|
Name |
Accession |
Description |
Interval |
E-value |
| Lon |
COG0466 |
ATP-dependent Lon protease, bacterial type [Posttranslational modification, protein turnover, ... |
2-782 |
0e+00 |
|
ATP-dependent Lon protease, bacterial type [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440234 [Multi-domain] Cd Length: 785 Bit Score: 1446.75 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196876950 2 KTKQTKQMIMPILPLRDVVVFPHMVIPLFVGRNKSIRCLESAMEMDKQVFLVTQKHPSQDEPNVEDLYEVGTVANVLQLL 81
Cdd:COG0466 5 KEEEELPETLPLLPLRDVVVFPGMVIPLFVGREKSIKALEEAMEGDKLIGLVAQKDAEVEDPGPDDLYEVGTVAKILQLL 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196876950 82 QLPDGTVKVLVEGVTRAKIGDIVErkEDDFLIADIKPLKESKKTDKINQAMTRVLLSNFDDYAKLNKKVTQEVVDSIHLI 161
Cdd:COG0466 85 KLPDGTVKVLVEGLQRARIKEFVQ--EEPYLEAEVEPLEEEEEDDKELEALMRSLKEQFEEYVKLNPKIPPELLAALSNI 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196876950 162 KEPSQLADSIAATLFIKVEQKQDILVTADLEKRFELLISLMEAEIDLLQVEKNIRQRVKQQMEKAQKEYYLNEQIKAIHK 241
Cdd:COG0466 163 EDPGRLADFIASHLPLKIEEKQELLETLDVKERLEKLLELLEKEIEVLELEKKIRSRVKEQMEKSQREYYLREQLKAIQK 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196876950 242 ELGDIDNKPDEFEELNLKISKAKMPQEAKEKTLSELNKLKMMPAMSAEATVVRGYIDWMLQLPWHKRSKVKKDIQAAQKV 321
Cdd:COG0466 243 ELGEKDDGEDEIEELREKIEKAKLPEEVKEKAEKELKKLERMPPMSAEATVIRNYLDWLLDLPWGKRTKDNLDLKKAEKI 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196876950 322 LDKDHYGLERVKDRILEYLAVQGRVNKVKGPILCLVGPPGVGKTSLGQSIAKATGRQYVRMALGGVRDEAEIRGHRRTYI 401
Cdd:COG0466 323 LDEDHYGLEKVKERILEYLAVRKLKKKLKGPILCLVGPPGVGKTSLGKSIARALGRKFVRISLGGVRDEAEIRGHRRTYI 402
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196876950 402 GSMPGKLIQRMVKVGVKNPLFLLDEIDKMASDMRGDPASALLEVLDPEQNNAFNDHYLEVDYDLSDVMFVATANSM-NIP 480
Cdd:COG0466 403 GAMPGRIIQGLKKAGTKNPVFLLDEIDKMGSDFRGDPASALLEVLDPEQNNTFSDHYLEVPFDLSKVMFIATANSLdTIP 482
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196876950 481 APLLDRMEVIRLSGYTEDEKLNIAKQHLISKQIANSGLKAKEIDIDDSAIIGIIRYYTREAGVRSLEREIAKICRKVVKQ 560
Cdd:COG0466 483 APLLDRMEIIELSGYTEEEKLEIAKRYLIPKQLKEHGLKKEELKISDEALRKIIRGYTREAGVRNLEREIAKICRKVAKK 562
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196876950 561 LALNSKLhKVNISQDNLKDFLGVQRFDYGKSESENRIGQVTGLAWTEVGGDLLTIESVSVVGKGKLTYTGSLGDVMQESI 640
Cdd:COG0466 563 IAEGKKK-KVTITPKNLEKYLGVPRFRYEKAEEEDQVGVVTGLAWTEVGGDILFIEATLMPGKGKLTLTGQLGDVMKESA 641
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196876950 641 QTALTVVRSRAEKLGINNDFYEKRDIHVHVPDGATPKDGPSAGIAMCTSLVSTLTGNPVRSDVAMTGEITLRGEVLPIGG 720
Cdd:COG0466 642 QAALSYVRSRAEELGIDPDFFEKYDIHIHVPEGATPKDGPSAGITMATALVSALTGRPVRSDVAMTGEITLRGRVLPIGG 721
|
730 740 750 760 770 780
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1196876950 721 LKEKLLAAHRGGIKTALIPIDNVKDLEDIPDNVKSEIEIKPVKWIDEVLTIALQNNPFGIEP 782
Cdd:COG0466 722 LKEKLLAAHRAGIKTVILPKENEKDLEEIPEEVKKGLEFHPVEHIDEVLKIALEKEPEPLPK 783
|
|
| PRK10787 |
PRK10787 |
DNA-binding ATP-dependent protease La; Provisional |
1-783 |
0e+00 |
|
DNA-binding ATP-dependent protease La; Provisional
Pssm-ID: 182730 [Multi-domain] Cd Length: 784 Bit Score: 1271.02 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196876950 1 MKTKQTKQMIMPILPLRDVVVFPHMVIPLFVGRNKSIRCLESAMEMDKQVFLVTQKHPSQDEPNVEDLYEVGTVANVLQL 80
Cdd:PRK10787 1 MNPERSERIEIPVLPLRDVVVYPHMVIPLFVGREKSIRCLEAAMDHDKKIMLVAQKEASTDEPGVNDLFTVGTVASILQM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196876950 81 LQLPDGTVKVLVEGVTRAKIGDIVERKEddFLIADIKPLKESKKTDKINQAMTRVLLSNFDDYAKLNKKVTQEVVDSIHL 160
Cdd:PRK10787 81 LKLPDGTVKVLVEGLQRARISALSDNGE--HFSAKAEYLESPTIDEREQEVLVRTAISQFEGYIKLNKKIPPEVLTSLNS 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196876950 161 IKEPSQLADSIAATLFIKVEQKQDILVTADLEKRFELLISLMEAEIDLLQVEKNIRQRVKQQMEKAQKEYYLNEQIKAIH 240
Cdd:PRK10787 159 IDDPARLADTIAAHMPLKLADKQSVLEMSDVNERLEYLMAMMESEIDLLQVEKRIRNRVKKQMEKSQREYYLNEQMKAIQ 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196876950 241 KELGDIDNKPDEFEELNLKISKAKMPQEAKEKTLSELNKLKMMPAMSAEATVVRGYIDWMLQLPWHKRSKVKKDIQAAQK 320
Cdd:PRK10787 239 KELGEMDDAPDENEALKRKIDAAKMPKEAKEKAEAELQKLKMMSPMSAEATVVRGYIDWMVQVPWNARSKVKKDLRQAQE 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196876950 321 VLDKDHYGLERVKDRILEYLAVQGRVNKVKGPILCLVGPPGVGKTSLGQSIAKATGRQYVRMALGGVRDEAEIRGHRRTY 400
Cdd:PRK10787 319 ILDTDHYGLERVKDRILEYLAVQSRVNKIKGPILCLVGPPGVGKTSLGQSIAKATGRKYVRMALGGVRDEAEIRGHRRTY 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196876950 401 IGSMPGKLIQRMVKVGVKNPLFLLDEIDKMASDMRGDPASALLEVLDPEQNNAFNDHYLEVDYDLSDVMFVATANSMNIP 480
Cdd:PRK10787 399 IGSMPGKLIQKMAKVGVKNPLFLLDEIDKMSSDMRGDPASALLEVLDPEQNVAFSDHYLEVDYDLSDVMFVATSNSMNIP 478
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196876950 481 APLLDRMEVIRLSGYTEDEKLNIAKQHLISKQIANSGLKAKEIDIDDSAIIGIIRYYTREAGVRSLEREIAKICRKVVKQ 560
Cdd:PRK10787 479 APLLDRMEVIRLSGYTEDEKLNIAKRHLLPKQIERNALKKGELTVDDSAIIGIIRYYTREAGVRSLEREISKLCRKAVKQ 558
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196876950 561 LALNSKLHKVNISQDNLKDFLGVQRFDYGKSESENRIGQVTGLAWTEVGGDLLTIESVSVVGKGKLTYTGSLGDVMQESI 640
Cdd:PRK10787 559 LLLDKSLKHIEINGDNLHDYLGVQRFDYGRADNENRVGQVTGLAWTEVGGDLLTIETACVPGKGKLTYTGSLGEVMQESI 638
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196876950 641 QTALTVVRSRAEKLGINNDFYEKRDIHVHVPDGATPKDGPSAGIAMCTSLVSTLTGNPVRSDVAMTGEITLRGEVLPIGG 720
Cdd:PRK10787 639 QAALTVVRARAEKLGINPDFYEKRDIHVHVPEGATPKDGPSAGIAMCTALVSCLTGNPVRADVAMTGEITLRGQVLPIGG 718
|
730 740 750 760 770 780
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1196876950 721 LKEKLLAAHRGGIKTALIPIDNVKDLEDIPDNVKSEIEIKPVKWIDEVLTIALQNNPFGIEPV 783
Cdd:PRK10787 719 LKEKLLAAHRGGIKTVLIPFENKRDLEEIPDNVIADLDIHPVKRIEEVLTLALQNEPSGMQVV 781
|
|
| lon |
TIGR00763 |
endopeptidase La; This protein, the ATP-dependent serine endopeptidase La, is induced by heat ... |
12-773 |
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: 1076.55 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196876950 12 PILPLRDVVVFPHMVIPLFVGRNKSIRCLESAMEMD-KQVFLVTQKHPSQDEPNVEDLYEVGTVANVLQLLQLPD---GT 87
Cdd:TIGR00763 1 PLLPLRRRPLFPGMIKPIDVGREKSIKLIKEALRLKqPYLGLFLQKDDDNEEPEEDDIYSVGVVAQILEMLPLPSsgtAT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196876950 88 VKVLVEGVTRAKIGDIVERKedDFLIADIKPLKES--KKTDKINQAMTRVLLSNFDDYAKLNK--KVTQEVVDSIHLIKE 163
Cdd:TIGR00763 81 YKVVVEGLRRIRIKELSDKG--GYLVVRVDNLKEEpfDKDDEEIKALTREIKETFRELISLSKlfREQPALLSALEDIDE 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196876950 164 PSQLADSIAATLFIK-VEQKQDILVTADLEKRFELLISLMEAEIDLLQVEKNIRQRVKQQMEKAQKEYYLNEQIKAIHKE 242
Cdd:TIGR00763 159 PGRLADFVAASLQLKeKDELQEVLETVNIEKRLKKALELLKKELELLKLQNKITKKVEEKMEKTQREYYLREQLKAIKKE 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196876950 243 LGDIDNKPDEFEELNLKISKAKMPQEAKEKTLSELNKLKMMPAMSAEATVVRGYIDWMLQLPWHKRSKVKKDIQAAQKVL 322
Cdd:TIGR00763 239 LGIEKDDKDELEKLKEKLEELKLPEEVKKVIEKELTKLSLLEPSSSEFTVTRNYLDWLTDLPWGKYSKENLDLKRAKEIL 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196876950 323 DKDHYGLERVKDRILEYLAVQGRVNKVKGPILCLVGPPGVGKTSLGQSIAKATGRQYVRMALGGVRDEAEIRGHRRTYIG 402
Cdd:TIGR00763 319 DEDHYGLKKVKERILEYLAVQKLRGKMKGPILCLVGPPGVGKTSLGKSIAKALNRKFVRFSLGGVRDEAEIRGHRRTYVG 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196876950 403 SMPGKLIQRMVKVGVKNPLFLLDEIDKMASDMRGDPASALLEVLDPEQNNAFNDHYLEVDYDLSDVMFVATANSMN-IPA 481
Cdd:TIGR00763 399 AMPGRIIQGLKKAKTKNPLFLLDEIDKIGSSFRGDPASALLEVLDPEQNNAFSDHYLDVPFDLSKVIFIATANSIDtIPR 478
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196876950 482 PLLDRMEVIRLSGYTEDEKLNIAKQHLISKQIANSGLKAKEIDIDDSAIIGIIRYYTREAGVRSLEREIAKICRKVVKQL 561
Cdd:TIGR00763 479 PLLDRMEVIELSGYTEEEKLEIAKKYLIPKALEDHGLKPDELKITDEALLLLIKYYTREAGVRNLERQIEKICRKAAVKL 558
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196876950 562 ALNSKLHK-----VNISQDNLKDFLGVQRFDYGKSESENRIGQVTGLAWTEVGGDLLTIESVSVVGKGKLTYTGSLGDVM 636
Cdd:TIGR00763 559 VEQGEKKKseaesVVITPDNLKKYLGKPVFTYERAYEVTPPGVVMGLAWTPMGGDTLFIETTKVAGKGSLELTGQLGDVM 638
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196876950 637 QESIQTALTVVRSRAEKLGINNDFYEKRDIHVHVPDGATPKDGPSAGIAMCTSLVSTLTGNPVRSDVAMTGEITLRGEVL 716
Cdd:TIGR00763 639 KESAQIALTYVRSIAADLGISPNFFEKADIHLHVPEGATPKDGPSAGITMATALLSLATGKPVRPDVAMTGEITLRGKVL 718
|
730 740 750 760 770
....*....|....*....|....*....|....*....|....*....|....*..
gi 1196876950 717 PIGGLKEKLLAAHRGGIKTALIPIDNVKDLEDIPDNVKSEIEIKPVKWIDEVLTIAL 773
Cdd:TIGR00763 719 PIGGLKEKTIAAKRAGIKTIILPEKNRRDLEELPENVKEGLEIHFVKHYDEVLKKAF 775
|
|
| RecA-like_Lon |
cd19500 |
lon protease homolog 2 peroxisomal; Lon protease (also known as Lon peptidase) is an ... |
315-495 |
1.17e-123 |
|
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: 368.42 E-value: 1.17e-123
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196876950 315 IQAAQKVLDKDHYGLERVKDRILEYLAVQGRVNKVKGPILCLVGPPGVGKTSLGQSIAKATGRQYVRMALGGVRDEAEIR 394
Cdd:cd19500 1 IKKARKVLDADHYGLEDVKERILEYLAVRKLKGSMKGPILCLVGPPGVGKTSLGKSIARALGRKFVRISLGGVRDEAEIR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196876950 395 GHRRTYIGSMPGKLIQRMVKVGVKNPLFLLDEIDKMASDMRGDPASALLEVLDPEQNNAFNDHYLEVDYDLSDVMFVATA 474
Cdd:cd19500 81 GHRRTYVGAMPGRIIQALKKAGTNNPVFLLDEIDKIGSSFRGDPASALLEVLDPEQNSTFSDHYLDVPFDLSKVLFIATA 160
|
170 180
....*....|....*....|..
gi 1196876950 475 NSM-NIPAPLLDRMEVIRLSGY 495
Cdd:cd19500 161 NSLdTIPGPLLDRMEIIELSGY 182
|
|
| Lon_C |
pfam05362 |
Lon protease (S16) C-terminal proteolytic domain; The Lon serine proteases must hydrolyse ATP ... |
571-773 |
1.23e-121 |
|
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: 364.25 E-value: 1.23e-121
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196876950 571 NISQDNLKDFLGVQRFDYGKSESENRIGQVTGLAWTEVGGDLLTIESVSVVGKGKLTYTGSLGDVMQESIQTALTVVRSR 650
Cdd:pfam05362 1 KVTAKNLEKYLGVPRFRYGEAEKEDQVGVVTGLAWTEVGGDLLTIEAVIMPGKGKLTLTGQLGDVMKESAQAALSYVRSR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196876950 651 AEKLGINNDFYEKRDIHVHVPDGATPKDGPSAGIAMCTSLVSTLTGNPVRSDVAMTGEITLRGEVLPIGGLKEKLLAAHR 730
Cdd:pfam05362 81 AEELGIDPDFFEKKDIHIHVPEGATPKDGPSAGVTMATALVSALTGIPVRKDVAMTGEITLRGRVLPIGGLKEKLLAAHR 160
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1196876950 731 GGIKTALIPIDNVKDLEDIPDNVKSEIEIKPVKWIDEVLTIAL 773
Cdd:pfam05362 161 AGIKTVIIPKENEKDLEDIPENVREGLEIIPVEHVDEVLKHAL 203
|
|
| LON |
smart00464 |
Found in ATP-dependent protease La (LON); N-terminal domain of the ATP-dependent protease La ... |
12-62 |
8.36e-08 |
|
Found in ATP-dependent protease La (LON); N-terminal domain of the ATP-dependent protease La (LON), present also in other bacterial ORFs.
Pssm-ID: 197740 [Multi-domain] Cd Length: 92 Bit Score: 50.51 E-value: 8.36e-08
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 1196876950 12 PILPLRDVVVFPHMVIPLFVGRNKSIRCLESAMeMDKQ---VFLVTQKHPSQDE 62
Cdd:smart00464 3 PLLPIRRRPLFPGFVLPIPVKRPKSVAAIKEAL-RRSQpyvIVFLLQDDPTETP 55
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| Lon |
COG0466 |
ATP-dependent Lon protease, bacterial type [Posttranslational modification, protein turnover, ... |
2-782 |
0e+00 |
|
ATP-dependent Lon protease, bacterial type [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440234 [Multi-domain] Cd Length: 785 Bit Score: 1446.75 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196876950 2 KTKQTKQMIMPILPLRDVVVFPHMVIPLFVGRNKSIRCLESAMEMDKQVFLVTQKHPSQDEPNVEDLYEVGTVANVLQLL 81
Cdd:COG0466 5 KEEEELPETLPLLPLRDVVVFPGMVIPLFVGREKSIKALEEAMEGDKLIGLVAQKDAEVEDPGPDDLYEVGTVAKILQLL 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196876950 82 QLPDGTVKVLVEGVTRAKIGDIVErkEDDFLIADIKPLKESKKTDKINQAMTRVLLSNFDDYAKLNKKVTQEVVDSIHLI 161
Cdd:COG0466 85 KLPDGTVKVLVEGLQRARIKEFVQ--EEPYLEAEVEPLEEEEEDDKELEALMRSLKEQFEEYVKLNPKIPPELLAALSNI 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196876950 162 KEPSQLADSIAATLFIKVEQKQDILVTADLEKRFELLISLMEAEIDLLQVEKNIRQRVKQQMEKAQKEYYLNEQIKAIHK 241
Cdd:COG0466 163 EDPGRLADFIASHLPLKIEEKQELLETLDVKERLEKLLELLEKEIEVLELEKKIRSRVKEQMEKSQREYYLREQLKAIQK 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196876950 242 ELGDIDNKPDEFEELNLKISKAKMPQEAKEKTLSELNKLKMMPAMSAEATVVRGYIDWMLQLPWHKRSKVKKDIQAAQKV 321
Cdd:COG0466 243 ELGEKDDGEDEIEELREKIEKAKLPEEVKEKAEKELKKLERMPPMSAEATVIRNYLDWLLDLPWGKRTKDNLDLKKAEKI 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196876950 322 LDKDHYGLERVKDRILEYLAVQGRVNKVKGPILCLVGPPGVGKTSLGQSIAKATGRQYVRMALGGVRDEAEIRGHRRTYI 401
Cdd:COG0466 323 LDEDHYGLEKVKERILEYLAVRKLKKKLKGPILCLVGPPGVGKTSLGKSIARALGRKFVRISLGGVRDEAEIRGHRRTYI 402
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196876950 402 GSMPGKLIQRMVKVGVKNPLFLLDEIDKMASDMRGDPASALLEVLDPEQNNAFNDHYLEVDYDLSDVMFVATANSM-NIP 480
Cdd:COG0466 403 GAMPGRIIQGLKKAGTKNPVFLLDEIDKMGSDFRGDPASALLEVLDPEQNNTFSDHYLEVPFDLSKVMFIATANSLdTIP 482
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196876950 481 APLLDRMEVIRLSGYTEDEKLNIAKQHLISKQIANSGLKAKEIDIDDSAIIGIIRYYTREAGVRSLEREIAKICRKVVKQ 560
Cdd:COG0466 483 APLLDRMEIIELSGYTEEEKLEIAKRYLIPKQLKEHGLKKEELKISDEALRKIIRGYTREAGVRNLEREIAKICRKVAKK 562
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196876950 561 LALNSKLhKVNISQDNLKDFLGVQRFDYGKSESENRIGQVTGLAWTEVGGDLLTIESVSVVGKGKLTYTGSLGDVMQESI 640
Cdd:COG0466 563 IAEGKKK-KVTITPKNLEKYLGVPRFRYEKAEEEDQVGVVTGLAWTEVGGDILFIEATLMPGKGKLTLTGQLGDVMKESA 641
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196876950 641 QTALTVVRSRAEKLGINNDFYEKRDIHVHVPDGATPKDGPSAGIAMCTSLVSTLTGNPVRSDVAMTGEITLRGEVLPIGG 720
Cdd:COG0466 642 QAALSYVRSRAEELGIDPDFFEKYDIHIHVPEGATPKDGPSAGITMATALVSALTGRPVRSDVAMTGEITLRGRVLPIGG 721
|
730 740 750 760 770 780
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1196876950 721 LKEKLLAAHRGGIKTALIPIDNVKDLEDIPDNVKSEIEIKPVKWIDEVLTIALQNNPFGIEP 782
Cdd:COG0466 722 LKEKLLAAHRAGIKTVILPKENEKDLEEIPEEVKKGLEFHPVEHIDEVLKIALEKEPEPLPK 783
|
|
| PRK10787 |
PRK10787 |
DNA-binding ATP-dependent protease La; Provisional |
1-783 |
0e+00 |
|
DNA-binding ATP-dependent protease La; Provisional
Pssm-ID: 182730 [Multi-domain] Cd Length: 784 Bit Score: 1271.02 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196876950 1 MKTKQTKQMIMPILPLRDVVVFPHMVIPLFVGRNKSIRCLESAMEMDKQVFLVTQKHPSQDEPNVEDLYEVGTVANVLQL 80
Cdd:PRK10787 1 MNPERSERIEIPVLPLRDVVVYPHMVIPLFVGREKSIRCLEAAMDHDKKIMLVAQKEASTDEPGVNDLFTVGTVASILQM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196876950 81 LQLPDGTVKVLVEGVTRAKIGDIVERKEddFLIADIKPLKESKKTDKINQAMTRVLLSNFDDYAKLNKKVTQEVVDSIHL 160
Cdd:PRK10787 81 LKLPDGTVKVLVEGLQRARISALSDNGE--HFSAKAEYLESPTIDEREQEVLVRTAISQFEGYIKLNKKIPPEVLTSLNS 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196876950 161 IKEPSQLADSIAATLFIKVEQKQDILVTADLEKRFELLISLMEAEIDLLQVEKNIRQRVKQQMEKAQKEYYLNEQIKAIH 240
Cdd:PRK10787 159 IDDPARLADTIAAHMPLKLADKQSVLEMSDVNERLEYLMAMMESEIDLLQVEKRIRNRVKKQMEKSQREYYLNEQMKAIQ 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196876950 241 KELGDIDNKPDEFEELNLKISKAKMPQEAKEKTLSELNKLKMMPAMSAEATVVRGYIDWMLQLPWHKRSKVKKDIQAAQK 320
Cdd:PRK10787 239 KELGEMDDAPDENEALKRKIDAAKMPKEAKEKAEAELQKLKMMSPMSAEATVVRGYIDWMVQVPWNARSKVKKDLRQAQE 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196876950 321 VLDKDHYGLERVKDRILEYLAVQGRVNKVKGPILCLVGPPGVGKTSLGQSIAKATGRQYVRMALGGVRDEAEIRGHRRTY 400
Cdd:PRK10787 319 ILDTDHYGLERVKDRILEYLAVQSRVNKIKGPILCLVGPPGVGKTSLGQSIAKATGRKYVRMALGGVRDEAEIRGHRRTY 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196876950 401 IGSMPGKLIQRMVKVGVKNPLFLLDEIDKMASDMRGDPASALLEVLDPEQNNAFNDHYLEVDYDLSDVMFVATANSMNIP 480
Cdd:PRK10787 399 IGSMPGKLIQKMAKVGVKNPLFLLDEIDKMSSDMRGDPASALLEVLDPEQNVAFSDHYLEVDYDLSDVMFVATSNSMNIP 478
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196876950 481 APLLDRMEVIRLSGYTEDEKLNIAKQHLISKQIANSGLKAKEIDIDDSAIIGIIRYYTREAGVRSLEREIAKICRKVVKQ 560
Cdd:PRK10787 479 APLLDRMEVIRLSGYTEDEKLNIAKRHLLPKQIERNALKKGELTVDDSAIIGIIRYYTREAGVRSLEREISKLCRKAVKQ 558
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196876950 561 LALNSKLHKVNISQDNLKDFLGVQRFDYGKSESENRIGQVTGLAWTEVGGDLLTIESVSVVGKGKLTYTGSLGDVMQESI 640
Cdd:PRK10787 559 LLLDKSLKHIEINGDNLHDYLGVQRFDYGRADNENRVGQVTGLAWTEVGGDLLTIETACVPGKGKLTYTGSLGEVMQESI 638
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196876950 641 QTALTVVRSRAEKLGINNDFYEKRDIHVHVPDGATPKDGPSAGIAMCTSLVSTLTGNPVRSDVAMTGEITLRGEVLPIGG 720
Cdd:PRK10787 639 QAALTVVRARAEKLGINPDFYEKRDIHVHVPEGATPKDGPSAGIAMCTALVSCLTGNPVRADVAMTGEITLRGQVLPIGG 718
|
730 740 750 760 770 780
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1196876950 721 LKEKLLAAHRGGIKTALIPIDNVKDLEDIPDNVKSEIEIKPVKWIDEVLTIALQNNPFGIEPV 783
Cdd:PRK10787 719 LKEKLLAAHRGGIKTVLIPFENKRDLEEIPDNVIADLDIHPVKRIEEVLTLALQNEPSGMQVV 781
|
|
| lon |
TIGR00763 |
endopeptidase La; This protein, the ATP-dependent serine endopeptidase La, is induced by heat ... |
12-773 |
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: 1076.55 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196876950 12 PILPLRDVVVFPHMVIPLFVGRNKSIRCLESAMEMD-KQVFLVTQKHPSQDEPNVEDLYEVGTVANVLQLLQLPD---GT 87
Cdd:TIGR00763 1 PLLPLRRRPLFPGMIKPIDVGREKSIKLIKEALRLKqPYLGLFLQKDDDNEEPEEDDIYSVGVVAQILEMLPLPSsgtAT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196876950 88 VKVLVEGVTRAKIGDIVERKedDFLIADIKPLKES--KKTDKINQAMTRVLLSNFDDYAKLNK--KVTQEVVDSIHLIKE 163
Cdd:TIGR00763 81 YKVVVEGLRRIRIKELSDKG--GYLVVRVDNLKEEpfDKDDEEIKALTREIKETFRELISLSKlfREQPALLSALEDIDE 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196876950 164 PSQLADSIAATLFIK-VEQKQDILVTADLEKRFELLISLMEAEIDLLQVEKNIRQRVKQQMEKAQKEYYLNEQIKAIHKE 242
Cdd:TIGR00763 159 PGRLADFVAASLQLKeKDELQEVLETVNIEKRLKKALELLKKELELLKLQNKITKKVEEKMEKTQREYYLREQLKAIKKE 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196876950 243 LGDIDNKPDEFEELNLKISKAKMPQEAKEKTLSELNKLKMMPAMSAEATVVRGYIDWMLQLPWHKRSKVKKDIQAAQKVL 322
Cdd:TIGR00763 239 LGIEKDDKDELEKLKEKLEELKLPEEVKKVIEKELTKLSLLEPSSSEFTVTRNYLDWLTDLPWGKYSKENLDLKRAKEIL 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196876950 323 DKDHYGLERVKDRILEYLAVQGRVNKVKGPILCLVGPPGVGKTSLGQSIAKATGRQYVRMALGGVRDEAEIRGHRRTYIG 402
Cdd:TIGR00763 319 DEDHYGLKKVKERILEYLAVQKLRGKMKGPILCLVGPPGVGKTSLGKSIAKALNRKFVRFSLGGVRDEAEIRGHRRTYVG 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196876950 403 SMPGKLIQRMVKVGVKNPLFLLDEIDKMASDMRGDPASALLEVLDPEQNNAFNDHYLEVDYDLSDVMFVATANSMN-IPA 481
Cdd:TIGR00763 399 AMPGRIIQGLKKAKTKNPLFLLDEIDKIGSSFRGDPASALLEVLDPEQNNAFSDHYLDVPFDLSKVIFIATANSIDtIPR 478
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196876950 482 PLLDRMEVIRLSGYTEDEKLNIAKQHLISKQIANSGLKAKEIDIDDSAIIGIIRYYTREAGVRSLEREIAKICRKVVKQL 561
Cdd:TIGR00763 479 PLLDRMEVIELSGYTEEEKLEIAKKYLIPKALEDHGLKPDELKITDEALLLLIKYYTREAGVRNLERQIEKICRKAAVKL 558
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196876950 562 ALNSKLHK-----VNISQDNLKDFLGVQRFDYGKSESENRIGQVTGLAWTEVGGDLLTIESVSVVGKGKLTYTGSLGDVM 636
Cdd:TIGR00763 559 VEQGEKKKseaesVVITPDNLKKYLGKPVFTYERAYEVTPPGVVMGLAWTPMGGDTLFIETTKVAGKGSLELTGQLGDVM 638
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196876950 637 QESIQTALTVVRSRAEKLGINNDFYEKRDIHVHVPDGATPKDGPSAGIAMCTSLVSTLTGNPVRSDVAMTGEITLRGEVL 716
Cdd:TIGR00763 639 KESAQIALTYVRSIAADLGISPNFFEKADIHLHVPEGATPKDGPSAGITMATALLSLATGKPVRPDVAMTGEITLRGKVL 718
|
730 740 750 760 770
....*....|....*....|....*....|....*....|....*....|....*..
gi 1196876950 717 PIGGLKEKLLAAHRGGIKTALIPIDNVKDLEDIPDNVKSEIEIKPVKWIDEVLTIAL 773
Cdd:TIGR00763 719 PIGGLKEKTIAAKRAGIKTIILPEKNRRDLEELPENVKEGLEIHFVKHYDEVLKKAF 775
|
|
| RecA-like_Lon |
cd19500 |
lon protease homolog 2 peroxisomal; Lon protease (also known as Lon peptidase) is an ... |
315-495 |
1.17e-123 |
|
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: 368.42 E-value: 1.17e-123
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196876950 315 IQAAQKVLDKDHYGLERVKDRILEYLAVQGRVNKVKGPILCLVGPPGVGKTSLGQSIAKATGRQYVRMALGGVRDEAEIR 394
Cdd:cd19500 1 IKKARKVLDADHYGLEDVKERILEYLAVRKLKGSMKGPILCLVGPPGVGKTSLGKSIARALGRKFVRISLGGVRDEAEIR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196876950 395 GHRRTYIGSMPGKLIQRMVKVGVKNPLFLLDEIDKMASDMRGDPASALLEVLDPEQNNAFNDHYLEVDYDLSDVMFVATA 474
Cdd:cd19500 81 GHRRTYVGAMPGRIIQALKKAGTNNPVFLLDEIDKIGSSFRGDPASALLEVLDPEQNSTFSDHYLDVPFDLSKVLFIATA 160
|
170 180
....*....|....*....|..
gi 1196876950 475 NSM-NIPAPLLDRMEVIRLSGY 495
Cdd:cd19500 161 NSLdTIPGPLLDRMEIIELSGY 182
|
|
| Lon_C |
pfam05362 |
Lon protease (S16) C-terminal proteolytic domain; The Lon serine proteases must hydrolyse ATP ... |
571-773 |
1.23e-121 |
|
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: 364.25 E-value: 1.23e-121
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196876950 571 NISQDNLKDFLGVQRFDYGKSESENRIGQVTGLAWTEVGGDLLTIESVSVVGKGKLTYTGSLGDVMQESIQTALTVVRSR 650
Cdd:pfam05362 1 KVTAKNLEKYLGVPRFRYGEAEKEDQVGVVTGLAWTEVGGDLLTIEAVIMPGKGKLTLTGQLGDVMKESAQAALSYVRSR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196876950 651 AEKLGINNDFYEKRDIHVHVPDGATPKDGPSAGIAMCTSLVSTLTGNPVRSDVAMTGEITLRGEVLPIGGLKEKLLAAHR 730
Cdd:pfam05362 81 AEELGIDPDFFEKKDIHIHVPEGATPKDGPSAGVTMATALVSALTGIPVRKDVAMTGEITLRGRVLPIGGLKEKLLAAHR 160
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1196876950 731 GGIKTALIPIDNVKDLEDIPDNVKSEIEIKPVKWIDEVLTIAL 773
Cdd:pfam05362 161 AGIKTVIIPKENEKDLEDIPENVREGLEIIPVEHVDEVLKHAL 203
|
|
| LON_substr_bdg |
pfam02190 |
ATP-dependent protease La (LON) substrate-binding domain; This domain has been shown to be ... |
11-203 |
6.85e-51 |
|
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: 176.76 E-value: 6.85e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196876950 11 MPILPLRDVVVFPHMVIPLFVGRNKSIRCLESAMEMDKQ--VFLVTQKHPSQDEPNVEDLYEVGTVANVLQLLQLPDGTV 88
Cdd:pfam02190 2 LPLLPLRNTVLFPGMVLPLFVGRPRSIAAIEAALNKDKLygVLLVSQKDAEDEEPTPDDLYEVGTVAKIVQILKLPDGTY 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196876950 89 KVLVEGVTRAKIGDIVErKEDDFLIADIKPLKESKKTDKinQAMTRVLLSNFDDYAKLNKKVTQ-EVVDSIHLIKEPSQL 167
Cdd:pfam02190 82 KVLVEGLERVRIVELVK-KEEPYLRAEVEDLPEDSDELS--EALKALVKELIEKLRRLLKLLLPlELLLKIKDIENPGRL 158
|
170 180 190
....*....|....*....|....*....|....*.
gi 1196876950 168 ADSIAATLFIKVEQKQDILVTADLEKRFELLISLME 203
Cdd:pfam02190 159 ADLVAAILPLSPEEKQELLETLDVKERLEKVLELLN 194
|
|
| AAA |
pfam00004 |
ATPase family associated with various cellular activities (AAA); AAA family proteins often ... |
354-495 |
6.47e-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: 100.75 E-value: 6.47e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196876950 354 LCLVGPPGVGKTSLGQSIAKATGRQYVRMALGGVRDeaeirghrrTYIGSMPGKLIQRMVKVGVKNP-LFLLDEIDKMAS 432
Cdd:pfam00004 1 LLLYGPPGTGKTTLAKAVAKELGAPFIEISGSELVS---------KYVGESEKRLRELFEAAKKLAPcVIFIDEIDALAG 71
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1196876950 433 D-------MRGDPASALLEVLDPEQNNAfndhylevdydlSDVMFVATANSM-NIPAPLLDRMEVIRLSGY 495
Cdd:pfam00004 72 SrgsggdsESRRVVNQLLTELDGFTSSN------------SKVIVIAATNRPdKLDPALLGRFDRIIEFPL 130
|
|
| LON/PUA |
COG2802 |
Uncharacterized conserved protein, LON_N-like domain, ASCH/PUA-like superfamily [Function ... |
9-205 |
9.56e-21 |
|
Uncharacterized conserved protein, LON_N-like domain, ASCH/PUA-like superfamily [Function unknown];
Pssm-ID: 442054 [Multi-domain] Cd Length: 194 Bit Score: 90.71 E-value: 9.56e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196876950 9 MIMPILPLrDVVVFPHMVIPL--F-------VGRnksirCLESAMEmdkqvFLVTQKHPSQDEPNVEDLYEVGTVANVLQ 79
Cdd:COG2802 5 MELPLFPL-GAVLFPGGRLPLhiFepryldmVRD-----CLAGDRP-----FGVVLIREGREVGGPPPLYDVGTLARITD 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196876950 80 LLQLPDGTVKVLVEGVTRAKIGDIVERkEDDFLIADIKPL--KESKKTDKINQAMTRVLLSNFDDYAKLNKkvtqevVDS 157
Cdd:COG2802 74 FEELEDGRLDITLRGVQRFRILEELQE-DDPYRVAEVEWLpdEPDLPVPEELEALRERLLRLLRRYPELAG------LEA 146
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1196876950 158 IHLIKEPSQLADSIAATLFIKVEQKQDILVTADLEKRFELLISLMEAE 205
Cdd:COG2802 147 DPDLDDPEWLSNRLAELLPLDPEEKQALLEAPDLLERLELLLALLERE 194
|
|
| COG1750 |
COG1750 |
Predicted archaeal serine protease, S18 family [General function prediction only]; |
633-742 |
2.34e-20 |
|
Predicted archaeal serine protease, S18 family [General function prediction only];
Pssm-ID: 441356 [Multi-domain] Cd Length: 213 Bit Score: 90.04 E-value: 2.34e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196876950 633 GDVMQESIQTALTVVRSRAeklGINndfYEKRDIHVHVPDGATPKDGPSAGIAMCTSLVSTLTGNPVRSDVAMTGEITLR 712
Cdd:COG1750 69 GPDTQASARIAALVASLLA---GVD---LSSYDVYISIESDSPIVGGPSAGGAMTVATYAALLGLPLNKSVTMTGMINPD 142
|
90 100 110
....*....|....*....|....*....|
gi 1196876950 713 GEVLPIGGLKEKLLAAHRGGIKTALIPIDN 742
Cdd:COG1750 143 GSIGPVGGVYEKLEAAASAGAKYFLIPKGQ 172
|
|
| SpoVK |
COG0464 |
AAA+-type ATPase, SpoVK/Ycf46/Vps4 family [Cell wall/membrane/envelope biogenesis, Cell cycle ... |
328-560 |
2.72e-13 |
|
AAA+-type ATPase, SpoVK/Ycf46/Vps4 family [Cell wall/membrane/envelope biogenesis, Cell cycle control, cell division, chromosome partitioning, Signal transduction mechanisms];
Pssm-ID: 440232 [Multi-domain] Cd Length: 397 Bit Score: 72.64 E-value: 2.72e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196876950 328 GLERVKDRI-------LEYLAVQGRVNKVKGPILCLVGPPGVGKTSLGQSIAKATGRQYVRMALGGVRDEaeirghrrtY 400
Cdd:COG0464 161 GLEEVKEELrelvalpLKRPELREEYGLPPPRGLLLYGPPGTGKTLLARALAGELGLPLIEVDLSDLVSK---------Y 231
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196876950 401 IGSmPGKLIQRMVKV--GVKNPLFLLDEIDKMASDmRGdpasallEVLDPEQNNAFNdhYL--EVDYDLSDVMFVATANS 476
Cdd:COG0464 232 VGE-TEKNLREVFDKarGLAPCVLFIDEADALAGK-RG-------EVGDGVGRRVVN--TLltEMEELRSDVVVIAATNR 300
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196876950 477 M-NIPAPLLDRM-EVIRLSGYTEDEKLNIAKQHLISKQIansglkAKEIDIDdsAIIGIIRYYTreaGvrsleREIAKIC 554
Cdd:COG0464 301 PdLLDPALLRRFdEIIFFPLPDAEERLEIFRIHLRKRPL------DEDVDLE--ELAEATEGLS---G-----ADIRNVV 364
|
....*.
gi 1196876950 555 RKVVKQ 560
Cdd:COG0464 365 RRAALQ 370
|
|
| RecA-like_protease |
cd19481 |
proteases similar to RecA; RecA-like NTPases. This family includes the NTP binding domain of ... |
332-483 |
2.83e-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: 65.38 E-value: 2.83e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196876950 332 VKDRILEYLAVQG------RVNKVKGPILCLVGPPGVGKTSLGQSIAKATGRQYVRMALGGVRDEAeirghrRTYIGSMP 405
Cdd:cd19481 1 LKASLREAVEAPRrgsrlrRYGLGLPKGILLYGPPGTGKTLLAKALAGELGLPLIVVKLSSLLSKY------VGESEKNL 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196876950 406 GKLIQRMVKvgVKNPLFLLDEIDKMASDmRGDPA---------SALLEVLDPEQNnafndhylevdydLSDVMFVATAN- 475
Cdd:cd19481 75 RKIFERARR--LAPCILFIDEIDAIGRK-RDSSGesgelrrvlNQLLTELDGVNS-------------RSKVLVIAATNr 138
|
....*....
gi 1196876950 476 -SMNIPAPL 483
Cdd:cd19481 139 pDLLDPALL 147
|
|
| AAA |
cd00009 |
The AAA+ (ATPases Associated with a wide variety of cellular Activities) superfamily ... |
333-490 |
4.06e-11 |
|
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: 61.78 E-value: 4.06e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196876950 333 KDRILEYLAVQGRVNKVKGPILCLVGPPGVGKTSLGQSIAKATGRQYVRMA---LGGVRDEAEIRGHRRTYIgsmpgKLI 409
Cdd:cd00009 1 VGQEEAIEALREALELPPPKNLLLYGPPGTGKTTLARAIANELFRPGAPFLylnASDLLEGLVVAELFGHFL-----VRL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196876950 410 QRMVKVGVKNPLFLLDEIDKMASDMRgdpaSALLEVLdpeqnnafnDHYLEVDYDLSDVMFVATANSMN---IPAPLLDR 486
Cdd:cd00009 76 LFELAEKAKPGVLFIDEIDSLSRGAQ----NALLRVL---------ETLNDLRIDRENVRVIGATNRPLlgdLDRALYDR 142
|
....
gi 1196876950 487 MEVI 490
Cdd:cd00009 143 LDIR 146
|
|
| AAA_5 |
pfam07728 |
AAA domain (dynein-related subfamily); This Pfam entry includes some of the AAA proteins not ... |
354-487 |
1.63e-10 |
|
AAA domain (dynein-related subfamily); This Pfam entry includes some of the AAA proteins not detected by the pfam00004 model.
Pssm-ID: 400191 [Multi-domain] Cd Length: 135 Bit Score: 59.61 E-value: 1.63e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196876950 354 LCLVGPPGVGKTSLGQSIAKATGRQYVRMALGGvRD--EAEIRGHRRtyIGSMPGKLIQRMVKVGVKNP-LFLLDEIDKM 430
Cdd:pfam07728 2 VLLVGPPGTGKTELAERLAAALSNRPVFYVQLT-RDttEEDLFGRRN--IDPGGASWVDGPLVRAAREGeIAVLDEINRA 78
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1196876950 431 ASDMrgdpASALLEVLDpeqnnafNDHYL------EVDYDLSDVMFVATANS-----MNIPAPLLDRM 487
Cdd:pfam07728 79 NPDV----LNSLLSLLD-------ERRLLlpdggeLVKAAPDGFRLIATMNPldrglNELSPALRSRF 135
|
|
| Sms |
COG1066 |
DNA repair protein RadA/Sms, contains AAA+ ATPase domain [Replication, recombination and ... |
662-773 |
1.68e-10 |
|
DNA repair protein RadA/Sms, contains AAA+ ATPase domain [Replication, recombination and repair];
Pssm-ID: 440685 [Multi-domain] Cd Length: 453 Bit Score: 63.91 E-value: 1.68e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196876950 662 EKR--------DIHVHVPDGATPKDgPSAGIAMCTSLVSTLTGNPVRSDVAMTGEITLRGEVLPIGGLKEKLLAAHRGGI 733
Cdd:COG1066 341 EKRaglplgdqDVYVNVVGGLKITE-PAADLAVALAIASSFRDRPLPPDTVFFGEVGLTGEIRPVSRIEQRLKEAAKLGF 419
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 1196876950 734 KTALIPIDNVKDLEDipdnvkSEIEIKPVKWIDEVLTIAL 773
Cdd:COG1066 420 KRAIVPKGNKKKLKP------KGIEIIGVSTLEEALEALF 453
|
|
| SdrC |
COG3480 |
Predicted secreted protein YlbL, contains PDZ domain [Signal transduction mechanisms]; |
679-774 |
1.84e-10 |
|
Predicted secreted protein YlbL, contains PDZ domain [Signal transduction mechanisms];
Pssm-ID: 442703 [Multi-domain] Cd Length: 344 Bit Score: 63.29 E-value: 1.84e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196876950 679 GPSAGIAMCTSLVSTLTGNPVRS--DVAMTGEITLRGEVLPIGGLKEKLLAAHRGGIKTALIPIDNVKD-LEDIPDNVKs 755
Cdd:COG3480 240 GPSAGLMFALGIYDQLTPGDLTGgkKIAGTGTIDADGTVGPIGGIDQKVVAARRAGATIFLAPASNCAEaVGTIPTGLK- 318
|
90
....*....|....*....
gi 1196876950 756 eieIKPVKWIDEVLTiALQ 774
Cdd:COG3480 319 ---VVPVDTLDDALD-ALE 333
|
|
| MoxR |
COG0714 |
MoxR-like ATPase [General function prediction only]; MoxR-like ATPase is part of the Pathway ... |
314-507 |
1.41e-09 |
|
MoxR-like ATPase [General function prediction only]; MoxR-like ATPase is part of the Pathway/BioSystem: Cobalamine/B12 biosynthesis
Pssm-ID: 440478 [Multi-domain] Cd Length: 292 Bit Score: 60.18 E-value: 1.41e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196876950 314 DIQAAQKVLDKDHYGLERVKDRILeyLAVQGRvnkvkGPILcLVGPPGVGKTSLGQSIAKATGRQYVRMalggvrdeaei 393
Cdd:COG0714 2 TEARLRAEIGKVYVGQEELIELVL--IALLAG-----GHLL-LEGVPGVGKTTLAKALARALGLPFIRI----------- 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196876950 394 rghrRTYIGSMPGKLIQRMV---KVG----VKNPLF----LLDEIDkmasdmRGDPA--SALLEVLDpeqnnafnDHYLE 460
Cdd:COG0714 63 ----QFTPDLLPSDILGTYIydqQTGefefRPGPLFanvlLADEIN------RAPPKtqSALLEAME--------ERQVT 124
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1196876950 461 VD---YDLSDVMFV-ATANSM------NIPAPLLDRMeVIRLS-GY-TEDEKLNIAKQH 507
Cdd:COG0714 125 IPggtYKLPEPFLViATQNPIeqegtyPLPEAQLDRF-LLKLYiGYpDAEEEREILRRH 182
|
|
| LonB |
COG1067 |
Predicted ATP-dependent protease [Posttranslational modification, protein turnover, chaperones] ... |
678-771 |
5.43e-09 |
|
Predicted ATP-dependent protease [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440686 [Multi-domain] Cd Length: 742 Bit Score: 59.57 E-value: 5.43e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196876950 678 DGPSAGIAMCTSLVSTLTGNPVRSDVAMTGEITLRGEVLPIGGLKEKL-----LAAHRG-----GIktaLIPIDNVKDL- 746
Cdd:COG1067 592 DGDSASSAELYALLSALSGVPIRQDIAVTGSVNQHGEVQPIGGVNEKIegffdVCKARGltgkqGV---IIPAANVKNLm 668
|
90 100
....*....|....*....|....*...
gi 1196876950 747 --EDIPDNVKS-EIEIKPVKWIDEVLTI 771
Cdd:COG1067 669 lrDEVVEAVKAgQFHIYAVEHVDEAIEL 696
|
|
| LON |
smart00464 |
Found in ATP-dependent protease La (LON); N-terminal domain of the ATP-dependent protease La ... |
12-62 |
8.36e-08 |
|
Found in ATP-dependent protease La (LON); N-terminal domain of the ATP-dependent protease La (LON), present also in other bacterial ORFs.
Pssm-ID: 197740 [Multi-domain] Cd Length: 92 Bit Score: 50.51 E-value: 8.36e-08
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 1196876950 12 PILPLRDVVVFPHMVIPLFVGRNKSIRCLESAMeMDKQ---VFLVTQKHPSQDE 62
Cdd:smart00464 3 PLLPIRRRPLFPGFVLPIPVKRPKSVAAIKEAL-RRSQpyvIVFLLQDDPTETP 55
|
|
| RarA |
COG2256 |
Replication-associated recombination protein RarA (DNA-dependent ATPase) [Replication, ... |
358-536 |
3.97e-07 |
|
Replication-associated recombination protein RarA (DNA-dependent ATPase) [Replication, recombination and repair];
Pssm-ID: 441857 [Multi-domain] Cd Length: 439 Bit Score: 53.14 E-value: 3.97e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196876950 358 GPPGVGKTSLGQSIAKATGRQYVRM--ALGGVrdeAEIRghrrtyigsmpgKLIQ--RMVKVGVKNPLFLLDEI---DKM 430
Cdd:COG2256 56 GPPGTGKTTLARLIANATDAEFVALsaVTSGV---KDIR------------EVIEeaRERRAYGRRTILFVDEIhrfNKA 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196876950 431 ASDmrgdpasALLevldpeqnnafndHYLEvdydlsD--VMFVA--TAN-SMNIPAPLLDRMEVIRLSGYTEDEKLNIAK 505
Cdd:COG2256 121 QQD-------ALL-------------PHVE------DgtITLIGatTENpSFEVNSALLSRCRVFVLKPLSEEDLEQLLE 174
|
170 180 190
....*....|....*....|....*....|.
gi 1196876950 506 QHLISKQIansGLKAKEIDIDDSAIIGIIRY 536
Cdd:COG2256 175 RALADDER---GLGGYKLELDDEALEALARL 202
|
|
| PRK13342 |
PRK13342 |
recombination factor protein RarA; Reviewed |
358-591 |
4.28e-06 |
|
recombination factor protein RarA; Reviewed
Pssm-ID: 237355 [Multi-domain] Cd Length: 413 Bit Score: 50.08 E-value: 4.28e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196876950 358 GPPGVGKTSLGQSIAKATGRQYVRM--ALGGVrdeAEIRghrrtyigsmpgKLIQ--RMVKVGVKNPLFLLDEI---DKM 430
Cdd:PRK13342 43 GPPGTGKTTLARIIAGATDAPFEALsaVTSGV---KDLR------------EVIEeaRQRRSAGRRTILFIDEIhrfNKA 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196876950 431 ASDmrgdpasALLEVLdpEQNNafndhylevdydlsdVMFVA--TAN-SMNIPAPLLDRMEVIRLSGYTEDEklnIakqh 507
Cdd:PRK13342 108 QQD-------ALLPHV--EDGT---------------ITLIGatTENpSFEVNPALLSRAQVFELKPLSEED---I---- 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196876950 508 lisKQIANSGLKAKE---IDIDDSAIIGIIRYytreAG--VRS----LEreiakicrkvvkqLALNSklhKVNISQDNLK 578
Cdd:PRK13342 157 ---EQLLKRALEDKErglVELDDEALDALARL----ANgdARRalnlLE-------------LAALG---VDSITLELLE 213
|
250
....*....|...
gi 1196876950 579 DFLGVQRFDYGKS 591
Cdd:PRK13342 214 EALQKRAARYDKD 226
|
|
| COG1223 |
COG1223 |
Predicted ATPase, AAA+ superfamily [General function prediction only]; |
324-581 |
6.97e-06 |
|
Predicted ATPase, AAA+ superfamily [General function prediction only];
Pssm-ID: 440836 [Multi-domain] Cd Length: 246 Bit Score: 48.34 E-value: 6.97e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196876950 324 KDHYGLERVKD---RILEYLAVQGRVNKVKGP----ILcLVGPPGVGKTSLGQSIAKATGRQYVRMALGGVrdeaeirgh 396
Cdd:COG1223 2 DDVVGQEEAKKklkLIIKELRRRENLRKFGLWpprkIL-FYGPPGTGKTMLAEALAGELKLPLLTVRLDSL--------- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196876950 397 rrtyIGSMPGKLIQRMVKV--------GVknplFLLDEIDKMASDmRGDPAsallevLDPEQNNAFNDHYLEVDYDLSDV 468
Cdd:COG1223 72 ----IGSYLGETARNLRKLfdfarrapCV----IFFDEFDAIAKD-RGDQN------DVGEVKRVVNALLQELDGLPSGS 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196876950 469 MFVATANSMNI--PApLLDRM-EVIRLSGYTEDEKLNIAKQHLiskqianSGLKaKEIDIDDSAIigiiryytreagVRS 545
Cdd:COG1223 137 VVIAATNHPELldSA-LWRRFdEVIEFPLPDKEERKEILELNL-------KKFP-LPFELDLKKL------------AKK 195
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 1196876950 546 LE----REIAKICRKVVKQLALNSklhKVNISQDNLKDFL 581
Cdd:COG1223 196 LEglsgADIEKVLKTALKKAILED---REKVTKEDLEEAL 232
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
350-487 |
1.20e-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: 45.83 E-value: 1.20e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196876950 350 KGPILCLVGPPGVGKTSLGQSIAKATGRQYVRM-------ALGGVRDEAEIRGHRRTYIGSMPGKLIQRMVKV--GVKNP 420
Cdd:smart00382 1 PGEVILIVGPPGSGKTTLARALARELGPPGGGViyidgedILEEVLDQLLLIIVGGKKASGSGELRLRLALALarKLKPD 80
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1196876950 421 LFLLDEIDKMASDMRGDPASALLEVLDPEQNNAFNdhylevdydlsDVMFVATANSMNIPAPLLDRM 487
Cdd:smart00382 81 VLILDEITSLLDAEQEALLLLLEELRLLLLLKSEK-----------NLTVILTTNDEKDLGPALLRR 136
|
|
| T7SS_EccA |
TIGR03922 |
type VII secretion AAA-ATPase EccA; This model represents the AAA family ATPase, EccA, of the ... |
318-505 |
2.35e-04 |
|
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: 44.45 E-value: 2.35e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196876950 318 AQKVLDKdHYGLERVKDRILEY--------------LAVQGRVNKvkgpiLCLVGPPGVGKTslgqSIAKATGRQYVrmA 383
Cdd:TIGR03922 271 AEAELAE-QIGLERVKRQVAALksstamalaraergLPVAQTSNH-----MLFAGPPGTGKT----TIARVVAKIYC--G 338
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196876950 384 LGGVRDEAEIRGHRRTYIGSMPG---KLIQRMVKVGVKNPLFlLDEIDKMASDMRGDPasallevlDPEQNNAFND--HY 458
Cdd:TIGR03922 339 LGVLRKPLVREVSRADLIGQYIGeseAKTNEIIDSALGGVLF-LDEAYTLVETGYGQK--------DPFGLEAIDTllAR 409
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1196876950 459 LEVDYDLSDVMFVATANSMNipaPLLDRME--------VIRLSGYTEDEKLNIAK 505
Cdd:TIGR03922 410 MENDRDRLVVIGAGYRKDLD---KFLEVNEglrsrftrVIEFPSYSPDELVEIAR 461
|
|
| AAA_16 |
pfam13191 |
AAA ATPase domain; This family of domains contain a P-loop motif that is characteriztic of the ... |
327-385 |
7.87e-04 |
|
AAA ATPase domain; This family of domains contain a P-loop motif that is characteriztic of the AAA superfamily.
Pssm-ID: 433025 [Multi-domain] Cd Length: 167 Bit Score: 40.95 E-value: 7.87e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 1196876950 327 YGLERVKDRILEYLavqGRVNKVKGPILCLVGPPGVGKTSLGQSIAKATGRQYVRMALG 385
Cdd:pfam13191 3 VGREEELEQLLDAL---DRVRSGRPPSVLLTGEAGTGKTTLLRELLRALERDGGYFLRG 58
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
350-428 |
1.18e-03 |
|
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213179 [Multi-domain] Cd Length: 157 Bit Score: 40.31 E-value: 1.18e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196876950 350 KGPILCLVGPPGVGKTSLGQSIAKATGRQYVRMALGGVRDEAEIRGHRRTYIGSMP---GKLIQR--MVKVGVKNP-LFL 423
Cdd:cd00267 24 AGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIAKLPLEELRRRIGYVPqlsGGQRQRvaLARALLLNPdLLL 103
|
....*
gi 1196876950 424 LDEID 428
Cdd:cd00267 104 LDEPT 108
|
|
| RPT1 |
COG1222 |
ATP-dependent 26S proteasome regulatory subunit [Posttranslational modification, protein ... |
321-556 |
1.28e-03 |
|
ATP-dependent 26S proteasome regulatory subunit [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440835 [Multi-domain] Cd Length: 326 Bit Score: 41.92 E-value: 1.28e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196876950 321 VLDKDHYGLERVKDRILEYLAVQGR---------VNKVKGpILcLVGPPGVGKTSLGQSIAKATGRQYVRMALggvrdeA 391
Cdd:COG1222 75 VTFDDIGGLDEQIEEIREAVELPLKnpelfrkygIEPPKG-VL-LYGPPGTGKTLLAKAVAGELGAPFIRVRG------S 146
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196876950 392 EIrghRRTYIGSMPGKLiqRMV--KVGVKNP--LFlLDEIDKMASdMRGDPAS---------ALLEVLDpeqnnafndhy 458
Cdd:COG1222 147 EL---VSKYIGEGARNV--REVfeLAREKAPsiIF-IDEIDAIAA-RRTDDGTsgevqrtvnQLLAELD----------- 208
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196876950 459 lEVDyDLSDVMFVATANSMNI--PAPL----LDRmeVIRLSGYTEDEKLNIAKQHLISKQIansglkAKEIDIDDSAIIG 532
Cdd:COG1222 209 -GFE-SRGDVLIIAATNRPDLldPALLrpgrFDR--VIEVPLPDEEAREEILKIHLRDMPL------ADDVDLDKLAKLT 278
|
250 260 270
....*....|....*....|....*....|
gi 1196876950 533 ------IIRYYTREAGVRSLEREIAKICRK 556
Cdd:COG1222 279 egfsgaDLKAIVTEAGMFAIREGRDTVTME 308
|
|
| 44 |
PHA02544 |
clamp loader, small subunit; Provisional |
330-537 |
1.31e-03 |
|
clamp loader, small subunit; Provisional
Pssm-ID: 222866 [Multi-domain] Cd Length: 316 Bit Score: 41.51 E-value: 1.31e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196876950 330 ERVKDRILEYLAvQGRVnkvkgPILCLVGP-PGVGKTSlgqsIAKATGRQ------YVRMALGGVRDeaeIRGHRRTYIG 402
Cdd:PHA02544 27 AADKETFKSIVK-KGRI-----PNMLLHSPsPGTGKTT----VAKALCNEvgaevlFVNGSDCRIDF---VRNRLTRFAS 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196876950 403 SM----PGKLIqrmvkvgvknplfLLDEIDKMASDMRGDPASALLEvldpeqnnAFNdhylevdydlSDVMFVATANSMN 478
Cdd:PHA02544 94 TVsltgGGKVI-------------IIDEFDRLGLADAQRHLRSFME--------AYS----------KNCSFIITANNKN 142
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1196876950 479 -IPAPLLDRMEVIRLSGYTEDEKLNIAKQHLI-SKQIansgLKAKEIDIDDSAIIGII-RYY 537
Cdd:PHA02544 143 gIIEPLRSRCRVIDFGVPTKEEQIEMMKQMIVrCKGI----LEAEGVEVDMKVLAALVkKNF 200
|
|
| aroK |
PRK00131 |
shikimate kinase; Reviewed |
350-380 |
1.83e-03 |
|
shikimate kinase; Reviewed
Pssm-ID: 234654 [Multi-domain] Cd Length: 175 Bit Score: 40.17 E-value: 1.83e-03
10 20 30
....*....|....*....|....*....|.
gi 1196876950 350 KGPILCLVGPPGVGKTSLGQSIAKATGRQYV 380
Cdd:PRK00131 3 KGPNIVLIGFMGAGKSTIGRLLAKRLGYDFI 33
|
|
| FlhF |
TIGR03499 |
flagellar biosynthetic protein FlhF; [Cellular processes, Chemotaxis and motility] |
193-373 |
2.12e-03 |
|
flagellar biosynthetic protein FlhF; [Cellular processes, Chemotaxis and motility]
Pssm-ID: 274609 [Multi-domain] Cd Length: 282 Bit Score: 40.78 E-value: 2.12e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196876950 193 KRFELLISLMEAEIDLLQVEKNIRQRVKQQMEKAQKEYYLNEQIKAIHkelgdidnkpdefEELNLKISKAKMPQEAKEK 272
Cdd:TIGR03499 42 KFVEVTAAIDEEEAAAASAEEEASKALEQADPKPLSATAEPLELPAPQ-------------EEPAAPAAQAAEPLLPEEE 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196876950 273 TLSELNKLK-MMPAMSAEATVVR---GYIDWMLQLpwhkrskVKKDIQA--AQKVLDK--DHYGLERVKDRILEYLAVQG 344
Cdd:TIGR03499 109 LRKELEALReLLERLLAGLAWLQrppERAKLYERL-------LEAGVSEelARELLEKlpEDADAEDAWRWLREALEGML 181
|
170 180 190
....*....|....*....|....*....|....*
gi 1196876950 345 RVNKVKGPIL------CLVGPPGVGKTSlgqSIAK 373
Cdd:TIGR03499 182 PVKPEEDPILeqggviALVGPTGVGKTT---TLAK 213
|
|
| AroK |
COG0703 |
Shikimate kinase [Amino acid transport and metabolism]; Shikimate kinase is part of the ... |
354-380 |
2.25e-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: 39.73 E-value: 2.25e-03
10 20
....*....|....*....|....*..
gi 1196876950 354 LCLVGPPGVGKTSLGQSIAKATGRQYV 380
Cdd:COG0703 1 IVLIGMMGAGKSTVGRLLAKRLGLPFV 27
|
|
| FlhF |
COG1419 |
Flagellar biosynthesis GTPase FlhF [Cell motility]; |
261-373 |
2.55e-03 |
|
Flagellar biosynthesis GTPase FlhF [Cell motility];
Pssm-ID: 441029 [Multi-domain] Cd Length: 361 Bit Score: 41.00 E-value: 2.55e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196876950 261 SKAKMPQEAKEKTLSELNKLK---------MMPAMSAEATVVRGYIDWMLQLpwhkrsKVKKDIqaAQKVLDK--DHYGL 329
Cdd:COG1419 67 ASAAAEEEELEELRRELAELKelleeqlsgLAGESARLPPELAELLERLLEA------GVSPEL--ARELLEKlpEDLSA 138
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 1196876950 330 ERVKDRILEYLAvqGRVNKVKGPIL------CLVGPPGVGKTSlgqSIAK 373
Cdd:COG1419 139 EEAWRALLEALA--RRLPVAEDPLLdeggviALVGPTGVGKTT---TIAK 183
|
|
| SK |
cd00464 |
Shikimate kinase (SK) is the fifth enzyme in the shikimate pathway, a seven-step biosynthetic ... |
356-380 |
2.71e-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: 39.08 E-value: 2.71e-03
10 20
....*....|....*....|....*
gi 1196876950 356 LVGPPGVGKTSLGQSIAKATGRQYV 380
Cdd:cd00464 4 LIGMMGAGKTTVGRLLAKALGLPFV 28
|
|
| PRK13341 |
PRK13341 |
AAA family ATPase; |
354-427 |
3.88e-03 |
|
AAA family ATPase;
Pssm-ID: 237354 [Multi-domain] Cd Length: 725 Bit Score: 40.81 E-value: 3.88e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1196876950 354 LCLVGPPGVGKTSLGQSIAKATGRQYVRM--ALGGVRD-EAEIRGHRrtyigsmpgkliQRMVKVGVKNPLFlLDEI 427
Cdd:PRK13341 55 LILYGPPGVGKTTLARIIANHTRAHFSSLnaVLAGVKDlRAEVDRAK------------ERLERHGKRTILF-IDEV 118
|
|
| AAA_PrkA |
pfam08298 |
PrkA AAA domain; This is a family of PrkA bacterial and archaeal serine kinases approximately ... |
324-374 |
7.11e-03 |
|
PrkA AAA domain; This is a family of PrkA bacterial and archaeal serine kinases approximately 630 residues long. This is the N-terminal AAA domain.
Pssm-ID: 116881 Cd Length: 358 Bit Score: 39.36 E-value: 7.11e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 1196876950 324 KDHYGLERVKDRILEYLAVQGRVNKVKGPILCLVGPPGVGKTSLGQSIAKA 374
Cdd:pfam08298 58 ADFFGMEETIERIVNYFRHAAQGLEERKQILYLLGPVGGGKSSLAERLKKL 108
|
|
| |
