|
Name |
Accession |
Description |
Interval |
E-value |
| Lon |
COG0466 |
ATP-dependent Lon protease, bacterial type [Posttranslational modification, protein turnover, ... |
2-789 |
0e+00 |
|
ATP-dependent Lon protease, bacterial type [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440234 [Multi-domain] Cd Length: 785 Bit Score: 1052.69 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502653703 2 SESLILPVLPLDDEVVLPGMVVPLDLS-ENEIRAAIDAAqalaDNKPEVLLV---------PRIDGRYgSVGVRAIVEQV 71
Cdd:COG0466 9 ELPETLPLLPLRDVVVFPGMVIPLFVGrEKSIKALEEAM----EGDKLIGLVaqkdaevedPGPDDLY-EVGTVAKILQL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502653703 72 GRLPGGEPAAVVRGVDRVRVGSGTTGpGAALWVQATLVEAVQV-GERAEELAKQYKALSTTILQ--KRGAWQVVDAVNQM 148
Cdd:COG0466 84 LKLPDGTVKVLVEGLQRARIKEFVQE-EPYLEAEVEPLEEEEEdDKELEALMRSLKEQFEEYVKlnPKIPPELLAALSNI 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502653703 149 DDPSVLADSSGYAPWLSTQRKAEILETADPADRLSLLVEWAREHLAELDVAETIRKDVQEGMEKQQREFLLRQQLAAVRK 228
Cdd:COG0466 163 EDPGRLADFIASHLPLKIEEKQELLETLDVKERLEKLLELLEKEIEVLELEKKIRSRVKEQMEKSQREYYLREQLKAIQK 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502653703 229 ELSElnGTSPETEEEDYRARVEAADLPEKVREAALKEVDKLERTSDQSPETGWIRTWLDTVLDIPWNERTEDSYDIAAAR 308
Cdd:COG0466 243 ELGE--KDDGEDEIEELREKIEKAKLPEEVKEKAEKELKKLERMPPMSAEATVIRNYLDWLLDLPWGKRTKDNLDLKKAE 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502653703 309 AVLDADHTGLDDVKDRIIEYLAVRGRRAEKglgvvggrrSGAVLALAGPPGVGKTSLGESVARAMGRKFVRVALGGVRDE 388
Cdd:COG0466 321 KILDEDHYGLEKVKERILEYLAVRKLKKKL---------KGPILCLVGPPGVGKTSLGKSIARALGRKFVRISLGGVRDE 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502653703 389 AEIRGHRRTYVGAQSGRIVRAVREAGSMNPVVLLDEVDKVGSDYRGDPTAALLEVLDPAQNHTFRDHYLEVELDLSDVLF 468
Cdd:COG0466 392 AEIRGHRRTYIGAMPGRIIQGLKKAGTKNPVFLLDEIDKMGSDFRGDPASALLEVLDPEQNNTFSDHYLEVPFDLSKVMF 471
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502653703 469 LATANVLESIPGPLLDRMEIVTLDGYTEDEKVAIARDHLLPRQLDKAGLTTEDVTVEEDALRRLAGEYTREAGVRSLERS 548
Cdd:COG0466 472 IATANSLDTIPAPLLDRMEIIELSGYTEEEKLEIAKRYLIPKQLKEHGLKKEELKISDEALRKIIRGYTREAGVRNLERE 551
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502653703 549 IARILRKVTANVALGEgELPVTVG--DLVPYLGRPRHvpessLPESRQRTAVPGVATGLAVTGAGGDVLYVEASLADpet 626
Cdd:COG0466 552 IAKICRKVAKKIAEGK-KKKVTITpkNLEKYLGVPRF-----RYEKAEEEDQVGVVTGLAWTEVGGDILFIEATLMP--- 622
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502653703 627 GDTGLTLTGQLGDVMKESAKIALSYLRSRGAELELPVASLKDRSVHIHFPAGAVPKDGPSAGVTLTTALASLLSGRPVRN 706
Cdd:COG0466 623 GKGKLTLTGQLGDVMKESAQAALSYVRSRAEELGIDPDFFEKYDIHIHVPEGATPKDGPSAGITMATALVSALTGRPVRS 702
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502653703 707 DVAMTGEVSLTGRVLPIGGVKQKLLAAHRAGITTVLIPARNEPDLDDVPEAVRSELTVHVVSDVREVLEIALTPAKVAER 786
Cdd:COG0466 703 DVAMTGEITLRGRVLPIGGLKEKLLAAHRAGIKTVILPKENEKDLEEIPEEVKKGLEFHPVEHIDEVLKIALEKEPEPLP 782
|
...
gi 502653703 787 AVA 789
Cdd:COG0466 783 KKE 785
|
|
| lon |
TIGR00763 |
endopeptidase La; This protein, the ATP-dependent serine endopeptidase La, is induced by heat ... |
8-778 |
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: 804.21 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502653703 8 PVLPLDDEVVLPGMVVPLDLSENeiRAAIDAAQALADNKPEVLLV---------PRIDGRYgSVGVRAIVEQVGRLPGGE 78
Cdd:TIGR00763 1 PLLPLRRRPLFPGMIKPIDVGRE--KSIKLIKEALRLKQPYLGLFlqkdddneePEEDDIY-SVGVVAQILEMLPLPSSG 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502653703 79 PAAVVRGVDRVRVGSGT--TGPGAALWVQATLVEAVQVGERAEE---LAKQYKALSTTILQKRGAWQV----VDAVNQMD 149
Cdd:TIGR00763 78 TATYKVVVEGLRRIRIKelSDKGGYLVVRVDNLKEEPFDKDDEEikaLTREIKETFRELISLSKLFREqpalLSALEDID 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502653703 150 DPSVLADSSGYA-PWLSTQRKAEILETADPADRLSLLVEWAREHLAELDVAETIRKDVQEGMEKQQREFLLRQQLAAVRK 228
Cdd:TIGR00763 158 EPGRLADFVAASlQLKEKDELQEVLETVNIEKRLKKALELLKKELELLKLQNKITKKVEEKMEKTQREYYLREQLKAIKK 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502653703 229 ELSElnGTSPETEEEDYRARVEAADLPEKVREAALKEVDKLERTSDQSPETGWIRTWLDTVLDIPWNERTEDSYDIAAAR 308
Cdd:TIGR00763 238 ELGI--EKDDKDELEKLKEKLEELKLPEEVKKVIEKELTKLSLLEPSSSEFTVTRNYLDWLTDLPWGKYSKENLDLKRAK 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502653703 309 AVLDADHTGLDDVKDRIIEYLAVRGRRaekglgvvgGRRSGAVLALAGPPGVGKTSLGESVARAMGRKFVRVALGGVRDE 388
Cdd:TIGR00763 316 EILDEDHYGLKKVKERILEYLAVQKLR---------GKMKGPILCLVGPPGVGKTSLGKSIAKALNRKFVRFSLGGVRDE 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502653703 389 AEIRGHRRTYVGAQSGRIVRAVREAGSMNPVVLLDEVDKVGSDYRGDPTAALLEVLDPAQNHTFRDHYLEVELDLSDVLF 468
Cdd:TIGR00763 387 AEIRGHRRTYVGAMPGRIIQGLKKAKTKNPLFLLDEIDKIGSSFRGDPASALLEVLDPEQNNAFSDHYLDVPFDLSKVIF 466
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502653703 469 LATANVLESIPGPLLDRMEIVTLDGYTEDEKVAIARDHLLPRQLDKAGLTTEDVTVEEDALRRLAGEYTREAGVRSLERS 548
Cdd:TIGR00763 467 IATANSIDTIPRPLLDRMEVIELSGYTEEEKLEIAKKYLIPKALEDHGLKPDELKITDEALLLLIKYYTREAGVRNLERQ 546
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502653703 549 IARILRKVTANVAL-GEGELP------VTVGDLVPYLGRPRHVpesslPESRQRTAVPGVATGLAVTGAGGDVLYVEASL 621
Cdd:TIGR00763 547 IEKICRKAAVKLVEqGEKKKSeaesvvITPDNLKKYLGKPVFT-----YERAYEVTPPGVVMGLAWTPMGGDTLFIETTK 621
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502653703 622 adpETGDTGLTLTGQLGDVMKESAKIALSYLRSRGAELELPVASLKDRSVHIHFPAGAVPKDGPSAGVTLTTALASLLSG 701
Cdd:TIGR00763 622 ---VAGKGSLELTGQLGDVMKESAQIALTYVRSIAADLGISPNFFEKADIHLHVPEGATPKDGPSAGITMATALLSLATG 698
|
730 740 750 760 770 780 790
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 502653703 702 RPVRNDVAMTGEVSLTGRVLPIGGVKQKLLAAHRAGITTVLIPARNEPDLDDVPEAVRSELTVHVVSDVREVLEIAL 778
Cdd:TIGR00763 699 KPVRPDVAMTGEITLRGKVLPIGGLKEKTIAAKRAGIKTIILPEKNRRDLEELPENVKEGLEIHFVKHYDEVLKKAF 775
|
|
| PRK10787 |
PRK10787 |
DNA-binding ATP-dependent protease La; Provisional |
2-778 |
0e+00 |
|
DNA-binding ATP-dependent protease La; Provisional
Pssm-ID: 182730 [Multi-domain] Cd Length: 784 Bit Score: 614.64 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502653703 2 SESLILPVLPLDDEVVLPGMVVPLDLS-ENEIRAAIDAAqalaDNKPEVLLV---------PRIDGRYgSVGVRAIVEQV 71
Cdd:PRK10787 6 SERIEIPVLPLRDVVVYPHMVIPLFVGrEKSIRCLEAAM----DHDKKIMLVaqkeastdePGVNDLF-TVGTVASILQM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502653703 72 GRLPGGEpAAVVRGVDRVRVGSGTTGPGAALWVQATLVEAVQVGERAEEL-----AKQYKALSTtiLQKRGAWQVVDAVN 146
Cdd:PRK10787 81 LKLPDGT-VKVLVEGLQRARISALSDNGEHFSAKAEYLESPTIDEREQEVlvrtaISQFEGYIK--LNKKIPPEVLTSLN 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502653703 147 QMDDPSVLADSSGYAPWLSTQRKAEILETADPADRLSLLVEWAREHLAELDVAETIRKDVQEGMEKQQREFLLRQQLAAV 226
Cdd:PRK10787 158 SIDDPARLADTIAAHMPLKLADKQSVLEMSDVNERLEYLMAMMESEIDLLQVEKRIRNRVKKQMEKSQREYYLNEQMKAI 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502653703 227 RKELSELNgTSPEtEEEDYRARVEAADLPEKVREAALKEVDKLERTSDQSPETGWIRTWLDTVLDIPWNERTEDSYDIAA 306
Cdd:PRK10787 238 QKELGEMD-DAPD-ENEALKRKIDAAKMPKEAKEKAEAELQKLKMMSPMSAEATVVRGYIDWMVQVPWNARSKVKKDLRQ 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502653703 307 ARAVLDADHTGLDDVKDRIIEYLAVRGRRAekglgvvggRRSGAVLALAGPPGVGKTSLGESVARAMGRKFVRVALGGVR 386
Cdd:PRK10787 316 AQEILDTDHYGLERVKDRILEYLAVQSRVN---------KIKGPILCLVGPPGVGKTSLGQSIAKATGRKYVRMALGGVR 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502653703 387 DEAEIRGHRRTYVGAQSGRIVRAVREAGSMNPVVLLDEVDKVGSDYRGDPTAALLEVLDPAQNHTFRDHYLEVELDLSDV 466
Cdd:PRK10787 387 DEAEIRGHRRTYIGSMPGKLIQKMAKVGVKNPLFLLDEIDKMSSDMRGDPASALLEVLDPEQNVAFSDHYLEVDYDLSDV 466
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502653703 467 LFLATANVLeSIPGPLLDRMEIVTLDGYTEDEKVAIARDHLLPRQLDKAGLTTEDVTVEEDALRRLAGEYTREAGVRSLE 546
Cdd:PRK10787 467 MFVATSNSM-NIPAPLLDRMEVIRLSGYTEDEKLNIAKRHLLPKQIERNALKKGELTVDDSAIIGIIRYYTREAGVRSLE 545
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502653703 547 RSIARILRKVTANVALGEG--ELPVTVGDLVPYLGRPRHVPESSLPESRQrtavpGVATGLAVTGAGGDVLYVEASLAdp 624
Cdd:PRK10787 546 REISKLCRKAVKQLLLDKSlkHIEINGDNLHDYLGVQRFDYGRADNENRV-----GQVTGLAWTEVGGDLLTIETACV-- 618
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502653703 625 eTGDTGLTLTGQLGDVMKESAKIALSYLRSRGAELELPVASLKDRSVHIHFPAGAVPKDGPSAGVTLTTALASLLSGRPV 704
Cdd:PRK10787 619 -PGKGKLTYTGSLGEVMQESIQAALTVVRARAEKLGINPDFYEKRDIHVHVPEGATPKDGPSAGIAMCTALVSCLTGNPV 697
|
730 740 750 760 770 780 790
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 502653703 705 RNDVAMTGEVSLTGRVLPIGGVKQKLLAAHRAGITTVLIPARNEPDLDDVPEAVRSELTVHVVSDVREVLEIAL 778
Cdd:PRK10787 698 RADVAMTGEITLRGQVLPIGGLKEKLLAAHRGGIKTVLIPFENKRDLEEIPDNVIADLDIHPVKRIEEVLTLAL 771
|
|
| RecA-like_Lon |
cd19500 |
lon protease homolog 2 peroxisomal; Lon protease (also known as Lon peptidase) is an ... |
304-494 |
2.63e-111 |
|
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: 336.07 E-value: 2.63e-111
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502653703 304 IAAARAVLDADHTGLDDVKDRIIEYLAVRGRRAEKglgvvggrrSGAVLALAGPPGVGKTSLGESVARAMGRKFVRVALG 383
Cdd:cd19500 1 IKKARKVLDADHYGLEDVKERILEYLAVRKLKGSM---------KGPILCLVGPPGVGKTSLGKSIARALGRKFVRISLG 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502653703 384 GVRDEAEIRGHRRTYVGAQSGRIVRAVREAGSMNPVVLLDEVDKVGSDYRGDPTAALLEVLDPAQNHTFRDHYLEVELDL 463
Cdd:cd19500 72 GVRDEAEIRGHRRTYVGAMPGRIIQALKKAGTNNPVFLLDEIDKIGSSFRGDPASALLEVLDPEQNSTFSDHYLDVPFDL 151
|
170 180 190
....*....|....*....|....*....|.
gi 502653703 464 SDVLFLATANVLESIPGPLLDRMEIVTLDGY 494
Cdd:cd19500 152 SKVLFIATANSLDTIPGPLLDRMEIIELSGY 182
|
|
| Lon_C |
pfam05362 |
Lon protease (S16) C-terminal proteolytic domain; The Lon serine proteases must hydrolyse ATP ... |
569-780 |
4.37e-94 |
|
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: 292.22 E-value: 4.37e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502653703 569 VTVGDLVPYLGRPRHVPESSLPESrqrtaVPGVATGLAVTGAGGDVLYVEASLAdpeTGDTGLTLTGQLGDVMKESAKIA 648
Cdd:pfam05362 2 VTAKNLEKYLGVPRFRYGEAEKED-----QVGVVTGLAWTEVGGDLLTIEAVIM---PGKGKLTLTGQLGDVMKESAQAA 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502653703 649 LSYLRSRGAELELPVASLKDRSVHIHFPAGAVPKDGPSAGVTLTTALASLLSGRPVRNDVAMTGEVSLTGRVLPIGGVKQ 728
Cdd:pfam05362 74 LSYVRSRAEELGIDPDFFEKKDIHIHVPEGATPKDGPSAGVTMATALVSALTGIPVRKDVAMTGEITLRGRVLPIGGLKE 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 502653703 729 KLLAAHRAGITTVLIPARNEPDLDDVPEAVRSELTVHVVSDVREVLEIALTP 780
Cdd:pfam05362 154 KLLAAHRAGIKTVIIPKENEKDLEDIPENVREGLEIIPVEHVDEVLKHALVG 205
|
|
| AAA |
pfam00004 |
ATPase family associated with various cellular activities (AAA); AAA family proteins often ... |
354-489 |
4.48e-23 |
|
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: 95.35 E-value: 4.48e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502653703 354 LAGPPGVGKTSLGESVARAMGRKFVRVALGGVRDeaeirghrrTYVGAQSGRIVRAVREAGSMNP-VVLLDEVDKVGSDy 432
Cdd:pfam00004 3 LYGPPGTGKTTLAKAVAKELGAPFIEISGSELVS---------KYVGESEKRLRELFEAAKKLAPcVIFIDEIDALAGS- 72
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 502653703 433 RGDPT--------AALLEVLDPAQNHTfrdhyleveldlSDVLFLATANVLESIPGPLLDRMEIV 489
Cdd:pfam00004 73 RGSGGdsesrrvvNQLLTELDGFTSSN------------SKVIVIAATNRPDKLDPALLGRFDRI 125
|
|
| COG1750 |
COG1750 |
Predicted archaeal serine protease, S18 family [General function prediction only]; |
605-777 |
5.85e-22 |
|
Predicted archaeal serine protease, S18 family [General function prediction only];
Pssm-ID: 441356 [Multi-domain] Cd Length: 213 Bit Score: 94.66 E-value: 5.85e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502653703 605 LAVTGAG-GDVLYVEASLADPETGDTGLTLTGQLGDVMKESAKIALSYlrsrgAELELPVaSLKDRSVHIHFPAGAVPKD 683
Cdd:COG1750 35 PAVSGTGeGVVINITVTVTYPGSGRVYVSTSPLTGPDTQASARIAALV-----ASLLAGV-DLSSYDVYISIESDSPIVG 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502653703 684 GPSAGVTLTTALASLLSGRPVRNDVAMTGEVSLTGRVLPIGGVKQKLLAAHRAGITTVLIPARNEPD----------LDD 753
Cdd:COG1750 109 GPSAGGAMTVATYAALLGLPLNKSVTMTGMINPDGSIGPVGGVYEKLEAAASAGAKYFLIPKGQAILtgyntqvgetVDL 188
|
170 180
....*....|....*....|....
gi 502653703 754 VPEAVRSELTVHVVSDVREVLEIA 777
Cdd:COG1750 189 VEYGKELGVKVIEVSTIADALQYF 212
|
|
| SpoVK |
COG0464 |
AAA+-type ATPase, SpoVK/Ycf46/Vps4 family [Cell wall/membrane/envelope biogenesis, Cell cycle ... |
161-575 |
2.50e-19 |
|
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: 91.13 E-value: 2.50e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502653703 161 APWLSTQRKAEILETADPADRLSLLVEWAREHLAELDVAETIRKDVQEGMEKQQREFLLRQQLAAVRKELSELNGTSPET 240
Cdd:COG0464 6 ALAVALALALLLLDDAALRLLLLLLLALAAALLLLLLLLLLLLLALLLVELLLLLLSGALAALLLLALLLLALLALLAAL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502653703 241 EEEDYRARVEAADLPEKVREAALKEVDKLERTSDQSPETGWIRTWLDTVLDIPWNERTEDSYDIAAARAVLDaDHTGLDD 320
Cdd:COG0464 86 LSALELLLLGELLLLLLLLLLLLLLLLDLERALLELLRESAEALALAAPLVTYEDIGGLEEELLELREAILD-DLGGLEE 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502653703 321 VKD---RIIEYLAVRGR-RAEKGLGVVGGrrsgavLALAGPPGVGKTSLGESVARAMGRKFVRVALGGVRDEaeirghrr 396
Cdd:COG0464 165 VKEelrELVALPLKRPElREEYGLPPPRG------LLLYGPPGTGKTLLARALAGELGLPLIEVDLSDLVSK-------- 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502653703 397 tYVGAQSGRIVRAVREAGSMNPVVLL-DEVDKVGSDYRGDPTAALLEVLDpaqnhtfrdhYL--EVELDLSDVLFLATAN 473
Cdd:COG0464 231 -YVGETEKNLREVFDKARGLAPCVLFiDEADALAGKRGEVGDGVGRRVVN----------TLltEMEELRSDVVVIAATN 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502653703 474 VLESIPGPLLDRM-EIVTLDGYTEDEKVAIARDHLLPRQLDkaglttedvtvEEDALRRLAGEYTREAGvrsleRSIARI 552
Cdd:COG0464 300 RPDLLDPALLRRFdEIIFFPLPDAEERLEIFRIHLRKRPLD-----------EDVDLEELAEATEGLSG-----ADIRNV 363
|
410 420
....*....|....*....|...
gi 502653703 553 LRKvTANVALGEGELPVTVGDLV 575
Cdd:COG0464 364 VRR-AALQALRLGREPVTTEDLL 385
|
|
| RecA-like_protease |
cd19481 |
proteases similar to RecA; RecA-like NTPases. This family includes the NTP binding domain of ... |
321-485 |
2.12e-12 |
|
proteases similar to RecA; RecA-like NTPases. This family includes the NTP binding domain of F1 and V1 H(+)ATPases, DnaB and related helicases as well as bacterial RecA and related eukaryotic and archaeal recombinases. This group also includes bacterial conjugation proteins and related DNA transfer proteins involved in type II and type IV secretion.
Pssm-ID: 410889 [Multi-domain] Cd Length: 158 Bit Score: 65.77 E-value: 2.12e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502653703 321 VKDRIIEYLAVRGRRAEKGLGVVGGRRSgaVLaLAGPPGVGKTSLGESVARAMGRKFVRVALGGVRDEaeirghrrtYVG 400
Cdd:cd19481 1 LKASLREAVEAPRRGSRLRRYGLGLPKG--IL-LYGPPGTGKTLLAKALAGELGLPLIVVKLSSLLSK---------YVG 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502653703 401 AQSGRIVRAVREAGSMNP-VVLLDEVDKVGSD--------YRGDPTAALLEVLDPAQNhtfrdhyleveldLSDVLFLAT 471
Cdd:cd19481 69 ESEKNLRKIFERARRLAPcILFIDEIDAIGRKrdssgesgELRRVLNQLLTELDGVNS-------------RSKVLVIAA 135
|
170
....*....|....
gi 502653703 472 ANVLESIPGPLLDR 485
Cdd:cd19481 136 TNRPDLLDPALLRP 149
|
|
| LonB |
COG1067 |
Predicted ATP-dependent protease [Posttranslational modification, protein turnover, chaperones] ... |
683-779 |
7.70e-12 |
|
Predicted ATP-dependent protease [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440686 [Multi-domain] Cd Length: 742 Bit Score: 68.82 E-value: 7.70e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502653703 683 DGPSAGVTLTTALASLLSGRPVRNDVAMTGEVSLTGRVLPIGGVKQKL-----LAAHRaGITT---VLIPARNEPDL--- 751
Cdd:COG1067 592 DGDSASSAELYALLSALSGVPIRQDIAVTGSVNQHGEVQPIGGVNEKIegffdVCKAR-GLTGkqgVIIPAANVKNLmlr 670
|
90 100
....*....|....*....|....*....
gi 502653703 752 DDVPEAVRSEL-TVHVVSDVREVLEIaLT 779
Cdd:COG1067 671 DEVVEAVKAGQfHIYAVEHVDEAIEL-LT 698
|
|
| LON_substr_bdg |
pfam02190 |
ATP-dependent protease La (LON) substrate-binding domain; This domain has been shown to be ... |
7-188 |
2.08e-11 |
|
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: 63.89 E-value: 2.08e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502653703 7 LPVLPLDDEVVLPGMVVPLDLSENEIRaAIDAAQALADNKPEVLLVPRIDGRYG--------SVGVRAIVEQVGRLPGGE 78
Cdd:pfam02190 2 LPLLPLRNTVLFPGMVLPLFVGRPRSI-AAIEAALNKDKLYGVLLVSQKDAEDEeptpddlyEVGTVAKIVQILKLPDGT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502653703 79 PAAVVRGVD---RVRVGSGTTGPGAALwVQATLVEAVQVGERAEELAKQYKALSTTILQKRGAWQVVDAVNQMDDPSVLA 155
Cdd:pfam02190 81 YKVLVEGLErvrIVELVKKEEPYLRAE-VEDLPEDSDELSEALKALVKELIEKLRRLLKLLLPLELLLKIKDIENPGRLA 159
|
170 180 190
....*....|....*....|....*....|...
gi 502653703 156 DSSGYAPWLSTQRKAEILETADPADRLSLLVEW 188
Cdd:pfam02190 160 DLVAAILPLSPEEKQELLETLDVKERLEKVLEL 192
|
|
| RPT1 |
COG1222 |
ATP-dependent 26S proteasome regulatory subunit [Posttranslational modification, protein ... |
223-552 |
1.06e-10 |
|
ATP-dependent 26S proteasome regulatory subunit [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440835 [Multi-domain] Cd Length: 326 Bit Score: 63.87 E-value: 1.06e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502653703 223 LAAVRKELSELNGTSPETEEEDYRARVEAADLPEKVREAALKEVDKLERTSDQSPETGWIRTWLDTVLDIpwnERTEDSY 302
Cdd:COG1222 1 GNDLLTIDENIKALLALIDALQERLGVELALLLQPVKALELLEEAPALLLNDANLTQKRLGTPRGTAVPA---ESPDVTF 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502653703 303 DiaaaravldaDHTGLDDVKDRIIEYLAVRGRRAEKgLGVVGGRRSGAVLaLAGPPGVGKTSLGESVARAMGRKFVRVAL 382
Cdd:COG1222 78 D----------DIGGLDEQIEEIREAVELPLKNPEL-FRKYGIEPPKGVL-LYGPPGTGKTLLAKAVAGELGAPFIRVRG 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502653703 383 ggvrdeAEIrghRRTYVGaQSGRIVRAV-REAGSMNP-VVLLDEVDKVGSDyRGDPT---------AALLEVLDpaqnht 451
Cdd:COG1222 146 ------SEL---VSKYIG-EGARNVREVfELAREKAPsIIFIDEIDAIAAR-RTDDGtsgevqrtvNQLLAELD------ 208
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502653703 452 frdhylEVElDLSDVLFLATANVLESI------PGPLLDRMEIVTLDgytEDEKVAIARDHLLPRQLDKaglttedvTVE 525
Cdd:COG1222 209 ------GFE-SRGDVLIIAATNRPDLLdpallrPGRFDRVIEVPLPD---EEAREEILKIHLRDMPLAD--------DVD 270
|
330 340 350
....*....|....*....|....*....|....*
gi 502653703 526 EDALRRLAGEYT--------REAGVRSLERSIARI 552
Cdd:COG1222 271 LDKLAKLTEGFSgadlkaivTEAGMFAIREGRDTV 305
|
|
| RecA-like_ClpB_Hsp104-like |
cd19499 |
Chaperone protein ClpB/Hsp104 subfamily; Bacterial Caseinolytic peptidase B (ClpB) and ... |
334-490 |
1.47e-10 |
|
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: 60.65 E-value: 1.47e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502653703 334 RRAEKGLGvvGGRRSGAVLALAGPPGVGKTSLGESVARAM---GRKFVRVALGGVRDE---AEIRGHRRTYVGA-QSGRI 406
Cdd:cd19499 28 RRARAGLS--DPNRPIGSFLFLGPTGVGKTELAKALAELLfgdEDNLIRIDMSEYMEKhsvSRLIGAPPGYVGYtEGGQL 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502653703 407 VRAVREagsmNP--VVLLDEVDKVGSDYRGdptaALLEVLDpaqNHTFRDHYlEVELDLSDVLFLATANVlesIPGPLLD 484
Cdd:cd19499 106 TEAVRR----KPysVVLLDEIEKAHPDVQN----LLLQVLD---DGRLTDSH-GRTVDFKNTIIIMTSNH---FRPEFLN 170
|
....*..
gi 502653703 485 RM-EIVT 490
Cdd:cd19499 171 RIdEIVV 177
|
|
| SdrC |
COG3480 |
Predicted secreted protein YlbL, contains PDZ domain [Signal transduction mechanisms]; |
684-764 |
2.19e-09 |
|
Predicted secreted protein YlbL, contains PDZ domain [Signal transduction mechanisms];
Pssm-ID: 442703 [Multi-domain] Cd Length: 344 Bit Score: 59.82 E-value: 2.19e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502653703 684 GPSAGvtLTTALA--------SLLSGRpvrnDVAMTGEVSLTGRVLPIGGVKQKLLAAHRAGITTVLIPARNEpdlDDVP 755
Cdd:COG3480 240 GPSAG--LMFALGiydqltpgDLTGGK----KIAGTGTIDADGTVGPIGGIDQKVVAARRAGATIFLAPASNC---AEAV 310
|
....*....
gi 502653703 756 EAVRSELTV 764
Cdd:COG3480 311 GTIPTGLKV 319
|
|
| AAA_5 |
pfam07728 |
AAA domain (dynein-related subfamily); This Pfam entry includes some of the AAA proteins not ... |
354-486 |
2.90e-09 |
|
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: 56.15 E-value: 2.90e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502653703 354 LAGPPGVGKTSLGESVARAM-GRKFVRVALGGVRDEAEIRGHRRTYVGAQS---GRIVRAVREAGsmnpVVLLDEVDKVG 429
Cdd:pfam07728 4 LVGPPGTGKTELAERLAAALsNRPVFYVQLTRDTTEEDLFGRRNIDPGGASwvdGPLVRAAREGE----IAVLDEINRAN 79
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 502653703 430 SDYrgdpTAALLEVLDPAQNHTFRDHYLEVElDLSDVLFLATANVL----ESIPGPLLDRM 486
Cdd:pfam07728 80 PDV----LNSLLSLLDERRLLLPDGGELVKA-APDGFRLIATMNPLdrglNELSPALRSRF 135
|
|
| AAA |
cd00009 |
The AAA+ (ATPases Associated with a wide variety of cellular Activities) superfamily ... |
346-489 |
4.35e-09 |
|
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: 56.00 E-value: 4.35e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502653703 346 RRSGAVLALAGPPGVGKTSLGESVARA---MGRKFVRVALGGVRDEAEIRGHRRTYVGAQSGRIVRAvreagSMNPVVLL 422
Cdd:cd00009 16 LPPPKNLLLYGPPGTGKTTLARAIANElfrPGAPFLYLNASDLLEGLVVAELFGHFLVRLLFELAEK-----AKPGVLFI 90
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 502653703 423 DEVDKVgsdyRGDPTAALLEVLdpaqnHTFRDHYLEVELDLsdVLFLATANVLESIPGPLLDRMEIV 489
Cdd:cd00009 91 DEIDSL----SRGAQNALLRVL-----ETLNDLRIDRENVR--VIGATNRPLLGDLDRALYDRLDIR 146
|
|
| AAA_2 |
pfam07724 |
AAA domain (Cdc48 subfamily); This Pfam entry includes some of the AAA proteins not detected ... |
354-474 |
1.68e-07 |
|
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: 51.81 E-value: 1.68e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502653703 354 LAGPPGVGKTSLGESVARAMG---RKFVRValggvrDEAEI---------RGHRRTYVGA-QSGRIVRAVREagSMNPVV 420
Cdd:pfam07724 8 FLGPTGVGKTELAKALAELLFgdeRALIRI------DMSEYmeehsvsrlIGAPPGYVGYeEGGQLTEAVRR--KPYSIV 79
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 502653703 421 LLDEVDKVGSD-YRgdptaALLEVLDpaqNHTFRDHYlEVELDLSDVLFLATANV 474
Cdd:pfam07724 80 LIDEIEKAHPGvQN-----DLLQILE---GGTLTDKQ-GRTVDFKNTLFIMTGNF 125
|
|
| COG1223 |
COG1223 |
Predicted ATPase, AAA+ superfamily [General function prediction only]; |
323-556 |
2.81e-06 |
|
Predicted ATPase, AAA+ superfamily [General function prediction only];
Pssm-ID: 440836 [Multi-domain] Cd Length: 246 Bit Score: 49.50 E-value: 2.81e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502653703 323 DRIIEYLAVRGRRAEKGLGVvggRRSgaVLaLAGPPGVGKTSLGESVARAMGRKFVRVALGGVRDEaeirghrrtYVGAQ 402
Cdd:COG1223 15 KLIIKELRRRENLRKFGLWP---PRK--IL-FYGPPGTGKTMLAEALAGELKLPLLTVRLDSLIGS---------YLGET 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502653703 403 SGRIVRAVREAGSMNPVVLLDEVDKVGSDyRGDPTA---------ALLevldpaqnhtfrdhyLEVELDLSDVLFLATAN 473
Cdd:COG1223 80 ARNLRKLFDFARRAPCVIFFDEFDAIAKD-RGDQNDvgevkrvvnALL---------------QELDGLPSGSVVIAATN 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502653703 474 VLESIPGPLLDRMEIV-TLDGYTEDEKVAIARDHLLPRQLDKaglttedvtveEDALRRLAGEYTREAGvrsleRSIARI 552
Cdd:COG1223 144 HPELLDSALWRRFDEViEFPLPDKEERKEILELNLKKFPLPF-----------ELDLKKLAKKLEGLSG-----ADIEKV 207
|
....
gi 502653703 553 LRKV 556
Cdd:COG1223 208 LKTA 211
|
|
| ChlI |
pfam13541 |
Subunit ChlI of Mg-chelatase; |
617-747 |
3.17e-06 |
|
Subunit ChlI of Mg-chelatase;
Pssm-ID: 433293 [Multi-domain] Cd Length: 121 Bit Score: 46.67 E-value: 3.17e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502653703 617 VEASLADpetGDTGLTLTGQLGDVMKESAKIALSYLRSRGaeLELPvaslkDRSVHIH-FPAGaVPKDGPSAGVTLTTAL 695
Cdd:pfam13541 1 VEVDVSK---GLPAFTIVGLPDTAVKESKERVRAALKNSG--FEFP-----PKRITVNlAPAD-LKKEGSSFDLPIAIGI 69
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 502653703 696 ASLLSGRPVRNDVAMTGEVSLTGRVLPIGGVKQKLLAAHRAGITTVLIPARN 747
Cdd:pfam13541 70 LAAQGQIPVLEETIFLGELSLDGSLRPVRGALPIALAARKHGFRGLIVPKEN 121
|
|
| T7SS_EccA |
TIGR03922 |
type VII secretion AAA-ATPase EccA; This model represents the AAA family ATPase, EccA, of the ... |
304-453 |
9.19e-06 |
|
type VII secretion AAA-ATPase EccA; This model represents the AAA family ATPase, EccA, of the actinobacterial flavor of type VII secretion systems. Species such as Mycobacterium tuberculosis have several instances of this system per genome, designated EccA1, EccA2, etc. [Protein fate, Protein and peptide secretion and trafficking]
Pssm-ID: 188437 [Multi-domain] Cd Length: 557 Bit Score: 49.07 E-value: 9.19e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502653703 304 IAAARAVLDAdHTGLDDVKDRIIEY---LAVRGRRAEKGLGVVGGRRSgavLALAGPPGVGKTslgeSVARAMGRKFvrV 380
Cdd:TIGR03922 268 LAEAEAELAE-QIGLERVKRQVAALkssTAMALARAERGLPVAQTSNH---MLFAGPPGTGKT----TIARVVAKIY--C 337
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502653703 381 ALGGVRDEAEIRGHRRTYVG---AQSGRIVRAVREaGSMNPVVLLDEVDKVGSDYRGDP----TAALLEVLDPAQNHTFR 453
Cdd:TIGR03922 338 GLGVLRKPLVREVSRADLIGqyiGESEAKTNEIID-SALGGVLFLDEAYTLVETGYGQKdpfgLEAIDTLLARMENDRDR 416
|
|
| McrB |
COG1401 |
5-methylcytosine-specific restriction endonuclease McrBC, GTP-binding regulatory subunit McrB ... |
168-477 |
2.12e-05 |
|
5-methylcytosine-specific restriction endonuclease McrBC, GTP-binding regulatory subunit McrB [Defense mechanisms];
Pssm-ID: 441011 [Multi-domain] Cd Length: 477 Bit Score: 47.84 E-value: 2.12e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502653703 168 RKAEILETADPADRLSLLVEWAREHLAELDVAETIRKDVQEGMEKQQREFLLRQQLAAVRKELSELNGTSPETEEEDYRA 247
Cdd:COG1401 45 RLAERLSEELLRADRAARATELVEELSAALEVVVLLLDLEKVELNEKLALSEAAVAIEELYELEADSEIEAVGLLLELAE 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502653703 248 RVEAADLPEKVREAALKEVDKLERTSDQSPETGWIRTWLDTVLDIPWNERTEDSYDIAAARAVLDADhtgLDDVKDRIIE 327
Cdd:COG1401 125 RSDALEALERARLLLELADLEERAALETEVLEALEAELEELLAAPEDLSADALAAELSAAEELYSED---LESEDDYLKD 201
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502653703 328 YLAVRGRRAEKGLgVVGGRRSGAVLaLAGPPGVGKTSLGESVARAMG----RKFVRVAlggVR----DEAEIRGHR---- 395
Cdd:COG1401 202 LLREKFEETLEAF-LAALKTKKNVI-LAGPPGTGKTYLARRLAEALGgednGRIEFVQ---FHpswsYEDFLLGYRpsld 276
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502653703 396 -RTYVgAQSGRIVRAVREAgSMNP----VVLLDE-----VDKVGSDyrgdptaaLLEVLDPAQnhtfRDHYLEVELDLSD 465
Cdd:COG1401 277 eGKYE-PTPGIFLRFCLKA-EKNPdkpyVLIIDEinranVEKYFGE--------LLSLLESDK----RGEELSIELPYSG 342
|
330 340
....*....|....*....|..
gi 502653703 466 ----------VLFLATANVLES 477
Cdd:COG1401 343 egeefsippnLYIIGTMNTDDR 364
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
348-486 |
2.16e-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: 45.06 E-value: 2.16e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502653703 348 SGAVLALAGPPGVGKTSLGESVARAMGRKFVRV----------ALGGVRDEAEIRGHRRTYVGAQSGRIVRAVREAgSMN 417
Cdd:smart00382 1 PGEVILIVGPPGSGKTTLARALARELGPPGGGViyidgedileEVLDQLLLIIVGGKKASGSGELRLRLALALARK-LKP 79
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 502653703 418 PVVLLDEvdkvgsdyrgdPTAALLEVLDPAQNHTFRDHYLEVELDLSDVLFLATANVLESIPGPLLDRM 486
Cdd:smart00382 80 DVLILDE-----------ITSLLDAEQEALLLLLEELRLLLLLKSEKNLTVILTTNDEKDLGPALLRRR 137
|
|
| MoxR |
COG0714 |
MoxR-like ATPase [General function prediction only]; MoxR-like ATPase is part of the Pathway ... |
350-531 |
2.48e-05 |
|
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: 47.08 E-value: 2.48e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502653703 350 AVLA-----LAGPPGVGKTSLGESVARAMGRKFVRVA----LggvrDEAEIRGHrrTYVGAQSGR---IVRAVreagsMN 417
Cdd:COG0714 27 ALLAgghllLEGVPGVGKTTLAKALARALGLPFIRIQftpdL----LPSDILGT--YIYDQQTGEfefRPGPL-----FA 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502653703 418 PVVLLDEVDkvgsdyRGDP-T-AALLEVLDPAQ----NHTFRdhyleveldLSDVLF-LATANVLESI-----PGPLLDR 485
Cdd:COG0714 96 NVLLADEIN------RAPPkTqSALLEAMEERQvtipGGTYK---------LPEPFLvIATQNPIEQEgtyplPEAQLDR 160
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 502653703 486 MEIVTLDGY-TEDEKVAIARDHLLPRQLD-KAGLTTEDVTVEEDALRR 531
Cdd:COG0714 161 FLLKLYIGYpDAEEEREILRRHTGRHLAEvEPVLSPEELLALQELVRQ 208
|
|
| PRK13342 |
PRK13342 |
recombination factor protein RarA; Reviewed |
356-533 |
1.07e-04 |
|
recombination factor protein RarA; Reviewed
Pssm-ID: 237355 [Multi-domain] Cd Length: 413 Bit Score: 45.46 E-value: 1.07e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502653703 356 GPPGVGKTSLGESVARAMGRKFVRV--ALGGVrdeAEIRghrrtyvgaqsgRIVRAVREAGSM--NPVVLLDEV---DKV 428
Cdd:PRK13342 43 GPPGTGKTTLARIIAGATDAPFEALsaVTSGV---KDLR------------EVIEEARQRRSAgrRTILFIDEIhrfNKA 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502653703 429 GSDyrgdptaALLEVLDpaqNHTFrdhyleveldlsdVLFLA-TANVLESIPGPLLDRMEIVTLDGYTEDEKVAIardhl 507
Cdd:PRK13342 108 QQD-------ALLPHVE---DGTI-------------TLIGAtTENPSFEVNPALLSRAQVFELKPLSEEDIEQL----- 159
|
170 180
....*....|....*....|....*...
gi 502653703 508 lprqLDKAGLTTE--DVTVEEDALRRLA 533
Cdd:PRK13342 160 ----LKRALEDKErgLVELDDEALDALA 183
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
164-414 |
1.30e-04 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 45.70 E-value: 1.30e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502653703 164 LSTQRKAEILETADPADRLSLLVEWAREHLAELDVAETIRKDVQEGMEKQQREFLLRQQLAAVRKELSELNGTSPETEEE 243
Cdd:COG1196 399 AAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAA 478
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502653703 244 DYRARVEAAdlpekvREAALKEVDKLERTSDQSPETGWIRTWL--------DTVLDIPWNERTEDSYDIAAARAVLDADH 315
Cdd:COG1196 479 LAELLEELA------EAAARLLLLLEAEADYEGFLEGVKAALLlaglrglaGAVAVLIGVEAAYEAALEAALAAALQNIV 552
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502653703 316 TGLDDVKDRIIEYLAVR--GRRAEKGLGVVGGRRSGAVLALAGPPGVGKTSLGESVARAMGRKFVRVALGGVRDEAEIRG 393
Cdd:COG1196 553 VEDDEVAAAAIEYLKAAkaGRATFLPLDKIRARAALAAALARGAIGAAVDLVASDLREADARYYVLGDTLLGRTLVAARL 632
|
250 260
....*....|....*....|.
gi 502653703 394 HRRTYVGAQSGRIVRAVREAG 414
Cdd:COG1196 633 EAALRRAVTLAGRLREVTLEG 653
|
|
| PRK04195 |
PRK04195 |
replication factor C large subunit; Provisional |
345-533 |
2.95e-04 |
|
replication factor C large subunit; Provisional
Pssm-ID: 235250 [Multi-domain] Cd Length: 482 Bit Score: 44.14 E-value: 2.95e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502653703 345 GRRSGAVLaLAGPPGVGKTSLGESVARAMGRKFVRV-AlggvRDEaeirghrRTYvgaqsGRIVRAVREAGSMNP----- 418
Cdd:PRK04195 36 GKPKKALL-LYGPPGVGKTSLAHALANDYGWEVIELnA----SDQ-------RTA-----DVIERVAGEAATSGSlfgar 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502653703 419 --VVLLDEVD--KVGSDYRGdpTAALLEVLDPAQNHTfrdhyleveldlsdVLflaTANVLESIPG-PLLDRMEIVTLDG 493
Cdd:PRK04195 99 rkLILLDEVDgiHGNEDRGG--ARAILELIKKAKQPI--------------IL---TANDPYDPSLrELRNACLMIEFKR 159
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 502653703 494 YTEDEKVAIARDHllprqldkagLTTEDVTVEEDALRRLA 533
Cdd:PRK04195 160 LSTRSIVPVLKRI----------CRKEGIECDDEALKEIA 189
|
|
| RarA |
COG2256 |
Replication-associated recombination protein RarA (DNA-dependent ATPase) [Replication, ... |
356-533 |
3.36e-04 |
|
Replication-associated recombination protein RarA (DNA-dependent ATPase) [Replication, recombination and repair];
Pssm-ID: 441857 [Multi-domain] Cd Length: 439 Bit Score: 43.89 E-value: 3.36e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502653703 356 GPPGVGKTSLGESVARAMGRKFVRV--ALGGVrdeAEIRghrrtyvgaqsgRIV-RAVREAGSMNPVVL-LDEV---DKV 428
Cdd:COG2256 56 GPPGTGKTTLARLIANATDAEFVALsaVTSGV---KDIR------------EVIeEARERRAYGRRTILfVDEIhrfNKA 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502653703 429 GSDyrgdptaALLevldpaqnhtfrdHYLE---VeldlsdVLFLATA-NVLESIPGPLLDRMEIVTLDGYTEDEKVAIAR 504
Cdd:COG2256 121 QQD-------ALL-------------PHVEdgtI------TLIGATTeNPSFEVNSALLSRCRVFVLKPLSEEDLEQLLE 174
|
170 180 190
....*....|....*....|....*....|.
gi 502653703 505 dhllpR--QLDKAGLTTEDVTVEEDALRRLA 533
Cdd:COG2256 175 -----RalADDERGLGGYKLELDDEALEALA 200
|
|
| clpA |
PRK11034 |
ATP-dependent Clp protease ATP-binding subunit; Provisional |
322-559 |
3.79e-04 |
|
ATP-dependent Clp protease ATP-binding subunit; Provisional
Pssm-ID: 236828 [Multi-domain] Cd Length: 758 Bit Score: 44.06 E-value: 3.79e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502653703 322 KDRIIEYL--AVRGRRAekGLGVvgGRRSGAVLALAGPPGVGKTSLGESVARAMGRKFVRValggvrDEAEIrGHRRT-- 397
Cdd:PRK11034 463 QDKAIEALteAIKMSRA--GLGH--EHKPVGSFLFAGPTGVGKTEVTVQLSKALGIELLRF------DMSEY-MERHTvs 531
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502653703 398 --------YVG-AQSGRIVRAVREagsmNP--VVLLDEVDKVGSDYRGdptaALLEVLDpaqNHTFRDHYLEvELDLSDV 466
Cdd:PRK11034 532 rligappgYVGfDQGGLLTDAVIK----HPhaVLLLDEIEKAHPDVFN----LLLQVMD---NGTLTDNNGR-KADFRNV 599
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502653703 467 LFLATAN--VLESIPGPLLDRMEIVTLDGYTEDEKV-----------AIARDHL---------------LPRQLDKAGLT 518
Cdd:PRK11034 600 VLVMTTNagVRETERKSIGLIHQDNSTDAMEEIKKIftpefrnrldnIIWFDHLstdvihqvvdkfiveLQAQLDQKGVS 679
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 502653703 519 TEdvtVEEDALRRLAGE-YTREAGVRSLERSIARILRKVTAN 559
Cdd:PRK11034 680 LE---VSQEARDWLAEKgYDRAMGARPMARVIQDNLKKPLAN 718
|
|
| RecA-like_Ycf46-like |
cd19507 |
ATPase domain of Ycf46 and similar ATPase domains; Ycf46 may play a role in the regulation of ... |
317-483 |
6.28e-04 |
|
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: 41.20 E-value: 6.28e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502653703 317 GLDDVKDriieYLAVRGRRAEK-----GLGVVGGrrsgavLALAGPPGVGKTSLGESVARAMGRKFVRVALGGVRDEaei 391
Cdd:cd19507 4 GLDNLKD----WLKKRKAAFSKqasayGLPTPKG------LLLVGIQGTGKSLTAKAIAGVWQLPLLRLDMGRLFGG--- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502653703 392 rghrrtYVGAQSGRIVRAVREAGSMNPVVLL-DEVDKV--GSDYRGD--PTAALLEvldpaqnhTFRDHYLEVEldlSDV 466
Cdd:cd19507 71 ------LVGESESRLRQMIQTAEAIAPCVLWiDEIEKGfsNADSKGDsgTSSRVLG--------TFLTWLQEKK---KPV 133
|
170
....*....|....*..
gi 502653703 467 LFLATANVLESIPGPLL 483
Cdd:cd19507 134 FVVATANNVQSLPPELL 150
|
|
| 44 |
PHA02544 |
clamp loader, small subunit; Provisional |
356-503 |
9.24e-04 |
|
clamp loader, small subunit; Provisional
Pssm-ID: 222866 [Multi-domain] Cd Length: 316 Bit Score: 42.28 E-value: 9.24e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502653703 356 GPPGVGKTSlgesVARAMGrkfvrvalggvrdeAEIrGHRRTYVGAQSGRI--VR--AVREAGSMN-----PVVLLDEVD 426
Cdd:PHA02544 50 PSPGTGKTT----VAKALC--------------NEV-GAEVLFVNGSDCRIdfVRnrLTRFASTVSltgggKVIIIDEFD 110
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 502653703 427 KVGsdyrgdpTAAllevldpAQNH--TFrdhyleVELDLSDVLFLATANVLESIPGPLLDRMEIVTLDGYTEDEKVAIA 503
Cdd:PHA02544 111 RLG-------LAD-------AQRHlrSF------MEAYSKNCSFIITANNKNGIIEPLRSRCRVIDFGVPTKEEQIEMM 169
|
|
| hflB |
PRK10733 |
ATP-dependent zinc metalloprotease FtsH; |
313-429 |
1.46e-03 |
|
ATP-dependent zinc metalloprotease FtsH;
Pssm-ID: 182683 [Multi-domain] Cd Length: 644 Bit Score: 41.94 E-value: 1.46e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502653703 313 ADHTGLDDVKDRI---IEYLAVRGRRAEkglgvVGGRRSGAVLaLAGPPGVGKTSLGESVARAMGRKFVRVAlggVRDEA 389
Cdd:PRK10733 152 ADVAGCDEAKEEVaelVEYLREPSRFQK-----LGGKIPKGVL-MVGPPGTGKTLLAKAIAGEAKVPFFTIS---GSDFV 222
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 502653703 390 EIrghrrtYVGAQSGRIVRAVREAGSMNP-VVLLDEVDKVG 429
Cdd:PRK10733 223 EM------FVGVGASRVRDMFEQAKKAAPcIIFIDEIDAVG 257
|
|
| RecA-like_NVL_r2-like |
cd19530 |
second of two ATPase domains of NVL (nuclear VCP-like protein) and similar ATPase domains; NVL ... |
318-426 |
4.03e-03 |
|
second 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: 410938 [Multi-domain] Cd Length: 161 Bit Score: 38.62 E-value: 4.03e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502653703 318 LDDVKDRIIEYLAVRGRRAE--KGLGVVggrrSGAVLALAGPPGVGKTSLGESVARAMGRKFVrvalggvrdeaEIRGHR 395
Cdd:cd19530 1 LDHVREELTMSILRPIKRPDiyKALGID----LPTGVLLYGPPGCGKTLLAKAVANESGANFI-----------SVKGPE 65
|
90 100 110
....*....|....*....|....*....|....*
gi 502653703 396 --RTYVGaQSGRIVRAV--REAGSMNPVVLLDEVD 426
Cdd:cd19530 66 llNKYVG-ESERAVRQVfqRARASAPCVIFFDEVD 99
|
|
| PRK09039 |
PRK09039 |
peptidoglycan -binding protein; |
104-271 |
4.06e-03 |
|
peptidoglycan -binding protein;
Pssm-ID: 181619 [Multi-domain] Cd Length: 343 Bit Score: 40.33 E-value: 4.06e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502653703 104 VQATLVEAVQVGERA-EELAKQYKALSTTI-LQKRGAWQVVDAVNQMDdpsvladssgyAPWLSTQRKAEILETADP--A 179
Cdd:PRK09039 40 AQFFLSREISGKDSAlDRLNSQIAELADLLsLERQGNQDLQDSVANLR-----------ASLSAAEAERSRLQALLAelA 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502653703 180 DRLSLLVEWAREHLAELDVAEtirkdvQEGMEKQQREFLLRQQLAAVRKELSELNGTSPETEEEDYRARVEAADLPEKVR 259
Cdd:PRK09039 109 GAGAAAEGRAGELAQELDSEK------QVSARALAQVELLNQQIAALRRQLAALEAALDASEKRDRESQAKIADLGRRLN 182
|
170
....*....|..
gi 502653703 260 EAALKEVDKLER 271
Cdd:PRK09039 183 VALAQRVQELNR 194
|
|
| RecA-like_CDC48_NLV2_r1-like |
cd19503 |
first of two ATPase domains of CDC48 and NLV2, and similar ATPase domains; CDC48 in yeast and ... |
317-426 |
4.26e-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: 4.26e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502653703 317 GLDDVKDRIIEYLAVRGRRAE--KGLGVVGGRrsgAVLaLAGPPGVGKTSLGESVARAMGRKFVrvalggVRDEAEIRGh 394
Cdd:cd19503 4 GLDEQIASLKELIELPLKYPElfRALGLKPPR---GVL-LHGPPGTGKTLLARAVANEAGANFL------SISGPSIVS- 72
|
90 100 110
....*....|....*....|....*....|...
gi 502653703 395 rrTYVGAQSGRIVRAVREAGSMNP-VVLLDEVD 426
Cdd:cd19503 73 --KYLGESEKNLREIFEEARSHAPsIIFIDEID 103
|
|
| RecA-like_PAN_like |
cd19502 |
proteasome activating nucleotidase PAN and related proteasome subunits; This subfamily ... |
354-443 |
4.61e-03 |
|
proteasome activating nucleotidase PAN and related proteasome subunits; This subfamily contains ATPase subunits of the eukaryotic 26S proteasome, and of the archaeal proteasome which carry out ATP-dependent degradation of substrates of the ubiquitin-proteasome pathway. The eukaryotic 26S proteasome consists of a proteolytic 20S core particle (CP), and a 19S regulatory particle (RP) which provides the ATP-dependence and the specificity for ubiquitinated proteins. In the archaea the RP is a homohexameric complex of proteasome-activating nucleotidase (PAN). This subfamily also includes various eukaryotic 26S subunits including, proteasome 26S subunit, ATPase 2 (PSMC2, also known as S7 and MSS1) which is a member of the 19S RP and has a chaperone like activity; and proteasome 20S subunit alpha 6 (PSMA6, also known as IOTA, p27K, and PROS27) which is a member of the 20S CP. This RecA-like_PAN subfamily belongs to the RecA-like NTPase family which includes the NTP binding domain of F1 and V1 H(+)ATPases, DnaB and related helicases as well as bacterial RecA and related eukaryotic and archaeal recombinases. The RecA-like NTPase family also includes bacterial conjugation proteins and related DNA transfer proteins involved in type II and type IV secretion.
Pssm-ID: 410910 [Multi-domain] Cd Length: 171 Bit Score: 38.86 E-value: 4.61e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502653703 354 LAGPPGVGKTSLGESVARAMGRKFVRVAlggvrdEAEIrghRRTYVGaQSGRIVRAVRE-AGSMNP-VVLLDEVDKVGSD 431
Cdd:cd19502 42 LYGPPGTGKTLLAKAVANHTDATFIRVV------GSEL---VQKYIG-EGARLVRELFEmAREKAPsIIFIDEIDAIGAK 111
|
90
....*....|..
gi 502653703 432 YRGDPTAALLEV 443
Cdd:cd19502 112 RFDSGTGGDREV 123
|
|
| SK |
cd00464 |
Shikimate kinase (SK) is the fifth enzyme in the shikimate pathway, a seven-step biosynthetic ... |
352-378 |
7.31e-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: 37.92 E-value: 7.31e-03
10 20
....*....|....*....|....*..
gi 502653703 352 LALAGPPGVGKTSLGESVARAMGRKFV 378
Cdd:cd00464 2 IVLIGMMGAGKTTVGRLLAKALGLPFV 28
|
|
| NTPase_1 |
pfam03266 |
NTPase; This domain is found across all species from bacteria to human, and the function was ... |
352-430 |
9.07e-03 |
|
NTPase; This domain is found across all species from bacteria to human, and the function was determined first in a hyperthermophilic bacterium to be an NTPase. The structure of one member-sequence represents a variation of the RecA fold, and implies that the function might be that of a DNA/RNA modifying enzyme. The sequence carries both a Walker A and Walker B motif which together are characteriztic of ATPases or GTPases. The protein exhibits an increased expression profile in human liver cholangiocarcinoma when compared to normal tissue.
Pssm-ID: 460869 Cd Length: 168 Bit Score: 37.99 E-value: 9.07e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502653703 352 LALAGPPGVGKTSLGESVARAMGRKFVRValGGVRDEaEIR--GHR--RTYVGAQSGRI-----VRAVREAGSMNPVVLL 422
Cdd:pfam03266 2 IFITGPPGVGKTTLVLKVAELLKSSGVKV--GGFYTP-EVRegGRRigFKIVDLASGEEgwlarVGAVSGPRVGKYVVNV 78
|
....*...
gi 502653703 423 DEVDKVGS 430
Cdd:pfam03266 79 ESFEEIAV 86
|
|
| RecA-like_NVL_r1-like |
cd19518 |
first of two ATPase domains of NVL (nuclear VCP-like protein) and similar ATPase domains; NVL ... |
317-430 |
9.43e-03 |
|
first of two ATPase domains of NVL (nuclear VCP-like protein) and similar ATPase domains; NVL exists in two forms with N-terminal extensions of different lengths in mammalian cells. NVL has two alternatively spliced isoforms, a short form, NVL1, and a long form, NVL2. NVL2, the major species, is mainly present in the nucleolus, whereas NVL1 is nucleoplasmic. Each has an N-terminal domain, followed by two tandem ATPase domains; this subfamily includes the first of the two ATPase domains. NVL2 is involved in the biogenesis of the 60S ribosome subunit by associating specifically with ribosome protein L5 and modulating the function of DOB1. NVL2 is also required for telomerase assembly and the regulation of telomerase activity, and is involved in pre-rRNA processing. The role of NVL1 is unclear. This RecA-like_NVL_r1-like subfamily belongs to the RecA-like NTPase family which includes the NTP binding domain of F1 and V1 H(+)ATPases, DnaB and related helicases as well as bacterial RecA and related eukaryotic and archaeal recombinases. The RecA-like NTPase family also includes bacterial conjugation proteins and related DNA transfer proteins involved in type II and type IV secretion.
Pssm-ID: 410926 [Multi-domain] Cd Length: 169 Bit Score: 37.77 E-value: 9.43e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502653703 317 GLDDVKDRIIEYLAVRGRRAE--KGLGVVGGRrsgAVLaLAGPPGVGKTSLGESVARAMGRKFVRVA----LGGVRDEAE 390
Cdd:cd19518 4 GMDSTLKELCELLIHPILPPEyfQHLGVEPPR---GVL-LHGPPGCGKTMLANAIAGELKVPFLKISateiVSGVSGESE 79
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 502653703 391 irghrrtyvgaqsGRIVRAVREAGSMNP-VVLLDEVDKVGS 430
Cdd:cd19518 80 -------------EKIRELFDQAISNAPcIVFIDEIDAITP 107
|
|
| |
