|
Name |
Accession |
Description |
Interval |
E-value |
| Lon |
COG0466 |
ATP-dependent Lon protease, bacterial type [Posttranslational modification, protein turnover, ... |
11-838 |
0e+00 |
|
ATP-dependent Lon protease, bacterial type [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 223542 [Multi-domain] Cd Length: 782 Bit Score: 846.07 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1128611449 11 SRLPLLLTHEGVLLPGSTMRTSVDSARNLQLVRSRLLKGTSLqstILGVIPNTPDPASDAQDlpPLHRIGTAALAVQVVg 90
Cdd:COG0466 8 IELPVLPLRDVVVFPGMVIPLFVGREKSIKALEEAMKNDQKY---ILLVTQKDASTDEPTED--DLYEVGTLAKILQIL- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1128611449 91 sNWPKPHYTLLITGLCRFQIVQVLKEKPYPIAEVEQLDRLEEFPNTcKMREELGELSEQFYKYA--------VQLVEMLD 162
Cdd:COG0466 82 -KLPDGTVKVLVEGLQRVRISKLSDEEEFFEAEIELLPDEPIDEER-EIEALVRSILSEFEEYAklnkkippEELQSLNS 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1128611449 163 MSVPavaklrrlldslprEALPDILTSIIRTSNKEKLQILDAVSLEERFKMTIPLLVRQIEGLKLLQK-TRKPKQDDDKR 241
Cdd:COG0466 160 IDDP--------------GKLADTIAAHLPLKLEEKQEILETLDVKERLEKLLDLLEKEIDLLQLEKRiRKKVKEQMEKS 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1128611449 242 VIA------IRPIRRithisgtlEDEDEDEDNDDIVMLEKKIRTSSMPEQAHKVCVKEIKRLKKMPQSMPEYALTRNYLE 315
Cdd:COG0466 226 QREyylreqLKAIQK--------ELGEDDDDKDEVEELREKIEKLKLPKEAKEKAEKELKKLETMSPMSAEATVIRNYLD 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1128611449 316 LMVELPWNKSTTDRLDIRAARILLDNDHYAMEKLKKRVLEYLAVRQLKNNLKGPILCFVGPPGVGKTSVGRSVAKTLGRE 395
Cdd:COG0466 298 WLLDLPWGKRSKDKLDLKKAEKILDKDHYGLEKVKERILEYLAVQKLTKKLKGPILCLVGPPGVGKTSLGKSIAKALGRK 377
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1128611449 396 FHRIALGGVCDQSDIRGHRRTYVGSMPGRIINGLKTVGVNNPVFLLDEVDKLGKSLQGDPAAALLEVLDPEQNHNFTDHY 475
Cdd:COG0466 378 FVRISLGGVRDEAEIRGHRRTYIGAMPGKIIQGMKKAGVKNPVFLLDEIDKMGSSFRGDPASALLEVLDPEQNNTFSDHY 457
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1128611449 476 LNVAFDLSQVLFIATANTTATIPAALLDRMEIIQVPGYTQEEKIEIAHRHLIPKQLEQHGLTPQQIQIPQVTTLDIITRY 555
Cdd:COG0466 458 LEVPYDLSKVMFIATANSLDTIPAPLLDRMEVIRLSGYTEDEKLEIAKRHLIPKQLKEHGLKKGELTITDEAIKDIIRYY 537
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1128611449 556 TREAGVRSLDRKLGAICRAVAVKvaegqhkeakldrsdvteregcrehILEDEKPESISdttdlalppempilIDFHALK 635
Cdd:COG0466 538 TREAGVRNLEREIAKICRKAAKK-------------------------ILLKKEKSIVK--------------IDEKNLK 578
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1128611449 636 DILGPPMYEMEVSQRLSQPGVAIGLAWTPLGGEIMFVEASRMDGEGQLTLTGQLGDVMKESAHLAISWLRSNAKKYqltn 715
Cdd:COG0466 579 KYLGVPVFRYGKAEEEDQVGVVTGLAWTEVGGDLLTIEAVKMPGKGKLTLTGSLGDVMKESAQAALSYVRSRAEKL---- 654
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1128611449 716 aFGSFDLLDNTDIHLHFPAGAVTKDGPSAGVTIVTCLASLFSGRLVRSDVAMTGEITLRGLVLPVGGIKDKVLAAHRAGL 795
Cdd:COG0466 655 -GIDPDFFEKRDIHIHVPEGATPKDGPSAGITMATALVSLLTGKPVRADVAMTGEITLRGRVLPIGGLKEKLLAAHRGGI 733
|
810 820 830 840
....*....|....*....|....*....|....*....|...
gi 1128611449 796 KQVIIPRRNEKDLEGIPGNVRQDLSFVTASCLDEVLNAAFDGG 838
Cdd:COG0466 734 KTVIIPKDNERDLEEIPDNVKEGLEIHPVKTIDEVLKLALVGN 776
|
|
| 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: 812.30 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1128611449 14 PLLLTHEGVLLPGSTMRTSVDSARNLQLVRsrllKGTSLQSTILGVIPNTPDPaSDAQDLPPLHRIGTAALAVQVVGS-N 92
Cdd:TIGR00763 1 PLLPLRRRPLFPGMIKPIDVGREKSIKLIK----EALRLKQPYLGLFLQKDDD-NEEPEEDDIYSVGVVAQILEMLPLpS 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1128611449 93 WPKPHYTLLITGLCRFQIVQVLKEKPYPIAEVeqlDRLEEFPNTcKMREELGELSEQFYKYAVQLVEMLDMSVPAVAKLR 172
Cdd:TIGR00763 76 SGTATYKVVVEGLRRIRIKELSDKGGYLVVRV---DNLKEEPFD-KDDEEIKALTREIKETFRELISLSKLFREQPALLS 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1128611449 173 RLLDSLPREALPDILTSIIRTSNKEKLQ-ILDAVSLEERFKMTIPLLVRQIEGLKLLQK-TRKPKQ---DDDKRVIAIRP 247
Cdd:TIGR00763 152 ALEDIDEPGRLADFVAASLQLKEKDELQeVLETVNIEKRLKKALELLKKELELLKLQNKiTKKVEEkmeKTQREYYLREQ 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1128611449 248 IRRITHISGTlededEDEDNDDIVMLEKKIRTSSMPEQAHKVCVKEIKRLKKMPQSMPEYALTRNYLELMVELPWNKSTT 327
Cdd:TIGR00763 232 LKAIKKELGI-----EKDDKDELEKLKEKLEELKLPEEVKKVIEKELTKLSLLEPSSSEFTVTRNYLDWLTDLPWGKYSK 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1128611449 328 DRLDIRAARILLDNDHYAMEKLKKRVLEYLAVRQLKNNLKGPILCFVGPPGVGKTSVGRSVAKTLGREFHRIALGGVCDQ 407
Cdd:TIGR00763 307 ENLDLKRAKEILDEDHYGLKKVKERILEYLAVQKLRGKMKGPILCLVGPPGVGKTSLGKSIAKALNRKFVRFSLGGVRDE 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1128611449 408 SDIRGHRRTYVGSMPGRIINGLKTVGVNNPVFLLDEVDKLGKSLQGDPAAALLEVLDPEQNHNFTDHYLNVAFDLSQVLF 487
Cdd:TIGR00763 387 AEIRGHRRTYVGAMPGRIIQGLKKAKTKNPLFLLDEIDKIGSSFRGDPASALLEVLDPEQNNAFSDHYLDVPFDLSKVIF 466
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1128611449 488 IATANTTATIPAALLDRMEIIQVPGYTQEEKIEIAHRHLIPKQLEQHGLTPQQIQIPQVTTLDIITRYTREAGVRSLDRK 567
Cdd:TIGR00763 467 IATANSIDTIPRPLLDRMEVIELSGYTEEEKLEIAKKYLIPKALEDHGLKPDELKITDEALLLLIKYYTREAGVRNLERQ 546
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1128611449 568 LGAICRAVAVKVAEGQHKEAkldrsdvteregcrehiledEKPESISDTTDLalppempilidfhaLKDILGPPMYEMEV 647
Cdd:TIGR00763 547 IEKICRKAAVKLVEQGEKKK--------------------SEAESVVITPDN--------------LKKYLGKPVFTYER 592
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1128611449 648 SQRLSQPGVAIGLAWTPLGGEIMFVEASRMDGEGQLTLTGQLGDVMKESAHLAISWLRSNAKKYQLTNafgsfDLLDNTD 727
Cdd:TIGR00763 593 AYEVTPPGVVMGLAWTPMGGDTLFIETTKVAGKGSLELTGQLGDVMKESAQIALTYVRSIAADLGISP-----NFFEKAD 667
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1128611449 728 IHLHFPAGAVTKDGPSAGVTIVTCLASLFSGRLVRSDVAMTGEITLRGLVLPVGGIKDKVLAAHRAGLKQVIIPRRNEKD 807
Cdd:TIGR00763 668 IHLHVPEGATPKDGPSAGITMATALLSLATGKPVRPDVAMTGEITLRGKVLPIGGLKEKTIAAKRAGIKTIILPEKNRRD 747
|
810 820
....*....|....*....|....*...
gi 1128611449 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: 543.76 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1128611449 65 DPASDAQDLPPLHRIGTAALAVQVVgsNWPKPHYTLLITGLCRFQIVQVLKEKPYPIAEVEQLD--RLEEFPNTCKMREE 142
Cdd:PRK10787 57 EASTDEPGVNDLFTVGTVASILQML--KLPDGTVKVLVEGLQRARISALSDNGEHFSAKAEYLEspTIDEREQEVLVRTA 134
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1128611449 143 LGELsEQFYKYAVQLVEMLDMSVPAVAKLRRLLDSLPREaLPDILtsiirtsnKEKLQILDAVSLEERFKMTIPLLVRQI 222
Cdd:PRK10787 135 ISQF-EGYIKLNKKIPPEVLTSLNSIDDPARLADTIAAH-MPLKL--------ADKQSVLEMSDVNERLEYLMAMMESEI 204
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1128611449 223 EGLKLLQKTR---KPKQDDDKRVIAI-RPIRRITHISGTLEDEDEDEDNddivmLEKKIRTSSMPEQAHKVCVKEIKRLK 298
Cdd:PRK10787 205 DLLQVEKRIRnrvKKQMEKSQREYYLnEQMKAIQKELGEMDDAPDENEA-----LKRKIDAAKMPKEAKEKAEAELQKLK 279
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1128611449 299 KMPQSMPEYALTRNYLELMVELPWNKSTTDRLDIRAARILLDNDHYAMEKLKKRVLEYLAVRQLKNNLKGPILCFVGPPG 378
Cdd:PRK10787 280 MMSPMSAEATVVRGYIDWMVQVPWNARSKVKKDLRQAQEILDTDHYGLERVKDRILEYLAVQSRVNKIKGPILCLVGPPG 359
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1128611449 379 VGKTSVGRSVAKTLGREFHRIALGGVCDQSDIRGHRRTYVGSMPGRIINGLKTVGVNNPVFLLDEVDKLGKSLQGDPAAA 458
Cdd:PRK10787 360 VGKTSLGQSIAKATGRKYVRMALGGVRDEAEIRGHRRTYIGSMPGKLIQKMAKVGVKNPLFLLDEIDKMSSDMRGDPASA 439
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1128611449 459 LLEVLDPEQNHNFTDHYLNVAFDLSQVLFIATANTTaTIPAALLDRMEIIQVPGYTQEEKIEIAHRHLIPKQLEQHGLTP 538
Cdd:PRK10787 440 LLEVLDPEQNVAFSDHYLEVDYDLSDVMFVATSNSM-NIPAPLLDRMEVIRLSGYTEDEKLNIAKRHLLPKQIERNALKK 518
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1128611449 539 QQIQIPQVTTLDIITRYTREAGVRSLDRKLGAICRAvAVKVaegqhkeakldrsdvteregcrehILEDEKPESisdttd 618
Cdd:PRK10787 519 GELTVDDSAIIGIIRYYTREAGVRSLEREISKLCRK-AVKQ------------------------LLLDKSLKH------ 567
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1128611449 619 lalppempILIDFHALKDILGPPMYEMEVSQRLSQPGVAIGLAWTPLGGEIMFVEASRMDGEGQLTLTGQLGDVMKESAH 698
Cdd:PRK10787 568 --------IEINGDNLHDYLGVQRFDYGRADNENRVGQVTGLAWTEVGGDLLTIETACVPGKGKLTYTGSLGEVMQESIQ 639
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1128611449 699 LAISWLRSNAKKYQLTNAFgsfdlLDNTDIHLHFPAGAVTKDGPSAGVTIVTCLASLFSGRLVRSDVAMTGEITLRGLVL 778
Cdd:PRK10787 640 AALTVVRARAEKLGINPDF-----YEKRDIHVHVPEGATPKDGPSAGIAMCTALVSCLTGNPVRADVAMTGEITLRGQVL 714
|
730 740 750 760 770
....*....|....*....|....*....|....*....|....*....|....*..
gi 1128611449 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 |
2.66e-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: 364.96 E-value: 2.66e-121
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1128611449 332 IRAARILLDNDHYAMEKLKKRVLEYLAVRQLKNNLKGPILCFVGPPGVGKTSVGRSVAKTLGREFHRIALGGVCDQSDIR 411
Cdd:cd19500 1 IKKARKVLDADHYGLEDVKERILEYLAVRKLKGSMKGPILCLVGPPGVGKTSLGKSIARALGRKFVRISLGGVRDEAEIR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1128611449 412 GHRRTYVGSMPGRIINGLKTVGVNNPVFLLDEVDKLGKSLQGDPAAALLEVLDPEQNHNFTDHYLNVAFDLSQVLFIATA 491
Cdd:cd19500 81 GHRRTYVGAMPGRIIQALKKAGTNNPVFLLDEIDKIGSSFRGDPASALLEVLDPEQNSTFSDHYLDVPFDLSKVLFIATA 160
|
170 180
....*....|....*....|..
gi 1128611449 492 NTTATIPAALLDRMEIIQVPGY 513
Cdd:cd19500 161 NSLDTIPGPLLDRMEIIELSGY 182
|
|
| Lon_C |
pfam05362 |
Lon protease (S16) C-terminal proteolytic domain; The Lon serine proteases must hydrolyze ATP ... |
634-837 |
4.83e-94 |
|
Lon protease (S16) C-terminal proteolytic domain; The Lon serine proteases must hydrolyze 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: 294.53 E-value: 4.83e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1128611449 634 LKDILGPPMYEMEVSQRLSQPGVAIGLAWTPLGGEIMFVEASRMDGEGQLTLTGQLGDVMKESAHLAISWLRSNAKKYQL 713
Cdd:pfam05362 7 LEKYLGVPRFRYGEAEKEDQVGVVTGLAWTEVGGDLLTIEAVIMPGKGKLTLTGQLGDVMKESAQAALSYVRSRAEELGI 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1128611449 714 tnafgSFDLLDNTDIHLHFPAGAVTKDGPSAGVTIVTCLASLFSGRLVRSDVAMTGEITLRGLVLPVGGIKDKVLAAHRA 793
Cdd:pfam05362 87 -----DPDFFEKKDIHIHVPEGATPKDGPSAGVTMATALVSALTGIPVRKDVAMTGEITLRGRVLPIGGLKEKLLAAHRA 161
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1128611449 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 |
1.78e-05 |
|
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a variety of cellular activities. This profile/alignment only detects a fraction of this vast family. The poorly conserved N-terminal helix is missing from the alignment.
Pssm-ID: 214640 [Multi-domain] Cd Length: 148 Bit Score: 45.44 E-value: 1.78e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1128611449 367 KGPILCFVGPPGVGKTSVGRSVAKTLGREFHRI-------ALGGVCDQSDIRGHRRTYVGSMPGRIINGLKTV--GVNNP 437
Cdd:smart00382 1 PGEVILIVGPPGSGKTTLARALARELGPPGGGViyidgedILEEVLDQLLLIIVGGKKASGSGELRLRLALALarKLKPD 80
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1128611449 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, ... |
11-838 |
0e+00 |
|
ATP-dependent Lon protease, bacterial type [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 223542 [Multi-domain] Cd Length: 782 Bit Score: 846.07 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1128611449 11 SRLPLLLTHEGVLLPGSTMRTSVDSARNLQLVRSRLLKGTSLqstILGVIPNTPDPASDAQDlpPLHRIGTAALAVQVVg 90
Cdd:COG0466 8 IELPVLPLRDVVVFPGMVIPLFVGREKSIKALEEAMKNDQKY---ILLVTQKDASTDEPTED--DLYEVGTLAKILQIL- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1128611449 91 sNWPKPHYTLLITGLCRFQIVQVLKEKPYPIAEVEQLDRLEEFPNTcKMREELGELSEQFYKYA--------VQLVEMLD 162
Cdd:COG0466 82 -KLPDGTVKVLVEGLQRVRISKLSDEEEFFEAEIELLPDEPIDEER-EIEALVRSILSEFEEYAklnkkippEELQSLNS 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1128611449 163 MSVPavaklrrlldslprEALPDILTSIIRTSNKEKLQILDAVSLEERFKMTIPLLVRQIEGLKLLQK-TRKPKQDDDKR 241
Cdd:COG0466 160 IDDP--------------GKLADTIAAHLPLKLEEKQEILETLDVKERLEKLLDLLEKEIDLLQLEKRiRKKVKEQMEKS 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1128611449 242 VIA------IRPIRRithisgtlEDEDEDEDNDDIVMLEKKIRTSSMPEQAHKVCVKEIKRLKKMPQSMPEYALTRNYLE 315
Cdd:COG0466 226 QREyylreqLKAIQK--------ELGEDDDDKDEVEELREKIEKLKLPKEAKEKAEKELKKLETMSPMSAEATVIRNYLD 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1128611449 316 LMVELPWNKSTTDRLDIRAARILLDNDHYAMEKLKKRVLEYLAVRQLKNNLKGPILCFVGPPGVGKTSVGRSVAKTLGRE 395
Cdd:COG0466 298 WLLDLPWGKRSKDKLDLKKAEKILDKDHYGLEKVKERILEYLAVQKLTKKLKGPILCLVGPPGVGKTSLGKSIAKALGRK 377
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1128611449 396 FHRIALGGVCDQSDIRGHRRTYVGSMPGRIINGLKTVGVNNPVFLLDEVDKLGKSLQGDPAAALLEVLDPEQNHNFTDHY 475
Cdd:COG0466 378 FVRISLGGVRDEAEIRGHRRTYIGAMPGKIIQGMKKAGVKNPVFLLDEIDKMGSSFRGDPASALLEVLDPEQNNTFSDHY 457
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1128611449 476 LNVAFDLSQVLFIATANTTATIPAALLDRMEIIQVPGYTQEEKIEIAHRHLIPKQLEQHGLTPQQIQIPQVTTLDIITRY 555
Cdd:COG0466 458 LEVPYDLSKVMFIATANSLDTIPAPLLDRMEVIRLSGYTEDEKLEIAKRHLIPKQLKEHGLKKGELTITDEAIKDIIRYY 537
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1128611449 556 TREAGVRSLDRKLGAICRAVAVKvaegqhkeakldrsdvteregcrehILEDEKPESISdttdlalppempilIDFHALK 635
Cdd:COG0466 538 TREAGVRNLEREIAKICRKAAKK-------------------------ILLKKEKSIVK--------------IDEKNLK 578
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1128611449 636 DILGPPMYEMEVSQRLSQPGVAIGLAWTPLGGEIMFVEASRMDGEGQLTLTGQLGDVMKESAHLAISWLRSNAKKYqltn 715
Cdd:COG0466 579 KYLGVPVFRYGKAEEEDQVGVVTGLAWTEVGGDLLTIEAVKMPGKGKLTLTGSLGDVMKESAQAALSYVRSRAEKL---- 654
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1128611449 716 aFGSFDLLDNTDIHLHFPAGAVTKDGPSAGVTIVTCLASLFSGRLVRSDVAMTGEITLRGLVLPVGGIKDKVLAAHRAGL 795
Cdd:COG0466 655 -GIDPDFFEKRDIHIHVPEGATPKDGPSAGITMATALVSLLTGKPVRADVAMTGEITLRGRVLPIGGLKEKLLAAHRGGI 733
|
810 820 830 840
....*....|....*....|....*....|....*....|...
gi 1128611449 796 KQVIIPRRNEKDLEGIPGNVRQDLSFVTASCLDEVLNAAFDGG 838
Cdd:COG0466 734 KTVIIPKDNERDLEEIPDNVKEGLEIHPVKTIDEVLKLALVGN 776
|
|
| 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: 812.30 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1128611449 14 PLLLTHEGVLLPGSTMRTSVDSARNLQLVRsrllKGTSLQSTILGVIPNTPDPaSDAQDLPPLHRIGTAALAVQVVGS-N 92
Cdd:TIGR00763 1 PLLPLRRRPLFPGMIKPIDVGREKSIKLIK----EALRLKQPYLGLFLQKDDD-NEEPEEDDIYSVGVVAQILEMLPLpS 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1128611449 93 WPKPHYTLLITGLCRFQIVQVLKEKPYPIAEVeqlDRLEEFPNTcKMREELGELSEQFYKYAVQLVEMLDMSVPAVAKLR 172
Cdd:TIGR00763 76 SGTATYKVVVEGLRRIRIKELSDKGGYLVVRV---DNLKEEPFD-KDDEEIKALTREIKETFRELISLSKLFREQPALLS 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1128611449 173 RLLDSLPREALPDILTSIIRTSNKEKLQ-ILDAVSLEERFKMTIPLLVRQIEGLKLLQK-TRKPKQ---DDDKRVIAIRP 247
Cdd:TIGR00763 152 ALEDIDEPGRLADFVAASLQLKEKDELQeVLETVNIEKRLKKALELLKKELELLKLQNKiTKKVEEkmeKTQREYYLREQ 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1128611449 248 IRRITHISGTlededEDEDNDDIVMLEKKIRTSSMPEQAHKVCVKEIKRLKKMPQSMPEYALTRNYLELMVELPWNKSTT 327
Cdd:TIGR00763 232 LKAIKKELGI-----EKDDKDELEKLKEKLEELKLPEEVKKVIEKELTKLSLLEPSSSEFTVTRNYLDWLTDLPWGKYSK 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1128611449 328 DRLDIRAARILLDNDHYAMEKLKKRVLEYLAVRQLKNNLKGPILCFVGPPGVGKTSVGRSVAKTLGREFHRIALGGVCDQ 407
Cdd:TIGR00763 307 ENLDLKRAKEILDEDHYGLKKVKERILEYLAVQKLRGKMKGPILCLVGPPGVGKTSLGKSIAKALNRKFVRFSLGGVRDE 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1128611449 408 SDIRGHRRTYVGSMPGRIINGLKTVGVNNPVFLLDEVDKLGKSLQGDPAAALLEVLDPEQNHNFTDHYLNVAFDLSQVLF 487
Cdd:TIGR00763 387 AEIRGHRRTYVGAMPGRIIQGLKKAKTKNPLFLLDEIDKIGSSFRGDPASALLEVLDPEQNNAFSDHYLDVPFDLSKVIF 466
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1128611449 488 IATANTTATIPAALLDRMEIIQVPGYTQEEKIEIAHRHLIPKQLEQHGLTPQQIQIPQVTTLDIITRYTREAGVRSLDRK 567
Cdd:TIGR00763 467 IATANSIDTIPRPLLDRMEVIELSGYTEEEKLEIAKKYLIPKALEDHGLKPDELKITDEALLLLIKYYTREAGVRNLERQ 546
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1128611449 568 LGAICRAVAVKVAEGQHKEAkldrsdvteregcrehiledEKPESISDTTDLalppempilidfhaLKDILGPPMYEMEV 647
Cdd:TIGR00763 547 IEKICRKAAVKLVEQGEKKK--------------------SEAESVVITPDN--------------LKKYLGKPVFTYER 592
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1128611449 648 SQRLSQPGVAIGLAWTPLGGEIMFVEASRMDGEGQLTLTGQLGDVMKESAHLAISWLRSNAKKYQLTNafgsfDLLDNTD 727
Cdd:TIGR00763 593 AYEVTPPGVVMGLAWTPMGGDTLFIETTKVAGKGSLELTGQLGDVMKESAQIALTYVRSIAADLGISP-----NFFEKAD 667
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1128611449 728 IHLHFPAGAVTKDGPSAGVTIVTCLASLFSGRLVRSDVAMTGEITLRGLVLPVGGIKDKVLAAHRAGLKQVIIPRRNEKD 807
Cdd:TIGR00763 668 IHLHVPEGATPKDGPSAGITMATALLSLATGKPVRPDVAMTGEITLRGKVLPIGGLKEKTIAAKRAGIKTIILPEKNRRD 747
|
810 820
....*....|....*....|....*...
gi 1128611449 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: 543.76 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1128611449 65 DPASDAQDLPPLHRIGTAALAVQVVgsNWPKPHYTLLITGLCRFQIVQVLKEKPYPIAEVEQLD--RLEEFPNTCKMREE 142
Cdd:PRK10787 57 EASTDEPGVNDLFTVGTVASILQML--KLPDGTVKVLVEGLQRARISALSDNGEHFSAKAEYLEspTIDEREQEVLVRTA 134
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1128611449 143 LGELsEQFYKYAVQLVEMLDMSVPAVAKLRRLLDSLPREaLPDILtsiirtsnKEKLQILDAVSLEERFKMTIPLLVRQI 222
Cdd:PRK10787 135 ISQF-EGYIKLNKKIPPEVLTSLNSIDDPARLADTIAAH-MPLKL--------ADKQSVLEMSDVNERLEYLMAMMESEI 204
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1128611449 223 EGLKLLQKTR---KPKQDDDKRVIAI-RPIRRITHISGTLEDEDEDEDNddivmLEKKIRTSSMPEQAHKVCVKEIKRLK 298
Cdd:PRK10787 205 DLLQVEKRIRnrvKKQMEKSQREYYLnEQMKAIQKELGEMDDAPDENEA-----LKRKIDAAKMPKEAKEKAEAELQKLK 279
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1128611449 299 KMPQSMPEYALTRNYLELMVELPWNKSTTDRLDIRAARILLDNDHYAMEKLKKRVLEYLAVRQLKNNLKGPILCFVGPPG 378
Cdd:PRK10787 280 MMSPMSAEATVVRGYIDWMVQVPWNARSKVKKDLRQAQEILDTDHYGLERVKDRILEYLAVQSRVNKIKGPILCLVGPPG 359
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1128611449 379 VGKTSVGRSVAKTLGREFHRIALGGVCDQSDIRGHRRTYVGSMPGRIINGLKTVGVNNPVFLLDEVDKLGKSLQGDPAAA 458
Cdd:PRK10787 360 VGKTSLGQSIAKATGRKYVRMALGGVRDEAEIRGHRRTYIGSMPGKLIQKMAKVGVKNPLFLLDEIDKMSSDMRGDPASA 439
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1128611449 459 LLEVLDPEQNHNFTDHYLNVAFDLSQVLFIATANTTaTIPAALLDRMEIIQVPGYTQEEKIEIAHRHLIPKQLEQHGLTP 538
Cdd:PRK10787 440 LLEVLDPEQNVAFSDHYLEVDYDLSDVMFVATSNSM-NIPAPLLDRMEVIRLSGYTEDEKLNIAKRHLLPKQIERNALKK 518
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1128611449 539 QQIQIPQVTTLDIITRYTREAGVRSLDRKLGAICRAvAVKVaegqhkeakldrsdvteregcrehILEDEKPESisdttd 618
Cdd:PRK10787 519 GELTVDDSAIIGIIRYYTREAGVRSLEREISKLCRK-AVKQ------------------------LLLDKSLKH------ 567
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1128611449 619 lalppempILIDFHALKDILGPPMYEMEVSQRLSQPGVAIGLAWTPLGGEIMFVEASRMDGEGQLTLTGQLGDVMKESAH 698
Cdd:PRK10787 568 --------IEINGDNLHDYLGVQRFDYGRADNENRVGQVTGLAWTEVGGDLLTIETACVPGKGKLTYTGSLGEVMQESIQ 639
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1128611449 699 LAISWLRSNAKKYQLTNAFgsfdlLDNTDIHLHFPAGAVTKDGPSAGVTIVTCLASLFSGRLVRSDVAMTGEITLRGLVL 778
Cdd:PRK10787 640 AALTVVRARAEKLGINPDF-----YEKRDIHVHVPEGATPKDGPSAGIAMCTALVSCLTGNPVRADVAMTGEITLRGQVL 714
|
730 740 750 760 770
....*....|....*....|....*....|....*....|....*....|....*..
gi 1128611449 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 |
2.66e-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: 364.96 E-value: 2.66e-121
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1128611449 332 IRAARILLDNDHYAMEKLKKRVLEYLAVRQLKNNLKGPILCFVGPPGVGKTSVGRSVAKTLGREFHRIALGGVCDQSDIR 411
Cdd:cd19500 1 IKKARKVLDADHYGLEDVKERILEYLAVRKLKGSMKGPILCLVGPPGVGKTSLGKSIARALGRKFVRISLGGVRDEAEIR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1128611449 412 GHRRTYVGSMPGRIINGLKTVGVNNPVFLLDEVDKLGKSLQGDPAAALLEVLDPEQNHNFTDHYLNVAFDLSQVLFIATA 491
Cdd:cd19500 81 GHRRTYVGAMPGRIIQALKKAGTNNPVFLLDEIDKIGSSFRGDPASALLEVLDPEQNSTFSDHYLDVPFDLSKVLFIATA 160
|
170 180
....*....|....*....|..
gi 1128611449 492 NTTATIPAALLDRMEIIQVPGY 513
Cdd:cd19500 161 NSLDTIPGPLLDRMEIIELSGY 182
|
|
| Lon_C |
pfam05362 |
Lon protease (S16) C-terminal proteolytic domain; The Lon serine proteases must hydrolyze ATP ... |
634-837 |
4.83e-94 |
|
Lon protease (S16) C-terminal proteolytic domain; The Lon serine proteases must hydrolyze 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: 294.53 E-value: 4.83e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1128611449 634 LKDILGPPMYEMEVSQRLSQPGVAIGLAWTPLGGEIMFVEASRMDGEGQLTLTGQLGDVMKESAHLAISWLRSNAKKYQL 713
Cdd:pfam05362 7 LEKYLGVPRFRYGEAEKEDQVGVVTGLAWTEVGGDLLTIEAVIMPGKGKLTLTGQLGDVMKESAQAALSYVRSRAEELGI 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1128611449 714 tnafgSFDLLDNTDIHLHFPAGAVTKDGPSAGVTIVTCLASLFSGRLVRSDVAMTGEITLRGLVLPVGGIKDKVLAAHRA 793
Cdd:pfam05362 87 -----DPDFFEKKDIHIHVPEGATPKDGPSAGVTMATALVSALTGIPVRKDVAMTGEITLRGRVLPIGGLKEKLLAAHRA 161
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1128611449 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 |
6.09e-28 |
|
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 organisms 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: 111.66 E-value: 6.09e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1128611449 13 LPLLLTHEGVLLPGSTMRTSVDSARNLQLVRSRLLKGtslQSTILGVIPNTpDPASDAQDLPPLHRIGTAALAVQVVGSn 92
Cdd:pfam02190 2 LPLLPLRNTVLFPGMVLPLFVGRPRSIAAIEAALNKD---KLYGVLLVSQK-DAEDEEPTPDDLYEVGTVAKIVQILKL- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1128611449 93 wPKPHYTLLITGLCRFQIVQVL-KEKPYPIAEVEQLDrleefpntcKMREELGELSEQFYKYAVQ-LVEMLDMSVPAVAK 170
Cdd:pfam02190 77 -PDGTYKVLVEGLERVRIVELVkKEEPYLRAEVEDLP---------EDSDELSEALKALVKELIEkLRRLLKLLLPLELL 146
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1128611449 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 |
9.36e-27 |
|
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: 425416 [Multi-domain] Cd Length: 130 Bit Score: 106.14 E-value: 9.36e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1128611449 371 LCFVGPPGVGKTSVGRSVAKTLGREFHRIALGGVCDqsdirghrrTYVGSMPGRIINGLKTVGVNNP-VFLLDEVDKLGK 449
Cdd:pfam00004 1 LLLYGPPGTGKTTLAKAVAKELGAPFIEISGSELVS---------KYVGESEKRLRELFEAAKKLAPcVIFIDEIDALAG 71
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1128611449 450 SLQG-------DPAAALLEVLDPEQNHNftdhylnvafdlSQVLFIATANTTATIPAALLDRMEIIQVPGY 513
Cdd:pfam00004 72 SRGSggdsesrRVVNQLLTELDGFTSSN------------SKVIVIAATNRPDKLDPALLGRFDRIIEFPL 130
|
|
| LonB |
COG1067 |
Predicted ATP-dependent protease [Posttranslational modification, protein turnover, chaperones] ... |
551-840 |
2.96e-24 |
|
Predicted ATP-dependent protease [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 223994 [Multi-domain] Cd Length: 647 Bit Score: 108.60 E-value: 2.96e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1128611449 551 IITRYTREAGVRSL----DRKLGAICRAVA-------VKVAEGQHKEAKLDRSdVTEREGCREHILEDEKPESISDTTDl 619
Cdd:COG1067 347 LIREAARRAGDQNKltlrLRDLGNLVREAGdiavsegRKLITAEDVEEALQKR-ELREGQLAERYIEDIKGGQILIETE- 424
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1128611449 620 alppempilidfhalkdilGPpmyemEVSQRLsqpgvaiGLAWTPLGGEIMFVEASRM-----DGEGQLTLTGQLGDvMK 694
Cdd:COG1067 425 -------------------GE-----RVGQIN-------GLSVIEVPGHHAFGEPARIscavhKGDGEIVDIERKAE-LA 472
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1128611449 695 ESAHLAISWLrsnaKKYQLTNAFgsfdlldNTDIHLHFPAGAV------TKDGPSAGVTIVTCLASLFSGRLVRSDVAMT 768
Cdd:COG1067 473 GNIHNKGMMI----KQAFLMSIL-------NYDIHIPFSASLVfeqsygEVDGDSASLAEACALISALSKIPVDQDIAIT 541
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1128611449 769 GEITLRGLVLPVGGIKDKV-------LAAHRAGLKQVIIPRRNEKDL---EGIPGNVRQDLSFVTASC-LDEVLNAAFDG 837
Cdd:COG1067 542 GSIDQFGEVQPVGGVNEKIegffrvcQAAGLTGEQGVIIPKANVKDLslsEDVVKAVKEGKFEIWPVEtIDEALELLLGK 621
|
...
gi 1128611449 838 GFT 840
Cdd:COG1067 622 GEG 624
|
|
| MoxR |
COG0714 |
MoxR-like ATPase [General function prediction only]; |
365-598 |
6.65e-16 |
|
MoxR-like ATPase [General function prediction only];
Pssm-ID: 223786 [Multi-domain] Cd Length: 329 Bit Score: 79.79 E-value: 6.65e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1128611449 365 NLKGPILcFVGPPGVGKTSVGRSVAKTLGREFHRI----------ALGGVCDQSDIRGHRRTyvgsmpgRIINGLKTVGV 434
Cdd:COG0714 41 LAGGHVL-LEGPPGVGKTLLARALARALGLPFVRIqctpdllpsdLLGTYAYAALLLEPGEF-------RFVPGPLFAAV 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1128611449 435 nNPVFLLDEVDKLGKSLQgdpaAALLEVLDPEQ--NHNFTDHYLNVAFdlsqvLFIATANT-----TATIPAALLDRMEI 507
Cdd:COG0714 113 -RVILLLDEINRAPPEVQ----NALLEALEERQvtVPGLTTIRLPPPF-----IVIATQNPgeyegTYPLPEALLDRFLL 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1128611449 508 IQVPGYT---QEEKIEIAHRHLIPKQLEQHGLTPQ---------QIQIPQVTTLDIITRYTRE---AGVRSLDRKLGAIC 572
Cdd:COG0714 183 RIYVDYPdseEEERIILARVGGVDELDLESLVKPVlsdeellrlQKEVKKVPVSDEVIDYIVTlvaALREAPDVALGASP 262
|
250 260
....*....|....*....|....*.
gi 1128611449 573 RAVAVKVAEGQHKeAKLDRSDVTERE 598
Cdd:COG0714 263 RASLALLAALRAL-ALLDGRDAVIPD 287
|
|
| RecA-like_protease |
cd19481 |
proteases similar to RecA; RecA-like NTPases. This family includes the NTP binding domain of ... |
345-504 |
3.41e-14 |
|
proteases similar to RecA; RecA-like NTPases. This family includes the NTP binding domain of F1 and V1 H(+)ATPases, DnaB and related helicases as well as bacterial RecA and related eukaryotic and archaeal recombinases. This group also includes bacterial conjugation proteins and related DNA transfer proteins involved in type II and type IV secretion.
Pssm-ID: 410889 [Multi-domain] Cd Length: 158 Bit Score: 70.77 E-value: 3.41e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1128611449 345 AMEKLKKRVLEYLAVRQL--KNNLKGPILCFVGPPGVGKTSVGRSVAKTLGREFHRIALGGVCDQSdirghrRTYVGSMP 422
Cdd:cd19481 1 LKASLREAVEAPRRGSRLrrYGLGLPKGILLYGPPGTGKTLLAKALAGELGLPLIVVKLSSLLSKY------VGESEKNL 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1128611449 423 GRIINGLKTVGvnNPVFLLDEVDKLGK--SLQGDPAA------ALLEVLDPEQNhnftdhylnvafdLSQVLFIATANTT 494
Cdd:cd19481 75 RKIFERARRLA--PCILFIDEIDAIGRkrDSSGESGElrrvlnQLLTELDGVNS-------------RSKVLVIAATNRP 139
|
170
....*....|
gi 1128611449 495 ATIPAALLDR 504
Cdd:cd19481 140 DLLDPALLRP 149
|
|
| AAA |
cd00009 |
The AAA+ (ATPases Associated with a wide variety of cellular Activities) superfamily ... |
352-513 |
4.01e-11 |
|
The AAA+ (ATPases Associated with a wide variety of cellular Activities) superfamily represents an ancient group of ATPases belonging to the ASCE (for additional strand, catalytic E) division of the P-loop NTPase fold. The ASCE division also includes ABC, RecA-like, VirD4-like, PilT-like, and SF1/2 helicases. Members of the AAA+ ATPases function as molecular chaperons, ATPase subunits of proteases, helicases, or nucleic-acid stimulated ATPases. The AAA+ proteins contain several distinct features in addition to the conserved alpha-beta-alpha core domain structure and the Walker A and B motifs of the P-loop NTPases.
Pssm-ID: 99707 [Multi-domain] Cd Length: 151 Bit Score: 61.78 E-value: 4.01e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1128611449 352 RVLEYLAVRQLKNNLKGPILCFVGPPGVGKTSVGRSVAKTLGR---EFHRIALGGVCDQSDIRGHRRTYvgsmPGRIING 428
Cdd:cd00009 3 QEEAIEALREALELPPPKNLLLYGPPGTGKTTLARAIANELFRpgaPFLYLNASDLLEGLVVAELFGHF----LVRLLFE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1128611449 429 LKTVGvNNPVFLLDEVDKLGKSLQgdpaAALLEVLDpeqnhnfTDHYLNVAFDLSQVLFIATANTTATIPAALLDRMEII 508
Cdd:cd00009 79 LAEKA-KPGVLFIDEIDSLSRGAQ----NALLRVLE-------TLNDLRIDRENVRVIGATNRPLLGDLDRALYDRLDIR 146
|
....*
gi 1128611449 509 QVPGY 513
Cdd:cd00009 147 IVIPL 151
|
|
| COG1750 |
COG1750 |
Predicted archaeal serine protease, S18 family [General function prediction only]; |
741-806 |
1.26e-09 |
|
Predicted archaeal serine protease, S18 family [General function prediction only];
Pssm-ID: 224664 Cd Length: 579 Bit Score: 61.72 E-value: 1.26e-09
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1128611449 741 GPSAGVTIVTCLASLFSGRLVRSDVAMTGEITLRGLVLPVGGIKDKVLAAHRAGLKQVIIPRRNEK 806
Cdd:COG1750 114 GPSAGGYMTVAIYAALMGWSIRKDVMMTGMINPDGSIGPVGGILEKLEAAAKAGAKIFLIPVGQRI 179
|
|
| SpoVK |
COG0464 |
AAA+-type ATPase, SpoVK/Ycf46/Vps4 family [Cell wall/membrane/envelope biogenesis, Cell cycle ... |
345-526 |
5.48e-08 |
|
AAA+-type ATPase, SpoVK/Ycf46/Vps4 family [Cell wall/membrane/envelope biogenesis, Cell cycle control, cell division, chromosome partitioning, Signal transduction mechanisms];
Pssm-ID: 223540 [Multi-domain] Cd Length: 494 Bit Score: 56.37 E-value: 5.48e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1128611449 345 AMEKLKKRV---LEYLAVRQLKNNLKGPILCFVGPPGVGKTSVGRSVAKTLGREFHRIalggvcDQSDIRGHrrtYVGSM 421
Cdd:COG0464 250 AKEELKEAIetpLKRPELFRKLGLRPPKGVLLYGPPGTGKTLLAKAVALESRSRFISV------KGSELLSK---WVGES 320
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1128611449 422 PGRIINGLKTVGVNNP-VFLLDEVDKLGKSLQGDPAAALLEVLdpeQNHNFTdhyLNVAFDLSQVLFIATANTTATIPAA 500
Cdd:COG0464 321 EKNIRELFEKARKLAPsIIFIDEIDSLASGRGPSEDGSGRRVV---GQLLTE---LDGIEKAEGVLVIAATNRPDDLDPA 394
|
170 180
....*....|....*....|....*....
gi 1128611449 501 LLDRM---EIIQVPGYTQEEKIEIAHRHL 526
Cdd:COG0464 395 LLRPGrfdRLIYVPLPDLEERLEIFKIHL 423
|
|
| AAA_5 |
pfam07728 |
AAA domain (dynein-related subfamily); This Pfam entry includes some of the AAA proteins not ... |
371-505 |
5.63e-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: 52.29 E-value: 5.63e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1128611449 371 LCFVGPPGVGKTSVGRSVAK-TLGREFHRIALGGVCDQSDIRGHRRtyVGSMPGRIING-LKTVGVNNPVFLLDEVDKLG 448
Cdd:pfam07728 2 VLLVGPPGTGKTELAERLAAaLSNRPVFYVQLTRDTTEEDLFGRRN--IDPGGASWVDGpLVRAAREGEIAVLDEINRAN 79
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1128611449 449 KSLQGdpaaALLEVLDPEQNHNFTDHYLnVAFDLSQVLFIATANT----TATIPAALLDRM 505
Cdd:pfam07728 80 PDVLN----SLLSLLDERRLLLPDGGEL-VKAAPDGFRLIATMNPldrgLNELSPALRSRF 135
|
|
| aroK |
PRK00131 |
shikimate kinase; Reviewed |
366-396 |
2.15e-06 |
|
shikimate kinase; Reviewed
Pssm-ID: 234654 [Multi-domain] Cd Length: 175 Bit Score: 48.65 E-value: 2.15e-06
10 20 30
....*....|....*....|....*....|.
gi 1128611449 366 LKGPILCFVGPPGVGKTSVGRSVAKTLGREF 396
Cdd:PRK00131 2 LKGPNIVLIGFMGAGKSTIGRLLAKRLGYDF 32
|
|
| PRK13342 |
PRK13342 |
recombination factor protein RarA; Reviewed |
373-524 |
1.08e-05 |
|
recombination factor protein RarA; Reviewed
Pssm-ID: 237355 [Multi-domain] Cd Length: 413 Bit Score: 48.93 E-value: 1.08e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1128611449 373 FVGPPGVGKTSVGRSVAKTLGREFHRI--ALGGVcdqSDIRghrrtyvgsmpgRIINGLKT--VGVNNPVFLLDEVDKLG 448
Cdd:PRK13342 41 LWGPPGTGKTTLARIIAGATDAPFEALsaVTSGV---KDLR------------EVIEEARQrrSAGRRTILFIDEIHRFN 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1128611449 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 |
1.21e-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: 46.42 E-value: 1.21e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1128611449 373 FVGPPGVGKTSVGRSVAKTLG---REFHRIalggvcDQSDIrgHRRTYV----GSMPGRII---NGLKTVGV-NNP--VF 439
Cdd:pfam07724 8 FLGPTGVGKTELAKALAELLFgdeRALIRI------DMSEY--MEEHSVsrliGAPPGYVGyeeGGQLTEAVrRKPysIV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1128611449 440 LLDEVDKLGKSLQGDpaaaLLEVLDpeqNHNFTDHY-LNVAFDlsQVLFIATANTTATIPaalLDRMEIIQVPGY--TQE 516
Cdd:pfam07724 80 LIDEIEKAHPGVQND----LLQILE---GGTLTDKQgRTVDFK--NTLFIMTGNFGSEKI---SDASRLGDSPDYelLKE 147
|
170
....*....|..
gi 1128611449 517 EKIEIAHRHLIP 528
Cdd:pfam07724 148 EVMDLLKKGFIP 159
|
|
| Sms |
COG1066 |
Predicted ATP-dependent serine protease [Posttranslational modification, protein turnover, ... |
734-836 |
1.21e-05 |
|
Predicted ATP-dependent serine protease [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 223993 [Multi-domain] Cd Length: 456 Bit Score: 48.76 E-value: 1.21e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1128611449 734 AGAVTKDGPSAGVTIVTCLASLFSGRLVRSDVAMTGEITLRGLVLPVGGIKDKVLAAHRAGLKQVIIPRRNEKDLEGIpg 813
Cdd:COG1066 361 AGGVKVTEPAADLAVALALVSSFRNRPLPQDTVVFGEVGLSGEIRPVPRGERRLKEAAKLGFKRAIVPKGNIPLPEGI-- 438
|
90 100
....*....|....*....|...
gi 1128611449 814 nvrqdlSFVTASCLDEVLNAAFD 836
Cdd:COG1066 439 ------KVIGVSTLAEALEVVFD 455
|
|
| 44 |
PHA02544 |
clamp loader, small subunit; Provisional |
369-522 |
1.30e-05 |
|
clamp loader, small subunit; Provisional
Pssm-ID: 222866 [Multi-domain] Cd Length: 316 Bit Score: 48.06 E-value: 1.30e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1128611449 369 PILCFVGP-PGVGKTSVGRSVAKTLGREFHRIAlGGVCDQSDIRGHRRTYVGSMpgriinglkTVGVNNPVFLLDEVDKL 447
Cdd:PHA02544 43 PNMLLHSPsPGTGKTTVAKALCNEVGAEVLFVN-GSDCRIDFVRNRLTRFASTV---------SLTGGGKVIIIDEFDRL 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1128611449 448 G-----KSLQGdpaaaLLEvldpeqnhnftdhylnvAFDlSQVLFIATANTTATIPAALLDRMEIIQVPGYTQEEKIEIA 522
Cdd:PHA02544 113 GladaqRHLRS-----FME-----------------AYS-KNCSFIITANNKNGIIEPLRSRCRVIDFGVPTKEEQIEMM 169
|
|
| RecA-like_ClpB_Hsp104-like |
cd19499 |
Chaperone protein ClpB/Hsp104 subfamily; Bacterial Caseinolytic peptidase B (ClpB) and ... |
358-508 |
1.41e-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: 46.40 E-value: 1.41e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1128611449 358 AVRQLKNNLKGP-----ILCFVGPPGVGKTSVGRSVAKTL-GREFHRIALggvcDQS-DIRGHRRTYVGSMPGRIIngLK 430
Cdd:cd19499 26 AIRRARAGLSDPnrpigSFLFLGPTGVGKTELAKALAELLfGDEDNLIRI----DMSeYMEKHSVSRLIGAPPGYV--GY 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1128611449 431 TVG-------VNNP--VFLLDEVDKLGKSLQGdpaaALLEVLDpeqNHNFTDHYLNVAfDLSQVLFIATANttaTIPAAL 501
Cdd:cd19499 100 TEGgqlteavRRKPysVVLLDEIEKAHPDVQN----LLLQVLD---DGRLTDSHGRTV-DFKNTIIIMTSN---HFRPEF 168
|
....*..
gi 1128611449 502 LDRMEII 508
Cdd:cd19499 169 LNRIDEI 175
|
|
| SdrC |
COG3480 |
Predicted secreted protein containing a PDZ domain [Signal transduction mechanisms]; |
740-804 |
1.59e-05 |
|
Predicted secreted protein containing a PDZ domain [Signal transduction mechanisms];
Pssm-ID: 226011 [Multi-domain] Cd Length: 342 Bit Score: 48.17 E-value: 1.59e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1128611449 740 DGPSAGVTIVTCLAS-LFSGRLVRS-DVAMTGEITLRGLVLPVGGIKDKVLAAHRAGLKQVIIPRRN 804
Cdd:COG3480 233 GGPSAGLMFSLAIYDqLTKGDLTGGrFIAGTGTIEVDGKVGPIGGIDQKVVAAAKAGADVFFVPADN 299
|
|
| RarA |
COG2256 |
Replication-associated recombination protein RarA (DNA-dependent ATPase) [Replication, ... |
373-556 |
1.67e-05 |
|
Replication-associated recombination protein RarA (DNA-dependent ATPase) [Replication, recombination and repair];
Pssm-ID: 225165 [Multi-domain] Cd Length: 436 Bit Score: 48.38 E-value: 1.67e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1128611449 373 FVGPPGVGKTSVGRSVAKTLGREFHRI--ALGGVcdqSDIRghrrtyvgsmpGRIINGLKTVGVNN-PVFLLDEVDKLGK 449
Cdd:COG2256 53 LWGPPGTGKTTLARLIAGTTNAAFEALsaVTSGV---KDLR-----------EIIEEARKNRLLGRrTILFLDEIHRFNK 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1128611449 450 SLQgDpaaALLEVLdpEQNHnftdhylnvafdlsqVLFIA--TANTTATIPAALLDRMEIIQVPGYTQEEKIEIAHRHLi 527
Cdd:COG2256 119 AQQ-D---ALLPHV--ENGT---------------IILIGatTENPSFELNPALLSRARVFELKPLSSEDIKKLLKRAL- 176
|
170 180
....*....|....*....|....*....
gi 1128611449 528 pkQLEQHGLTPQQIQIPQvTTLDIITRYT 556
Cdd:COG2256 177 --LDEERGLGGQIIVLDE-EALDYLVRLS 202
|
|
| LON |
COG2802 |
Uncharacterized protein, LON-like domain, ASCH/PUA-like superfamily [Function unknown]; |
4-144 |
1.72e-05 |
|
Uncharacterized protein, LON-like domain, ASCH/PUA-like superfamily [Function unknown];
Pssm-ID: 225362 [Multi-domain] Cd Length: 221 Bit Score: 47.02 E-value: 1.72e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1128611449 4 VSPIQIPSRLPLLLTHEGVLLPGSTMRTSVDSARNLQLVRSRLlkgtsLQSTILGVIPNTPDPASDAQDLPPLHRIGTAA 83
Cdd:COG2802 3 SSPDDLPLELPLFPLPGAVLLPGGLLPLNIFEPRYLAMVRTCL-----AEGRRFGVVLIDRGREVGGGLPPELSDVGCLA 77
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1128611449 84 LAVQVvgSNWPKPHYTLLITGLCRFQIVQVL-KEKPYPIAEVEQLDRLEEFPNTCKMREELG 144
Cdd:COG2802 78 RITEF--EELGDGRYLILVRGGQRFRVLEELaDDDPYRRARVPFWPDLPSDPDGAEEVDRRL 137
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
367-505 |
1.78e-05 |
|
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a variety of cellular activities. This profile/alignment only detects a fraction of this vast family. The poorly conserved N-terminal helix is missing from the alignment.
Pssm-ID: 214640 [Multi-domain] Cd Length: 148 Bit Score: 45.44 E-value: 1.78e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1128611449 367 KGPILCFVGPPGVGKTSVGRSVAKTLGREFHRI-------ALGGVCDQSDIRGHRRTYVGSMPGRIINGLKTV--GVNNP 437
Cdd:smart00382 1 PGEVILIVGPPGSGKTTLARALARELGPPGGGViyidgedILEEVLDQLLLIIVGGKKASGSGELRLRLALALarKLKPD 80
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1128611449 438 VFLLDEVDKLGKSLQgdpaAALLEVLDPEQNHNFTDHYLNvafdlsqVLFIATANTTATIPAALLDRM 505
Cdd:smart00382 81 VLILDEITSLLDAEQ----EALLLLLEELRLLLLLKSEKN-------LTVILTTNDEKDLGPALLRRR 137
|
|
| SK |
cd00464 |
Shikimate kinase (SK) is the fifth enzyme in the shikimate pathway, a seven-step biosynthetic ... |
374-396 |
9.33e-05 |
|
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: 43.70 E-value: 9.33e-05
|
| clpA |
PRK11034 |
ATP-dependent Clp protease ATP-binding subunit; Provisional |
373-492 |
4.66e-04 |
|
ATP-dependent Clp protease ATP-binding subunit; Provisional
Pssm-ID: 236828 [Multi-domain] Cd Length: 758 Bit Score: 44.06 E-value: 4.66e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1128611449 373 FVGPPGVGKTSVGRSVAKTLGREFHRIalggvcDQSDIrGHRRT---YVGSMPGRI---INGLKTVGV-NNP--VFLLDE 443
Cdd:PRK11034 493 FAGPTGVGKTEVTVQLSKALGIELLRF------DMSEY-MERHTvsrLIGAPPGYVgfdQGGLLTDAViKHPhaVLLLDE 565
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 1128611449 444 VDKlgksLQGDPAAALLEVLDpeqNHNFTDHYLNVAfDLSQVLFIATAN 492
Cdd:PRK11034 566 IEK----AHPDVFNLLLQVMD---NGTLTDNNGRKA-DFRNVVLVMTTN 606
|
|
| AroK |
COG0703 |
Shikimate kinase [Amino acid transport and metabolism]; |
373-396 |
7.22e-04 |
|
Shikimate kinase [Amino acid transport and metabolism];
Pssm-ID: 223775 [Multi-domain] Cd Length: 172 Bit Score: 41.43 E-value: 7.22e-04
|
| COG4930 |
COG4930 |
Predicted ATP-dependent Lon-type protease [Posttranslational modification, protein turnover, ... |
651-812 |
8.82e-04 |
|
Predicted ATP-dependent Lon-type protease [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 227267 [Multi-domain] Cd Length: 683 Bit Score: 42.99 E-value: 8.82e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1128611449 651 LSQPGVAIGLAWTPLGGEIMF-VEASRMDGEGQLTLTGqLGD--VMKESAHLAISWLRSNAKKYQLTNAFgsfdllDNTD 727
Cdd:COG4930 500 MPKPGVVHLVTQAESGMTGLYrFETQMTAGNGKHSVSG-LGSstSAKEAIRVGFDYFKGNLSRVSATAKF------SEHE 572
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1128611449 728 IHLHfpAGAVTKDGPSAGVTIvTCLASLFSGRLVRS---DVAMTGEITLRGLVLPVGGIKDKVLAAHRAGLKQVIIPRRN 804
Cdd:COG4930 573 YHLH--VVELHNTGPSTATSL-AALIALCSVLLAKPvqeQMVVLGSMTLGGVINPVQDLAASLQLAFDSGAKKVLLPMSS 649
|
....*...
gi 1128611449 805 EKDLEGIP 812
Cdd:COG4930 650 AVDIPTVP 657
|
|
| MDN1 |
COG5271 |
Midasin, AAA ATPase with vWA domain, involved in ribosome maturation [Translation, ribosomal ... |
369-529 |
1.52e-03 |
|
Midasin, AAA ATPase with vWA domain, involved in ribosome maturation [Translation, ribosomal structure and biogenesis];
Pssm-ID: 227596 [Multi-domain] Cd Length: 4600 Bit Score: 42.68 E-value: 1.52e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1128611449 369 PILcFVGPPGVGKTSVGRSVAKTLGREFHRIALG---GVCD--QSDIRGHRRTYVGSMPGRIINGLKtvgvNNPVFLLDE 443
Cdd:COG5271 1545 PIL-LEGSPGVGKTSLITALARKTGKKLIRINLSeqtDLCDlfGSDLPVEEGGEFRWMDAPFLHAMR----DGGWVLLDE 1619
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1128611449 444 VDKLGKS-LQGdpaaaLLEVLD-------PEQNHNFTDHylnvafdlSQVLFIATANTTAT------IPAALLDRMEIIQ 509
Cdd:COG5271 1620 INLASQSvLEG-----LNACLDhrreayiPELDKTFDVH--------PNFRVFAAQNPQDQgggrkgLPKSFLNRFSVVK 1686
|
170 180
....*....|....*....|
gi 1128611449 510 VPGYTQEEKIEIAhRHLIPK 529
Cdd:COG5271 1687 MDGLTTDDITHIA-NKMYPQ 1705
|
|
| AAA_3 |
pfam07726 |
ATPase family associated with various cellular activities (AAA); This Pfam entry includes some ... |
375-504 |
2.25e-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: 39.08 E-value: 2.25e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1128611449 375 GPPGVGKTSVGRSVAKTLGREFHRIALGGVCDQSDIRG------HRRTYVgSMPGriinglktvgvnnPVF----LLDEV 444
Cdd:pfam07726 6 GVPGLAKTLLVRTLARSLGLDFRRIQFTPDLLPSDITGtevfdqKTREFE-FRPG-------------PVFanvlLADEI 71
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1128611449 445 DKLGKSLQgdpaAALLEVLdpeQNHNFTdhYLNVAFDLSQVLF-IATANT-----TATIPAALLDR 504
Cdd:pfam07726 72 NRAPPKTQ----SALLEAM---QERQVT--IDGETHPLPEPFFvLATQNPieqegTYPLPEAQLDR 128
|
|
|