|
Name |
Accession |
Description |
Interval |
E-value |
| Lon |
COG0466 |
ATP-dependent Lon protease, bacterial type [Posttranslational modification, protein turnover, ... |
1-823 |
0e+00 |
|
ATP-dependent Lon protease, bacterial type [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440234 [Multi-domain] Cd Length: 785 Bit Score: 1003.38 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56693217 1 MS-SNSGIQIPSRLPLLCTHDGVLLPGSTMRVSVDTARNMQLVKsRLLKGTSLkstiIGVIPnTRDPEHDSDELPSLHSI 79
Cdd:COG0466 1 MSeEKEEEELPETLPLLPLRDVVVFPGMVIPLFVGREKSIKALE-EAMEGDKL----IGLVA-QKDAEVEDPGPDDLYEV 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56693217 80 GTAGLAVQVVgsNWPKPHYTLLITGLCRFRVSQLLRERPFPVAEVEQLDkleqytEGDPADGELGELSQRFYQAAVQLVg 159
Cdd:COG0466 75 GTVAKILQLL--KLPDGTVKVLVEGLQRARIKEFVQEEPYLEAEVEPLE------EEEEDDKELEALMRSLKEQFEEYV- 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56693217 160 MLDMSVP--VVAKLRRLLDSlpkETLPDVLAAMIRTSNKEKLQVLDAVDLEERFKKALPLLTRQIEGLKLLQKTR-KLRP 236
Cdd:COG0466 146 KLNPKIPpeLLAALSNIEDP---GRLADFIASHLPLKIEEKQELLETLDVKERLEKLLELLEKEIEVLELEKKIRsRVKE 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56693217 237 DDDKR----VL-----SIRK--GGVFPGRQfsldeevededsdDTALLERKVKAAAMPEAALRVCLKELRRLKKMPQSMP 305
Cdd:COG0466 223 QMEKSqreyYLreqlkAIQKelGEKDDGED-------------EIEELREKIEKAKLPEEVKEKAEKELKKLERMPPMSA 289
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56693217 306 EYALTRNYLEMMVELPWSKSTTDCLDIRAARVLLDNDHYAMEKLKKRVLEYLAVRQLKSTLKGPILCFVGPPGVGKTSVG 385
Cdd:COG0466 290 EATVIRNYLDWLLDLPWGKRTKDNLDLKKAEKILDEDHYGLEKVKERILEYLAVRKLKKKLKGPILCLVGPPGVGKTSLG 369
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56693217 386 RSIARTLGREFHRIALGGVCDQSDIRGHRRTYVGSMPGRIINGLKTVGVNNPVFLLDEVDKLGKSLQGDPAAALLEVLDP 465
Cdd:COG0466 370 KSIARALGRKFVRISLGGVRDEAEIRGHRRTYIGAMPGRIIQGLKKAGTKNPVFLLDEIDKMGSDFRGDPASALLEVLDP 449
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56693217 466 EQNHSFTDHYLNVPFDLSQVLFIATANTTATIPPALLDRMEVLQVPGYTQEEKVEIAHRHLIPHQLEQHGLTPQQLQIPQ 545
Cdd:COG0466 450 EQNNTFSDHYLEVPFDLSKVMFIATANSLDTIPAPLLDRMEIIELSGYTEEEKLEIAKRYLIPKQLKEHGLKKEELKISD 529
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56693217 546 DTTLQIISKYTREAGVRSLERKIGAVCRAVAVKVAEGQKVsrseapteqhaeqntdskvedsgiaappemPIVIDHVALK 625
Cdd:COG0466 530 EALRKIIRGYTREAGVRNLEREIAKICRKVAKKIAEGKKK------------------------------KVTITPKNLE 579
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56693217 626 DILGPPLFEMEVSERLTLPGVAIGLAWTPMGGEIMFVEASRMEGEGQLTLTGQLGDVMKESAHLAISWLRSNAKTYLLND 705
Cdd:COG0466 580 KYLGVPRFRYEKAEEEDQVGVVTGLAWTEVGGDILFIEATLMPGKGKLTLTGQLGDVMKESAQAALSYVRSRAEELGIDP 659
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56693217 706 gsaDLLEGTDIHLHFPAGAVTKDGPSAGVTIVTCLASLLSGRLVRSDVAMTGEITLRGLVLPVGGIKDKVLAAHRANLKR 785
Cdd:COG0466 660 ---DFFEKYDIHIHVPEGATPKDGPSAGITMATALVSALTGRPVRSDVAMTGEITLRGRVLPIGGLKEKLLAAHRAGIKT 736
|
810 820 830
....*....|....*....|....*....|....*...
gi 56693217 786 IIIPKRNEKDLEEIPANVRADLDFVLAGTLDEVLNAAF 823
Cdd:COG0466 737 VILPKENEKDLEEIPEEVKKGLEFHPVEHIDEVLKIAL 774
|
|
| lon |
TIGR00763 |
endopeptidase La; This protein, the ATP-dependent serine endopeptidase La, is induced by heat ... |
14-823 |
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: 850.05 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56693217 14 PLLCTHDGVLLPGSTMRVSVDTARNMQLVKsrllKGTSLKSTIIGVIpNTRDPEHDSDELPSLHSIGTAGLAVQVVGS-N 92
Cdd:TIGR00763 1 PLLPLRRRPLFPGMIKPIDVGREKSIKLIK----EALRLKQPYLGLF-LQKDDDNEEPEEDDIYSVGVVAQILEMLPLpS 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56693217 93 WPKPHYTLLITGLCRFRVSQLLRERPFPVAEVEQLDKLEQytegDPADGELGELSQRFYQAAVQLVGMLDMSVPVVAKLR 172
Cdd:TIGR00763 76 SGTATYKVVVEGLRRIRIKELSDKGGYLVVRVDNLKEEPF----DKDDEEIKALTREIKETFRELISLSKLFREQPALLS 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56693217 173 RLLDSLPKETLPDVLAAMIRTSNKEKLQ-VLDAVDLEERFKKALPLLTRQIEGLKLLQK-TRKLRPDDDKR--------- 241
Cdd:TIGR00763 152 ALEDIDEPGRLADFVAASLQLKEKDELQeVLETVNIEKRLKKALELLKKELELLKLQNKiTKKVEEKMEKTqreyylreq 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56693217 242 VLSIRKG-GVFPGRQFSLdeevededsddtALLERKVKAAAMPEAALRVCLKELRRLKKMPQSMPEYALTRNYLEMMVEL 320
Cdd:TIGR00763 232 LKAIKKElGIEKDDKDEL------------EKLKEKLEELKLPEEVKKVIEKELTKLSLLEPSSSEFTVTRNYLDWLTDL 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56693217 321 PWSKSTTDCLDIRAARVLLDNDHYAMEKLKKRVLEYLAVRQLKSTLKGPILCFVGPPGVGKTSVGRSIARTLGREFHRIA 400
Cdd:TIGR00763 300 PWGKYSKENLDLKRAKEILDEDHYGLKKVKERILEYLAVQKLRGKMKGPILCLVGPPGVGKTSLGKSIAKALNRKFVRFS 379
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56693217 401 LGGVCDQSDIRGHRRTYVGSMPGRIINGLKTVGVNNPVFLLDEVDKLGKSLQGDPAAALLEVLDPEQNHSFTDHYLNVPF 480
Cdd:TIGR00763 380 LGGVRDEAEIRGHRRTYVGAMPGRIIQGLKKAKTKNPLFLLDEIDKIGSSFRGDPASALLEVLDPEQNNAFSDHYLDVPF 459
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56693217 481 DLSQVLFIATANTTATIPPALLDRMEVLQVPGYTQEEKVEIAHRHLIPHQLEQHGLTPQQLQIPQDTTLQIISKYTREAG 560
Cdd:TIGR00763 460 DLSKVIFIATANSIDTIPRPLLDRMEVIELSGYTEEEKLEIAKKYLIPKALEDHGLKPDELKITDEALLLLIKYYTREAG 539
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56693217 561 VRSLERKIGAVCRAVAVKVAEGQKVSRSEApteqhaeqntdskvedsgiaappeMPIVIDHVALKDILGPPLFEMEVSER 640
Cdd:TIGR00763 540 VRNLERQIEKICRKAAVKLVEQGEKKKSEA------------------------ESVVITPDNLKKYLGKPVFTYERAYE 595
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56693217 641 LTLPGVAIGLAWTPMGGEIMFVEASRMEGEGQLTLTGQLGDVMKESAHLAISWLRSNAKTYLLNDgsaDLLEGTDIHLHF 720
Cdd:TIGR00763 596 VTPPGVVMGLAWTPMGGDTLFIETTKVAGKGSLELTGQLGDVMKESAQIALTYVRSIAADLGISP---NFFEKADIHLHV 672
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56693217 721 PAGAVTKDGPSAGVTIVTCLASLLSGRLVRSDVAMTGEITLRGLVLPVGGIKDKVLAAHRANLKRIIIPKRNEKDLEEIP 800
Cdd:TIGR00763 673 PEGATPKDGPSAGITMATALLSLATGKPVRPDVAMTGEITLRGKVLPIGGLKEKTIAAKRAGIKTIILPEKNRRDLEELP 752
|
810 820
....*....|....*....|...
gi 56693217 801 ANVRADLDFVLAGTLDEVLNAAF 823
Cdd:TIGR00763 753 ENVKEGLEIHFVKHYDEVLKKAF 775
|
|
| PRK10787 |
PRK10787 |
DNA-binding ATP-dependent protease La; Provisional |
67-823 |
0e+00 |
|
DNA-binding ATP-dependent protease La; Provisional
Pssm-ID: 182730 [Multi-domain] Cd Length: 784 Bit Score: 559.94 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56693217 67 EHDSDE--LPSLHSIGTAGLAVQVVgsNWPKPHYTLLITGLCRFRVSQLLRERPFPVAEVEQLDKLEqytegdpADGELG 144
Cdd:PRK10787 57 EASTDEpgVNDLFTVGTVASILQML--KLPDGTVKVLVEGLQRARISALSDNGEHFSAKAEYLESPT-------IDEREQ 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56693217 145 ELSQRfyQAAVQLVGMLDMSVPVVAKLRRLLDSLPKET-LPDVLAAMIRTSNKEKLQVLDAVDLEERFKKALPLLTRQIE 223
Cdd:PRK10787 128 EVLVR--TAISQFEGYIKLNKKIPPEVLTSLNSIDDPArLADTIAAHMPLKLADKQSVLEMSDVNERLEYLMAMMESEID 205
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56693217 224 glkLLQKTRKLRpdddKRVlsiRKGGVFPGRQFSLDEEVEDEDSDDTAL---------LERKVKAAAMPEAALRVCLKEL 294
Cdd:PRK10787 206 ---LLQVEKRIR----NRV---KKQMEKSQREYYLNEQMKAIQKELGEMddapdeneaLKRKIDAAKMPKEAKEKAEAEL 275
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56693217 295 RRLKKMPQSMPEYALTRNYLEMMVELPWSKSTTDCLDIRAARVLLDNDHYAMEKLKKRVLEYLAVRQLKSTLKGPILCFV 374
Cdd:PRK10787 276 QKLKMMSPMSAEATVVRGYIDWMVQVPWNARSKVKKDLRQAQEILDTDHYGLERVKDRILEYLAVQSRVNKIKGPILCLV 355
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56693217 375 GPPGVGKTSVGRSIARTLGREFHRIALGGVCDQSDIRGHRRTYVGSMPGRIINGLKTVGVNNPVFLLDEVDKLGKSLQGD 454
Cdd:PRK10787 356 GPPGVGKTSLGQSIAKATGRKYVRMALGGVRDEAEIRGHRRTYIGSMPGKLIQKMAKVGVKNPLFLLDEIDKMSSDMRGD 435
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56693217 455 PAAALLEVLDPEQNHSFTDHYLNVPFDLSQVLFIATANTTaTIPPALLDRMEVLQVPGYTQEEKVEIAHRHLIPHQLEQH 534
Cdd:PRK10787 436 PASALLEVLDPEQNVAFSDHYLEVDYDLSDVMFVATSNSM-NIPAPLLDRMEVIRLSGYTEDEKLNIAKRHLLPKQIERN 514
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56693217 535 GLTPQQLQIPQDTTLQIISKYTREAGVRSLERKIGAVCRAvAVKVAEGQKvsrseapTEQHAEQNTDSkvedsgiaappe 614
Cdd:PRK10787 515 ALKKGELTVDDSAIIGIIRYYTREAGVRSLEREISKLCRK-AVKQLLLDK-------SLKHIEINGDN------------ 574
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56693217 615 mpividhvaLKDILGPPLFEMEVSERLTLPGVAIGLAWTPMGGEIMFVEASRMEGEGQLTLTGQLGDVMKESAHLAISWL 694
Cdd:PRK10787 575 ---------LHDYLGVQRFDYGRADNENRVGQVTGLAWTEVGGDLLTIETACVPGKGKLTYTGSLGEVMQESIQAALTVV 645
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56693217 695 RSNAKTYLLNdgsADLLEGTDIHLHFPAGAVTKDGPSAGVTIVTCLASLLSGRLVRSDVAMTGEITLRGLVLPVGGIKDK 774
Cdd:PRK10787 646 RARAEKLGIN---PDFYEKRDIHVHVPEGATPKDGPSAGIAMCTALVSCLTGNPVRADVAMTGEITLRGQVLPIGGLKEK 722
|
730 740 750 760
....*....|....*....|....*....|....*....|....*....
gi 56693217 775 VLAAHRANLKRIIIPKRNEKDLEEIPANVRADLDFVLAGTLDEVLNAAF 823
Cdd:PRK10787 723 LLAAHRGGIKTVLIPFENKRDLEEIPDNVIADLDIHPVKRIEEVLTLAL 771
|
|
| RecA-like_Lon |
cd19500 |
lon protease homolog 2 peroxisomal; Lon protease (also known as Lon peptidase) is an ... |
332-513 |
5.75e-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: 367.65 E-value: 5.75e-123
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56693217 332 IRAARVLLDNDHYAMEKLKKRVLEYLAVRQLKSTLKGPILCFVGPPGVGKTSVGRSIARTLGREFHRIALGGVCDQSDIR 411
Cdd:cd19500 1 IKKARKVLDADHYGLEDVKERILEYLAVRKLKGSMKGPILCLVGPPGVGKTSLGKSIARALGRKFVRISLGGVRDEAEIR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56693217 412 GHRRTYVGSMPGRIINGLKTVGVNNPVFLLDEVDKLGKSLQGDPAAALLEVLDPEQNHSFTDHYLNVPFDLSQVLFIATA 491
Cdd:cd19500 81 GHRRTYVGAMPGRIIQALKKAGTNNPVFLLDEIDKIGSSFRGDPASALLEVLDPEQNSTFSDHYLDVPFDLSKVLFIATA 160
|
170 180
....*....|....*....|..
gi 56693217 492 NTTATIPPALLDRMEVLQVPGY 513
Cdd:cd19500 161 NSLDTIPGPLLDRMEIIELSGY 182
|
|
| Lon_C |
pfam05362 |
Lon protease (S16) C-terminal proteolytic domain; The Lon serine proteases must hydrolyse ATP ... |
618-825 |
5.94e-95 |
|
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: 295.69 E-value: 5.94e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56693217 618 VIDHVALKDILGPPLFEMEVSERLTLPGVAIGLAWTPMGGEIMFVEASRMEGEGQLTLTGQLGDVMKESAHLAISWLRSN 697
Cdd:pfam05362 1 KVTAKNLEKYLGVPRFRYGEAEKEDQVGVVTGLAWTEVGGDLLTIEAVIMPGKGKLTLTGQLGDVMKESAQAALSYVRSR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56693217 698 AKTYllnDGSADLLEGTDIHLHFPAGAVTKDGPSAGVTIVTCLASLLSGRLVRSDVAMTGEITLRGLVLPVGGIKDKVLA 777
Cdd:pfam05362 81 AEEL---GIDPDFFEKKDIHIHVPEGATPKDGPSAGVTMATALVSALTGIPVRKDVAMTGEITLRGRVLPIGGLKEKLLA 157
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 56693217 778 AHRANLKRIIIPKRNEKDLEEIPANVRADLDFVLAGTLDEVLNAAFDG 825
Cdd:pfam05362 158 AHRAGIKTVIIPKENEKDLEDIPENVREGLEIIPVEHVDEVLKHALVG 205
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
367-505 |
7.13e-07 |
|
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a variety of cellular activities. This profile/alignment only detects a fraction of this vast family. The poorly conserved N-terminal helix is missing from the alignment.
Pssm-ID: 214640 [Multi-domain] Cd Length: 148 Bit Score: 49.68 E-value: 7.13e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56693217 367 KGPILCFVGPPGVGKTSVGRSIARTLGREFHRI-------ALGGVCDQSDIRGHRRTYVGSMPGRIINGLKTV--GVNNP 437
Cdd:smart00382 1 PGEVILIVGPPGSGKTTLARALARELGPPGGGViyidgedILEEVLDQLLLIIVGGKKASGSGELRLRLALALarKLKPD 80
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 56693217 438 VFLLDEVDKLGKSLQgdpaAALLEVLDPEQNHSFTDHYLNVPfdlsqvlFIATANTTATIPPALLDRM 505
Cdd:smart00382 81 VLILDEITSLLDAEQ----EALLLLLEELRLLLLLKSEKNLT-------VILTTNDEKDLGPALLRRR 137
|
|
|
|
Name |
Accession |
Description |
Interval |
E-value |
| Lon |
COG0466 |
ATP-dependent Lon protease, bacterial type [Posttranslational modification, protein turnover, ... |
1-823 |
0e+00 |
|
ATP-dependent Lon protease, bacterial type [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440234 [Multi-domain] Cd Length: 785 Bit Score: 1003.38 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56693217 1 MS-SNSGIQIPSRLPLLCTHDGVLLPGSTMRVSVDTARNMQLVKsRLLKGTSLkstiIGVIPnTRDPEHDSDELPSLHSI 79
Cdd:COG0466 1 MSeEKEEEELPETLPLLPLRDVVVFPGMVIPLFVGREKSIKALE-EAMEGDKL----IGLVA-QKDAEVEDPGPDDLYEV 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56693217 80 GTAGLAVQVVgsNWPKPHYTLLITGLCRFRVSQLLRERPFPVAEVEQLDkleqytEGDPADGELGELSQRFYQAAVQLVg 159
Cdd:COG0466 75 GTVAKILQLL--KLPDGTVKVLVEGLQRARIKEFVQEEPYLEAEVEPLE------EEEEDDKELEALMRSLKEQFEEYV- 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56693217 160 MLDMSVP--VVAKLRRLLDSlpkETLPDVLAAMIRTSNKEKLQVLDAVDLEERFKKALPLLTRQIEGLKLLQKTR-KLRP 236
Cdd:COG0466 146 KLNPKIPpeLLAALSNIEDP---GRLADFIASHLPLKIEEKQELLETLDVKERLEKLLELLEKEIEVLELEKKIRsRVKE 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56693217 237 DDDKR----VL-----SIRK--GGVFPGRQfsldeevededsdDTALLERKVKAAAMPEAALRVCLKELRRLKKMPQSMP 305
Cdd:COG0466 223 QMEKSqreyYLreqlkAIQKelGEKDDGED-------------EIEELREKIEKAKLPEEVKEKAEKELKKLERMPPMSA 289
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56693217 306 EYALTRNYLEMMVELPWSKSTTDCLDIRAARVLLDNDHYAMEKLKKRVLEYLAVRQLKSTLKGPILCFVGPPGVGKTSVG 385
Cdd:COG0466 290 EATVIRNYLDWLLDLPWGKRTKDNLDLKKAEKILDEDHYGLEKVKERILEYLAVRKLKKKLKGPILCLVGPPGVGKTSLG 369
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56693217 386 RSIARTLGREFHRIALGGVCDQSDIRGHRRTYVGSMPGRIINGLKTVGVNNPVFLLDEVDKLGKSLQGDPAAALLEVLDP 465
Cdd:COG0466 370 KSIARALGRKFVRISLGGVRDEAEIRGHRRTYIGAMPGRIIQGLKKAGTKNPVFLLDEIDKMGSDFRGDPASALLEVLDP 449
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56693217 466 EQNHSFTDHYLNVPFDLSQVLFIATANTTATIPPALLDRMEVLQVPGYTQEEKVEIAHRHLIPHQLEQHGLTPQQLQIPQ 545
Cdd:COG0466 450 EQNNTFSDHYLEVPFDLSKVMFIATANSLDTIPAPLLDRMEIIELSGYTEEEKLEIAKRYLIPKQLKEHGLKKEELKISD 529
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56693217 546 DTTLQIISKYTREAGVRSLERKIGAVCRAVAVKVAEGQKVsrseapteqhaeqntdskvedsgiaappemPIVIDHVALK 625
Cdd:COG0466 530 EALRKIIRGYTREAGVRNLEREIAKICRKVAKKIAEGKKK------------------------------KVTITPKNLE 579
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56693217 626 DILGPPLFEMEVSERLTLPGVAIGLAWTPMGGEIMFVEASRMEGEGQLTLTGQLGDVMKESAHLAISWLRSNAKTYLLND 705
Cdd:COG0466 580 KYLGVPRFRYEKAEEEDQVGVVTGLAWTEVGGDILFIEATLMPGKGKLTLTGQLGDVMKESAQAALSYVRSRAEELGIDP 659
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56693217 706 gsaDLLEGTDIHLHFPAGAVTKDGPSAGVTIVTCLASLLSGRLVRSDVAMTGEITLRGLVLPVGGIKDKVLAAHRANLKR 785
Cdd:COG0466 660 ---DFFEKYDIHIHVPEGATPKDGPSAGITMATALVSALTGRPVRSDVAMTGEITLRGRVLPIGGLKEKLLAAHRAGIKT 736
|
810 820 830
....*....|....*....|....*....|....*...
gi 56693217 786 IIIPKRNEKDLEEIPANVRADLDFVLAGTLDEVLNAAF 823
Cdd:COG0466 737 VILPKENEKDLEEIPEEVKKGLEFHPVEHIDEVLKIAL 774
|
|
| lon |
TIGR00763 |
endopeptidase La; This protein, the ATP-dependent serine endopeptidase La, is induced by heat ... |
14-823 |
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: 850.05 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56693217 14 PLLCTHDGVLLPGSTMRVSVDTARNMQLVKsrllKGTSLKSTIIGVIpNTRDPEHDSDELPSLHSIGTAGLAVQVVGS-N 92
Cdd:TIGR00763 1 PLLPLRRRPLFPGMIKPIDVGREKSIKLIK----EALRLKQPYLGLF-LQKDDDNEEPEEDDIYSVGVVAQILEMLPLpS 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56693217 93 WPKPHYTLLITGLCRFRVSQLLRERPFPVAEVEQLDKLEQytegDPADGELGELSQRFYQAAVQLVGMLDMSVPVVAKLR 172
Cdd:TIGR00763 76 SGTATYKVVVEGLRRIRIKELSDKGGYLVVRVDNLKEEPF----DKDDEEIKALTREIKETFRELISLSKLFREQPALLS 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56693217 173 RLLDSLPKETLPDVLAAMIRTSNKEKLQ-VLDAVDLEERFKKALPLLTRQIEGLKLLQK-TRKLRPDDDKR--------- 241
Cdd:TIGR00763 152 ALEDIDEPGRLADFVAASLQLKEKDELQeVLETVNIEKRLKKALELLKKELELLKLQNKiTKKVEEKMEKTqreyylreq 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56693217 242 VLSIRKG-GVFPGRQFSLdeevededsddtALLERKVKAAAMPEAALRVCLKELRRLKKMPQSMPEYALTRNYLEMMVEL 320
Cdd:TIGR00763 232 LKAIKKElGIEKDDKDEL------------EKLKEKLEELKLPEEVKKVIEKELTKLSLLEPSSSEFTVTRNYLDWLTDL 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56693217 321 PWSKSTTDCLDIRAARVLLDNDHYAMEKLKKRVLEYLAVRQLKSTLKGPILCFVGPPGVGKTSVGRSIARTLGREFHRIA 400
Cdd:TIGR00763 300 PWGKYSKENLDLKRAKEILDEDHYGLKKVKERILEYLAVQKLRGKMKGPILCLVGPPGVGKTSLGKSIAKALNRKFVRFS 379
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56693217 401 LGGVCDQSDIRGHRRTYVGSMPGRIINGLKTVGVNNPVFLLDEVDKLGKSLQGDPAAALLEVLDPEQNHSFTDHYLNVPF 480
Cdd:TIGR00763 380 LGGVRDEAEIRGHRRTYVGAMPGRIIQGLKKAKTKNPLFLLDEIDKIGSSFRGDPASALLEVLDPEQNNAFSDHYLDVPF 459
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56693217 481 DLSQVLFIATANTTATIPPALLDRMEVLQVPGYTQEEKVEIAHRHLIPHQLEQHGLTPQQLQIPQDTTLQIISKYTREAG 560
Cdd:TIGR00763 460 DLSKVIFIATANSIDTIPRPLLDRMEVIELSGYTEEEKLEIAKKYLIPKALEDHGLKPDELKITDEALLLLIKYYTREAG 539
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56693217 561 VRSLERKIGAVCRAVAVKVAEGQKVSRSEApteqhaeqntdskvedsgiaappeMPIVIDHVALKDILGPPLFEMEVSER 640
Cdd:TIGR00763 540 VRNLERQIEKICRKAAVKLVEQGEKKKSEA------------------------ESVVITPDNLKKYLGKPVFTYERAYE 595
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56693217 641 LTLPGVAIGLAWTPMGGEIMFVEASRMEGEGQLTLTGQLGDVMKESAHLAISWLRSNAKTYLLNDgsaDLLEGTDIHLHF 720
Cdd:TIGR00763 596 VTPPGVVMGLAWTPMGGDTLFIETTKVAGKGSLELTGQLGDVMKESAQIALTYVRSIAADLGISP---NFFEKADIHLHV 672
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56693217 721 PAGAVTKDGPSAGVTIVTCLASLLSGRLVRSDVAMTGEITLRGLVLPVGGIKDKVLAAHRANLKRIIIPKRNEKDLEEIP 800
Cdd:TIGR00763 673 PEGATPKDGPSAGITMATALLSLATGKPVRPDVAMTGEITLRGKVLPIGGLKEKTIAAKRAGIKTIILPEKNRRDLEELP 752
|
810 820
....*....|....*....|...
gi 56693217 801 ANVRADLDFVLAGTLDEVLNAAF 823
Cdd:TIGR00763 753 ENVKEGLEIHFVKHYDEVLKKAF 775
|
|
| PRK10787 |
PRK10787 |
DNA-binding ATP-dependent protease La; Provisional |
67-823 |
0e+00 |
|
DNA-binding ATP-dependent protease La; Provisional
Pssm-ID: 182730 [Multi-domain] Cd Length: 784 Bit Score: 559.94 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56693217 67 EHDSDE--LPSLHSIGTAGLAVQVVgsNWPKPHYTLLITGLCRFRVSQLLRERPFPVAEVEQLDKLEqytegdpADGELG 144
Cdd:PRK10787 57 EASTDEpgVNDLFTVGTVASILQML--KLPDGTVKVLVEGLQRARISALSDNGEHFSAKAEYLESPT-------IDEREQ 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56693217 145 ELSQRfyQAAVQLVGMLDMSVPVVAKLRRLLDSLPKET-LPDVLAAMIRTSNKEKLQVLDAVDLEERFKKALPLLTRQIE 223
Cdd:PRK10787 128 EVLVR--TAISQFEGYIKLNKKIPPEVLTSLNSIDDPArLADTIAAHMPLKLADKQSVLEMSDVNERLEYLMAMMESEID 205
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56693217 224 glkLLQKTRKLRpdddKRVlsiRKGGVFPGRQFSLDEEVEDEDSDDTAL---------LERKVKAAAMPEAALRVCLKEL 294
Cdd:PRK10787 206 ---LLQVEKRIR----NRV---KKQMEKSQREYYLNEQMKAIQKELGEMddapdeneaLKRKIDAAKMPKEAKEKAEAEL 275
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56693217 295 RRLKKMPQSMPEYALTRNYLEMMVELPWSKSTTDCLDIRAARVLLDNDHYAMEKLKKRVLEYLAVRQLKSTLKGPILCFV 374
Cdd:PRK10787 276 QKLKMMSPMSAEATVVRGYIDWMVQVPWNARSKVKKDLRQAQEILDTDHYGLERVKDRILEYLAVQSRVNKIKGPILCLV 355
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56693217 375 GPPGVGKTSVGRSIARTLGREFHRIALGGVCDQSDIRGHRRTYVGSMPGRIINGLKTVGVNNPVFLLDEVDKLGKSLQGD 454
Cdd:PRK10787 356 GPPGVGKTSLGQSIAKATGRKYVRMALGGVRDEAEIRGHRRTYIGSMPGKLIQKMAKVGVKNPLFLLDEIDKMSSDMRGD 435
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56693217 455 PAAALLEVLDPEQNHSFTDHYLNVPFDLSQVLFIATANTTaTIPPALLDRMEVLQVPGYTQEEKVEIAHRHLIPHQLEQH 534
Cdd:PRK10787 436 PASALLEVLDPEQNVAFSDHYLEVDYDLSDVMFVATSNSM-NIPAPLLDRMEVIRLSGYTEDEKLNIAKRHLLPKQIERN 514
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56693217 535 GLTPQQLQIPQDTTLQIISKYTREAGVRSLERKIGAVCRAvAVKVAEGQKvsrseapTEQHAEQNTDSkvedsgiaappe 614
Cdd:PRK10787 515 ALKKGELTVDDSAIIGIIRYYTREAGVRSLEREISKLCRK-AVKQLLLDK-------SLKHIEINGDN------------ 574
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56693217 615 mpividhvaLKDILGPPLFEMEVSERLTLPGVAIGLAWTPMGGEIMFVEASRMEGEGQLTLTGQLGDVMKESAHLAISWL 694
Cdd:PRK10787 575 ---------LHDYLGVQRFDYGRADNENRVGQVTGLAWTEVGGDLLTIETACVPGKGKLTYTGSLGEVMQESIQAALTVV 645
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56693217 695 RSNAKTYLLNdgsADLLEGTDIHLHFPAGAVTKDGPSAGVTIVTCLASLLSGRLVRSDVAMTGEITLRGLVLPVGGIKDK 774
Cdd:PRK10787 646 RARAEKLGIN---PDFYEKRDIHVHVPEGATPKDGPSAGIAMCTALVSCLTGNPVRADVAMTGEITLRGQVLPIGGLKEK 722
|
730 740 750 760
....*....|....*....|....*....|....*....|....*....
gi 56693217 775 VLAAHRANLKRIIIPKRNEKDLEEIPANVRADLDFVLAGTLDEVLNAAF 823
Cdd:PRK10787 723 LLAAHRGGIKTVLIPFENKRDLEEIPDNVIADLDIHPVKRIEEVLTLAL 771
|
|
| RecA-like_Lon |
cd19500 |
lon protease homolog 2 peroxisomal; Lon protease (also known as Lon peptidase) is an ... |
332-513 |
5.75e-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: 367.65 E-value: 5.75e-123
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56693217 332 IRAARVLLDNDHYAMEKLKKRVLEYLAVRQLKSTLKGPILCFVGPPGVGKTSVGRSIARTLGREFHRIALGGVCDQSDIR 411
Cdd:cd19500 1 IKKARKVLDADHYGLEDVKERILEYLAVRKLKGSMKGPILCLVGPPGVGKTSLGKSIARALGRKFVRISLGGVRDEAEIR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56693217 412 GHRRTYVGSMPGRIINGLKTVGVNNPVFLLDEVDKLGKSLQGDPAAALLEVLDPEQNHSFTDHYLNVPFDLSQVLFIATA 491
Cdd:cd19500 81 GHRRTYVGAMPGRIIQALKKAGTNNPVFLLDEIDKIGSSFRGDPASALLEVLDPEQNSTFSDHYLDVPFDLSKVLFIATA 160
|
170 180
....*....|....*....|..
gi 56693217 492 NTTATIPPALLDRMEVLQVPGY 513
Cdd:cd19500 161 NSLDTIPGPLLDRMEIIELSGY 182
|
|
| Lon_C |
pfam05362 |
Lon protease (S16) C-terminal proteolytic domain; The Lon serine proteases must hydrolyse ATP ... |
618-825 |
5.94e-95 |
|
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: 295.69 E-value: 5.94e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56693217 618 VIDHVALKDILGPPLFEMEVSERLTLPGVAIGLAWTPMGGEIMFVEASRMEGEGQLTLTGQLGDVMKESAHLAISWLRSN 697
Cdd:pfam05362 1 KVTAKNLEKYLGVPRFRYGEAEKEDQVGVVTGLAWTEVGGDLLTIEAVIMPGKGKLTLTGQLGDVMKESAQAALSYVRSR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56693217 698 AKTYllnDGSADLLEGTDIHLHFPAGAVTKDGPSAGVTIVTCLASLLSGRLVRSDVAMTGEITLRGLVLPVGGIKDKVLA 777
Cdd:pfam05362 81 AEEL---GIDPDFFEKKDIHIHVPEGATPKDGPSAGVTMATALVSALTGIPVRKDVAMTGEITLRGRVLPIGGLKEKLLA 157
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 56693217 778 AHRANLKRIIIPKRNEKDLEEIPANVRADLDFVLAGTLDEVLNAAFDG 825
Cdd:pfam05362 158 AHRAGIKTVIIPKENEKDLEDIPENVREGLEIIPVEHVDEVLKHALVG 205
|
|
| LON_substr_bdg |
pfam02190 |
ATP-dependent protease La (LON) substrate-binding domain; This domain has been shown to be ... |
13-220 |
1.29e-26 |
|
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: 107.81 E-value: 1.29e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56693217 13 LPLLCTHDGVLLPGSTMRVSVDTARNMQLVKSRLLKGtslKSTIIGVIPNtRDPEHDSDELPSLHSIGTAGLAVQVVGSn 92
Cdd:pfam02190 2 LPLLPLRNTVLFPGMVLPLFVGRPRSIAAIEAALNKD---KLYGVLLVSQ-KDAEDEEPTPDDLYEVGTVAKIVQILKL- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56693217 93 wPKPHYTLLITGLCRFRV-SQLLRERPFPVAEVEQLDkleqytegDPADGELGELSQRFYQAAVQLVGMLDMSVPVVAKL 171
Cdd:pfam02190 77 -PDGTYKVLVEGLERVRIvELVKKEEPYLRAEVEDLP--------EDSDELSEALKALVKELIEKLRRLLKLLLPLELLL 147
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 56693217 172 RRLLDSLPkETLPDVLAAMIRTSNKEKLQVLDAVDLEERFKKALPLLTR 220
Cdd:pfam02190 148 KIKDIENP-GRLADLVAAILPLSPEEKQELLETLDVKERLEKVLELLNR 195
|
|
| AAA |
pfam00004 |
ATPase family associated with various cellular activities (AAA); AAA family proteins often ... |
371-513 |
3.67e-26 |
|
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: 104.21 E-value: 3.67e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56693217 371 LCFVGPPGVGKTSVGRSIARTLGREFHRIALGGVCDqsdirghrrTYVGSMPGRIINGLKTVGVNNP-VFLLDEVDKLGK 449
Cdd:pfam00004 1 LLLYGPPGTGKTTLAKAVAKELGAPFIEISGSELVS---------KYVGESEKRLRELFEAAKKLAPcVIFIDEIDALAG 71
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 56693217 450 SLQG-------DPAAALLEVLDPEQNHSftdhylnvpfdlSQVLFIATANTTATIPPALLDRMEVLQVPGY 513
Cdd:pfam00004 72 SRGSggdsesrRVVNQLLTELDGFTSSN------------SKVIVIAATNRPDKLDPALLGRFDRIIEFPL 130
|
|
| COG1750 |
COG1750 |
Predicted archaeal serine protease, S18 family [General function prediction only]; |
715-798 |
2.24e-15 |
|
Predicted archaeal serine protease, S18 family [General function prediction only];
Pssm-ID: 441356 [Multi-domain] Cd Length: 213 Bit Score: 75.79 E-value: 2.24e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56693217 715 DIHLHFPAGAVTKDGPSAGVTIVTCLASLLSGRLVRSDVAMTGEITLRGLVLPVGGIKDKVLAAHRANLKRIIIPKRNEK 794
Cdd:COG1750 95 DVYISIESDSPIVGGPSAGGAMTVATYAALLGLPLNKSVTMTGMINPDGSIGPVGGVYEKLEAAASAGAKYFLIPKGQAI 174
|
....
gi 56693217 795 DLEE 798
Cdd:COG1750 175 LTGY 178
|
|
| RecA-like_protease |
cd19481 |
proteases similar to RecA; RecA-like NTPases. This family includes the NTP binding domain of ... |
349-504 |
5.33e-15 |
|
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: 73.09 E-value: 5.33e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56693217 349 LKKRVLEYLAVRQLKSTL------KGPILCFVGPPGVGKTSVGRSIARTLGREFHRIALGGVCDQSdirghrRTYVGSMP 422
Cdd:cd19481 1 LKASLREAVEAPRRGSRLrryglgLPKGILLYGPPGTGKTLLAKALAGELGLPLIVVKLSSLLSKY------VGESEKNL 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56693217 423 GRIINGLKTVGvnNPVFLLDEVDKLGK--SLQGDPAA------ALLEVLDPEQNhsftdhylnvpfdLSQVLFIATANTT 494
Cdd:cd19481 75 RKIFERARRLA--PCILFIDEIDAIGRkrDSSGESGElrrvlnQLLTELDGVNS-------------RSKVLVIAATNRP 139
|
170
....*....|
gi 56693217 495 ATIPPALLDR 504
Cdd:cd19481 140 DLLDPALLRP 149
|
|
| SpoVK |
COG0464 |
AAA+-type ATPase, SpoVK/Ycf46/Vps4 family [Cell wall/membrane/envelope biogenesis, Cell cycle ... |
337-532 |
6.12e-14 |
|
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: 74.56 E-value: 6.12e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56693217 337 VLLDNdhyAMEKLKKRVLEYLAVRQLKSTLKGPI---LCFVGPPGVGKTSVGRSIARTLGREFHRIALGGVCDQsdirgh 413
Cdd:COG0464 160 GGLEE---VKEELRELVALPLKRPELREEYGLPPprgLLLYGPPGTGKTLLARALAGELGLPLIEVDLSDLVSK------ 230
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56693217 414 rrtYVGSMPGRIINGLKTV-GVNNPVFLLDEVDKLGKSLQGDPA-------AALLEVLDpeqnhsftdhylNVPFDlsqV 485
Cdd:COG0464 231 ---YVGETEKNLREVFDKArGLAPCVLFIDEADALAGKRGEVGDgvgrrvvNTLLTEME------------ELRSD---V 292
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 56693217 486 LFIATANTTATIPPALLDRM-EVLQVPGYTQEEKVEIAHRHLIPHQLE 532
Cdd:COG0464 293 VVIAATNRPDLLDPALLRRFdEIIFFPLPDAEERLEIFRIHLRKRPLD 340
|
|
| AAA |
cd00009 |
The AAA+ (ATPases Associated with a wide variety of cellular Activities) superfamily ... |
352-506 |
3.05e-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: 62.16 E-value: 3.05e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56693217 352 RVLEYLAVRQLKSTLKGPILCFVGPPGVGKTSVGRSIARTL---GREFHRIALGGVCDQSDIRGHRRTYvgsmPGRIING 428
Cdd:cd00009 3 QEEAIEALREALELPPPKNLLLYGPPGTGKTTLARAIANELfrpGAPFLYLNASDLLEGLVVAELFGHF----LVRLLFE 78
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 56693217 429 LKTVGvNNPVFLLDEVDKLGKSLQgdpaAALLEVLDpeqnhsfTDHYLNVPFDLSQVLFIATANTTATIPPALLDRME 506
Cdd:cd00009 79 LAEKA-KPGVLFIDEIDSLSRGAQ----NALLRVLE-------TLNDLRIDRENVRVIGATNRPLLGDLDRALYDRLD 144
|
|
| MoxR |
COG0714 |
MoxR-like ATPase [General function prediction only]; MoxR-like ATPase is part of the Pathway ... |
366-551 |
5.85e-11 |
|
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: 64.42 E-value: 5.85e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56693217 366 LKGPILcFVGPPGVGKTSVGRSIARTLGREFHRIalggvcdQsdirghrrTYVGSMPGRIInglktvGVNN--------- 436
Cdd:COG0714 30 AGGHLL-LEGVPGVGKTTLAKALARALGLPFIRI-------Q--------FTPDLLPSDIL------GTYIydqqtgefe 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56693217 437 ----PVF----LLDEVDKlgkslqGDPA--AALLEVLdpeQNHSFT----DHYLNVPFdlsqvLFIATANT-----TATI 497
Cdd:COG0714 88 frpgPLFanvlLADEINR------APPKtqSALLEAM---EERQVTipggTYKLPEPF-----LVIATQNPieqegTYPL 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 56693217 498 PPALLDRMEV-LQVpGY-TQEEKVEIAHRHLIPHQLE-QHGLTPQQLQIPQDTTLQI 551
Cdd:COG0714 154 PEAQLDRFLLkLYI-GYpDAEEEREILRRHTGRHLAEvEPVLSPEELLALQELVRQV 209
|
|
| AAA_5 |
pfam07728 |
AAA domain (dynein-related subfamily); This Pfam entry includes some of the AAA proteins not ... |
371-505 |
5.54e-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: 55.38 E-value: 5.54e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56693217 371 LCFVGPPGVGKTSVGRSIA-RTLGREFHRIALGGVCDQSDIRGHRRtyVGSMPGRIING-LKTVGVNNPVFLLDEVDKLG 448
Cdd:pfam07728 2 VLLVGPPGTGKTELAERLAaALSNRPVFYVQLTRDTTEEDLFGRRN--IDPGGASWVDGpLVRAAREGEIAVLDEINRAN 79
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 56693217 449 KSLQGdpaaALLEVLDPEQNHSFTDHYLnVPFDLSQVLFIATANT----TATIPPALLDRM 505
Cdd:pfam07728 80 PDVLN----SLLSLLDERRLLLPDGGEL-VKAAPDGFRLIATMNPldrgLNELSPALRSRF 135
|
|
| COG1223 |
COG1223 |
Predicted ATPase, AAA+ superfamily [General function prediction only]; |
341-532 |
5.22e-08 |
|
Predicted ATPase, AAA+ superfamily [General function prediction only];
Pssm-ID: 440836 [Multi-domain] Cd Length: 246 Bit Score: 54.89 E-value: 5.22e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56693217 341 NDHYAMEKLK---KRVLEYLAVRQ-LKSTLKGP---ILcFVGPPGVGKTSVGRSIARTLGREFHRIALGGVCDQsdirgh 413
Cdd:COG1223 2 DDVVGQEEAKkklKLIIKELRRREnLRKFGLWPprkIL-FYGPPGTGKTMLAEALAGELKLPLLTVRLDSLIGS------ 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56693217 414 rrtYVGSMPGRI------INGLKTvgvnnpVFLLDEVDKLGK-----SLQGDPAA---ALLEVLDPEQNHSftdhylnvp 479
Cdd:COG1223 75 ---YLGETARNLrklfdfARRAPC------VIFFDEFDAIAKdrgdqNDVGEVKRvvnALLQELDGLPSGS--------- 136
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 56693217 480 fdlsqvLFIATANTTATIPPALLDRM-EVLQVPGYTQEEKVEIAHRHLIPHQLE 532
Cdd:COG1223 137 ------VVIAATNHPELLDSALWRRFdEVIEFPLPDKEERKEILELNLKKFPLP 184
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
367-505 |
7.13e-07 |
|
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a variety of cellular activities. This profile/alignment only detects a fraction of this vast family. The poorly conserved N-terminal helix is missing from the alignment.
Pssm-ID: 214640 [Multi-domain] Cd Length: 148 Bit Score: 49.68 E-value: 7.13e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56693217 367 KGPILCFVGPPGVGKTSVGRSIARTLGREFHRI-------ALGGVCDQSDIRGHRRTYVGSMPGRIINGLKTV--GVNNP 437
Cdd:smart00382 1 PGEVILIVGPPGSGKTTLARALARELGPPGGGViyidgedILEEVLDQLLLIIVGGKKASGSGELRLRLALALarKLKPD 80
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 56693217 438 VFLLDEVDKLGKSLQgdpaAALLEVLDPEQNHSFTDHYLNVPfdlsqvlFIATANTTATIPPALLDRM 505
Cdd:smart00382 81 VLILDEITSLLDAEQ----EALLLLLEELRLLLLLKSEKNLT-------VILTTNDEKDLGPALLRRR 137
|
|
| PRK13342 |
PRK13342 |
recombination factor protein RarA; Reviewed |
373-524 |
7.42e-07 |
|
recombination factor protein RarA; Reviewed
Pssm-ID: 237355 [Multi-domain] Cd Length: 413 Bit Score: 52.39 E-value: 7.42e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56693217 373 FVGPPGVGKTSVGRSIARTLGREFHRI--ALGGVcdqSDIRghrrtyvgsmpgRIINGLKT--VGVNNPVFLLDEVDKLG 448
Cdd:PRK13342 41 LWGPPGTGKTTLARIIAGATDAPFEALsaVTSGV---KDLR------------EVIEEARQrrSAGRRTILFIDEIHRFN 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56693217 449 KSLQgDpaaALLEVLdpEQNHsftdhylnvpfdlsqVLFIATanTTA----TIPPALLDRMEVLQVPGYTQEEKVEIAHR 524
Cdd:PRK13342 106 KAQQ-D---ALLPHV--EDGT---------------ITLIGA--TTEnpsfEVNPALLSRAQVFELKPLSEEDIEQLLKR 162
|
|
| RecA-like_ClpB_Hsp104-like |
cd19499 |
Chaperone protein ClpB/Hsp104 subfamily; Bacterial Caseinolytic peptidase B (ClpB) and ... |
358-506 |
1.22e-06 |
|
Chaperone protein ClpB/Hsp104 subfamily; Bacterial Caseinolytic peptidase B (ClpB) and eukaryotic Heat shock protein 104 (Hsp104) are ATP-dependent molecular chaperones and essential proteins of the heat-shock response. ClpB/Hsp104 ATPases, in concert with the DnaK/Hsp70 chaperone system, disaggregate and reactivate aggregated proteins. This RecA-like_ClpB_Hsp104_like subfamily belongs to the RecA-like NTPase family which includes the NTP binding domain of F1 and V1 H(+)ATPases, DnaB and related helicases as well as bacterial RecA and related eukaryotic and archaeal recombinases. The RecA-like NTPase family also includes bacterial conjugation proteins and related DNA transfer proteins involved in type II and type IV secretion.
Pssm-ID: 410907 [Multi-domain] Cd Length: 178 Bit Score: 49.48 E-value: 1.22e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56693217 358 AVRQLKSTLKGP-----ILCFVGPPGVGKTSVGRSIARTL-GREFHRIALggvcDQS-DIRGHRRTYVGSMPGRIIngLK 430
Cdd:cd19499 26 AIRRARAGLSDPnrpigSFLFLGPTGVGKTELAKALAELLfGDEDNLIRI----DMSeYMEKHSVSRLIGAPPGYV--GY 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56693217 431 TVG-------VNNP--VFLLDEVDKLGKSLQGdpaaALLEVLDpeqNHSFTDHYLNVpFDLSQVLFIATANttaTIPPAL 501
Cdd:cd19499 100 TEGgqlteavRRKPysVVLLDEIEKAHPDVQN----LLLQVLD---DGRLTDSHGRT-VDFKNTIIIMTSN---HFRPEF 168
|
....*
gi 56693217 502 LDRME 506
Cdd:cd19499 169 LNRID 173
|
|
| RarA |
COG2256 |
Replication-associated recombination protein RarA (DNA-dependent ATPase) [Replication, ... |
375-552 |
6.89e-06 |
|
Replication-associated recombination protein RarA (DNA-dependent ATPase) [Replication, recombination and repair];
Pssm-ID: 441857 [Multi-domain] Cd Length: 439 Bit Score: 49.28 E-value: 6.89e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56693217 375 GPPGVGKTSVGRSIARTLGREFHRI--ALGGVcdqSDIR------GHRRTYvgsmpgriinGLKTVgvnnpVFlLDEVDK 446
Cdd:COG2256 56 GPPGTGKTTLARLIANATDAEFVALsaVTSGV---KDIRevieeaRERRAY----------GRRTI-----LF-VDEIHR 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56693217 447 LGKSLQgDpaaALLEVLdpEQNHsftdhylnvpfdlsqVLFIA--TANTTATIPPALLDRMEVLQVPGYTQEEKVEIAHR 524
Cdd:COG2256 117 FNKAQQ-D---ALLPHV--EDGT---------------ITLIGatTENPSFEVNSALLSRCRVFVLKPLSEEDLEQLLER 175
|
170 180
....*....|....*....|....*...
gi 56693217 525 HLiphQLEQHGLTPQQLQIPQDTTLQII 552
Cdd:COG2256 176 AL---ADDERGLGGYKLELDDEALEALA 200
|
|
| 44 |
PHA02544 |
clamp loader, small subunit; Provisional |
363-522 |
8.05e-06 |
|
clamp loader, small subunit; Provisional
Pssm-ID: 222866 [Multi-domain] Cd Length: 316 Bit Score: 48.83 E-value: 8.05e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56693217 363 KSTLKG-------PILCFVGP-PGVGKTSVGRSIARTLGREFHRIAlGGVCDQSDIRGHRRTYVGSMpgriinglkTVGV 434
Cdd:PHA02544 30 KETFKSivkkgriPNMLLHSPsPGTGKTTVAKALCNEVGAEVLFVN-GSDCRIDFVRNRLTRFASTV---------SLTG 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56693217 435 NNPVFLLDEVDKLGkslqgdpaaaLLEVldpeQNH--SFTDHYlnvpfdLSQVLFIATANTTATIPPALLDRMEVLQVPG 512
Cdd:PHA02544 100 GGKVIIIDEFDRLG----------LADA----QRHlrSFMEAY------SKNCSFIITANNKNGIIEPLRSRCRVIDFGV 159
|
170
....*....|
gi 56693217 513 YTQEEKVEIA 522
Cdd:PHA02544 160 PTKEEQIEMM 169
|
|
| AAA_2 |
pfam07724 |
AAA domain (Cdc48 subfamily); This Pfam entry includes some of the AAA proteins not detected ... |
373-528 |
8.61e-06 |
|
AAA domain (Cdc48 subfamily); This Pfam entry includes some of the AAA proteins not detected by the pfam00004 model.
Pssm-ID: 400187 [Multi-domain] Cd Length: 168 Bit Score: 46.80 E-value: 8.61e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56693217 373 FVGPPGVGKTSVGRSIARTLG---REFHRIalggvcDQSDIrgHRRTYV----GSMPGRII---NGLKTVGV-NNP--VF 439
Cdd:pfam07724 8 FLGPTGVGKTELAKALAELLFgdeRALIRI------DMSEY--MEEHSVsrliGAPPGYVGyeeGGQLTEAVrRKPysIV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56693217 440 LLDEVDKLGKSLQGDpaaaLLEVLDpeqNHSFTDHYlNVPFDLSQVLFIATANTTATIPpalLDRMEVLQVPGY--TQEE 517
Cdd:pfam07724 80 LIDEIEKAHPGVQND----LLQILE---GGTLTDKQ-GRTVDFKNTLFIMTGNFGSEKI---SDASRLGDSPDYelLKEE 148
|
170
....*....|.
gi 56693217 518 KVEIAHRHLIP 528
Cdd:pfam07724 149 VMDLLKKGFIP 159
|
|
| aroK |
PRK00131 |
shikimate kinase; Reviewed |
366-396 |
9.44e-06 |
|
shikimate kinase; Reviewed
Pssm-ID: 234654 [Multi-domain] Cd Length: 175 Bit Score: 46.72 E-value: 9.44e-06
10 20 30
....*....|....*....|....*....|.
gi 56693217 366 LKGPILCFVGPPGVGKTSVGRSIARTLGREF 396
Cdd:PRK00131 2 LKGPNIVLIGFMGAGKSTIGRLLAKRLGYDF 32
|
|
| SdrC |
COG3480 |
Predicted secreted protein YlbL, contains PDZ domain [Signal transduction mechanisms]; |
729-821 |
1.41e-05 |
|
Predicted secreted protein YlbL, contains PDZ domain [Signal transduction mechanisms];
Pssm-ID: 442703 [Multi-domain] Cd Length: 344 Bit Score: 48.27 E-value: 1.41e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56693217 729 GPSAGvTIVTcLA--------SLLSGRlvrsDVAMTGEITLRGLVLPVGGIKDKVLAAHRANLKRIIIPKRNEKDLEEip 800
Cdd:COG3480 240 GPSAG-LMFA-LGiydqltpgDLTGGK----KIAGTGTIDADGTVGPIGGIDQKVVAARRAGATIFLAPASNCAEAVG-- 311
|
90 100
....*....|....*....|.
gi 56693217 801 aNVRADLDFVLAGTLDEVLNA 821
Cdd:COG3480 312 -TIPTGLKVVPVDTLDDALDA 331
|
|
| AroK |
COG0703 |
Shikimate kinase [Amino acid transport and metabolism]; Shikimate kinase is part of the ... |
371-397 |
8.55e-05 |
|
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: 43.96 E-value: 8.55e-05
10 20
....*....|....*....|....*..
gi 56693217 371 LCFVGPPGVGKTSVGRSIARTLGREFH 397
Cdd:COG0703 1 IVLIGMMGAGKSTVGRLLAKRLGLPFV 27
|
|
| SK |
cd00464 |
Shikimate kinase (SK) is the fifth enzyme in the shikimate pathway, a seven-step biosynthetic ... |
374-396 |
2.17e-04 |
|
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: 42.54 E-value: 2.17e-04
10 20
....*....|....*....|...
gi 56693217 374 VGPPGVGKTSVGRSIARTLGREF 396
Cdd:cd00464 5 IGMMGAGKTTVGRLLAKALGLPF 27
|
|
| FlhF |
COG1419 |
Flagellar biosynthesis GTPase FlhF [Cell motility]; |
291-382 |
6.52e-04 |
|
Flagellar biosynthesis GTPase FlhF [Cell motility];
Pssm-ID: 441029 [Multi-domain] Cd Length: 361 Bit Score: 42.93 E-value: 6.52e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56693217 291 LKELRRLKKMPQSMpeyaLTRNYLEMMVELPWSKSTTDCL-----DIRAARVLLD------NDHYAMEKLKKRVLEYLAV 359
Cdd:COG1419 80 RRELAELKELLEEQ----LSGLAGESARLPPELAELLERLleagvSPELARELLEklpedlSAEEAWRALLEALARRLPV 155
|
90 100
....*....|....*....|...
gi 56693217 360 RQLKSTLKGPILCFVGPPGVGKT 382
Cdd:COG1419 156 AEDPLLDEGGVIALVGPTGVGKT 178
|
|
| AAA_3 |
pfam07726 |
ATPase family associated with various cellular activities (AAA); This Pfam entry includes some ... |
375-504 |
1.31e-03 |
|
ATPase family associated with various cellular activities (AAA); This Pfam entry includes some of the AAA proteins not detected by the pfam00004 model.
Pssm-ID: 429622 [Multi-domain] Cd Length: 131 Bit Score: 39.46 E-value: 1.31e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56693217 375 GPPGVGKTSVGRSIARTLGREFHRIALGGVCDQSDIRG------HRRTYVgSMPGriinglktvgvnnPVF----LLDEV 444
Cdd:pfam07726 6 GVPGLAKTLLVRTLARSLGLDFRRIQFTPDLLPSDITGtevfdqKTREFE-FRPG-------------PVFanvlLADEI 71
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 56693217 445 DKLGKSLQgdpaAALLEVLdpeQNHSFTdhYLNVPFDLSQVLF-IATANT-----TATIPPALLDR 504
Cdd:pfam07726 72 NRAPPKTQ----SALLEAM---QERQVT--IDGETHPLPEPFFvLATQNPieqegTYPLPEAQLDR 128
|
|
| LonB |
COG1067 |
Predicted ATP-dependent protease [Posttranslational modification, protein turnover, chaperones] ... |
728-796 |
2.76e-03 |
|
Predicted ATP-dependent protease [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440686 [Multi-domain] Cd Length: 742 Bit Score: 41.47 E-value: 2.76e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 56693217 728 DGPSAGVTIVTCLASLLSGRLVRSDVAMTGEITLRGLVLPVGGIKDKV-----LAAHRaNLKR---IIIPKRNEKDL 796
Cdd:COG1067 592 DGDSASSAELYALLSALSGVPIRQDIAVTGSVNQHGEVQPIGGVNEKIegffdVCKAR-GLTGkqgVIIPAANVKNL 667
|
|
| clpA |
PRK11034 |
ATP-dependent Clp protease ATP-binding subunit; Provisional |
373-492 |
3.12e-03 |
|
ATP-dependent Clp protease ATP-binding subunit; Provisional
Pssm-ID: 236828 [Multi-domain] Cd Length: 758 Bit Score: 41.36 E-value: 3.12e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56693217 373 FVGPPGVGKTSVGRSIARTLGREFHRIalggvcDQSDIrGHRRT---YVGSMPGRI---INGLKTVGV-NNP--VFLLDE 443
Cdd:PRK11034 493 FAGPTGVGKTEVTVQLSKALGIELLRF------DMSEY-MERHTvsrLIGAPPGYVgfdQGGLLTDAViKHPhaVLLLDE 565
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 56693217 444 VDKlgksLQGDPAAALLEVLDpeqNHSFTDHYlNVPFDLSQVLFIATAN 492
Cdd:PRK11034 566 IEK----AHPDVFNLLLQVMD---NGTLTDNN-GRKADFRNVVLVMTTN 606
|
|
| PRK13341 |
PRK13341 |
AAA family ATPase; |
371-460 |
3.74e-03 |
|
AAA family ATPase;
Pssm-ID: 237354 [Multi-domain] Cd Length: 725 Bit Score: 40.81 E-value: 3.74e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56693217 371 LCFVGPPGVGKTSVGRSIARTLGREFHRI--ALGGVcdqSDIR------GHRRTYvgsmpgriiNGLKTvgvnnpVFLLD 442
Cdd:PRK13341 55 LILYGPPGVGKTTLARIIANHTRAHFSSLnaVLAGV---KDLRaevdraKERLER---------HGKRT------ILFID 116
|
90
....*....|....*...
gi 56693217 443 EVDKLGKSLQgdpaAALL 460
Cdd:PRK13341 117 EVHRFNKAQQ----DALL 130
|
|
| Kti12 |
COG4088 |
tRNA uridine 5-carbamoylmethylation protein Kti12 (Killer toxin insensitivity protein) ... |
366-413 |
5.03e-03 |
|
tRNA uridine 5-carbamoylmethylation protein Kti12 (Killer toxin insensitivity protein) [Translation, ribosomal structure and biogenesis, Defense mechanisms];
Pssm-ID: 443264 [Multi-domain] Cd Length: 179 Bit Score: 38.94 E-value: 5.03e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*...
gi 56693217 366 LKGPILCFVGPPGVGKTSVGRSIARTLGREFHRIAlggVCDQSDIRGH 413
Cdd:COG4088 2 DSPMLLILTGPPGSGKTTFAKALAQRLYAEGIAVA---LLHSDDFRRF 46
|
|
|