|
Name |
Accession |
Description |
Interval |
E-value |
| Lon |
COG0466 |
ATP-dependent Lon protease, bacterial type [Posttranslational modification, protein turnover, ... |
1-835 |
0e+00 |
|
ATP-dependent Lon protease, bacterial type [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440234 [Multi-domain] Cd Length: 785 Bit Score: 978.73 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74727668 1 MS-SVSPIQIPSRLPLLLTHEGVLLPGSTMRTSVDSARNLQLVRsRLLKGTSLqstiLGVI----PNTPDPASDAqdlpp 75
Cdd:COG0466 1 MSeEKEEEELPETLPLLPLRDVVVFPGMVIPLFVGREKSIKALE-EAMEGDKL----IGLVaqkdAEVEDPGPDD----- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74727668 76 LHRIGTAALAVQVVgsNWPKPHYTLLITGLCRFQIVQVLKEKPYPIAEVEQLDrlEEFPNTCKMREELGELSEQFYKYAv 155
Cdd:COG0466 71 LYEVGTVAKILQLL--KLPDGTVKVLVEGLQRARIKEFVQEEPYLEAEVEPLE--EEEEDDKELEALMRSLKEQFEEYV- 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74727668 156 qlveMLDMSVP--AVAKLRRLLDSlprEALPDILTSIIRTSNKEKLQILDAVSLEERFKMTIPLLVRQIEGLKLLQKTR- 232
Cdd:COG0466 146 ----KLNPKIPpeLLAALSNIEDP---GRLADFIASHLPLKIEEKQELLETLDVKERLEKLLELLEKEIEVLELEKKIRs 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74727668 233 KPKQDDDKR---------VIAIR-----------PIRRithisgtledededednddivmLEKKIRTSSMPEQAHKVCVK 292
Cdd:COG0466 219 RVKEQMEKSqreyylreqLKAIQkelgekddgedEIEE----------------------LREKIEKAKLPEEVKEKAEK 276
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74727668 293 EIKRLKKMPQSMPEYALTRNYLELMVELPWNKSTTDRLDIRAARILLDNDHYAMEKLKKRVLEYLAVRQLKNNLKGPILC 372
Cdd:COG0466 277 ELKKLERMPPMSAEATVIRNYLDWLLDLPWGKRTKDNLDLKKAEKILDEDHYGLEKVKERILEYLAVRKLKKKLKGPILC 356
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74727668 373 FVGPPGVGKTSVGRSVAKTLGREFHRIALGGVCDQSDIRGHRRTYVGSMPGRIINGLKTVGVNNPVFLLDEVDKLGKSLQ 452
Cdd:COG0466 357 LVGPPGVGKTSLGKSIARALGRKFVRISLGGVRDEAEIRGHRRTYIGAMPGRIIQGLKKAGTKNPVFLLDEIDKMGSDFR 436
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74727668 453 GDPAAALLEVLDPEQNHNFTDHYLNVAFDLSQVLFIATANTTATIPAALLDRMEIIQVPGYTQEEKIEIAHRHLIPKQLE 532
Cdd:COG0466 437 GDPASALLEVLDPEQNNTFSDHYLEVPFDLSKVMFIATANSLDTIPAPLLDRMEIIELSGYTEEEKLEIAKRYLIPKQLK 516
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74727668 533 QHGLTPQQIQIPQVTTLDIITRYTREAGVRSLDRKLGAICRAVAVKVAEGQHKEAKLDRSDvteregcrehiledekpes 612
Cdd:COG0466 517 EHGLKKEELKISDEALRKIIRGYTREAGVRNLEREIAKICRKVAKKIAEGKKKKVTITPKN------------------- 577
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74727668 613 isdttdlalppempilidfhaLKDILGPPMYEMEVSQRLSQPGVAIGLAWTPLGGEIMFVEASRMDGEGQLTLTGQLGDV 692
Cdd:COG0466 578 ---------------------LEKYLGVPRFRYEKAEEEDQVGVVTGLAWTEVGGDILFIEATLMPGKGKLTLTGQLGDV 636
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74727668 693 MKESAHLAISWLRSNAKKYQLtnafgSFDLLDNTDIHLHFPAGAVTKDGPSAGVTIVTCLASLFSGRLVRSDVAMTGEIT 772
Cdd:COG0466 637 MKESAQAALSYVRSRAEELGI-----DPDFFEKYDIHIHVPEGATPKDGPSAGITMATALVSALTGRPVRSDVAMTGEIT 711
|
810 820 830 840 850 860
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 74727668 773 LRGLVLPVGGIKDKVLAAHRAGLKQVIIPRRNEKDLEGIPGNVRQDLSFVTASCLDEVLNAAF 835
Cdd:COG0466 712 LRGRVLPIGGLKEKLLAAHRAGIKTVILPKENEKDLEEIPEEVKKGLEFHPVEHIDEVLKIAL 774
|
|
| lon |
TIGR00763 |
endopeptidase La; This protein, the ATP-dependent serine endopeptidase La, is induced by heat ... |
14-835 |
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: 807.29 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74727668 14 PLLLTHEGVLLPGSTMRTSVDSARNLQLVRsrllKGTSLQSTILGVIPNTPDPaSDAQDLPPLHRIGTAALAVQVVGS-N 92
Cdd:TIGR00763 1 PLLPLRRRPLFPGMIKPIDVGREKSIKLIK----EALRLKQPYLGLFLQKDDD-NEEPEEDDIYSVGVVAQILEMLPLpS 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74727668 93 WPKPHYTLLITGLCRFQIVQVLKEKPYPIAEVeqlDRLEEFPNTcKMREELGELSEQFYKYAVQLVEMLDMSVPAVAKLR 172
Cdd:TIGR00763 76 SGTATYKVVVEGLRRIRIKELSDKGGYLVVRV---DNLKEEPFD-KDDEEIKALTREIKETFRELISLSKLFREQPALLS 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74727668 173 RLLDSLPREALPDILTSIIRTSNKEKLQ-ILDAVSLEERFKMTIPLLVRQIEGLKLLQK-TRKPKQ---DDDKRVIAIRP 247
Cdd:TIGR00763 152 ALEDIDEPGRLADFVAASLQLKEKDELQeVLETVNIEKRLKKALELLKKELELLKLQNKiTKKVEEkmeKTQREYYLREQ 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74727668 248 IRRITHISGTlededEDEDNDDIVMLEKKIRTSSMPEQAHKVCVKEIKRLKKMPQSMPEYALTRNYLELMVELPWNKSTT 327
Cdd:TIGR00763 232 LKAIKKELGI-----EKDDKDELEKLKEKLEELKLPEEVKKVIEKELTKLSLLEPSSSEFTVTRNYLDWLTDLPWGKYSK 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74727668 328 DRLDIRAARILLDNDHYAMEKLKKRVLEYLAVRQLKNNLKGPILCFVGPPGVGKTSVGRSVAKTLGREFHRIALGGVCDQ 407
Cdd:TIGR00763 307 ENLDLKRAKEILDEDHYGLKKVKERILEYLAVQKLRGKMKGPILCLVGPPGVGKTSLGKSIAKALNRKFVRFSLGGVRDE 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74727668 408 SDIRGHRRTYVGSMPGRIINGLKTVGVNNPVFLLDEVDKLGKSLQGDPAAALLEVLDPEQNHNFTDHYLNVAFDLSQVLF 487
Cdd:TIGR00763 387 AEIRGHRRTYVGAMPGRIIQGLKKAKTKNPLFLLDEIDKIGSSFRGDPASALLEVLDPEQNNAFSDHYLDVPFDLSKVIF 466
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74727668 488 IATANTTATIPAALLDRMEIIQVPGYTQEEKIEIAHRHLIPKQLEQHGLTPQQIQIPQVTTLDIITRYTREAGVRSLDRK 567
Cdd:TIGR00763 467 IATANSIDTIPRPLLDRMEVIELSGYTEEEKLEIAKKYLIPKALEDHGLKPDELKITDEALLLLIKYYTREAGVRNLERQ 546
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74727668 568 LGAICRAVAVKVAEGQHKEAkldrsdvteregcrehiledEKPESISDTTDLalppempilidfhaLKDILGPPMYEMEV 647
Cdd:TIGR00763 547 IEKICRKAAVKLVEQGEKKK--------------------SEAESVVITPDN--------------LKKYLGKPVFTYER 592
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74727668 648 SQRLSQPGVAIGLAWTPLGGEIMFVEASRMDGEGQLTLTGQLGDVMKESAHLAISWLRSNAKKYQLTNafgsfDLLDNTD 727
Cdd:TIGR00763 593 AYEVTPPGVVMGLAWTPMGGDTLFIETTKVAGKGSLELTGQLGDVMKESAQIALTYVRSIAADLGISP-----NFFEKAD 667
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74727668 728 IHLHFPAGAVTKDGPSAGVTIVTCLASLFSGRLVRSDVAMTGEITLRGLVLPVGGIKDKVLAAHRAGLKQVIIPRRNEKD 807
Cdd:TIGR00763 668 IHLHVPEGATPKDGPSAGITMATALLSLATGKPVRPDVAMTGEITLRGKVLPIGGLKEKTIAAKRAGIKTIILPEKNRRD 747
|
810 820
....*....|....*....|....*...
gi 74727668 808 LEGIPGNVRQDLSFVTASCLDEVLNAAF 835
Cdd:TIGR00763 748 LEELPENVKEGLEIHFVKHYDEVLKKAF 775
|
|
| PRK10787 |
PRK10787 |
DNA-binding ATP-dependent protease La; Provisional |
65-835 |
0e+00 |
|
DNA-binding ATP-dependent protease La; Provisional
Pssm-ID: 182730 [Multi-domain] Cd Length: 784 Bit Score: 539.91 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74727668 65 DPASDAQDLPPLHRIGTAALAVQVVgsNWPKPHYTLLITGLCRFQIVQVLKEKPYPIAEVEQLD--RLEEFPNTCKMREE 142
Cdd:PRK10787 57 EASTDEPGVNDLFTVGTVASILQML--KLPDGTVKVLVEGLQRARISALSDNGEHFSAKAEYLEspTIDEREQEVLVRTA 134
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74727668 143 LGELsEQFYKYAVQLVEMLDMSVPAVAKLRRLLDSLPREaLPDILtsiirtsnKEKLQILDAVSLEERFKMTIPLLVRQI 222
Cdd:PRK10787 135 ISQF-EGYIKLNKKIPPEVLTSLNSIDDPARLADTIAAH-MPLKL--------ADKQSVLEMSDVNERLEYLMAMMESEI 204
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74727668 223 EGLKLLQKTR---KPKQDDDKRVIAI-RPIRRITHISGTLEDEDEDEDNddivmLEKKIRTSSMPEQAHKVCVKEIKRLK 298
Cdd:PRK10787 205 DLLQVEKRIRnrvKKQMEKSQREYYLnEQMKAIQKELGEMDDAPDENEA-----LKRKIDAAKMPKEAKEKAEAELQKLK 279
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74727668 299 KMPQSMPEYALTRNYLELMVELPWNKSTTDRLDIRAARILLDNDHYAMEKLKKRVLEYLAVRQLKNNLKGPILCFVGPPG 378
Cdd:PRK10787 280 MMSPMSAEATVVRGYIDWMVQVPWNARSKVKKDLRQAQEILDTDHYGLERVKDRILEYLAVQSRVNKIKGPILCLVGPPG 359
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74727668 379 VGKTSVGRSVAKTLGREFHRIALGGVCDQSDIRGHRRTYVGSMPGRIINGLKTVGVNNPVFLLDEVDKLGKSLQGDPAAA 458
Cdd:PRK10787 360 VGKTSLGQSIAKATGRKYVRMALGGVRDEAEIRGHRRTYIGSMPGKLIQKMAKVGVKNPLFLLDEIDKMSSDMRGDPASA 439
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74727668 459 LLEVLDPEQNHNFTDHYLNVAFDLSQVLFIATANTTaTIPAALLDRMEIIQVPGYTQEEKIEIAHRHLIPKQLEQHGLTP 538
Cdd:PRK10787 440 LLEVLDPEQNVAFSDHYLEVDYDLSDVMFVATSNSM-NIPAPLLDRMEVIRLSGYTEDEKLNIAKRHLLPKQIERNALKK 518
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74727668 539 QQIQIPQVTTLDIITRYTREAGVRSLDRKLGAICRAvAVKVaegqhkeakldrsdvteregcrehILEDEKPESisdttd 618
Cdd:PRK10787 519 GELTVDDSAIIGIIRYYTREAGVRSLEREISKLCRK-AVKQ------------------------LLLDKSLKH------ 567
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74727668 619 lalppempILIDFHALKDILGPPMYEMEVSQRLSQPGVAIGLAWTPLGGEIMFVEASRMDGEGQLTLTGQLGDVMKESAH 698
Cdd:PRK10787 568 --------IEINGDNLHDYLGVQRFDYGRADNENRVGQVTGLAWTEVGGDLLTIETACVPGKGKLTYTGSLGEVMQESIQ 639
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74727668 699 LAISWLRSNAKKYQLTNAFgsfdlLDNTDIHLHFPAGAVTKDGPSAGVTIVTCLASLFSGRLVRSDVAMTGEITLRGLVL 778
Cdd:PRK10787 640 AALTVVRARAEKLGINPDF-----YEKRDIHVHVPEGATPKDGPSAGIAMCTALVSCLTGNPVRADVAMTGEITLRGQVL 714
|
730 740 750 760 770
....*....|....*....|....*....|....*....|....*....|....*..
gi 74727668 779 PVGGIKDKVLAAHRAGLKQVIIPRRNEKDLEGIPGNVRQDLSFVTASCLDEVLNAAF 835
Cdd:PRK10787 715 PIGGLKEKLLAAHRGGIKTVLIPFENKRDLEEIPDNVIADLDIHPVKRIEEVLTLAL 771
|
|
| RecA-like_Lon |
cd19500 |
lon protease homolog 2 peroxisomal; Lon protease (also known as Lon peptidase) is an ... |
332-513 |
4.81e-121 |
|
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: 363.03 E-value: 4.81e-121
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74727668 332 IRAARILLDNDHYAMEKLKKRVLEYLAVRQLKNNLKGPILCFVGPPGVGKTSVGRSVAKTLGREFHRIALGGVCDQSDIR 411
Cdd:cd19500 1 IKKARKVLDADHYGLEDVKERILEYLAVRKLKGSMKGPILCLVGPPGVGKTSLGKSIARALGRKFVRISLGGVRDEAEIR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74727668 412 GHRRTYVGSMPGRIINGLKTVGVNNPVFLLDEVDKLGKSLQGDPAAALLEVLDPEQNHNFTDHYLNVAFDLSQVLFIATA 491
Cdd:cd19500 81 GHRRTYVGAMPGRIIQALKKAGTNNPVFLLDEIDKIGSSFRGDPASALLEVLDPEQNSTFSDHYLDVPFDLSKVLFIATA 160
|
170 180
....*....|....*....|..
gi 74727668 492 NTTATIPAALLDRMEIIQVPGY 513
Cdd:cd19500 161 NSLDTIPGPLLDRMEIIELSGY 182
|
|
| Lon_C |
pfam05362 |
Lon protease (S16) C-terminal proteolytic domain; The Lon serine proteases must hydrolyse ATP ... |
634-837 |
1.07e-93 |
|
Lon protease (S16) C-terminal proteolytic domain; The Lon serine proteases must hydrolyse ATP to degrade protein substrates. In Escherichia coli, these proteases are involved in turnover of intracellular proteins, including abnormal proteins following heat-shock. The active site for protease activity resides in a C-terminal domain. The Lon proteases are classified as family S16 in Merops.
Pssm-ID: 428442 [Multi-domain] Cd Length: 205 Bit Score: 292.61 E-value: 1.07e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74727668 634 LKDILGPPMYEMEVSQRLSQPGVAIGLAWTPLGGEIMFVEASRMDGEGQLTLTGQLGDVMKESAHLAISWLRSNAKKYQL 713
Cdd:pfam05362 7 LEKYLGVPRFRYGEAEKEDQVGVVTGLAWTEVGGDLLTIEAVIMPGKGKLTLTGQLGDVMKESAQAALSYVRSRAEELGI 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74727668 714 tnafgSFDLLDNTDIHLHFPAGAVTKDGPSAGVTIVTCLASLFSGRLVRSDVAMTGEITLRGLVLPVGGIKDKVLAAHRA 793
Cdd:pfam05362 87 -----DPDFFEKKDIHIHVPEGATPKDGPSAGVTMATALVSALTGIPVRKDVAMTGEITLRGRVLPIGGLKEKLLAAHRA 161
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 74727668 794 GLKQVIIPRRNEKDLEGIPGNVRQDLSFVTASCLDEVLNAAFDG 837
Cdd:pfam05362 162 GIKTVIIPKENEKDLEDIPENVREGLEIIPVEHVDEVLKHALVG 205
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
367-505 |
3.39e-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: 44.67 E-value: 3.39e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74727668 367 KGPILCFVGPPGVGKTSVGRSVAKTLGREFHRI-------ALGGVCDQSDIRGHRRTYVGSMPGRIINGLKTV--GVNNP 437
Cdd:smart00382 1 PGEVILIVGPPGSGKTTLARALARELGPPGGGViyidgedILEEVLDQLLLIIVGGKKASGSGELRLRLALALarKLKPD 80
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 74727668 438 VFLLDEVDKLGKSLQgdpaAALLEVLDPEQNHNFTDHYLNvafdlsqVLFIATANTTATIPAALLDRM 505
Cdd:smart00382 81 VLILDEITSLLDAEQ----EALLLLLEELRLLLLLKSEKN-------LTVILTTNDEKDLGPALLRRR 137
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| Lon |
COG0466 |
ATP-dependent Lon protease, bacterial type [Posttranslational modification, protein turnover, ... |
1-835 |
0e+00 |
|
ATP-dependent Lon protease, bacterial type [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440234 [Multi-domain] Cd Length: 785 Bit Score: 978.73 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74727668 1 MS-SVSPIQIPSRLPLLLTHEGVLLPGSTMRTSVDSARNLQLVRsRLLKGTSLqstiLGVI----PNTPDPASDAqdlpp 75
Cdd:COG0466 1 MSeEKEEEELPETLPLLPLRDVVVFPGMVIPLFVGREKSIKALE-EAMEGDKL----IGLVaqkdAEVEDPGPDD----- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74727668 76 LHRIGTAALAVQVVgsNWPKPHYTLLITGLCRFQIVQVLKEKPYPIAEVEQLDrlEEFPNTCKMREELGELSEQFYKYAv 155
Cdd:COG0466 71 LYEVGTVAKILQLL--KLPDGTVKVLVEGLQRARIKEFVQEEPYLEAEVEPLE--EEEEDDKELEALMRSLKEQFEEYV- 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74727668 156 qlveMLDMSVP--AVAKLRRLLDSlprEALPDILTSIIRTSNKEKLQILDAVSLEERFKMTIPLLVRQIEGLKLLQKTR- 232
Cdd:COG0466 146 ----KLNPKIPpeLLAALSNIEDP---GRLADFIASHLPLKIEEKQELLETLDVKERLEKLLELLEKEIEVLELEKKIRs 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74727668 233 KPKQDDDKR---------VIAIR-----------PIRRithisgtledededednddivmLEKKIRTSSMPEQAHKVCVK 292
Cdd:COG0466 219 RVKEQMEKSqreyylreqLKAIQkelgekddgedEIEE----------------------LREKIEKAKLPEEVKEKAEK 276
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74727668 293 EIKRLKKMPQSMPEYALTRNYLELMVELPWNKSTTDRLDIRAARILLDNDHYAMEKLKKRVLEYLAVRQLKNNLKGPILC 372
Cdd:COG0466 277 ELKKLERMPPMSAEATVIRNYLDWLLDLPWGKRTKDNLDLKKAEKILDEDHYGLEKVKERILEYLAVRKLKKKLKGPILC 356
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74727668 373 FVGPPGVGKTSVGRSVAKTLGREFHRIALGGVCDQSDIRGHRRTYVGSMPGRIINGLKTVGVNNPVFLLDEVDKLGKSLQ 452
Cdd:COG0466 357 LVGPPGVGKTSLGKSIARALGRKFVRISLGGVRDEAEIRGHRRTYIGAMPGRIIQGLKKAGTKNPVFLLDEIDKMGSDFR 436
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74727668 453 GDPAAALLEVLDPEQNHNFTDHYLNVAFDLSQVLFIATANTTATIPAALLDRMEIIQVPGYTQEEKIEIAHRHLIPKQLE 532
Cdd:COG0466 437 GDPASALLEVLDPEQNNTFSDHYLEVPFDLSKVMFIATANSLDTIPAPLLDRMEIIELSGYTEEEKLEIAKRYLIPKQLK 516
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74727668 533 QHGLTPQQIQIPQVTTLDIITRYTREAGVRSLDRKLGAICRAVAVKVAEGQHKEAKLDRSDvteregcrehiledekpes 612
Cdd:COG0466 517 EHGLKKEELKISDEALRKIIRGYTREAGVRNLEREIAKICRKVAKKIAEGKKKKVTITPKN------------------- 577
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74727668 613 isdttdlalppempilidfhaLKDILGPPMYEMEVSQRLSQPGVAIGLAWTPLGGEIMFVEASRMDGEGQLTLTGQLGDV 692
Cdd:COG0466 578 ---------------------LEKYLGVPRFRYEKAEEEDQVGVVTGLAWTEVGGDILFIEATLMPGKGKLTLTGQLGDV 636
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74727668 693 MKESAHLAISWLRSNAKKYQLtnafgSFDLLDNTDIHLHFPAGAVTKDGPSAGVTIVTCLASLFSGRLVRSDVAMTGEIT 772
Cdd:COG0466 637 MKESAQAALSYVRSRAEELGI-----DPDFFEKYDIHIHVPEGATPKDGPSAGITMATALVSALTGRPVRSDVAMTGEIT 711
|
810 820 830 840 850 860
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 74727668 773 LRGLVLPVGGIKDKVLAAHRAGLKQVIIPRRNEKDLEGIPGNVRQDLSFVTASCLDEVLNAAF 835
Cdd:COG0466 712 LRGRVLPIGGLKEKLLAAHRAGIKTVILPKENEKDLEEIPEEVKKGLEFHPVEHIDEVLKIAL 774
|
|
| lon |
TIGR00763 |
endopeptidase La; This protein, the ATP-dependent serine endopeptidase La, is induced by heat ... |
14-835 |
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: 807.29 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74727668 14 PLLLTHEGVLLPGSTMRTSVDSARNLQLVRsrllKGTSLQSTILGVIPNTPDPaSDAQDLPPLHRIGTAALAVQVVGS-N 92
Cdd:TIGR00763 1 PLLPLRRRPLFPGMIKPIDVGREKSIKLIK----EALRLKQPYLGLFLQKDDD-NEEPEEDDIYSVGVVAQILEMLPLpS 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74727668 93 WPKPHYTLLITGLCRFQIVQVLKEKPYPIAEVeqlDRLEEFPNTcKMREELGELSEQFYKYAVQLVEMLDMSVPAVAKLR 172
Cdd:TIGR00763 76 SGTATYKVVVEGLRRIRIKELSDKGGYLVVRV---DNLKEEPFD-KDDEEIKALTREIKETFRELISLSKLFREQPALLS 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74727668 173 RLLDSLPREALPDILTSIIRTSNKEKLQ-ILDAVSLEERFKMTIPLLVRQIEGLKLLQK-TRKPKQ---DDDKRVIAIRP 247
Cdd:TIGR00763 152 ALEDIDEPGRLADFVAASLQLKEKDELQeVLETVNIEKRLKKALELLKKELELLKLQNKiTKKVEEkmeKTQREYYLREQ 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74727668 248 IRRITHISGTlededEDEDNDDIVMLEKKIRTSSMPEQAHKVCVKEIKRLKKMPQSMPEYALTRNYLELMVELPWNKSTT 327
Cdd:TIGR00763 232 LKAIKKELGI-----EKDDKDELEKLKEKLEELKLPEEVKKVIEKELTKLSLLEPSSSEFTVTRNYLDWLTDLPWGKYSK 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74727668 328 DRLDIRAARILLDNDHYAMEKLKKRVLEYLAVRQLKNNLKGPILCFVGPPGVGKTSVGRSVAKTLGREFHRIALGGVCDQ 407
Cdd:TIGR00763 307 ENLDLKRAKEILDEDHYGLKKVKERILEYLAVQKLRGKMKGPILCLVGPPGVGKTSLGKSIAKALNRKFVRFSLGGVRDE 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74727668 408 SDIRGHRRTYVGSMPGRIINGLKTVGVNNPVFLLDEVDKLGKSLQGDPAAALLEVLDPEQNHNFTDHYLNVAFDLSQVLF 487
Cdd:TIGR00763 387 AEIRGHRRTYVGAMPGRIIQGLKKAKTKNPLFLLDEIDKIGSSFRGDPASALLEVLDPEQNNAFSDHYLDVPFDLSKVIF 466
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74727668 488 IATANTTATIPAALLDRMEIIQVPGYTQEEKIEIAHRHLIPKQLEQHGLTPQQIQIPQVTTLDIITRYTREAGVRSLDRK 567
Cdd:TIGR00763 467 IATANSIDTIPRPLLDRMEVIELSGYTEEEKLEIAKKYLIPKALEDHGLKPDELKITDEALLLLIKYYTREAGVRNLERQ 546
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74727668 568 LGAICRAVAVKVAEGQHKEAkldrsdvteregcrehiledEKPESISDTTDLalppempilidfhaLKDILGPPMYEMEV 647
Cdd:TIGR00763 547 IEKICRKAAVKLVEQGEKKK--------------------SEAESVVITPDN--------------LKKYLGKPVFTYER 592
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74727668 648 SQRLSQPGVAIGLAWTPLGGEIMFVEASRMDGEGQLTLTGQLGDVMKESAHLAISWLRSNAKKYQLTNafgsfDLLDNTD 727
Cdd:TIGR00763 593 AYEVTPPGVVMGLAWTPMGGDTLFIETTKVAGKGSLELTGQLGDVMKESAQIALTYVRSIAADLGISP-----NFFEKAD 667
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74727668 728 IHLHFPAGAVTKDGPSAGVTIVTCLASLFSGRLVRSDVAMTGEITLRGLVLPVGGIKDKVLAAHRAGLKQVIIPRRNEKD 807
Cdd:TIGR00763 668 IHLHVPEGATPKDGPSAGITMATALLSLATGKPVRPDVAMTGEITLRGKVLPIGGLKEKTIAAKRAGIKTIILPEKNRRD 747
|
810 820
....*....|....*....|....*...
gi 74727668 808 LEGIPGNVRQDLSFVTASCLDEVLNAAF 835
Cdd:TIGR00763 748 LEELPENVKEGLEIHFVKHYDEVLKKAF 775
|
|
| PRK10787 |
PRK10787 |
DNA-binding ATP-dependent protease La; Provisional |
65-835 |
0e+00 |
|
DNA-binding ATP-dependent protease La; Provisional
Pssm-ID: 182730 [Multi-domain] Cd Length: 784 Bit Score: 539.91 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74727668 65 DPASDAQDLPPLHRIGTAALAVQVVgsNWPKPHYTLLITGLCRFQIVQVLKEKPYPIAEVEQLD--RLEEFPNTCKMREE 142
Cdd:PRK10787 57 EASTDEPGVNDLFTVGTVASILQML--KLPDGTVKVLVEGLQRARISALSDNGEHFSAKAEYLEspTIDEREQEVLVRTA 134
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74727668 143 LGELsEQFYKYAVQLVEMLDMSVPAVAKLRRLLDSLPREaLPDILtsiirtsnKEKLQILDAVSLEERFKMTIPLLVRQI 222
Cdd:PRK10787 135 ISQF-EGYIKLNKKIPPEVLTSLNSIDDPARLADTIAAH-MPLKL--------ADKQSVLEMSDVNERLEYLMAMMESEI 204
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74727668 223 EGLKLLQKTR---KPKQDDDKRVIAI-RPIRRITHISGTLEDEDEDEDNddivmLEKKIRTSSMPEQAHKVCVKEIKRLK 298
Cdd:PRK10787 205 DLLQVEKRIRnrvKKQMEKSQREYYLnEQMKAIQKELGEMDDAPDENEA-----LKRKIDAAKMPKEAKEKAEAELQKLK 279
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74727668 299 KMPQSMPEYALTRNYLELMVELPWNKSTTDRLDIRAARILLDNDHYAMEKLKKRVLEYLAVRQLKNNLKGPILCFVGPPG 378
Cdd:PRK10787 280 MMSPMSAEATVVRGYIDWMVQVPWNARSKVKKDLRQAQEILDTDHYGLERVKDRILEYLAVQSRVNKIKGPILCLVGPPG 359
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74727668 379 VGKTSVGRSVAKTLGREFHRIALGGVCDQSDIRGHRRTYVGSMPGRIINGLKTVGVNNPVFLLDEVDKLGKSLQGDPAAA 458
Cdd:PRK10787 360 VGKTSLGQSIAKATGRKYVRMALGGVRDEAEIRGHRRTYIGSMPGKLIQKMAKVGVKNPLFLLDEIDKMSSDMRGDPASA 439
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74727668 459 LLEVLDPEQNHNFTDHYLNVAFDLSQVLFIATANTTaTIPAALLDRMEIIQVPGYTQEEKIEIAHRHLIPKQLEQHGLTP 538
Cdd:PRK10787 440 LLEVLDPEQNVAFSDHYLEVDYDLSDVMFVATSNSM-NIPAPLLDRMEVIRLSGYTEDEKLNIAKRHLLPKQIERNALKK 518
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74727668 539 QQIQIPQVTTLDIITRYTREAGVRSLDRKLGAICRAvAVKVaegqhkeakldrsdvteregcrehILEDEKPESisdttd 618
Cdd:PRK10787 519 GELTVDDSAIIGIIRYYTREAGVRSLEREISKLCRK-AVKQ------------------------LLLDKSLKH------ 567
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74727668 619 lalppempILIDFHALKDILGPPMYEMEVSQRLSQPGVAIGLAWTPLGGEIMFVEASRMDGEGQLTLTGQLGDVMKESAH 698
Cdd:PRK10787 568 --------IEINGDNLHDYLGVQRFDYGRADNENRVGQVTGLAWTEVGGDLLTIETACVPGKGKLTYTGSLGEVMQESIQ 639
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74727668 699 LAISWLRSNAKKYQLTNAFgsfdlLDNTDIHLHFPAGAVTKDGPSAGVTIVTCLASLFSGRLVRSDVAMTGEITLRGLVL 778
Cdd:PRK10787 640 AALTVVRARAEKLGINPDF-----YEKRDIHVHVPEGATPKDGPSAGIAMCTALVSCLTGNPVRADVAMTGEITLRGQVL 714
|
730 740 750 760 770
....*....|....*....|....*....|....*....|....*....|....*..
gi 74727668 779 PVGGIKDKVLAAHRAGLKQVIIPRRNEKDLEGIPGNVRQDLSFVTASCLDEVLNAAF 835
Cdd:PRK10787 715 PIGGLKEKLLAAHRGGIKTVLIPFENKRDLEEIPDNVIADLDIHPVKRIEEVLTLAL 771
|
|
| RecA-like_Lon |
cd19500 |
lon protease homolog 2 peroxisomal; Lon protease (also known as Lon peptidase) is an ... |
332-513 |
4.81e-121 |
|
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: 363.03 E-value: 4.81e-121
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74727668 332 IRAARILLDNDHYAMEKLKKRVLEYLAVRQLKNNLKGPILCFVGPPGVGKTSVGRSVAKTLGREFHRIALGGVCDQSDIR 411
Cdd:cd19500 1 IKKARKVLDADHYGLEDVKERILEYLAVRKLKGSMKGPILCLVGPPGVGKTSLGKSIARALGRKFVRISLGGVRDEAEIR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74727668 412 GHRRTYVGSMPGRIINGLKTVGVNNPVFLLDEVDKLGKSLQGDPAAALLEVLDPEQNHNFTDHYLNVAFDLSQVLFIATA 491
Cdd:cd19500 81 GHRRTYVGAMPGRIIQALKKAGTNNPVFLLDEIDKIGSSFRGDPASALLEVLDPEQNSTFSDHYLDVPFDLSKVLFIATA 160
|
170 180
....*....|....*....|..
gi 74727668 492 NTTATIPAALLDRMEIIQVPGY 513
Cdd:cd19500 161 NSLDTIPGPLLDRMEIIELSGY 182
|
|
| Lon_C |
pfam05362 |
Lon protease (S16) C-terminal proteolytic domain; The Lon serine proteases must hydrolyse ATP ... |
634-837 |
1.07e-93 |
|
Lon protease (S16) C-terminal proteolytic domain; The Lon serine proteases must hydrolyse ATP to degrade protein substrates. In Escherichia coli, these proteases are involved in turnover of intracellular proteins, including abnormal proteins following heat-shock. The active site for protease activity resides in a C-terminal domain. The Lon proteases are classified as family S16 in Merops.
Pssm-ID: 428442 [Multi-domain] Cd Length: 205 Bit Score: 292.61 E-value: 1.07e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74727668 634 LKDILGPPMYEMEVSQRLSQPGVAIGLAWTPLGGEIMFVEASRMDGEGQLTLTGQLGDVMKESAHLAISWLRSNAKKYQL 713
Cdd:pfam05362 7 LEKYLGVPRFRYGEAEKEDQVGVVTGLAWTEVGGDLLTIEAVIMPGKGKLTLTGQLGDVMKESAQAALSYVRSRAEELGI 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74727668 714 tnafgSFDLLDNTDIHLHFPAGAVTKDGPSAGVTIVTCLASLFSGRLVRSDVAMTGEITLRGLVLPVGGIKDKVLAAHRA 793
Cdd:pfam05362 87 -----DPDFFEKKDIHIHVPEGATPKDGPSAGVTMATALVSALTGIPVRKDVAMTGEITLRGRVLPIGGLKEKLLAAHRA 161
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 74727668 794 GLKQVIIPRRNEKDLEGIPGNVRQDLSFVTASCLDEVLNAAFDG 837
Cdd:pfam05362 162 GIKTVIIPKENEKDLEDIPENVREGLEIIPVEHVDEVLKHALVG 205
|
|
| LON_substr_bdg |
pfam02190 |
ATP-dependent protease La (LON) substrate-binding domain; This domain has been shown to be ... |
13-220 |
2.63e-27 |
|
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: 109.73 E-value: 2.63e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74727668 13 LPLLLTHEGVLLPGSTMRTSVDSARNLQLVRSRLLKGtslQSTILGVIPNTpDPASDAQDLPPLHRIGTAALAVQVVGSn 92
Cdd:pfam02190 2 LPLLPLRNTVLFPGMVLPLFVGRPRSIAAIEAALNKD---KLYGVLLVSQK-DAEDEEPTPDDLYEVGTVAKIVQILKL- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74727668 93 wPKPHYTLLITGLCRFQIVQVL-KEKPYPIAEVEQLDrleefpntcKMREELGELSEQFYKYAVQ-LVEMLDMSVPAVAK 170
Cdd:pfam02190 77 -PDGTYKVLVEGLERVRIVELVkKEEPYLRAEVEDLP---------EDSDELSEALKALVKELIEkLRRLLKLLLPLELL 146
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 74727668 171 LRRLLDSLPrEALPDILTSIIRTSNKEKLQILDAVSLEERFKMTIPLLVR 220
Cdd:pfam02190 147 LKIKDIENP-GRLADLVAAILPLSPEEKQELLETLDVKERLEKVLELLNR 195
|
|
| AAA |
pfam00004 |
ATPase family associated with various cellular activities (AAA); AAA family proteins often ... |
371-513 |
2.30e-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: 104.98 E-value: 2.30e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74727668 371 LCFVGPPGVGKTSVGRSVAKTLGREFHRIALGGVCDqsdirghrrTYVGSMPGRIINGLKTVGVNNP-VFLLDEVDKLGK 449
Cdd:pfam00004 1 LLLYGPPGTGKTTLAKAVAKELGAPFIEISGSELVS---------KYVGESEKRLRELFEAAKKLAPcVIFIDEIDALAG 71
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 74727668 450 SLQG-------DPAAALLEVLDPEQNHNftdhylnvafdlSQVLFIATANTTATIPAALLDRMEIIQVPGY 513
Cdd:pfam00004 72 SRGSggdsesrRVVNQLLTELDGFTSSN------------SKVIVIAATNRPDKLDPALLGRFDRIIEFPL 130
|
|
| COG1750 |
COG1750 |
Predicted archaeal serine protease, S18 family [General function prediction only]; |
723-805 |
9.87e-16 |
|
Predicted archaeal serine protease, S18 family [General function prediction only];
Pssm-ID: 441356 [Multi-domain] Cd Length: 213 Bit Score: 76.94 E-value: 9.87e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74727668 723 LDNTDIHLHFPAGAVTKDGPSAGVTIVTCLASLFSGRLVRSDVAMTGEITLRGLVLPVGGIKDKVLAAHRAGLKQVIIPR 802
Cdd:COG1750 91 LSSYDVYISIESDSPIVGGPSAGGAMTVATYAALLGLPLNKSVTMTGMINPDGSIGPVGGVYEKLEAAASAGAKYFLIPK 170
|
...
gi 74727668 803 RNE 805
Cdd:COG1750 171 GQA 173
|
|
| SpoVK |
COG0464 |
AAA+-type ATPase, SpoVK/Ycf46/Vps4 family [Cell wall/membrane/envelope biogenesis, Cell cycle ... |
337-532 |
4.33e-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: 74.95 E-value: 4.33e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74727668 337 ILLDNdhyAMEKLKKRVLEYLAVRQLKNNLKGPI---LCFVGPPGVGKTSVGRSVAKTLGREFHRIALGGVCDQsdirgh 413
Cdd:COG0464 160 GGLEE---VKEELRELVALPLKRPELREEYGLPPprgLLLYGPPGTGKTLLARALAGELGLPLIEVDLSDLVSK------ 230
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74727668 414 rrtYVGSMPGRIINGLKTV-GVNNPVFLLDEVDKLGKSLQGDpaaallevldpeqnhnfTDHYLNVAFD---------LS 483
Cdd:COG0464 231 ---YVGETEKNLREVFDKArGLAPCVLFIDEADALAGKRGEV-----------------GDGVGRRVVNtlltemeelRS 290
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 74727668 484 QVLFIATANTTATIPAALLDRM-EIIQVPGYTQEEKIEIAHRHLIPKQLE 532
Cdd:COG0464 291 DVVVIAATNRPDLLDPALLRRFdEIIFFPLPDAEERLEIFRIHLRKRPLD 340
|
|
| RecA-like_protease |
cd19481 |
proteases similar to RecA; RecA-like NTPases. This family includes the NTP binding domain of ... |
345-504 |
6.45e-14 |
|
proteases similar to RecA; RecA-like NTPases. This family includes the NTP binding domain of F1 and V1 H(+)ATPases, DnaB and related helicases as well as bacterial RecA and related eukaryotic and archaeal recombinases. This group also includes bacterial conjugation proteins and related DNA transfer proteins involved in type II and type IV secretion.
Pssm-ID: 410889 [Multi-domain] Cd Length: 158 Bit Score: 70.00 E-value: 6.45e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74727668 345 AMEKLKKRVLEYLAVRQL--KNNLKGPILCFVGPPGVGKTSVGRSVAKTLGREFHRIALGGVCDQSdirghrRTYVGSMP 422
Cdd:cd19481 1 LKASLREAVEAPRRGSRLrrYGLGLPKGILLYGPPGTGKTLLAKALAGELGLPLIVVKLSSLLSKY------VGESEKNL 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74727668 423 GRIINGLKTVGvnNPVFLLDEVDKLGK--SLQGDPAA------ALLEVLDPEQNhnftdhylnvafdLSQVLFIATANTT 494
Cdd:cd19481 75 RKIFERARRLA--PCILFIDEIDAIGRkrDSSGESGElrrvlnQLLTELDGVNS-------------RSKVLVIAATNRP 139
|
170
....*....|
gi 74727668 495 ATIPAALLDR 504
Cdd:cd19481 140 DLLDPALLRP 149
|
|
| AAA |
cd00009 |
The AAA+ (ATPases Associated with a wide variety of cellular Activities) superfamily ... |
352-513 |
7.37e-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: 61.01 E-value: 7.37e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74727668 352 RVLEYLAVRQLKNNLKGPILCFVGPPGVGKTSVGRSVAKTL---GREFHRIALGGVCDQSDIRGHRRTYvgsmPGRIING 428
Cdd:cd00009 3 QEEAIEALREALELPPPKNLLLYGPPGTGKTTLARAIANELfrpGAPFLYLNASDLLEGLVVAELFGHF----LVRLLFE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74727668 429 LKTVGvNNPVFLLDEVDKLGKSLQgdpaAALLEVLDpeqnhnfTDHYLNVAFDLSQVLFIATANTTATIPAALLDRMEII 508
Cdd:cd00009 79 LAEKA-KPGVLFIDEIDSLSRGAQ----NALLRVLE-------TLNDLRIDRENVRVIGATNRPLLGDLDRALYDRLDIR 146
|
....*
gi 74727668 509 QVPGY 513
Cdd:cd00009 147 IVIPL 151
|
|
| MoxR |
COG0714 |
MoxR-like ATPase [General function prediction only]; MoxR-like ATPase is part of the Pathway ... |
366-570 |
7.08e-10 |
|
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: 60.95 E-value: 7.08e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74727668 366 LKGPILcFVGPPGVGKTSVGRSVAKTLGREFHRIalggvcdQsdirghrrTYVGSMPGRIInglktvGVNN--------- 436
Cdd:COG0714 30 AGGHLL-LEGVPGVGKTTLAKALARALGLPFIRI-------Q--------FTPDLLPSDIL------GTYIydqqtgefe 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74727668 437 ----PVF----LLDEVDKlgkslqGDPA--AALLEVLdpeQNHNFT-DhylNVAFDLSQVLF-IATANT-----TATIPA 499
Cdd:COG0714 88 frpgPLFanvlLADEINR------APPKtqSALLEAM---EERQVTiP---GGTYKLPEPFLvIATQNPieqegTYPLPE 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74727668 500 ALLDRMEI-IQVpGY-TQEEKIEIAHRHLIPKQLE-QHGLTPQQI-----QIPQVTTLDIITRY-------TREAGvrsl 564
Cdd:COG0714 156 AQLDRFLLkLYI-GYpDAEEEREILRRHTGRHLAEvEPVLSPEELlalqeLVRQVHVSEAVLDYivdlvraTREHP---- 230
|
....*.
gi 74727668 565 DRKLGA 570
Cdd:COG0714 231 DLRKGP 236
|
|
| AAA_5 |
pfam07728 |
AAA domain (dynein-related subfamily); This Pfam entry includes some of the AAA proteins not ... |
371-505 |
8.39e-08 |
|
AAA domain (dynein-related subfamily); This Pfam entry includes some of the AAA proteins not detected by the pfam00004 model.
Pssm-ID: 400191 [Multi-domain] Cd Length: 135 Bit Score: 51.91 E-value: 8.39e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74727668 371 LCFVGPPGVGKTSVGRSVAK-TLGREFHRIALGGVCDQSDIRGHRRtyVGSMPGRIING-LKTVGVNNPVFLLDEVDKLG 448
Cdd:pfam07728 2 VLLVGPPGTGKTELAERLAAaLSNRPVFYVQLTRDTTEEDLFGRRN--IDPGGASWVDGpLVRAAREGEIAVLDEINRAN 79
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 74727668 449 KSLQGdpaaALLEVLDPEQNHNFTDHYLnVAFDLSQVLFIATANT----TATIPAALLDRM 505
Cdd:pfam07728 80 PDVLN----SLLSLLDERRLLLPDGGEL-VKAAPDGFRLIATMNPldrgLNELSPALRSRF 135
|
|
| COG1223 |
COG1223 |
Predicted ATPase, AAA+ superfamily [General function prediction only]; |
341-526 |
2.35e-07 |
|
Predicted ATPase, AAA+ superfamily [General function prediction only];
Pssm-ID: 440836 [Multi-domain] Cd Length: 246 Bit Score: 52.96 E-value: 2.35e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74727668 341 NDHYAMEKLK---KRVLEYLAVRQL--KNNLKGP--ILcFVGPPGVGKTSVGRSVAKTLGREFHRIALGGVCDQsdirgh 413
Cdd:COG1223 2 DDVVGQEEAKkklKLIIKELRRRENlrKFGLWPPrkIL-FYGPPGTGKTMLAEALAGELKLPLLTVRLDSLIGS------ 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74727668 414 rrtYVGSMPGRI------INGLKTvgvnnpVFLLDEVDKLGK-----SLQGDPAA---ALLEVLDPEQNHnftdhylnva 479
Cdd:COG1223 75 ---YLGETARNLrklfdfARRAPC------VIFFDEFDAIAKdrgdqNDVGEVKRvvnALLQELDGLPSG---------- 135
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 74727668 480 fdlsqVLFIATANTTATIPAALLDRM-EIIQVPGYTQEEKIEIAHRHL 526
Cdd:COG1223 136 -----SVVIAATNHPELLDSALWRRFdEVIEFPLPDKEERKEILELNL 178
|
|
| aroK |
PRK00131 |
shikimate kinase; Reviewed |
366-396 |
2.63e-06 |
|
shikimate kinase; Reviewed
Pssm-ID: 234654 [Multi-domain] Cd Length: 175 Bit Score: 48.65 E-value: 2.63e-06
10 20 30
....*....|....*....|....*....|.
gi 74727668 366 LKGPILCFVGPPGVGKTSVGRSVAKTLGREF 396
Cdd:PRK00131 2 LKGPNIVLIGFMGAGKSTIGRLLAKRLGYDF 32
|
|
| 44 |
PHA02544 |
clamp loader, small subunit; Provisional |
369-522 |
1.44e-05 |
|
clamp loader, small subunit; Provisional
Pssm-ID: 222866 [Multi-domain] Cd Length: 316 Bit Score: 48.06 E-value: 1.44e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74727668 369 PILCFVGP-PGVGKTSVGRSVAKTLGREFHRIAlGGVCDQSDIRGHRRTYVGSMpgriinglkTVGVNNPVFLLDEVDKL 447
Cdd:PHA02544 43 PNMLLHSPsPGTGKTTVAKALCNEVGAEVLFVN-GSDCRIDFVRNRLTRFASTV---------SLTGGGKVIIIDEFDRL 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74727668 448 G-----KSLQGdpaaaLLEvldpeqnhnftdhylnvAFDlSQVLFIATANTTATIPAALLDRMEIIQVPGYTQEEKIEIA 522
Cdd:PHA02544 113 GladaqRHLRS-----FME-----------------AYS-KNCSFIITANNKNGIIEPLRSRCRVIDFGVPTKEEQIEMM 169
|
|
| PRK13342 |
PRK13342 |
recombination factor protein RarA; Reviewed |
373-524 |
1.55e-05 |
|
recombination factor protein RarA; Reviewed
Pssm-ID: 237355 [Multi-domain] Cd Length: 413 Bit Score: 48.16 E-value: 1.55e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74727668 373 FVGPPGVGKTSVGRSVAKTLGREFHRI--ALGGVcdqSDIRghrrtyvgsmpgRIINGLKT--VGVNNPVFLLDEVDKLG 448
Cdd:PRK13342 41 LWGPPGTGKTTLARIIAGATDAPFEALsaVTSGV---KDLR------------EVIEEARQrrSAGRRTILFIDEIHRFN 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74727668 449 KSLQgDpaaALLEVLdpEQNHnftdhylnvafdlsqVLFIATanTTA----TIPAALLDRMEIIQVPGYTQEEKIEIAHR 524
Cdd:PRK13342 106 KAQQ-D---ALLPHV--EDGT---------------ITLIGA--TTEnpsfEVNPALLSRAQVFELKPLSEEDIEQLLKR 162
|
|
| AAA_2 |
pfam07724 |
AAA domain (Cdc48 subfamily); This Pfam entry includes some of the AAA proteins not detected ... |
373-528 |
1.81e-05 |
|
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: 46.03 E-value: 1.81e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74727668 373 FVGPPGVGKTSVGRSVAKTLG---REFHRIalggvcDQSDIrgHRRTYV----GSMPGRII---NGLKTVGVN-NP--VF 439
Cdd:pfam07724 8 FLGPTGVGKTELAKALAELLFgdeRALIRI------DMSEY--MEEHSVsrliGAPPGYVGyeeGGQLTEAVRrKPysIV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74727668 440 LLDEVDKLGKSLQGDpaaaLLEVLDpeqNHNFTDHY-LNVAFDlsQVLFIATANTTATIPaalLDRMEIIQVPGY--TQE 516
Cdd:pfam07724 80 LIDEIEKAHPGVQND----LLQILE---GGTLTDKQgRTVDFK--NTLFIMTGNFGSEKI---SDASRLGDSPDYelLKE 147
|
170
....*....|..
gi 74727668 517 EKIEIAHRHLIP 528
Cdd:pfam07724 148 EVMDLLKKGFIP 159
|
|
| RecA-like_ClpB_Hsp104-like |
cd19499 |
Chaperone protein ClpB/Hsp104 subfamily; Bacterial Caseinolytic peptidase B (ClpB) and ... |
358-508 |
1.94e-05 |
|
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: 46.02 E-value: 1.94e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74727668 358 AVRQLKNNLKGP-----ILCFVGPPGVGKTSVGRSVAKTL-GREFHRIALggvcDQS-DIRGHRRTYVGSMPGRIIngLK 430
Cdd:cd19499 26 AIRRARAGLSDPnrpigSFLFLGPTGVGKTELAKALAELLfGDEDNLIRI----DMSeYMEKHSVSRLIGAPPGYV--GY 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74727668 431 TVG-------VNNP--VFLLDEVDKLGKSLQGdpaaALLEVLDpeqNHNFTDHYLNVAfDLSQVLFIATANttaTIPAAL 501
Cdd:cd19499 100 TEGgqlteavRRKPysVVLLDEIEKAHPDVQN----LLLQVLD---DGRLTDSHGRTV-DFKNTIIIMTSN---HFRPEF 168
|
....*..
gi 74727668 502 LDRMEII 508
Cdd:cd19499 169 LNRIDEI 175
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
367-505 |
3.39e-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: 44.67 E-value: 3.39e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74727668 367 KGPILCFVGPPGVGKTSVGRSVAKTLGREFHRI-------ALGGVCDQSDIRGHRRTYVGSMPGRIINGLKTV--GVNNP 437
Cdd:smart00382 1 PGEVILIVGPPGSGKTTLARALARELGPPGGGViyidgedILEEVLDQLLLIIVGGKKASGSGELRLRLALALarKLKPD 80
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 74727668 438 VFLLDEVDKLGKSLQgdpaAALLEVLDPEQNHNFTDHYLNvafdlsqVLFIATANTTATIPAALLDRM 505
Cdd:smart00382 81 VLILDEITSLLDAEQ----EALLLLLEELRLLLLLKSEKN-------LTVILTTNDEKDLGPALLRRR 137
|
|
| SdrC |
COG3480 |
Predicted secreted protein YlbL, contains PDZ domain [Signal transduction mechanisms]; |
741-833 |
5.65e-05 |
|
Predicted secreted protein YlbL, contains PDZ domain [Signal transduction mechanisms];
Pssm-ID: 442703 [Multi-domain] Cd Length: 344 Bit Score: 46.34 E-value: 5.65e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74727668 741 GPSAGvTIVTcLA--------SLFSGRlvrsDVAMTGEITLRGLVLPVGGIKDKVLAAHRAGLKQVIIPRRNEKDLEgip 812
Cdd:COG3480 240 GPSAG-LMFA-LGiydqltpgDLTGGK----KIAGTGTIDADGTVGPIGGIDQKVVAARRAGATIFLAPASNCAEAV--- 310
|
90 100
....*....|....*....|.
gi 74727668 813 GNVRQDLSFVTASCLDEVLNA 833
Cdd:COG3480 311 GTIPTGLKVVPVDTLDDALDA 331
|
|
| LonB |
COG1067 |
Predicted ATP-dependent protease [Posttranslational modification, protein turnover, chaperones] ... |
740-843 |
6.21e-05 |
|
Predicted ATP-dependent protease [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440686 [Multi-domain] Cd Length: 742 Bit Score: 46.86 E-value: 6.21e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74727668 740 DGPSAGVTIVTCLASLFSGRLVRSDVAMTGEITLRGLVLPVGGIKDKV-----LAAHRaGL--KQ-VIIPRRNEKDLegi 811
Cdd:COG1067 592 DGDSASSAELYALLSALSGVPIRQDIAVTGSVNQHGEVQPIGGVNEKIegffdVCKAR-GLtgKQgVIIPAANVKNL--- 667
|
90 100 110
....*....|....*....|....*....|....*.
gi 74727668 812 pgnvrqdlsfvtasCL-DEVLNAAFDGGF---TVKT 843
Cdd:COG1067 668 --------------MLrDEVVEAVKAGQFhiyAVEH 689
|
|
| AroK |
COG0703 |
Shikimate kinase [Amino acid transport and metabolism]; Shikimate kinase is part of the ... |
371-397 |
7.76e-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: 7.76e-05
10 20
....*....|....*....|....*..
gi 74727668 371 LCFVGPPGVGKTSVGRSVAKTLGREFH 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 |
1.06e-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: 43.31 E-value: 1.06e-04
10 20
....*....|....*....|...
gi 74727668 374 VGPPGVGKTSVGRSVAKTLGREF 396
Cdd:cd00464 5 IGMMGAGKTTVGRLLAKALGLPF 27
|
|
| FlhF |
COG1419 |
Flagellar biosynthesis GTPase FlhF [Cell motility]; |
292-390 |
1.40e-04 |
|
Flagellar biosynthesis GTPase FlhF [Cell motility];
Pssm-ID: 441029 [Multi-domain] Cd Length: 361 Bit Score: 44.86 E-value: 1.40e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74727668 292 KEIKRLKKMPQSMpeyaLTRNYLELMVELPWNKSTTDRL-----DIRAARILLDN--DHYAMEKLKKRVLEYLAvRQLKN 364
Cdd:COG1419 81 RELAELKELLEEQ----LSGLAGESARLPPELAELLERLleagvSPELARELLEKlpEDLSAEEAWRALLEALA-RRLPV 155
|
90 100 110
....*....|....*....|....*....|.
gi 74727668 365 NL-----KGPILCFVGPPGVGKTSvgrSVAK 390
Cdd:COG1419 156 AEdplldEGGVIALVGPTGVGKTT---TIAK 183
|
|
| RarA |
COG2256 |
Replication-associated recombination protein RarA (DNA-dependent ATPase) [Replication, ... |
375-411 |
2.44e-04 |
|
Replication-associated recombination protein RarA (DNA-dependent ATPase) [Replication, recombination and repair];
Pssm-ID: 441857 [Multi-domain] Cd Length: 439 Bit Score: 44.28 E-value: 2.44e-04
10 20 30
....*....|....*....|....*....|....*....
gi 74727668 375 GPPGVGKTSVGRSVAKTLGREFHRI--ALGGVcdqSDIR 411
Cdd:COG2256 56 GPPGTGKTTLARLIANATDAEFVALsaVTSGV---KDIR 91
|
|
| clpA |
PRK11034 |
ATP-dependent Clp protease ATP-binding subunit; Provisional |
373-492 |
6.28e-04 |
|
ATP-dependent Clp protease ATP-binding subunit; Provisional
Pssm-ID: 236828 [Multi-domain] Cd Length: 758 Bit Score: 43.29 E-value: 6.28e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74727668 373 FVGPPGVGKTSVGRSVAKTLGREFHRIalggvcDQSDIrGHRRT---YVGSMPGRI---INGLKTVGV-NNP--VFLLDE 443
Cdd:PRK11034 493 FAGPTGVGKTEVTVQLSKALGIELLRF------DMSEY-MERHTvsrLIGAPPGYVgfdQGGLLTDAViKHPhaVLLLDE 565
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 74727668 444 VDKlgksLQGDPAAALLEVLDpeqNHNFTDHYLNVAfDLSQVLFIATAN 492
Cdd:PRK11034 566 IEK----AHPDVFNLLLQVMD---NGTLTDNNGRKA-DFRNVVLVMTTN 606
|
|
| AAA_3 |
pfam07726 |
ATPase family associated with various cellular activities (AAA); This Pfam entry includes some ... |
375-504 |
2.71e-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: 38.69 E-value: 2.71e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74727668 375 GPPGVGKTSVGRSVAKTLGREFHRIALGGVCDQSDIRG------HRRTYVgSMPGriinglktvgvnnPVF----LLDEV 444
Cdd:pfam07726 6 GVPGLAKTLLVRTLARSLGLDFRRIQFTPDLLPSDITGtevfdqKTREFE-FRPG-------------PVFanvlLADEI 71
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 74727668 445 DKLGKSLQgdpaAALLEVLdpeQNHNFTdhYLNVAFDLSQVLF-IATANT-----TATIPAALLDR 504
Cdd:pfam07726 72 NRAPPKTQ----SALLEAM---QERQVT--IDGETHPLPEPFFvLATQNPieqegTYPLPEAQLDR 128
|
|
| Kti12 |
COG4088 |
tRNA uridine 5-carbamoylmethylation protein Kti12 (Killer toxin insensitivity protein) ... |
366-413 |
4.70e-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: 4.70e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*...
gi 74727668 366 LKGPILCFVGPPGVGKTSVGRSVAKTLGREFHRIAlggVCDQSDIRGH 413
Cdd:COG4088 2 DSPMLLILTGPPGSGKTTFAKALAQRLYAEGIAVA---LLHSDDFRRF 46
|
|
| |
