|
Name |
Accession |
Description |
Interval |
E-value |
| Lon |
COG0466 |
ATP-dependent Lon protease, bacterial type [Posttranslational modification, protein turnover, ... |
7-799 |
0e+00 |
|
ATP-dependent Lon protease, bacterial type [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440234 [Multi-domain] Cd Length: 785 Bit Score: 1048.84 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518974840 7 PLTLPVLPLDDEVVLPGMVVPLDLN-DTDVRAAVeaaqaaaRSTPGKPQVLLV---------PRLDGTYaSTGVLGTVEQ 76
Cdd:COG0466 11 PETLPLLPLRDVVVFPGMVIPLFVGrEKSIKALE-------EAMEGDKLIGLVaqkdaevedPGPDDLY-EVGTVAKILQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518974840 77 VGRLADGDPGALIRGRGRVQIGAGTTGpGAALWVEGTRIEQTVPEPLpgHVAELVKEYKALATAW--LRKRAAWQVVDRV 154
Cdd:COG0466 83 LLKLPDGTVKVLVEGLQRARIKEFVQE-EPYLEAEVEPLEEEEEDDK--ELEALMRSLKEQFEEYvkLNPKIPPELLAAL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518974840 155 QAIDDVSALADNSGYSPFLTTEQKVELLETADPVARLKLATQQLRDHLAEQDVAETIAKDVQEGVDKQQREFLLRRQLEA 234
Cdd:COG0466 160 SNIEDPGRLADFIASHLPLKIEEKQELLETLDVKERLEKLLELLEKEIEVLELEKKIRSRVKEQMEKSQREYYLREQLKA 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518974840 235 VRKELRElnGEQEGEESDDYRARVEAADLPEKVREAALKEVDKLERSSDQSPEGSWIRTWLDTVLELPWNERTEDRYDIQ 314
Cdd:COG0466 240 IQKELGE--KDDGEDEIEELREKIEKAKLPEEVKEKAEKELKKLERMPPMSAEATVIRNYLDWLLDLPWGKRTKDNLDLK 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518974840 315 GARAVLDAEHAGLDDVKERITEYLAVRKRRGERGLGVvggrrggavLALVGPPGVGKTSLGESVAHAMGRKFVRVALGGV 394
Cdd:COG0466 318 KAEKILDEDHYGLEKVKERILEYLAVRKLKKKLKGPI---------LCLVGPPGVGKTSLGKSIARALGRKFVRISLGGV 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518974840 395 RDEAEIRGHRRTYVGALPGRIVRAIKEAGSLNPVVLLDEIDKVGSDFRGDPAAALLEVLDPAQNHTFRDHYLEVELDLSD 474
Cdd:COG0466 389 RDEAEIRGHRRTYIGAMPGRIIQGLKKAGTKNPVFLLDEIDKMGSDFRGDPASALLEVLDPEQNNTFSDHYLEVPFDLSK 468
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518974840 475 VVFLATANVLEAIPEALLDRMELVRLDGYTEDEKVVIARDHLLPRQLERAGLDSDEVALDESALRKLAGEYTREAGVRTL 554
Cdd:COG0466 469 VMFIATANSLDTIPAPLLDRMEIIELSGYTEEEKLEIAKRYLIPKQLKEHGLKKEELKISDEALRKIIRGYTREAGVRNL 548
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518974840 555 ERSIARLLRKVAAQHELGERKlPFTIGDEDLRALIGRPHHVPESAQdpaerRTAVPGVATGLAVTGAGGDVLFVEASLAD 634
Cdd:COG0466 549 EREIAKICRKVAKKIAEGKKK-KVTITPKNLEKYLGVPRFRYEKAE-----EEDQVGVVTGLAWTEVGGDILFIEATLMP 622
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518974840 635 petGAAGLTLTGQLGDVMKESAQIALSFLRSHGAELELPVGDLKDRGVHIHFPAGAVPKDGPSAGVTMTTALASLLSGRL 714
Cdd:COG0466 623 ---GKGKLTLTGQLGDVMKESAQAALSYVRSRAEELGIDPDFFEKYDIHIHVPEGATPKDGPSAGITMATALVSALTGRP 699
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518974840 715 VRTDVAMTGEVSLTGRVLPIGGVKQKLLAAHRAGVTTVVIPKRNEPDLDDVPAEVLDKLDVHAVTDVRQVLELALAPATN 794
Cdd:COG0466 700 VRSDVAMTGEITLRGRVLPIGGLKEKLLAAHRAGIKTVILPKENEKDLEEIPEEVKKGLEFHPVEHIDEVLKIALEKEPE 779
|
....*
gi 518974840 795 GAAPE 799
Cdd:COG0466 780 PLPKK 784
|
|
| lon |
TIGR00763 |
endopeptidase La; This protein, the ATP-dependent serine endopeptidase La, is induced by heat ... |
11-789 |
0e+00 |
|
endopeptidase La; This protein, the ATP-dependent serine endopeptidase La, is induced by heat shock and other stresses in E. coli, B. subtilis, and other species. The yeast member, designated PIM1, is located in the mitochondrial matrix, required for mitochondrial function, and also induced by heat shock. [Protein fate, Degradation of proteins, peptides, and glycopeptides]
Pssm-ID: 273258 [Multi-domain] Cd Length: 775 Bit Score: 793.43 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518974840 11 PVLPLDDEVVLPGMVVPLDLNDTDVRAAVEAAQAAArstpgKPQVLLV---------PRLDGTYaSTGVLGTVEQVGRLA 81
Cdd:TIGR00763 1 PLLPLRRRPLFPGMIKPIDVGREKSIKLIKEALRLK-----QPYLGLFlqkdddneePEEDDIY-SVGVVAQILEMLPLP 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518974840 82 DGDPG---ALIRGRGRVQIGAgTTGPGAALWVEGTRIEQTVP-------EPLPGHVAELVKEYKALATAWlrkRAAWQVV 151
Cdd:TIGR00763 75 SSGTAtykVVVEGLRRIRIKE-LSDKGGYLVVRVDNLKEEPFdkddeeiKALTREIKETFRELISLSKLF---REQPALL 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518974840 152 DRVQAIDDVSALADNSGYS-PFLTTEQKVELLETADPVARLKLATQQLRDHLAEQDVAETIAKDVQEGVDKQQREFLLRR 230
Cdd:TIGR00763 151 SALEDIDEPGRLADFVAASlQLKEKDELQEVLETVNIEKRLKKALELLKKELELLKLQNKITKKVEEKMEKTQREYYLRE 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518974840 231 QLEAVRKELRELNGEQEgeESDDYRARVEAADLPEKVREAALKEVDKLERSSDQSPEGSWIRTWLDTVLELPWNERTEDR 310
Cdd:TIGR00763 231 QLKAIKKELGIEKDDKD--ELEKLKEKLEELKLPEEVKKVIEKELTKLSLLEPSSSEFTVTRNYLDWLTDLPWGKYSKEN 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518974840 311 YDIQGARAVLDAEHAGLDDVKERITEYLAVRKRRGerglgvvggRRGGAVLALVGPPGVGKTSLGESVAHAMGRKFVRVA 390
Cdd:TIGR00763 309 LDLKRAKEILDEDHYGLKKVKERILEYLAVQKLRG---------KMKGPILCLVGPPGVGKTSLGKSIAKALNRKFVRFS 379
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518974840 391 LGGVRDEAEIRGHRRTYVGALPGRIVRAIKEAGSLNPVVLLDEIDKVGSDFRGDPAAALLEVLDPAQNHTFRDHYLEVEL 470
Cdd:TIGR00763 380 LGGVRDEAEIRGHRRTYVGAMPGRIIQGLKKAKTKNPLFLLDEIDKIGSSFRGDPASALLEVLDPEQNNAFSDHYLDVPF 459
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518974840 471 DLSDVVFLATANVLEAIPEALLDRMELVRLDGYTEDEKVVIARDHLLPRQLERAGLDSDEVALDESALRKLAGEYTREAG 550
Cdd:TIGR00763 460 DLSKVIFIATANSIDTIPRPLLDRMEVIELSGYTEEEKLEIAKKYLIPKALEDHGLKPDELKITDEALLLLIKYYTREAG 539
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518974840 551 VRTLERSIARLLRKVAAQ-----HELGERKLPFTIGDEDLRALIGRPHHVPESAQdpaerRTAVPGVATGLAVTGAGGDV 625
Cdd:TIGR00763 540 VRNLERQIEKICRKAAVKlveqgEKKKSEAESVVITPDNLKKYLGKPVFTYERAY-----EVTPPGVVMGLAWTPMGGDT 614
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518974840 626 LFVEASLadpETGAAGLTLTGQLGDVMKESAQIALSFLRSHGAELELPVGDLKDRGVHIHFPAGAVPKDGPSAGVTMTTA 705
Cdd:TIGR00763 615 LFIETTK---VAGKGSLELTGQLGDVMKESAQIALTYVRSIAADLGISPNFFEKADIHLHVPEGATPKDGPSAGITMATA 691
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518974840 706 LASLLSGRLVRTDVAMTGEVSLTGRVLPIGGVKQKLLAAHRAGVTTVVIPKRNEPDLDDVPAEVLDKLDVHAVTDVRQVL 785
Cdd:TIGR00763 692 LLSLATGKPVRPDVAMTGEITLRGKVLPIGGLKEKTIAAKRAGIKTIILPEKNRRDLEELPENVKEGLEIHFVKHYDEVL 771
|
....
gi 518974840 786 ELAL 789
Cdd:TIGR00763 772 KKAF 775
|
|
| PRK10787 |
PRK10787 |
DNA-binding ATP-dependent protease La; Provisional |
5-796 |
0e+00 |
|
DNA-binding ATP-dependent protease La; Provisional
Pssm-ID: 182730 [Multi-domain] Cd Length: 784 Bit Score: 594.61 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518974840 5 SAPLTLPVLPLDDEVVLPGMVVPLDLN------------DTDVRAAVEAAQAAARSTPGKPQVLlvprldgtyaSTGVLG 72
Cdd:PRK10787 6 SERIEIPVLPLRDVVVYPHMVIPLFVGreksircleaamDHDKKIMLVAQKEASTDEPGVNDLF----------TVGTVA 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518974840 73 TVEQVGRLADGDPGALIRGRGRVQIGA----GTTGPGAALWVEGTRIEQTVPEPLpghVAELVKEYKALATawLRKRAAW 148
Cdd:PRK10787 76 SILQMLKLPDGTVKVLVEGLQRARISAlsdnGEHFSAKAEYLESPTIDEREQEVL---VRTAISQFEGYIK--LNKKIPP 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518974840 149 QVVDRVQAIDDVSALADNSGYSPFLTTEQKVELLETADPVARLKLATQQLRDHLAEQDVAETIAKDVQEGVDKQQREFLL 228
Cdd:PRK10787 151 EVLTSLNSIDDPARLADTIAAHMPLKLADKQSVLEMSDVNERLEYLMAMMESEIDLLQVEKRIRNRVKKQMEKSQREYYL 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518974840 229 RRQLEAVRKELRELngEQEGEESDDYRARVEAADLPEKVREAALKEVDKLERSSDQSPEGSWIRTWLDTVLELPWNERTE 308
Cdd:PRK10787 231 NEQMKAIQKELGEM--DDAPDENEALKRKIDAAKMPKEAKEKAEAELQKLKMMSPMSAEATVVRGYIDWMVQVPWNARSK 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518974840 309 DRYDIQGARAVLDAEHAGLDDVKERITEYLAVRKRrgerglgvvGGRRGGAVLALVGPPGVGKTSLGESVAHAMGRKFVR 388
Cdd:PRK10787 309 VKKDLRQAQEILDTDHYGLERVKDRILEYLAVQSR---------VNKIKGPILCLVGPPGVGKTSLGQSIAKATGRKYVR 379
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518974840 389 VALGGVRDEAEIRGHRRTYVGALPGRIVRAIKEAGSLNPVVLLDEIDKVGSDFRGDPAAALLEVLDPAQNHTFRDHYLEV 468
Cdd:PRK10787 380 MALGGVRDEAEIRGHRRTYIGSMPGKLIQKMAKVGVKNPLFLLDEIDKMSSDMRGDPASALLEVLDPEQNVAFSDHYLEV 459
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518974840 469 ELDLSDVVFLATANVLEaIPEALLDRMELVRLDGYTEDEKVVIARDHLLPRQLERAGLDSDEVALDESALRKLAGEYTRE 548
Cdd:PRK10787 460 DYDLSDVMFVATSNSMN-IPAPLLDRMEVIRLSGYTEDEKLNIAKRHLLPKQIERNALKKGELTVDDSAIIGIIRYYTRE 538
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518974840 549 AGVRTLERSIARLLRKVAAQHELGERKLPFTIGDEDLRALIGrphhVPESAQDPAERRTAVpGVATGLAVTGAGGDVLFV 628
Cdd:PRK10787 539 AGVRSLEREISKLCRKAVKQLLLDKSLKHIEINGDNLHDYLG----VQRFDYGRADNENRV-GQVTGLAWTEVGGDLLTI 613
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518974840 629 EASLAdpeTGAAGLTLTGQLGDVMKESAQIALSFLRSHGAELELPVGDLKDRGVHIHFPAGAVPKDGPSAGVTMTTALAS 708
Cdd:PRK10787 614 ETACV---PGKGKLTYTGSLGEVMQESIQAALTVVRARAEKLGINPDFYEKRDIHVHVPEGATPKDGPSAGIAMCTALVS 690
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518974840 709 LLSGRLVRTDVAMTGEVSLTGRVLPIGGVKQKLLAAHRAGVTTVVIPKRNEPDLDDVPAEVLDKLDVHAVTDVRQVLELA 788
Cdd:PRK10787 691 CLTGNPVRADVAMTGEITLRGQVLPIGGLKEKLLAAHRGGIKTVLIPFENKRDLEEIPDNVIADLDIHPVKRIEEVLTLA 770
|
....*...
gi 518974840 789 LAPATNGA 796
Cdd:PRK10787 771 LQNEPSGM 778
|
|
| RecA-like_Lon |
cd19500 |
lon protease homolog 2 peroxisomal; Lon protease (also known as Lon peptidase) is an ... |
313-503 |
1.78e-109 |
|
lon protease homolog 2 peroxisomal; Lon protease (also known as Lon peptidase) is an evolutionarily conserved ATP-dependent serine protease, present in bacteria and eukaryotic mitochondria and peroxisomes, which mediates the selective degradation of mutant and abnormal proteins as well as certain short-lived regulatory proteins. Lon protease is both an ATP-dependent peptidase and a protein-activated ATPase. This RecA-like Lon domain subfamily belongs to the RecA-like NTPase family which includes the NTP binding domain of F1 and V1 H(+)ATPases, DnaB and related helicases as well as bacterial RecA and related eukaryotic and archaeal recombinases. The RecA-like NTPase family also includes bacterial conjugation proteins and related DNA transfer proteins involved in type II and type IV secretion.
Pssm-ID: 410908 [Multi-domain] Cd Length: 182 Bit Score: 331.83 E-value: 1.78e-109
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518974840 313 IQGARAVLDAEHAGLDDVKERITEYLAVRKRRGERGLGVvggrrggavLALVGPPGVGKTSLGESVAHAMGRKFVRVALG 392
Cdd:cd19500 1 IKKARKVLDADHYGLEDVKERILEYLAVRKLKGSMKGPI---------LCLVGPPGVGKTSLGKSIARALGRKFVRISLG 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518974840 393 GVRDEAEIRGHRRTYVGALPGRIVRAIKEAGSLNPVVLLDEIDKVGSDFRGDPAAALLEVLDPAQNHTFRDHYLEVELDL 472
Cdd:cd19500 72 GVRDEAEIRGHRRTYVGAMPGRIIQALKKAGTNNPVFLLDEIDKIGSSFRGDPASALLEVLDPEQNSTFSDHYLDVPFDL 151
|
170 180 190
....*....|....*....|....*....|.
gi 518974840 473 SDVVFLATANVLEAIPEALLDRMELVRLDGY 503
Cdd:cd19500 152 SKVLFIATANSLDTIPGPLLDRMEIIELSGY 182
|
|
| Lon_C |
pfam05362 |
Lon protease (S16) C-terminal proteolytic domain; The Lon serine proteases must hydrolyse ATP ... |
579-789 |
2.46e-91 |
|
Lon protease (S16) C-terminal proteolytic domain; The Lon serine proteases must hydrolyse ATP to degrade protein substrates. In Escherichia coli, these proteases are involved in turnover of intracellular proteins, including abnormal proteins following heat-shock. The active site for protease activity resides in a C-terminal domain. The Lon proteases are classified as family S16 in Merops.
Pssm-ID: 428442 [Multi-domain] Cd Length: 205 Bit Score: 285.29 E-value: 2.46e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518974840 579 TIGDEDLRALIGRPHHVPESAqdpaeRRTAVPGVATGLAVTGAGGDVLFVEASLAdpeTGAAGLTLTGQLGDVMKESAQI 658
Cdd:pfam05362 1 KVTAKNLEKYLGVPRFRYGEA-----EKEDQVGVVTGLAWTEVGGDLLTIEAVIM---PGKGKLTLTGQLGDVMKESAQA 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518974840 659 ALSFLRSHGAELELPVGDLKDRGVHIHFPAGAVPKDGPSAGVTMTTALASLLSGRLVRTDVAMTGEVSLTGRVLPIGGVK 738
Cdd:pfam05362 73 ALSYVRSRAEELGIDPDFFEKKDIHIHVPEGATPKDGPSAGVTMATALVSALTGIPVRKDVAMTGEITLRGRVLPIGGLK 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 518974840 739 QKLLAAHRAGVTTVVIPKRNEPDLDDVPAEVLDKLDVHAVTDVRQVLELAL 789
Cdd:pfam05362 153 EKLLAAHRAGIKTVIIPKENEKDLEDIPENVREGLEIIPVEHVDEVLKHAL 203
|
|
| AAA |
pfam00004 |
ATPase family associated with various cellular activities (AAA); AAA family proteins often ... |
363-503 |
1.97e-25 |
|
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: 101.90 E-value: 1.97e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518974840 363 LVGPPGVGKTSLGESVAHAMGRKFVRVALGGVRDeaeirghrrTYVGALPGRIVRAIKEAGSLNP-VVLLDEIDKVGSD- 440
Cdd:pfam00004 3 LYGPPGTGKTTLAKAVAKELGAPFIEISGSELVS---------KYVGESEKRLRELFEAAKKLAPcVIFIDEIDALAGSr 73
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 518974840 441 ------FRGDPAAALLEVLDPAQNHTfrdhyleveldlSDVVFLATANVLEAIPEALLDRMELVRLDGY 503
Cdd:pfam00004 74 gsggdsESRRVVNQLLTELDGFTSSN------------SKVIVIAATNRPDKLDPALLGRFDRIIEFPL 130
|
|
| COG1750 |
COG1750 |
Predicted archaeal serine protease, S18 family [General function prediction only]; |
595-759 |
7.72e-21 |
|
Predicted archaeal serine protease, S18 family [General function prediction only];
Pssm-ID: 441356 [Multi-domain] Cd Length: 213 Bit Score: 91.58 E-value: 7.72e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518974840 595 VPESAQDPAERRTAVPGVatgLAVTGAG-GDVLFVEASLADPETGAAGLTLTGQLGDVMKESAQIALSFlrshgAELELP 673
Cdd:COG1750 17 SPLAAQSNSAVRSVTIYA---PAVSGTGeGVVINITVTVTYPGSGRVYVSTSPLTGPDTQASARIAALV-----ASLLAG 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518974840 674 VgDLKDRGVHIHFPAGAVPKDGPSAGVTMTTALASLLSGRLVRTDVAMTGEVSLTGRVLPIGGVKQKLLAAHRAGVTTVV 753
Cdd:COG1750 89 V-DLSSYDVYISIESDSPIVGGPSAGGAMTVATYAALLGLPLNKSVTMTGMINPDGSIGPVGGVYEKLEAAASAGAKYFL 167
|
....*.
gi 518974840 754 IPKRNE 759
Cdd:COG1750 168 IPKGQA 173
|
|
| SpoVK |
COG0464 |
AAA+-type ATPase, SpoVK/Ycf46/Vps4 family [Cell wall/membrane/envelope biogenesis, Cell cycle ... |
180-532 |
1.81e-18 |
|
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: 88.43 E-value: 1.81e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518974840 180 ELLETADPVARLKLATQQLRDHLAEQDVAETIAKDVQEGVDKQQREFLLRRQLEAVRKELRELNGEQEGEESDDYRARVE 259
Cdd:COG0464 16 LLLDDAALRLLLLLLLALAAALLLLLLLLLLLLLALLLVELLLLLLSGALAALLLLALLLLALLALLAALLSALELLLLG 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518974840 260 AADLPEKVREAALKEVDKLERSSDQSPEGSWIRTWLDTVLELPWNERTEDRYDIQGARAVLDAEhAGLDDVKERITEYLA 339
Cdd:COG0464 96 ELLLLLLLLLLLLLLLLDLERALLELLRESAEALALAAPLVTYEDIGGLEEELLELREAILDDL-GGLEEVKEELRELVA 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518974840 340 VRKRRGERGLGVVGGRRGGavLALVGPPGVGKTSLGESVAHAMGRKFVRVALGGVRDEaeirghrrtYVGALPGRIVRAI 419
Cdd:COG0464 175 LPLKRPELREEYGLPPPRG--LLLYGPPGTGKTLLARALAGELGLPLIEVDLSDLVSK---------YVGETEKNLREVF 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518974840 420 KEAGSLNPVVLL-DEIDKVGSDFRGDPAAALLEVLDpaqnhtfrdhYL--EVELDLSDVVFLATANVLEAIPEALLDRM- 495
Cdd:COG0464 244 DKARGLAPCVLFiDEADALAGKRGEVGDGVGRRVVN----------TLltEMEELRSDVVVIAATNRPDLLDPALLRRFd 313
|
330 340 350
....*....|....*....|....*....|....*..
gi 518974840 496 ELVRLDGYTEDEKVVIARDHLLPRQLErAGLDSDEVA 532
Cdd:COG0464 314 EIIFFPLPDAEERLEIFRIHLRKRPLD-EDVDLEELA 349
|
|
| LON_substr_bdg |
pfam02190 |
ATP-dependent protease La (LON) substrate-binding domain; This domain has been shown to be ... |
9-200 |
2.70e-14 |
|
ATP-dependent protease La (LON) substrate-binding domain; This domain has been shown to be part of the PUA superfamily. This domain represents a general protein and polypeptide interaction domain for the ATP-dependent serine peptidase, LON, Peptidase_S16, pfam05362. ATP-dependent Lon proteases are conserved in all living organizms and catalyze rapid turnover of short-lived regulatory proteins and many damaged or denatured proteins.
Pssm-ID: 426647 [Multi-domain] Cd Length: 195 Bit Score: 71.98 E-value: 2.70e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518974840 9 TLPVLPLDDEVVLPGMVVPLDLNDTDVRaaveAAQAAARSTPGKPQVLLVPRLDGT--------YASTGVLGTVEQVGRL 80
Cdd:pfam02190 1 ELPLLPLRNTVLFPGMVLPLFVGRPRSI----AAIEAALNKDKLYGVLLVSQKDAEdeeptpddLYEVGTVAKIVQILKL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518974840 81 ADGDPGALIRGRGRVQI---GAGTTGPGAAlwvegtRIEQTVPEPLPGHVA--ELVKEYKALATAWLRKRAAWQVVDRVQ 155
Cdd:pfam02190 77 PDGTYKVLVEGLERVRIvelVKKEEPYLRA------EVEDLPEDSDELSEAlkALVKELIEKLRRLLKLLLPLELLLKIK 150
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 518974840 156 AIDDVSALADNSGYSPFLTTEQKVELLETADPVARLKLATQQLRD 200
Cdd:pfam02190 151 DIENPGRLADLVAAILPLSPEEKQELLETLDVKERLEKVLELLNR 195
|
|
| RecA-like_protease |
cd19481 |
proteases similar to RecA; RecA-like NTPases. This family includes the NTP binding domain of ... |
363-501 |
3.05e-14 |
|
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: 70.77 E-value: 3.05e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518974840 363 LVGPPGVGKTSLGESVAHAMGRKFVRVALGGVRDEaeirghrrtYVGALPGRIVRAIKEAGSLNP-VVLLDEIDKVGSDf 441
Cdd:cd19481 31 LYGPPGTGKTLLAKALAGELGLPLIVVKLSSLLSK---------YVGESEKNLRKIFERARRLAPcILFIDEIDAIGRK- 100
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 518974840 442 RGDPA---------AALLEVLDPAQNhtfrdhyleveldLSDVVFLATANVLEAIPEALLDRMelvRLD 501
Cdd:cd19481 101 RDSSGesgelrrvlNQLLTELDGVNS-------------RSKVLVIAATNRPDLLDPALLRPG---RFD 153
|
|
| AAA_5 |
pfam07728 |
AAA domain (dynein-related subfamily); This Pfam entry includes some of the AAA proteins not ... |
363-495 |
4.87e-11 |
|
AAA domain (dynein-related subfamily); This Pfam entry includes some of the AAA proteins not detected by the pfam00004 model.
Pssm-ID: 400191 [Multi-domain] Cd Length: 135 Bit Score: 61.15 E-value: 4.87e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518974840 363 LVGPPGVGKTSLGESVAHAM-GRKFVRVALGGVRDEAEIRGHRRTYVGAL---PGRIVRAIKEAGslnpVVLLDEIDKVG 438
Cdd:pfam07728 4 LVGPPGTGKTELAERLAAALsNRPVFYVQLTRDTTEEDLFGRRNIDPGGAswvDGPLVRAAREGE----IAVLDEINRAN 79
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 518974840 439 SDFrgdpAAALLEVLDPAQNHTFRDHYLEVElDLSDVVFLATANVLEA----IPEALLDRM 495
Cdd:pfam07728 80 PDV----LNSLLSLLDERRLLLPDGGELVKA-APDGFRLIATMNPLDRglneLSPALRSRF 135
|
|
| AAA |
cd00009 |
The AAA+ (ATPases Associated with a wide variety of cellular Activities) superfamily ... |
361-498 |
6.08e-10 |
|
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: 58.31 E-value: 6.08e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518974840 361 LALVGPPGVGKTSLGESVAHA---MGRKFVRVALGGVRDEAEIRGHRRTYVGALPGRIVRAIKeagslNPVVLLDEIDKV 437
Cdd:cd00009 22 LLLYGPPGTGKTTLARAIANElfrPGAPFLYLNASDLLEGLVVAELFGHFLVRLLFELAEKAK-----PGVLFIDEIDSL 96
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 518974840 438 GSDFRgdpaAALLEVLdpaqnHTFRDHYLEVELDLsdVVFLATANVLEAIPEALLDRMELV 498
Cdd:cd00009 97 SRGAQ----NALLRVL-----ETLNDLRIDRENVR--VIGATNRPLLGDLDRALYDRLDIR 146
|
|
| RPT1 |
COG1222 |
ATP-dependent 26S proteasome regulatory subunit [Posttranslational modification, protein ... |
363-532 |
6.96e-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: 6.96e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518974840 363 LVGPPGVGKTSLGESVAHAMGRKFVRVALggvrdeAEIrghRRTYVGAlPGRIVRAI-KEAGSLNP-VVLLDEIDKVGSD 440
Cdd:COG1222 117 LYGPPGTGKTLLAKAVAGELGAPFIRVRG------SEL---VSKYIGE-GARNVREVfELAREKAPsIIFIDEIDAIAAR 186
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518974840 441 fRGDPA---------AALLEVLDpaqnhtfrdhylEVElDLSDVVFLATANVLEAIPEALL-----DRMELVRLDgyTED 506
Cdd:COG1222 187 -RTDDGtsgevqrtvNQLLAELD------------GFE-SRGDVLIIAATNRPDLLDPALLrpgrfDRVIEVPLP--DEE 250
|
170 180
....*....|....*....|....*.
gi 518974840 507 EKVVIARDHLLPRQLERaGLDSDEVA 532
Cdd:COG1222 251 AREEILKIHLRDMPLAD-DVDLDKLA 275
|
|
| COG1223 |
COG1223 |
Predicted ATPase, AAA+ superfamily [General function prediction only]; |
363-569 |
3.65e-08 |
|
Predicted ATPase, AAA+ superfamily [General function prediction only];
Pssm-ID: 440836 [Multi-domain] Cd Length: 246 Bit Score: 55.28 E-value: 3.65e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518974840 363 LVGPPGVGKTSLGESVAHAMGRKFVRVALGGVRDEaeirghrrtYVGALPGRIVRAIKEAGSLNPVVLLDEIDKVGSDfR 442
Cdd:COG1223 40 FYGPPGTGKTMLAEALAGELKLPLLTVRLDSLIGS---------YLGETARNLRKLFDFARRAPCVIFFDEFDAIAKD-R 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518974840 443 GDPAA---------ALLevldpaqnhtfrdhyLEVELDLSDVVFLATANVLEAIPEALLDRMELV-RLDGYTEDEkvvia 512
Cdd:COG1223 110 GDQNDvgevkrvvnALL---------------QELDGLPSGSVVIAATNHPELLDSALWRRFDEViEFPLPDKEE----- 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 518974840 513 RDHLLPRQLERAGLDSDEvaldesALRKLAGEYTREAGvrtleRSIARLLRKVAAQH 569
Cdd:COG1223 170 RKEILELNLKKFPLPFEL------DLKKLAKKLEGLSG-----ADIEKVLKTALKKA 215
|
|
| MoxR |
COG0714 |
MoxR-like ATPase [General function prediction only]; MoxR-like ATPase is part of the Pathway ... |
363-540 |
4.48e-08 |
|
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: 55.56 E-value: 4.48e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518974840 363 LVGPPGVGKTSLGESVAHAMGRKFVRVA----LggvrDEAEIRGH-------RRTYVgaLPGRIvraikeagsLNPVVLL 431
Cdd:COG0714 36 LEGVPGVGKTTLAKALARALGLPFIRIQftpdL----LPSDILGTyiydqqtGEFEF--RPGPL---------FANVLLA 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518974840 432 DEIDkvgsdfRGDPA--AALLEVLDPAQ----NHTFRdhyleveldLSDVVF-LATANVLEAI-----PEALLDRMeLVR 499
Cdd:COG0714 101 DEIN------RAPPKtqSALLEAMEERQvtipGGTYK---------LPEPFLvIATQNPIEQEgtyplPEAQLDRF-LLK 164
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 518974840 500 LD-GY--TEDEKVVIARDHLLPRQLERAGLDSDEVALDESALRK 540
Cdd:COG0714 165 LYiGYpdAEEEREILRRHTGRHLAEVEPVLSPEELLALQELVRQ 208
|
|
| SdrC |
COG3480 |
Predicted secreted protein YlbL, contains PDZ domain [Signal transduction mechanisms]; |
695-786 |
1.21e-07 |
|
Predicted secreted protein YlbL, contains PDZ domain [Signal transduction mechanisms];
Pssm-ID: 442703 [Multi-domain] Cd Length: 344 Bit Score: 54.43 E-value: 1.21e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518974840 695 GPSAGvtMTTALA--------SLLSGRlvrtDVAMTGEVSLTGRVLPIGGVKQKLLAAHRAGVTTVVIPKRNEpdlDDVP 766
Cdd:COG3480 240 GPSAG--LMFALGiydqltpgDLTGGK----KIAGTGTIDADGTVGPIGGIDQKVVAARRAGATIFLAPASNC---AEAV 310
|
90 100
....*....|....*....|...
gi 518974840 767 AEVLDKLDVHAV---TDVRQVLE 786
Cdd:COG3480 311 GTIPTGLKVVPVdtlDDALDALE 333
|
|
| LonB |
COG1067 |
Predicted ATP-dependent protease [Posttranslational modification, protein turnover, chaperones] ... |
694-787 |
4.65e-07 |
|
Predicted ATP-dependent protease [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440686 [Multi-domain] Cd Length: 742 Bit Score: 53.41 E-value: 4.65e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518974840 694 DGPSAGVTMTTALASLLSGRLVRTDVAMTGEVSLTGRVLPIGGVKQKL-----LAAHRaGVTT---VVIPKRNEPD--LD 763
Cdd:COG1067 592 DGDSASSAELYALLSALSGVPIRQDIAVTGSVNQHGEVQPIGGVNEKIegffdVCKAR-GLTGkqgVIIPAANVKNlmLR 670
|
90 100
....*....|....*....|....*....
gi 518974840 764 DvpaEVLD-----KLDVHAVTDVRQVLEL 787
Cdd:COG1067 671 D---EVVEavkagQFHIYAVEHVDEAIEL 696
|
|
| RecA-like_ClpB_Hsp104-like |
cd19499 |
Chaperone protein ClpB/Hsp104 subfamily; Bacterial Caseinolytic peptidase B (ClpB) and ... |
361-496 |
1.33e-06 |
|
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: 49.48 E-value: 1.33e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518974840 361 LALVGPPGVGKTSLGESVAHAM---GRKFVRVALGgvrdeAEIRGHRRTYVGALPGRIVRA-----IKEAGSLNP--VVL 430
Cdd:cd19499 44 FLFLGPTGVGKTELAKALAELLfgdEDNLIRIDMS-----EYMEKHSVSRLIGAPPGYVGYteggqLTEAVRRKPysVVL 118
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 518974840 431 LDEIDKVGSDFRGdpaaALLEVLDpaqNHTFRDHYlEVELDLSDVVFLATANvleAIPEALLDRME 496
Cdd:cd19499 119 LDEIEKAHPDVQN----LLLQVLD---DGRLTDSH-GRTVDFKNTIIIMTSN---HFRPEFLNRID 173
|
|
| AAA_2 |
pfam07724 |
AAA domain (Cdc48 subfamily); This Pfam entry includes some of the AAA proteins not detected ... |
363-518 |
6.53e-06 |
|
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: 47.19 E-value: 6.53e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518974840 363 LVGPPGVGKTSLGESVAHAMG---RKFVRValggvrdEAeirghrRTY---------VGALPGRIVRA----IKEAGSLN 426
Cdd:pfam07724 8 FLGPTGVGKTELAKALAELLFgdeRALIRI-------DM------SEYmeehsvsrlIGAPPGYVGYEeggqLTEAVRRK 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518974840 427 P--VVLLDEIDKVGSD-FRgdpaaALLEVLDpaqNHTFRDHYlEVELDLSDVVFLATANVLEAIPealLDRMELVRLDGY 503
Cdd:pfam07724 75 PysIVLIDEIEKAHPGvQN-----DLLQILE---GGTLTDKQ-GRTVDFKNTLFIMTGNFGSEKI---SDASRLGDSPDY 142
|
170
....*....|....*..
gi 518974840 504 TEDEKVV--IARDHLLP 518
Cdd:pfam07724 143 ELLKEEVmdLLKKGFIP 159
|
|
| McrB |
COG1401 |
5-methylcytosine-specific restriction endonuclease McrBC, GTP-binding regulatory subunit McrB ... |
180-591 |
6.82e-06 |
|
5-methylcytosine-specific restriction endonuclease McrBC, GTP-binding regulatory subunit McrB [Defense mechanisms];
Pssm-ID: 441011 [Multi-domain] Cd Length: 477 Bit Score: 49.38 E-value: 6.82e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518974840 180 ELLETADPVARLKLATQQLRDHLAEQDVAETIAKDVQEGVDKQQREFLLRRQLEAVRKELRELNGEQEGEESDDYRARVE 259
Cdd:COG1401 45 RLAERLSEELLRADRAARATELVEELSAALEVVVLLLDLEKVELNEKLALSEAAVAIEELYELEADSEIEAVGLLLELAE 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518974840 260 AADLPEKVREAALKEvdKLERSSDQSPEGSWIRTWLDTVLELPWNERTEDRYDIQGARAVLDAEHAGLDDVKERITEYLA 339
Cdd:COG1401 125 RSDALEALERARLLL--ELADLEERAALETEVLEALEAELEELLAAPEDLSADALAAELSAAEELYSEDLESEDDYLKDL 202
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518974840 340 VRKRRGERGLGVVGGRRGGAVLALVGPPGVGKTSLGESVAHAMG----RKFVRVAlggVR----DEAEIRGHR-RTYVGA 410
Cdd:COG1401 203 LREKFEETLEAFLAALKTKKNVILAGPPGTGKTYLARRLAEALGgednGRIEFVQ---FHpswsYEDFLLGYRpSLDEGK 279
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518974840 411 L---PGRIVRAIKEAgSLNP----VVLLDEIDkvgsdfRGDPAAA---LLEVLDPAQnhtfRDHYLEVELDLSD------ 474
Cdd:COG1401 280 YeptPGIFLRFCLKA-EKNPdkpyVLIIDEIN------RANVEKYfgeLLSLLESDK----RGEELSIELPYSGegeefs 348
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518974840 475 ----VVFLATANV----LEAIPEAlLDR---MELVRLDGYTEDEKVVIARDHLLPRQLERAGLDSDEVALDESALRKLAG 543
Cdd:COG1401 349 ippnLYIIGTMNTddrsLALSDKA-LRRrftFEFLDPDLDKLSNEEVVDLLEELNEILEKRDFQIGHRALLLLDGLLSGD 427
|
410 420 430 440
....*....|....*....|....*....|....*....|....*...
gi 518974840 544 EYTREAGVRTLERSIARLLRKVAAQHELGERKLPFTIGDEDLRALIGR 591
Cdd:COG1401 428 LDLLLLLLLLLLELLLLLLDKLDLLGMAEFEDRLELSEYLPLLLRASL 475
|
|
| PRK13342 |
PRK13342 |
recombination factor protein RarA; Reviewed |
365-434 |
1.58e-05 |
|
recombination factor protein RarA; Reviewed
Pssm-ID: 237355 [Multi-domain] Cd Length: 413 Bit Score: 48.16 E-value: 1.58e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 518974840 365 GPPGVGKTSLGESVAHAMGRKFVRV--ALGGVrdeAEIRghrrtyvgalpgrivRAIKEAGSL-----NPVVLLDEI 434
Cdd:PRK13342 43 GPPGTGKTTLARIIAGATDAPFEALsaVTSGV---KDLR---------------EVIEEARQRrsagrRTILFIDEI 101
|
|
| RecA-like_Ycf46-like |
cd19507 |
ATPase domain of Ycf46 and similar ATPase domains; Ycf46 may play a role in the regulation of ... |
361-492 |
3.93e-05 |
|
ATPase domain of Ycf46 and similar ATPase domains; Ycf46 may play a role in the regulation of photosynthesis in cyanobacteria, especially in CO2 uptake and utilization. This subfamily belongs to the RecA-like NTPase family which includes the NTP binding domain of F1 and V1 H(+)ATPases, DnaB and related helicases as well as bacterial RecA and related eukaryotic and archaeal recombinases. The RecA-like NTPase family also includes bacterial conjugation proteins and related DNA transfer proteins involved in type II and type IV secretion.
Pssm-ID: 410915 [Multi-domain] Cd Length: 161 Bit Score: 44.67 E-value: 3.93e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518974840 361 LALVGPPGVGKTSLGESVAHAMGRKFVRVALGGVRDEaeirghrrtYVGALPGRIVRAIKEAGSLNPVVLL-DEIDKV-- 437
Cdd:cd19507 34 LLLVGIQGTGKSLTAKAIAGVWQLPLLRLDMGRLFGG---------LVGESESRLRQMIQTAEAIAPCVLWiDEIEKGfs 104
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 518974840 438 GSDFRGD--PAAALLEvldpaqnhTFRDHYLEVEldlSDVVFLATANVLEAIPEALL 492
Cdd:cd19507 105 NADSKGDsgTSSRVLG--------TFLTWLQEKK---KPVFVVATANNVQSLPPELL 150
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
361-495 |
7.72e-05 |
|
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: 43.52 E-value: 7.72e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518974840 361 LALVGPPGVGKTSLGESVAHAMGRKFVRV-------ALGGVRDEAEIRGHRRTYVGALPGRIVRAIKE--AGSLNPVVLL 431
Cdd:smart00382 5 ILIVGPPGSGKTTLARALARELGPPGGGViyidgedILEEVLDQLLLIIVGGKKASGSGELRLRLALAlaRKLKPDVLIL 84
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 518974840 432 DEIDKVGSDFRgdpaAALLEVLDpaqnhtfRDHYLEVELDLSDVVFLATANVLEAIPEALLDRM 495
Cdd:smart00382 85 DEITSLLDAEQ----EALLLLLE-------ELRLLLLLKSEKNLTVILTTNDEKDLGPALLRRR 137
|
|
| RarA |
COG2256 |
Replication-associated recombination protein RarA (DNA-dependent ATPase) [Replication, ... |
365-434 |
1.93e-04 |
|
Replication-associated recombination protein RarA (DNA-dependent ATPase) [Replication, recombination and repair];
Pssm-ID: 441857 [Multi-domain] Cd Length: 439 Bit Score: 44.66 E-value: 1.93e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 518974840 365 GPPGVGKTSLGESVAHAMGRKFVRV--ALGGVrdeAEIRghrrtyvgalpgrivRAIKEAGSL-----NPVVLLDEI 434
Cdd:COG2256 56 GPPGTGKTTLARLIANATDAEFVALsaVTSGV---KDIR---------------EVIEEARERraygrRTILFVDEI 114
|
|
| ChlI |
pfam13541 |
Subunit ChlI of Mg-chelatase; |
628-758 |
3.87e-04 |
|
Subunit ChlI of Mg-chelatase;
Pssm-ID: 433293 [Multi-domain] Cd Length: 121 Bit Score: 40.90 E-value: 3.87e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518974840 628 VEASLADpetGAAGLTLTGQLGDVMKESAQIALSFLRSHGaeLELPVG----DLKdrgvhihfPAGaVPKDGPSAGVTMT 703
Cdd:pfam13541 1 VEVDVSK---GLPAFTIVGLPDTAVKESKERVRAALKNSG--FEFPPKritvNLA--------PAD-LKKEGSSFDLPIA 66
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 518974840 704 TALASLLSGRLVRTDVAMTGEVSLTGRVLPIGGVKQKLLAAHRAGVTTVVIPKRN 758
Cdd:pfam13541 67 IGILAAQGQIPVLEETIFLGELSLDGSLRPVRGALPIALAARKHGFRGLIVPKEN 121
|
|
| RecA-like_NVL_r1-like |
cd19518 |
first of two ATPase domains of NVL (nuclear VCP-like protein) and similar ATPase domains; NVL ... |
312-439 |
1.01e-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: 40.85 E-value: 1.01e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518974840 312 DIQGARAVLD--AEHAGLDDVKERITEYLAVRKRRGerglgvvggrrggavLALVGPPGVGKTSLGESVAHAMGRKFVRV 389
Cdd:cd19518 1 DIGGMDSTLKelCELLIHPILPPEYFQHLGVEPPRG---------------VLLHGPPGCGKTMLANAIAGELKVPFLKI 65
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 518974840 390 A----LGGVRDEAEirghrrtyvgalpGRIVRAIKEAGSLNP-VVLLDEIDKVGS 439
Cdd:cd19518 66 SateiVSGVSGESE-------------EKIRELFDQAISNAPcIVFIDEIDAITP 107
|
|
| RecA-like_PAN_like |
cd19502 |
proteasome activating nucleotidase PAN and related proteasome subunits; This subfamily ... |
363-439 |
1.09e-03 |
|
proteasome activating nucleotidase PAN and related proteasome subunits; This subfamily contains ATPase subunits of the eukaryotic 26S proteasome, and of the archaeal proteasome which carry out ATP-dependent degradation of substrates of the ubiquitin-proteasome pathway. The eukaryotic 26S proteasome consists of a proteolytic 20S core particle (CP), and a 19S regulatory particle (RP) which provides the ATP-dependence and the specificity for ubiquitinated proteins. In the archaea the RP is a homohexameric complex of proteasome-activating nucleotidase (PAN). This subfamily also includes various eukaryotic 26S subunits including, proteasome 26S subunit, ATPase 2 (PSMC2, also known as S7 and MSS1) which is a member of the 19S RP and has a chaperone like activity; and proteasome 20S subunit alpha 6 (PSMA6, also known as IOTA, p27K, and PROS27) which is a member of the 20S CP. This RecA-like_PAN subfamily belongs to the RecA-like NTPase family which includes the NTP binding domain of F1 and V1 H(+)ATPases, DnaB and related helicases as well as bacterial RecA and related eukaryotic and archaeal recombinases. The RecA-like NTPase family also includes bacterial conjugation proteins and related DNA transfer proteins involved in type II and type IV secretion.
Pssm-ID: 410910 [Multi-domain] Cd Length: 171 Bit Score: 40.78 E-value: 1.09e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 518974840 363 LVGPPGVGKTSLGESVAHAMGRKFVRVAlggvrdEAEIrghRRTYVGALPgRIVRAIKE-AGSLNP-VVLLDEIDKVGS 439
Cdd:cd19502 42 LYGPPGTGKTLLAKAVANHTDATFIRVV------GSEL---VQKYIGEGA-RLVRELFEmAREKAPsIIFIDEIDAIGA 110
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
172-567 |
1.33e-03 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 42.23 E-value: 1.33e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518974840 172 FLTTEQKVELLETADPVARLKLATQQLRDHLAEQDVAETIAKDVQEGVDKQQREFLLRRQLEAVRKELRELNGEQEGEES 251
Cdd:COG1196 398 LAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEA 477
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518974840 252 DDYRARVEAAdlpekvREAALKEVDKLERSSDQSPEGSWIRTWLDTVLELPWNERTEDRYDIQGARAVLDAEHAGLddVK 331
Cdd:COG1196 478 ALAELLEELA------EAAARLLLLLEAEADYEGFLEGVKAALLLAGLRGLAGAVAVLIGVEAAYEAALEAALAAA--LQ 549
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518974840 332 ERITEYLAVRKRRGERGLGVVGGRRGGAVLALVGPPgvgKTSLGESVAHAMGRKFVRVALGGVRDEAEIRGHRRTYVGAl 411
Cdd:COG1196 550 NIVVEDDEVAAAAIEYLKAAKAGRATFLPLDKIRAR---AALAAALARGAIGAAVDLVASDLREADARYYVLGDTLLGR- 625
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518974840 412 pgRIVRAIKEAGSLNPVVLLDEIDKV---GSDFRGDPAAALLEVLDPAQNHTFRDHYLEVELDLSDVVFLATANVLEAIP 488
Cdd:COG1196 626 --TLVAARLEAALRRAVTLAGRLREVtleGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEE 703
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 518974840 489 EALLDRMELVRLDGYTEDEKVVIARDHLLPRQLERAGLDSDEVALDESALRKLAGEYTREAgvrtLERSIARLLRKVAA 567
Cdd:COG1196 704 EEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEELPEPPDLEE----LERELERLEREIEA 778
|
|
| AAA_16 |
pfam13191 |
AAA ATPase domain; This family of domains contain a P-loop motif that is characteriztic of the ... |
363-500 |
1.70e-03 |
|
AAA ATPase domain; This family of domains contain a P-loop motif that is characteriztic of the AAA superfamily.
Pssm-ID: 433025 [Multi-domain] Cd Length: 167 Bit Score: 40.18 E-value: 1.70e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518974840 363 LVGPPGVGKTSLGESVAHAMGRKFVRVALGGVRDEAEIRG-----HRRTYVGALPGRIVRAIKEAGSLNPVVLLDEIDKV 437
Cdd:pfam13191 29 LTGEAGTGKTTLLRELLRALERDGGYFLRGKCDENLPYSPllealTREGLLRQLLDELESSLLEAWRAALLEALAPVPEL 108
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 518974840 438 GSDFRGDPAAALLEVLDPAQNhtfRDHYLEVELDLSDVVFLATANVLeaipEALLDRMELVRL 500
Cdd:pfam13191 109 PGDLAERLLDLLLRLLDLLAR---GERPLVLVLDDLQWADEASLQLL----AALLRLLESLPL 164
|
|
| SK |
cd00464 |
Shikimate kinase (SK) is the fifth enzyme in the shikimate pathway, a seven-step biosynthetic ... |
361-387 |
1.81e-03 |
|
Shikimate kinase (SK) is the fifth enzyme in the shikimate pathway, a seven-step biosynthetic pathway which converts erythrose-4-phosphate to chorismic acid, found in bacteria, fungi and plants. Chorismic acid is a important intermediate in the synthesis of aromatic compounds, such as aromatic amino acids, p-aminobenzoic acid, folate and ubiquinone. Shikimate kinase catalyses the phosphorylation of the 3-hydroxyl group of shikimic acid using ATP.
Pssm-ID: 238260 [Multi-domain] Cd Length: 154 Bit Score: 39.85 E-value: 1.81e-03
10 20
....*....|....*....|....*..
gi 518974840 361 LALVGPPGVGKTSLGESVAHAMGRKFV 387
Cdd:cd00464 2 IVLIGMMGAGKTTVGRLLAKALGLPFV 28
|
|
| AroK |
COG0703 |
Shikimate kinase [Amino acid transport and metabolism]; Shikimate kinase is part of the ... |
361-387 |
3.01e-03 |
|
Shikimate kinase [Amino acid transport and metabolism]; Shikimate kinase is part of the Pathway/BioSystem: Aromatic amino acid biosynthesis
Pssm-ID: 440467 [Multi-domain] Cd Length: 165 Bit Score: 39.34 E-value: 3.01e-03
10 20
....*....|....*....|....*..
gi 518974840 361 LALVGPPGVGKTSLGESVAHAMGRKFV 387
Cdd:COG0703 1 IVLIGMMGAGKSTVGRLLAKRLGLPFV 27
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
174-339 |
3.15e-03 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 41.20 E-value: 3.15e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518974840 174 TTEQKVELletADPVARLKLATQQLRDHLAEQDVAETIAKDVQ-EGVDKQQREFLLRRQLEAVRKELRELNGEQEGEESD 252
Cdd:TIGR02168 672 ILERRREI---EELEEKIEELEEKIAELEKALAELRKELEELEeELEQLRKELEELSRQISALRKDLARLEAEVEQLEER 748
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518974840 253 DYRARVEAADLPEKVREAAlkevDKLERSSDQSPEGSWIRTWLDTVLELPWNERTEDRYDIQGARAVLDAEHAGLDDVKE 332
Cdd:TIGR02168 749 IAQLSKELTELEAEIEELE----ERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRE 824
|
....*..
gi 518974840 333 RITEYLA 339
Cdd:TIGR02168 825 RLESLER 831
|
|
| RecA-like_VPS4-like |
cd19509 |
ATPase domain of VPS4, ATAD1, K, KTNA1, Spastin, FIGL-1 and similar ATPase domains; This ... |
325-496 |
3.84e-03 |
|
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: 38.87 E-value: 3.84e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518974840 325 AGLDDVKERITEYLAVRKRRGERGLGVVGGRRGgavLALVGPPGVGKTSLGESVAHAMGRKFVRVALGGVRDEaeirghr 404
Cdd:cd19509 2 AGLDDAKEALKEAVILPSLRPDLFPGLRGPPRG---ILLYGPPGTGKTLLARAVASESGSTFFSISASSLVSK------- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518974840 405 rtYVGAlPGRIVRAIKE-AGSLNP-VVLLDEIDKVGSDFRGDpaaallevlDPAQNHTFRDHYLeVELD------LSDVV 476
Cdd:cd19509 72 --WVGE-SEKIVRALFAlARELQPsIIFIDEIDSLLSERGSG---------EHEASRRVKTEFL-VQMDgvlnkpEDRVL 138
|
170 180
....*....|....*....|
gi 518974840 477 FLATANVLEAIPEALLDRME 496
Cdd:cd19509 139 VLGATNRPWELDEAFLRRFE 158
|
|
| hflB |
PRK10733 |
ATP-dependent zinc metalloprotease FtsH; |
322-529 |
3.91e-03 |
|
ATP-dependent zinc metalloprotease FtsH;
Pssm-ID: 182683 [Multi-domain] Cd Length: 644 Bit Score: 40.79 E-value: 3.91e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518974840 322 AEHAGLDDVKERITEYLAVRKrrgERGLGVVGGRRGGAVLALVGPPGVGKTSLGESVAHAMGRKFVRVAlggVRDEAEIr 401
Cdd:PRK10733 152 ADVAGCDEAKEEVAELVEYLR---EPSRFQKLGGKIPKGVLMVGPPGTGKTLLAKAIAGEAKVPFFTIS---GSDFVEM- 224
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518974840 402 ghrrtYVGALPGRIVRAIKEAGSLNP-VVLLDEIDKVGSDfRGdpaAALlevldpAQNHTFRDHYLE---VELDLSD--- 474
Cdd:PRK10733 225 -----FVGVGASRVRDMFEQAKKAAPcIIFIDEIDAVGRQ-RG---AGL------GGGHDEREQTLNqmlVEMDGFEgne 289
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 518974840 475 -VVFLATANVLEAIPEALL-----DRMELVRLDGytedekvVIARDHLLPRQLERAGLDSD 529
Cdd:PRK10733 290 gIIVIAATNRPDVLDPALLrpgrfDRQVVVGLPD-------VRGREQILKVHMRRVPLAPD 343
|
|
| aroK |
PRK00131 |
shikimate kinase; Reviewed |
361-387 |
4.93e-03 |
|
shikimate kinase; Reviewed
Pssm-ID: 234654 [Multi-domain] Cd Length: 175 Bit Score: 38.63 E-value: 4.93e-03
10 20
....*....|....*....|....*..
gi 518974840 361 LALVGPPGVGKTSLGESVAHAMGRKFV 387
Cdd:PRK00131 7 IVLIGFMGAGKSTIGRLLAKRLGYDFI 33
|
|
| |
