replication initiation protein; Members of this protein family are found ... |
98-301 |
9.74e-03 |
|
orc1/cdc6 family replication initiation protein; Members of this protein family are found exclusively in the archaea. This set of DNA binding proteins shows homology to the origin recognition complex subunit 1/cell division control protein 6 family in eukaryotes. Several members may be found in genome and interact with each other. [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 274354 [Multi-domain] Cd Length: 365 Bit Score: 38.77 E-value: 9.74e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 997579501 98 DPVIGRDKEIQETA----EVLSRRTKNNPILVGEAGVGKTAIVEGLAQAIVEGnvpAAIKDKEIISIDISSLEAGTQYR- 172
Cdd:TIGR02928 15 DRIVHRDEQIEELAkalrPILRGSRPSNVFIYGKTGTGKTAVTKYVMKELEEA---AEDRDVRVVTVYVNCQILDTLYQv 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 997579501 173 --------GAFEENI-----------QKLVEGVKSSQNAVLF-FDEIHQIIGSGatgsdsgskglSDILKpALSR----- 227
Cdd:TIGR02928 92 lvelanqlRGSGEEVpttglstsevfRRLYKELNERGDSLIIvLDEIDYLVGDD-----------DDLLY-QLSRarsng 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 997579501 228 ----GEISIIGATTQDEYRNNImkDAALTRRFN-EVLVNEP-SAKDTVEILKGIREK-FethHQVKLPDDVLKACVDLSI 300
Cdd:TIGR02928 160 dldnAKVGVIGISNDLKFRENL--DPRVKSSLCeEEIIFPPyDAEELRDILENRAEKaF---YDGVLDDGVIPLCAALAA 234
|
.
gi 997579501 301 Q 301
Cdd:TIGR02928 235 Q 235
|
|
| |
