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Conserved domains on  [gi|31377667|ref|NP_113678|]
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lon protease homolog 2, peroxisomal isoform 1 [Homo sapiens]

Protein Classification

endopeptidase La( domain architecture ID 11422032)

endopeptidase La is an ATP-dependent serine protease that degrades polypeptides processively to yield small peptide fragments that are 5 to 10 amino acids long; it binds to DNA in a double-stranded, site-specific manner

CATH:  1.10.8.60
EC:  3.4.21.53
Gene Ontology:  GO:0005524|GO:0016887|GO:0004176|GO:0004252|GO:0043565
MEROPS:  S16
PubMed:  34563541|9115177

Graphical summary

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List of domain hits

 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 31377667   1 MS-SVSPIQIPSRLPLLLTHEGVLLPGSTMRTSVDSARNLQLVRsRLLKGTSLqstiLGVI----PNTPDPASDAqdlpp 75
Cdd:COG0466   1 MSeEKEEEELPETLPLLPLRDVVVFPGMVIPLFVGREKSIKALE-EAMEGDKL----IGLVaqkdAEVEDPGPDD----- 70

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31377667  76 LHRIGTAALAVQVVgsNWPKPHYTLLITGLCRFQIVQVLKEKPYPIAEVEQLDrlEEFPNTCKMREELGELSEQFYKYAv 155
Cdd:COG0466  71 LYEVGTVAKILQLL--KLPDGTVKVLVEGLQRARIKEFVQEEPYLEAEVEPLE--EEEEDDKELEALMRSLKEQFEEYV- 145

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31377667 156 qlveMLDMSVP--AVAKLRRLLDSlprEALPDILTSIIRTSNKEKLQILDAVSLEERFKMTIPLLVRQIEGLKLLQKTR- 232
Cdd:COG0466 146 ----KLNPKIPpeLLAALSNIEDP---GRLADFIASHLPLKIEEKQELLETLDVKERLEKLLELLEKEIEVLELEKKIRs 218

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31377667 233 KPKQDDDKR---------VIAIR-----------PIRRithisgtledededednddivmLEKKIRTSSMPEQAHKVCVK 292
Cdd:COG0466 219 RVKEQMEKSqreyylreqLKAIQkelgekddgedEIEE----------------------LREKIEKAKLPEEVKEKAEK 276

                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31377667 293 EIKRLKKMPQSMPEYALTRNYLELMVELPWNKSTTDRLDIRAARILLDNDHYAMEKLKKRVLEYLAVRQLKNNLKGPILC 372
Cdd:COG0466 277 ELKKLERMPPMSAEATVIRNYLDWLLDLPWGKRTKDNLDLKKAEKILDEDHYGLEKVKERILEYLAVRKLKKKLKGPILC 356

                       410       420       430       440       450       460       470       480
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31377667 373 FVGPPGVGKTSVGRSVAKTLGREFHRIALGGVCDQSDIRGHRRTYVGSMPGRIINGLKTVGVNNPVFLLDEVDKLGKSLQ 452
Cdd:COG0466 357 LVGPPGVGKTSLGKSIARALGRKFVRISLGGVRDEAEIRGHRRTYIGAMPGRIIQGLKKAGTKNPVFLLDEIDKMGSDFR 436

                       490       500       510       520       530       540       550       560
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31377667 453 GDPAAALLEVLDPEQNHNFTDHYLNVAFDLSQVLFIATANTTATIPAALLDRMEIIQVPGYTQEEKIEIAHRHLIPKQLE 532
Cdd:COG0466 437 GDPASALLEVLDPEQNNTFSDHYLEVPFDLSKVMFIATANSLDTIPAPLLDRMEIIELSGYTEEEKLEIAKRYLIPKQLK 516

                       570       580       590       600       610       620       630       640
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31377667 533 QHGLTPQQIQIPQVTTLDIITRYTREAGVRSLDRKLGAICRAVAVKVAEGQHKEAKLDRSDvteregcrehiledekpes 612
Cdd:COG0466 517 EHGLKKEELKISDEALRKIIRGYTREAGVRNLEREIAKICRKVAKKIAEGKKKKVTITPKN------------------- 577

                       650       660       670       680       690       700       710       720
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31377667 613 isdttdlalppempilidfhaLKDILGPPMYEMEVSQRLSQPGVAIGLAWTPLGGEIMFVEASRMDGEGQLTLTGQLGDV 692
Cdd:COG0466 578 ---------------------LEKYLGVPRFRYEKAEEEDQVGVVTGLAWTEVGGDILFIEATLMPGKGKLTLTGQLGDV 636

                       730       740       750       760       770       780       790       800
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31377667 693 MKESAHLAISWLRSNAKKYQLtnafgSFDLLDNTDIHLHFPAGAVTKDGPSAGVTIVTCLASLFSGRLVRSDVAMTGEIT 772
Cdd:COG0466 637 MKESAQAALSYVRSRAEELGI-----DPDFFEKYDIHIHVPEGATPKDGPSAGITMATALVSALTGRPVRSDVAMTGEIT 711

                       810       820       830       840       850       860
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 31377667 773 LRGLVLPVGGIKDKVLAAHRAGLKQVIIPRRNEKDLEGIPGNVRQDLSFVTASCLDEVLNAAF 835
Cdd:COG0466 712 LRGRVLPIGGLKEKLLAAHRAGIKTVILPKENEKDLEEIPEEVKKGLEFHPVEHIDEVLKIAL 774
 
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 31377667   1 MS-SVSPIQIPSRLPLLLTHEGVLLPGSTMRTSVDSARNLQLVRsRLLKGTSLqstiLGVI----PNTPDPASDAqdlpp 75
Cdd:COG0466   1 MSeEKEEEELPETLPLLPLRDVVVFPGMVIPLFVGREKSIKALE-EAMEGDKL----IGLVaqkdAEVEDPGPDD----- 70

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31377667  76 LHRIGTAALAVQVVgsNWPKPHYTLLITGLCRFQIVQVLKEKPYPIAEVEQLDrlEEFPNTCKMREELGELSEQFYKYAv 155
Cdd:COG0466  71 LYEVGTVAKILQLL--KLPDGTVKVLVEGLQRARIKEFVQEEPYLEAEVEPLE--EEEEDDKELEALMRSLKEQFEEYV- 145

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31377667 156 qlveMLDMSVP--AVAKLRRLLDSlprEALPDILTSIIRTSNKEKLQILDAVSLEERFKMTIPLLVRQIEGLKLLQKTR- 232
Cdd:COG0466 146 ----KLNPKIPpeLLAALSNIEDP---GRLADFIASHLPLKIEEKQELLETLDVKERLEKLLELLEKEIEVLELEKKIRs 218

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31377667 233 KPKQDDDKR---------VIAIR-----------PIRRithisgtledededednddivmLEKKIRTSSMPEQAHKVCVK 292
Cdd:COG0466 219 RVKEQMEKSqreyylreqLKAIQkelgekddgedEIEE----------------------LREKIEKAKLPEEVKEKAEK 276

                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31377667 293 EIKRLKKMPQSMPEYALTRNYLELMVELPWNKSTTDRLDIRAARILLDNDHYAMEKLKKRVLEYLAVRQLKNNLKGPILC 372
Cdd:COG0466 277 ELKKLERMPPMSAEATVIRNYLDWLLDLPWGKRTKDNLDLKKAEKILDEDHYGLEKVKERILEYLAVRKLKKKLKGPILC 356

                       410       420       430       440       450       460       470       480
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31377667 373 FVGPPGVGKTSVGRSVAKTLGREFHRIALGGVCDQSDIRGHRRTYVGSMPGRIINGLKTVGVNNPVFLLDEVDKLGKSLQ 452
Cdd:COG0466 357 LVGPPGVGKTSLGKSIARALGRKFVRISLGGVRDEAEIRGHRRTYIGAMPGRIIQGLKKAGTKNPVFLLDEIDKMGSDFR 436

                       490       500       510       520       530       540       550       560
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31377667 453 GDPAAALLEVLDPEQNHNFTDHYLNVAFDLSQVLFIATANTTATIPAALLDRMEIIQVPGYTQEEKIEIAHRHLIPKQLE 532
Cdd:COG0466 437 GDPASALLEVLDPEQNNTFSDHYLEVPFDLSKVMFIATANSLDTIPAPLLDRMEIIELSGYTEEEKLEIAKRYLIPKQLK 516

                       570       580       590       600       610       620       630       640
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31377667 533 QHGLTPQQIQIPQVTTLDIITRYTREAGVRSLDRKLGAICRAVAVKVAEGQHKEAKLDRSDvteregcrehiledekpes 612
Cdd:COG0466 517 EHGLKKEELKISDEALRKIIRGYTREAGVRNLEREIAKICRKVAKKIAEGKKKKVTITPKN------------------- 577

                       650       660       670       680       690       700       710       720
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31377667 613 isdttdlalppempilidfhaLKDILGPPMYEMEVSQRLSQPGVAIGLAWTPLGGEIMFVEASRMDGEGQLTLTGQLGDV 692
Cdd:COG0466 578 ---------------------LEKYLGVPRFRYEKAEEEDQVGVVTGLAWTEVGGDILFIEATLMPGKGKLTLTGQLGDV 636

                       730       740       750       760       770       780       790       800
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31377667 693 MKESAHLAISWLRSNAKKYQLtnafgSFDLLDNTDIHLHFPAGAVTKDGPSAGVTIVTCLASLFSGRLVRSDVAMTGEIT 772
Cdd:COG0466 637 MKESAQAALSYVRSRAEELGI-----DPDFFEKYDIHIHVPEGATPKDGPSAGITMATALVSALTGRPVRSDVAMTGEIT 711

                       810       820       830       840       850       860
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 31377667 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 31377667    14 PLLLTHEGVLLPGSTMRTSVDSARNLQLVRsrllKGTSLQSTILGVIPNTPDPaSDAQDLPPLHRIGTAALAVQVVGS-N 92
Cdd:TIGR00763   1 PLLPLRRRPLFPGMIKPIDVGREKSIKLIK----EALRLKQPYLGLFLQKDDD-NEEPEEDDIYSVGVVAQILEMLPLpS 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31377667    93 WPKPHYTLLITGLCRFQIVQVLKEKPYPIAEVeqlDRLEEFPNTcKMREELGELSEQFYKYAVQLVEMLDMSVPAVAKLR 172
Cdd:TIGR00763  76 SGTATYKVVVEGLRRIRIKELSDKGGYLVVRV---DNLKEEPFD-KDDEEIKALTREIKETFRELISLSKLFREQPALLS 151

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31377667   173 RLLDSLPREALPDILTSIIRTSNKEKLQ-ILDAVSLEERFKMTIPLLVRQIEGLKLLQK-TRKPKQ---DDDKRVIAIRP 247
Cdd:TIGR00763 152 ALEDIDEPGRLADFVAASLQLKEKDELQeVLETVNIEKRLKKALELLKKELELLKLQNKiTKKVEEkmeKTQREYYLREQ 231

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31377667   248 IRRITHISGTlededEDEDNDDIVMLEKKIRTSSMPEQAHKVCVKEIKRLKKMPQSMPEYALTRNYLELMVELPWNKSTT 327
Cdd:TIGR00763 232 LKAIKKELGI-----EKDDKDELEKLKEKLEELKLPEEVKKVIEKELTKLSLLEPSSSEFTVTRNYLDWLTDLPWGKYSK 306

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31377667   328 DRLDIRAARILLDNDHYAMEKLKKRVLEYLAVRQLKNNLKGPILCFVGPPGVGKTSVGRSVAKTLGREFHRIALGGVCDQ 407
Cdd:TIGR00763 307 ENLDLKRAKEILDEDHYGLKKVKERILEYLAVQKLRGKMKGPILCLVGPPGVGKTSLGKSIAKALNRKFVRFSLGGVRDE 386

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31377667   408 SDIRGHRRTYVGSMPGRIINGLKTVGVNNPVFLLDEVDKLGKSLQGDPAAALLEVLDPEQNHNFTDHYLNVAFDLSQVLF 487
Cdd:TIGR00763 387 AEIRGHRRTYVGAMPGRIIQGLKKAKTKNPLFLLDEIDKIGSSFRGDPASALLEVLDPEQNNAFSDHYLDVPFDLSKVIF 466

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31377667   488 IATANTTATIPAALLDRMEIIQVPGYTQEEKIEIAHRHLIPKQLEQHGLTPQQIQIPQVTTLDIITRYTREAGVRSLDRK 567
Cdd:TIGR00763 467 IATANSIDTIPRPLLDRMEVIELSGYTEEEKLEIAKKYLIPKALEDHGLKPDELKITDEALLLLIKYYTREAGVRNLERQ 546

                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31377667   568 LGAICRAVAVKVAEGQHKEAkldrsdvteregcrehiledEKPESISDTTDLalppempilidfhaLKDILGPPMYEMEV 647
Cdd:TIGR00763 547 IEKICRKAAVKLVEQGEKKK--------------------SEAESVVITPDN--------------LKKYLGKPVFTYER 592

                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31377667   648 SQRLSQPGVAIGLAWTPLGGEIMFVEASRMDGEGQLTLTGQLGDVMKESAHLAISWLRSNAKKYQLTNafgsfDLLDNTD 727
Cdd:TIGR00763 593 AYEVTPPGVVMGLAWTPMGGDTLFIETTKVAGKGSLELTGQLGDVMKESAQIALTYVRSIAADLGISP-----NFFEKAD 667

                         730       740       750       760       770       780       790       800
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31377667   728 IHLHFPAGAVTKDGPSAGVTIVTCLASLFSGRLVRSDVAMTGEITLRGLVLPVGGIKDKVLAAHRAGLKQVIIPRRNEKD 807
Cdd:TIGR00763 668 IHLHVPEGATPKDGPSAGITMATALLSLATGKPVRPDVAMTGEITLRGKVLPIGGLKEKTIAAKRAGIKTIILPEKNRRD 747

                         810       820
                  ....*....|....*....|....*...
gi 31377667   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 31377667   65 DPASDAQDLPPLHRIGTAALAVQVVgsNWPKPHYTLLITGLCRFQIVQVLKEKPYPIAEVEQLD--RLEEFPNTCKMREE 142
Cdd:PRK10787  57 EASTDEPGVNDLFTVGTVASILQML--KLPDGTVKVLVEGLQRARISALSDNGEHFSAKAEYLEspTIDEREQEVLVRTA 134

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31377667  143 LGELsEQFYKYAVQLVEMLDMSVPAVAKLRRLLDSLPREaLPDILtsiirtsnKEKLQILDAVSLEERFKMTIPLLVRQI 222
Cdd:PRK10787 135 ISQF-EGYIKLNKKIPPEVLTSLNSIDDPARLADTIAAH-MPLKL--------ADKQSVLEMSDVNERLEYLMAMMESEI 204

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31377667  223 EGLKLLQKTR---KPKQDDDKRVIAI-RPIRRITHISGTLEDEDEDEDNddivmLEKKIRTSSMPEQAHKVCVKEIKRLK 298
Cdd:PRK10787 205 DLLQVEKRIRnrvKKQMEKSQREYYLnEQMKAIQKELGEMDDAPDENEA-----LKRKIDAAKMPKEAKEKAEAELQKLK 279

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31377667  299 KMPQSMPEYALTRNYLELMVELPWNKSTTDRLDIRAARILLDNDHYAMEKLKKRVLEYLAVRQLKNNLKGPILCFVGPPG 378
Cdd:PRK10787 280 MMSPMSAEATVVRGYIDWMVQVPWNARSKVKKDLRQAQEILDTDHYGLERVKDRILEYLAVQSRVNKIKGPILCLVGPPG 359

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31377667  379 VGKTSVGRSVAKTLGREFHRIALGGVCDQSDIRGHRRTYVGSMPGRIINGLKTVGVNNPVFLLDEVDKLGKSLQGDPAAA 458
Cdd:PRK10787 360 VGKTSLGQSIAKATGRKYVRMALGGVRDEAEIRGHRRTYIGSMPGKLIQKMAKVGVKNPLFLLDEIDKMSSDMRGDPASA 439

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31377667  459 LLEVLDPEQNHNFTDHYLNVAFDLSQVLFIATANTTaTIPAALLDRMEIIQVPGYTQEEKIEIAHRHLIPKQLEQHGLTP 538
Cdd:PRK10787 440 LLEVLDPEQNVAFSDHYLEVDYDLSDVMFVATSNSM-NIPAPLLDRMEVIRLSGYTEDEKLNIAKRHLLPKQIERNALKK 518

                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31377667  539 QQIQIPQVTTLDIITRYTREAGVRSLDRKLGAICRAvAVKVaegqhkeakldrsdvteregcrehILEDEKPESisdttd 618
Cdd:PRK10787 519 GELTVDDSAIIGIIRYYTREAGVRSLEREISKLCRK-AVKQ------------------------LLLDKSLKH------ 567

                        570       580       590       600       610       620       630       640
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31377667  619 lalppempILIDFHALKDILGPPMYEMEVSQRLSQPGVAIGLAWTPLGGEIMFVEASRMDGEGQLTLTGQLGDVMKESAH 698
Cdd:PRK10787 568 --------IEINGDNLHDYLGVQRFDYGRADNENRVGQVTGLAWTEVGGDLLTIETACVPGKGKLTYTGSLGEVMQESIQ 639

                        650       660       670       680       690       700       710       720
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31377667  699 LAISWLRSNAKKYQLTNAFgsfdlLDNTDIHLHFPAGAVTKDGPSAGVTIVTCLASLFSGRLVRSDVAMTGEITLRGLVL 778
Cdd:PRK10787 640 AALTVVRARAEKLGINPDF-----YEKRDIHVHVPEGATPKDGPSAGIAMCTALVSCLTGNPVRADVAMTGEITLRGQVL 714

                        730       740       750       760       770
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 31377667  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 31377667 332 IRAARILLDNDHYAMEKLKKRVLEYLAVRQLKNNLKGPILCFVGPPGVGKTSVGRSVAKTLGREFHRIALGGVCDQSDIR 411
Cdd:cd19500   1 IKKARKVLDADHYGLEDVKERILEYLAVRKLKGSMKGPILCLVGPPGVGKTSLGKSIARALGRKFVRISLGGVRDEAEIR 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31377667 412 GHRRTYVGSMPGRIINGLKTVGVNNPVFLLDEVDKLGKSLQGDPAAALLEVLDPEQNHNFTDHYLNVAFDLSQVLFIATA 491
Cdd:cd19500  81 GHRRTYVGAMPGRIIQALKKAGTNNPVFLLDEIDKIGSSFRGDPASALLEVLDPEQNSTFSDHYLDVPFDLSKVLFIATA 160

                       170       180
                ....*....|....*....|..
gi 31377667 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 31377667   634 LKDILGPPMYEMEVSQRLSQPGVAIGLAWTPLGGEIMFVEASRMDGEGQLTLTGQLGDVMKESAHLAISWLRSNAKKYQL 713
Cdd:pfam05362   7 LEKYLGVPRFRYGEAEKEDQVGVVTGLAWTEVGGDLLTIEAVIMPGKGKLTLTGQLGDVMKESAQAALSYVRSRAEELGI 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31377667   714 tnafgSFDLLDNTDIHLHFPAGAVTKDGPSAGVTIVTCLASLFSGRLVRSDVAMTGEITLRGLVLPVGGIKDKVLAAHRA 793
Cdd:pfam05362  87 -----DPDFFEKKDIHIHVPEGATPKDGPSAGVTMATALVSALTGIPVRKDVAMTGEITLRGRVLPIGGLKEKLLAAHRA 161

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 31377667   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 31377667    367 KGPILCFVGPPGVGKTSVGRSVAKTLGREFHRI-------ALGGVCDQSDIRGHRRTYVGSMPGRIINGLKTV--GVNNP 437
Cdd:smart00382   1 PGEVILIVGPPGSGKTTLARALARELGPPGGGViyidgedILEEVLDQLLLIIVGGKKASGSGELRLRLALALarKLKPD 80

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 31377667    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 31377667   1 MS-SVSPIQIPSRLPLLLTHEGVLLPGSTMRTSVDSARNLQLVRsRLLKGTSLqstiLGVI----PNTPDPASDAqdlpp 75
Cdd:COG0466   1 MSeEKEEEELPETLPLLPLRDVVVFPGMVIPLFVGREKSIKALE-EAMEGDKL----IGLVaqkdAEVEDPGPDD----- 70

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31377667  76 LHRIGTAALAVQVVgsNWPKPHYTLLITGLCRFQIVQVLKEKPYPIAEVEQLDrlEEFPNTCKMREELGELSEQFYKYAv 155
Cdd:COG0466  71 LYEVGTVAKILQLL--KLPDGTVKVLVEGLQRARIKEFVQEEPYLEAEVEPLE--EEEEDDKELEALMRSLKEQFEEYV- 145

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31377667 156 qlveMLDMSVP--AVAKLRRLLDSlprEALPDILTSIIRTSNKEKLQILDAVSLEERFKMTIPLLVRQIEGLKLLQKTR- 232
Cdd:COG0466 146 ----KLNPKIPpeLLAALSNIEDP---GRLADFIASHLPLKIEEKQELLETLDVKERLEKLLELLEKEIEVLELEKKIRs 218

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31377667 233 KPKQDDDKR---------VIAIR-----------PIRRithisgtledededednddivmLEKKIRTSSMPEQAHKVCVK 292
Cdd:COG0466 219 RVKEQMEKSqreyylreqLKAIQkelgekddgedEIEE----------------------LREKIEKAKLPEEVKEKAEK 276

                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31377667 293 EIKRLKKMPQSMPEYALTRNYLELMVELPWNKSTTDRLDIRAARILLDNDHYAMEKLKKRVLEYLAVRQLKNNLKGPILC 372
Cdd:COG0466 277 ELKKLERMPPMSAEATVIRNYLDWLLDLPWGKRTKDNLDLKKAEKILDEDHYGLEKVKERILEYLAVRKLKKKLKGPILC 356

                       410       420       430       440       450       460       470       480
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31377667 373 FVGPPGVGKTSVGRSVAKTLGREFHRIALGGVCDQSDIRGHRRTYVGSMPGRIINGLKTVGVNNPVFLLDEVDKLGKSLQ 452
Cdd:COG0466 357 LVGPPGVGKTSLGKSIARALGRKFVRISLGGVRDEAEIRGHRRTYIGAMPGRIIQGLKKAGTKNPVFLLDEIDKMGSDFR 436

                       490       500       510       520       530       540       550       560
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31377667 453 GDPAAALLEVLDPEQNHNFTDHYLNVAFDLSQVLFIATANTTATIPAALLDRMEIIQVPGYTQEEKIEIAHRHLIPKQLE 532
Cdd:COG0466 437 GDPASALLEVLDPEQNNTFSDHYLEVPFDLSKVMFIATANSLDTIPAPLLDRMEIIELSGYTEEEKLEIAKRYLIPKQLK 516

                       570       580       590       600       610       620       630       640
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31377667 533 QHGLTPQQIQIPQVTTLDIITRYTREAGVRSLDRKLGAICRAVAVKVAEGQHKEAKLDRSDvteregcrehiledekpes 612
Cdd:COG0466 517 EHGLKKEELKISDEALRKIIRGYTREAGVRNLEREIAKICRKVAKKIAEGKKKKVTITPKN------------------- 577

                       650       660       670       680       690       700       710       720
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31377667 613 isdttdlalppempilidfhaLKDILGPPMYEMEVSQRLSQPGVAIGLAWTPLGGEIMFVEASRMDGEGQLTLTGQLGDV 692
Cdd:COG0466 578 ---------------------LEKYLGVPRFRYEKAEEEDQVGVVTGLAWTEVGGDILFIEATLMPGKGKLTLTGQLGDV 636

                       730       740       750       760       770       780       790       800
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31377667 693 MKESAHLAISWLRSNAKKYQLtnafgSFDLLDNTDIHLHFPAGAVTKDGPSAGVTIVTCLASLFSGRLVRSDVAMTGEIT 772
Cdd:COG0466 637 MKESAQAALSYVRSRAEELGI-----DPDFFEKYDIHIHVPEGATPKDGPSAGITMATALVSALTGRPVRSDVAMTGEIT 711

                       810       820       830       840       850       860
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 31377667 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 31377667    14 PLLLTHEGVLLPGSTMRTSVDSARNLQLVRsrllKGTSLQSTILGVIPNTPDPaSDAQDLPPLHRIGTAALAVQVVGS-N 92
Cdd:TIGR00763   1 PLLPLRRRPLFPGMIKPIDVGREKSIKLIK----EALRLKQPYLGLFLQKDDD-NEEPEEDDIYSVGVVAQILEMLPLpS 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31377667    93 WPKPHYTLLITGLCRFQIVQVLKEKPYPIAEVeqlDRLEEFPNTcKMREELGELSEQFYKYAVQLVEMLDMSVPAVAKLR 172
Cdd:TIGR00763  76 SGTATYKVVVEGLRRIRIKELSDKGGYLVVRV---DNLKEEPFD-KDDEEIKALTREIKETFRELISLSKLFREQPALLS 151

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31377667   173 RLLDSLPREALPDILTSIIRTSNKEKLQ-ILDAVSLEERFKMTIPLLVRQIEGLKLLQK-TRKPKQ---DDDKRVIAIRP 247
Cdd:TIGR00763 152 ALEDIDEPGRLADFVAASLQLKEKDELQeVLETVNIEKRLKKALELLKKELELLKLQNKiTKKVEEkmeKTQREYYLREQ 231

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31377667   248 IRRITHISGTlededEDEDNDDIVMLEKKIRTSSMPEQAHKVCVKEIKRLKKMPQSMPEYALTRNYLELMVELPWNKSTT 327
Cdd:TIGR00763 232 LKAIKKELGI-----EKDDKDELEKLKEKLEELKLPEEVKKVIEKELTKLSLLEPSSSEFTVTRNYLDWLTDLPWGKYSK 306

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31377667   328 DRLDIRAARILLDNDHYAMEKLKKRVLEYLAVRQLKNNLKGPILCFVGPPGVGKTSVGRSVAKTLGREFHRIALGGVCDQ 407
Cdd:TIGR00763 307 ENLDLKRAKEILDEDHYGLKKVKERILEYLAVQKLRGKMKGPILCLVGPPGVGKTSLGKSIAKALNRKFVRFSLGGVRDE 386

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31377667   408 SDIRGHRRTYVGSMPGRIINGLKTVGVNNPVFLLDEVDKLGKSLQGDPAAALLEVLDPEQNHNFTDHYLNVAFDLSQVLF 487
Cdd:TIGR00763 387 AEIRGHRRTYVGAMPGRIIQGLKKAKTKNPLFLLDEIDKIGSSFRGDPASALLEVLDPEQNNAFSDHYLDVPFDLSKVIF 466

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31377667   488 IATANTTATIPAALLDRMEIIQVPGYTQEEKIEIAHRHLIPKQLEQHGLTPQQIQIPQVTTLDIITRYTREAGVRSLDRK 567
Cdd:TIGR00763 467 IATANSIDTIPRPLLDRMEVIELSGYTEEEKLEIAKKYLIPKALEDHGLKPDELKITDEALLLLIKYYTREAGVRNLERQ 546

                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31377667   568 LGAICRAVAVKVAEGQHKEAkldrsdvteregcrehiledEKPESISDTTDLalppempilidfhaLKDILGPPMYEMEV 647
Cdd:TIGR00763 547 IEKICRKAAVKLVEQGEKKK--------------------SEAESVVITPDN--------------LKKYLGKPVFTYER 592

                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31377667   648 SQRLSQPGVAIGLAWTPLGGEIMFVEASRMDGEGQLTLTGQLGDVMKESAHLAISWLRSNAKKYQLTNafgsfDLLDNTD 727
Cdd:TIGR00763 593 AYEVTPPGVVMGLAWTPMGGDTLFIETTKVAGKGSLELTGQLGDVMKESAQIALTYVRSIAADLGISP-----NFFEKAD 667

                         730       740       750       760       770       780       790       800
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31377667   728 IHLHFPAGAVTKDGPSAGVTIVTCLASLFSGRLVRSDVAMTGEITLRGLVLPVGGIKDKVLAAHRAGLKQVIIPRRNEKD 807
Cdd:TIGR00763 668 IHLHVPEGATPKDGPSAGITMATALLSLATGKPVRPDVAMTGEITLRGKVLPIGGLKEKTIAAKRAGIKTIILPEKNRRD 747

                         810       820
                  ....*....|....*....|....*...
gi 31377667   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 31377667   65 DPASDAQDLPPLHRIGTAALAVQVVgsNWPKPHYTLLITGLCRFQIVQVLKEKPYPIAEVEQLD--RLEEFPNTCKMREE 142
Cdd:PRK10787  57 EASTDEPGVNDLFTVGTVASILQML--KLPDGTVKVLVEGLQRARISALSDNGEHFSAKAEYLEspTIDEREQEVLVRTA 134

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31377667  143 LGELsEQFYKYAVQLVEMLDMSVPAVAKLRRLLDSLPREaLPDILtsiirtsnKEKLQILDAVSLEERFKMTIPLLVRQI 222
Cdd:PRK10787 135 ISQF-EGYIKLNKKIPPEVLTSLNSIDDPARLADTIAAH-MPLKL--------ADKQSVLEMSDVNERLEYLMAMMESEI 204

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31377667  223 EGLKLLQKTR---KPKQDDDKRVIAI-RPIRRITHISGTLEDEDEDEDNddivmLEKKIRTSSMPEQAHKVCVKEIKRLK 298
Cdd:PRK10787 205 DLLQVEKRIRnrvKKQMEKSQREYYLnEQMKAIQKELGEMDDAPDENEA-----LKRKIDAAKMPKEAKEKAEAELQKLK 279

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31377667  299 KMPQSMPEYALTRNYLELMVELPWNKSTTDRLDIRAARILLDNDHYAMEKLKKRVLEYLAVRQLKNNLKGPILCFVGPPG 378
Cdd:PRK10787 280 MMSPMSAEATVVRGYIDWMVQVPWNARSKVKKDLRQAQEILDTDHYGLERVKDRILEYLAVQSRVNKIKGPILCLVGPPG 359

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31377667  379 VGKTSVGRSVAKTLGREFHRIALGGVCDQSDIRGHRRTYVGSMPGRIINGLKTVGVNNPVFLLDEVDKLGKSLQGDPAAA 458
Cdd:PRK10787 360 VGKTSLGQSIAKATGRKYVRMALGGVRDEAEIRGHRRTYIGSMPGKLIQKMAKVGVKNPLFLLDEIDKMSSDMRGDPASA 439

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31377667  459 LLEVLDPEQNHNFTDHYLNVAFDLSQVLFIATANTTaTIPAALLDRMEIIQVPGYTQEEKIEIAHRHLIPKQLEQHGLTP 538
Cdd:PRK10787 440 LLEVLDPEQNVAFSDHYLEVDYDLSDVMFVATSNSM-NIPAPLLDRMEVIRLSGYTEDEKLNIAKRHLLPKQIERNALKK 518

                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31377667  539 QQIQIPQVTTLDIITRYTREAGVRSLDRKLGAICRAvAVKVaegqhkeakldrsdvteregcrehILEDEKPESisdttd 618
Cdd:PRK10787 519 GELTVDDSAIIGIIRYYTREAGVRSLEREISKLCRK-AVKQ------------------------LLLDKSLKH------ 567

                        570       580       590       600       610       620       630       640
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31377667  619 lalppempILIDFHALKDILGPPMYEMEVSQRLSQPGVAIGLAWTPLGGEIMFVEASRMDGEGQLTLTGQLGDVMKESAH 698
Cdd:PRK10787 568 --------IEINGDNLHDYLGVQRFDYGRADNENRVGQVTGLAWTEVGGDLLTIETACVPGKGKLTYTGSLGEVMQESIQ 639

                        650       660       670       680       690       700       710       720
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31377667  699 LAISWLRSNAKKYQLTNAFgsfdlLDNTDIHLHFPAGAVTKDGPSAGVTIVTCLASLFSGRLVRSDVAMTGEITLRGLVL 778
Cdd:PRK10787 640 AALTVVRARAEKLGINPDF-----YEKRDIHVHVPEGATPKDGPSAGIAMCTALVSCLTGNPVRADVAMTGEITLRGQVL 714

                        730       740       750       760       770
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 31377667  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 31377667 332 IRAARILLDNDHYAMEKLKKRVLEYLAVRQLKNNLKGPILCFVGPPGVGKTSVGRSVAKTLGREFHRIALGGVCDQSDIR 411
Cdd:cd19500   1 IKKARKVLDADHYGLEDVKERILEYLAVRKLKGSMKGPILCLVGPPGVGKTSLGKSIARALGRKFVRISLGGVRDEAEIR 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31377667 412 GHRRTYVGSMPGRIINGLKTVGVNNPVFLLDEVDKLGKSLQGDPAAALLEVLDPEQNHNFTDHYLNVAFDLSQVLFIATA 491
Cdd:cd19500  81 GHRRTYVGAMPGRIIQALKKAGTNNPVFLLDEIDKIGSSFRGDPASALLEVLDPEQNSTFSDHYLDVPFDLSKVLFIATA 160

                       170       180
                ....*....|....*....|..
gi 31377667 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 31377667   634 LKDILGPPMYEMEVSQRLSQPGVAIGLAWTPLGGEIMFVEASRMDGEGQLTLTGQLGDVMKESAHLAISWLRSNAKKYQL 713
Cdd:pfam05362   7 LEKYLGVPRFRYGEAEKEDQVGVVTGLAWTEVGGDLLTIEAVIMPGKGKLTLTGQLGDVMKESAQAALSYVRSRAEELGI 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31377667   714 tnafgSFDLLDNTDIHLHFPAGAVTKDGPSAGVTIVTCLASLFSGRLVRSDVAMTGEITLRGLVLPVGGIKDKVLAAHRA 793
Cdd:pfam05362  87 -----DPDFFEKKDIHIHVPEGATPKDGPSAGVTMATALVSALTGIPVRKDVAMTGEITLRGRVLPIGGLKEKLLAAHRA 161

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 31377667   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 31377667    13 LPLLLTHEGVLLPGSTMRTSVDSARNLQLVRSRLLKGtslQSTILGVIPNTpDPASDAQDLPPLHRIGTAALAVQVVGSn 92
Cdd:pfam02190   2 LPLLPLRNTVLFPGMVLPLFVGRPRSIAAIEAALNKD---KLYGVLLVSQK-DAEDEEPTPDDLYEVGTVAKIVQILKL- 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31377667    93 wPKPHYTLLITGLCRFQIVQVL-KEKPYPIAEVEQLDrleefpntcKMREELGELSEQFYKYAVQ-LVEMLDMSVPAVAK 170
Cdd:pfam02190  77 -PDGTYKVLVEGLERVRIVELVkKEEPYLRAEVEDLP---------EDSDELSEALKALVKELIEkLRRLLKLLLPLELL 146

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 31377667   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 31377667   371 LCFVGPPGVGKTSVGRSVAKTLGREFHRIALGGVCDqsdirghrrTYVGSMPGRIINGLKTVGVNNP-VFLLDEVDKLGK 449
Cdd:pfam00004   1 LLLYGPPGTGKTTLAKAVAKELGAPFIEISGSELVS---------KYVGESEKRLRELFEAAKKLAPcVIFIDEIDALAG 71

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 31377667   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 31377667 723 LDNTDIHLHFPAGAVTKDGPSAGVTIVTCLASLFSGRLVRSDVAMTGEITLRGLVLPVGGIKDKVLAAHRAGLKQVIIPR 802
Cdd:COG1750  91 LSSYDVYISIESDSPIVGGPSAGGAMTVATYAALLGLPLNKSVTMTGMINPDGSIGPVGGVYEKLEAAASAGAKYFLIPK 170


                ...
gi 31377667 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 31377667 337 ILLDNdhyAMEKLKKRVLEYLAVRQLKNNLKGPI---LCFVGPPGVGKTSVGRSVAKTLGREFHRIALGGVCDQsdirgh 413
Cdd:COG0464 160 GGLEE---VKEELRELVALPLKRPELREEYGLPPprgLLLYGPPGTGKTLLARALAGELGLPLIEVDLSDLVSK------ 230

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31377667 414 rrtYVGSMPGRIINGLKTV-GVNNPVFLLDEVDKLGKSLQGDpaaallevldpeqnhnfTDHYLNVAFD---------LS 483
Cdd:COG0464 231 ---YVGETEKNLREVFDKArGLAPCVLFIDEADALAGKRGEV-----------------GDGVGRRVVNtlltemeelRS 290

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|
gi 31377667 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 31377667 345 AMEKLKKRVLEYLAVRQL--KNNLKGPILCFVGPPGVGKTSVGRSVAKTLGREFHRIALGGVCDQSdirghrRTYVGSMP 422
Cdd:cd19481   1 LKASLREAVEAPRRGSRLrrYGLGLPKGILLYGPPGTGKTLLAKALAGELGLPLIVVKLSSLLSKY------VGESEKNL 74

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31377667 423 GRIINGLKTVGvnNPVFLLDEVDKLGK--SLQGDPAA------ALLEVLDPEQNhnftdhylnvafdLSQVLFIATANTT 494
Cdd:cd19481  75 RKIFERARRLA--PCILFIDEIDAIGRkrDSSGESGElrrvlnQLLTELDGVNS-------------RSKVLVIAATNRP 139

                       170
                ....*....|
gi 31377667 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 31377667 352 RVLEYLAVRQLKNNLKGPILCFVGPPGVGKTSVGRSVAKTL---GREFHRIALGGVCDQSDIRGHRRTYvgsmPGRIING 428
Cdd:cd00009   3 QEEAIEALREALELPPPKNLLLYGPPGTGKTTLARAIANELfrpGAPFLYLNASDLLEGLVVAELFGHF----LVRLLFE 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31377667 429 LKTVGvNNPVFLLDEVDKLGKSLQgdpaAALLEVLDpeqnhnfTDHYLNVAFDLSQVLFIATANTTATIPAALLDRMEII 508
Cdd:cd00009  79 LAEKA-KPGVLFIDEIDSLSRGAQ----NALLRVLE-------TLNDLRIDRENVRVIGATNRPLLGDLDRALYDRLDIR 146


                ....*
gi 31377667 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 31377667 366 LKGPILcFVGPPGVGKTSVGRSVAKTLGREFHRIalggvcdQsdirghrrTYVGSMPGRIInglktvGVNN--------- 436
Cdd:COG0714  30 AGGHLL-LEGVPGVGKTTLAKALARALGLPFIRI-------Q--------FTPDLLPSDIL------GTYIydqqtgefe 87

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31377667 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 31377667 500 ALLDRMEI-IQVpGY-TQEEKIEIAHRHLIPKQLE-QHGLTPQQI-----QIPQVTTLDIITRY-------TREAGvrsl 564
Cdd:COG0714 156 AQLDRFLLkLYI-GYpDAEEEREILRRHTGRHLAEvEPVLSPEELlalqeLVRQVHVSEAVLDYivdlvraTREHP---- 230


                ....*.
gi 31377667 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 31377667   371 LCFVGPPGVGKTSVGRSVAK-TLGREFHRIALGGVCDQSDIRGHRRtyVGSMPGRIING-LKTVGVNNPVFLLDEVDKLG 448
Cdd:pfam07728   2 VLLVGPPGTGKTELAERLAAaLSNRPVFYVQLTRDTTEEDLFGRRN--IDPGGASWVDGpLVRAAREGEIAVLDEINRAN 79

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 31377667   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 31377667 341 NDHYAMEKLK---KRVLEYLAVRQL--KNNLKGP--ILcFVGPPGVGKTSVGRSVAKTLGREFHRIALGGVCDQsdirgh 413
Cdd:COG1223   2 DDVVGQEEAKkklKLIIKELRRRENlrKFGLWPPrkIL-FYGPPGTGKTMLAEALAGELKLPLLTVRLDSLIGS------ 74

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31377667 414 rrtYVGSMPGRI------INGLKTvgvnnpVFLLDEVDKLGK-----SLQGDPAA---ALLEVLDPEQNHnftdhylnva 479
Cdd:COG1223  75 ---YLGETARNLrklfdfARRAPC------VIFFDEFDAIAKdrgdqNDVGEVKRvvnALLQELDGLPSG---------- 135

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*...
gi 31377667 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 31377667  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 31377667  369 PILCFVGP-PGVGKTSVGRSVAKTLGREFHRIAlGGVCDQSDIRGHRRTYVGSMpgriinglkTVGVNNPVFLLDEVDKL 447
Cdd:PHA02544  43 PNMLLHSPsPGTGKTTVAKALCNEVGAEVLFVN-GSDCRIDFVRNRLTRFASTV---------SLTGGGKVIIIDEFDRL 112

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31377667  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 31377667  373 FVGPPGVGKTSVGRSVAKTLGREFHRI--ALGGVcdqSDIRghrrtyvgsmpgRIINGLKT--VGVNNPVFLLDEVDKLG 448
Cdd:PRK13342  41 LWGPPGTGKTTLARIIAGATDAPFEALsaVTSGV---KDLR------------EVIEEARQrrSAGRRTILFIDEIHRFN 105

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31377667  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 31377667   373 FVGPPGVGKTSVGRSVAKTLG---REFHRIalggvcDQSDIrgHRRTYV----GSMPGRII---NGLKTVGVN-NP--VF 439
Cdd:pfam07724   8 FLGPTGVGKTELAKALAELLFgdeRALIRI------DMSEY--MEEHSVsrliGAPPGYVGyeeGGQLTEAVRrKPysIV 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31377667   440 LLDEVDKLGKSLQGDpaaaLLEVLDpeqNHNFTDHY-LNVAFDlsQVLFIATANTTATIPaalLDRMEIIQVPGY--TQE 516
Cdd:pfam07724  80 LIDEIEKAHPGVQND----LLQILE---GGTLTDKQgRTVDFK--NTLFIMTGNFGSEKI---SDASRLGDSPDYelLKE 147

                         170
                  ....*....|..
gi 31377667   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 31377667 358 AVRQLKNNLKGP-----ILCFVGPPGVGKTSVGRSVAKTL-GREFHRIALggvcDQS-DIRGHRRTYVGSMPGRIIngLK 430
Cdd:cd19499  26 AIRRARAGLSDPnrpigSFLFLGPTGVGKTELAKALAELLfGDEDNLIRI----DMSeYMEKHSVSRLIGAPPGYV--GY 99

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31377667 431 TVG-------VNNP--VFLLDEVDKLGKSLQGdpaaALLEVLDpeqNHNFTDHYLNVAfDLSQVLFIATANttaTIPAAL 501
Cdd:cd19499 100 TEGgqlteavRRKPysVVLLDEIEKAHPDVQN----LLLQVLD---DGRLTDSHGRTV-DFKNTIIIMTSN---HFRPEF 168


                ....*..
gi 31377667 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 31377667    367 KGPILCFVGPPGVGKTSVGRSVAKTLGREFHRI-------ALGGVCDQSDIRGHRRTYVGSMPGRIINGLKTV--GVNNP 437
Cdd:smart00382   1 PGEVILIVGPPGSGKTTLARALARELGPPGGGViyidgedILEEVLDQLLLIIVGGKKASGSGELRLRLALALarKLKPD 80

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 31377667    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 31377667 741 GPSAGvTIVTcLA--------SLFSGRlvrsDVAMTGEITLRGLVLPVGGIKDKVLAAHRAGLKQVIIPRRNEKDLEgip 812
Cdd:COG3480 240 GPSAG-LMFA-LGiydqltpgDLTGGK----KIAGTGTIDADGTVGPIGGIDQKVVAARRAGATIFLAPASNCAEAV--- 310

                        90       100
                ....*....|....*....|.
gi 31377667 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 31377667 740 DGPSAGVTIVTCLASLFSGRLVRSDVAMTGEITLRGLVLPVGGIKDKV-----LAAHRaGL--KQ-VIIPRRNEKDLegi 811
Cdd:COG1067 592 DGDSASSAELYALLSALSGVPIRQDIAVTGSVNQHGEVQPIGGVNEKIegffdVCKAR-GLtgKQgVIIPAANVKNL--- 667

                        90       100       110
                ....*....|....*....|....*....|....*.
gi 31377667 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 31377667 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 31377667 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 31377667 292 KEIKRLKKMPQSMpeyaLTRNYLELMVELPWNKSTTDRL-----DIRAARILLDN--DHYAMEKLKKRVLEYLAvRQLKN 364
Cdd:COG1419  81 RELAELKELLEEQ----LSGLAGESARLPPELAELLERLleagvSPELARELLEKlpEDLSAEEAWRALLEALA-RRLPV 155

                        90       100       110
                ....*....|....*....|....*....|.
gi 31377667 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 31377667 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 31377667  373 FVGPPGVGKTSVGRSVAKTLGREFHRIalggvcDQSDIrGHRRT---YVGSMPGRI---INGLKTVGV-NNP--VFLLDE 443
Cdd:PRK11034 493 FAGPTGVGKTEVTVQLSKALGIELLRF------DMSEY-MERHTvsrLIGAPPGYVgfdQGGLLTDAViKHPhaVLLLDE 565

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 31377667  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 31377667   375 GPPGVGKTSVGRSVAKTLGREFHRIALGGVCDQSDIRG------HRRTYVgSMPGriinglktvgvnnPVF----LLDEV 444
Cdd:pfam07726   6 GVPGLAKTLLVRTLARSLGLDFRRIQFTPDLLPSDITGtevfdqKTREFE-FRPG-------------PVFanvlLADEI 71

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 31377667   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 31377667 366 LKGPILCFVGPPGVGKTSVGRSVAKTLGREFHRIAlggVCDQSDIRGH 413
Cdd:COG4088   2 DSPMLLILTGPPGSGKTTFAKALAQRLYAEGIAVA---LLHSDDFRRF 46
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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