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Conserved domains on  [gi|1128611449|ref|NP_001335007|]
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lon protease homolog 2, peroxisomal isoform 3 [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: 984.89  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1128611449   1 MS-SVSPIQIPSRLPLLLTHEGVLLPGSTMRTSVDSARNLQLVRsRLLKGTSLqstiLGVI----PNTPDPASDAqdlpp 75
Cdd:COG0466     1 MSeEKEEEELPETLPLLPLRDVVVFPGMVIPLFVGREKSIKALE-EAMEGDKL----IGLVaqkdAEVEDPGPDD----- 70

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1128611449  76 LHRIGTAALAVQVVgsNWPKPHYTLLITGLCRFQIVQVLKEKPYPIAEVEQLDrlEEFPNTCKMREELGELSEQFYKYAv 155
Cdd:COG0466    71 LYEVGTVAKILQLL--KLPDGTVKVLVEGLQRARIKEFVQEEPYLEAEVEPLE--EEEEDDKELEALMRSLKEQFEEYV- 145

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1128611449 156 qlveMLDMSVP--AVAKLRRLLDSlprEALPDILTSIIRTSNKEKLQILDAVSLEERFKMTIPLLVRQIEGLKLLQKTR- 232
Cdd:COG0466   146 ----KLNPKIPpeLLAALSNIEDP---GRLADFIASHLPLKIEEKQELLETLDVKERLEKLLELLEKEIEVLELEKKIRs 218

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1128611449 233 KPKQDDDKR---------VIAIR-----------PIRRithisgtledededednddivmLEKKIRTSSMPEQAHKVCVK 292
Cdd:COG0466   219 RVKEQMEKSqreyylreqLKAIQkelgekddgedEIEE----------------------LREKIEKAKLPEEVKEKAEK 276

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1128611449 293 EIKRLKKMPQSMPEYALTRNYLELMVELPWNKSTTDRLDIRAARILLDNDHYAMEKLKKRVLEYLAVRQLKNNLKGPILC 372
Cdd:COG0466   277 ELKKLERMPPMSAEATVIRNYLDWLLDLPWGKRTKDNLDLKKAEKILDEDHYGLEKVKERILEYLAVRKLKKKLKGPILC 356

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1128611449 373 FVGPPGVGKTSVGRSVAKTLGREFHRIALGGVCDQSDIRGHRRTYVGSMPGRIINGLKTVGVNNPVFLLDEVDKLGKSLQ 452
Cdd:COG0466   357 LVGPPGVGKTSLGKSIARALGRKFVRISLGGVRDEAEIRGHRRTYIGAMPGRIIQGLKKAGTKNPVFLLDEIDKMGSDFR 436

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1128611449 453 GDPAAALLEVLDPEQNHNFTDHYLNVAFDLSQVLFIATANTTATIPAALLDRMEIIQVPGYTQEEKIEIAHRHLIPKQLE 532
Cdd:COG0466   437 GDPASALLEVLDPEQNNTFSDHYLEVPFDLSKVMFIATANSLDTIPAPLLDRMEIIELSGYTEEEKLEIAKRYLIPKQLK 516

                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1128611449 533 QHGLTPQQIQIPQVTTLDIITRYTREAGVRSLDRKLGAICRAVAVKVAEGQHKEAKLDRSDvteregcrehiledekpes 612
Cdd:COG0466   517 EHGLKKEELKISDEALRKIIRGYTREAGVRNLEREIAKICRKVAKKIAEGKKKKVTITPKN------------------- 577

                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1128611449 613 isdttdlalppempilidfhaLKDILGPPMYEMEVSQRLSQPGVAIGLAWTPLGGEIMFVEASRMDGEGQLTLTGQLGDV 692
Cdd:COG0466   578 ---------------------LEKYLGVPRFRYEKAEEEDQVGVVTGLAWTEVGGDILFIEATLMPGKGKLTLTGQLGDV 636

                         730       740       750       760       770       780       790       800
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1128611449 693 MKESAHLAISWLRSNAKKYQLtnafgSFDLLDNTDIHLHFPAGAVTKDGPSAGVTIVTCLASLFSGRLVRSDVAMTGEIT 772
Cdd:COG0466   637 MKESAQAALSYVRSRAEELGI-----DPDFFEKYDIHIHVPEGATPKDGPSAGITMATALVSALTGRPVRSDVAMTGEIT 711

                         810       820       830       840       850       860
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1128611449 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: 984.89  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1128611449   1 MS-SVSPIQIPSRLPLLLTHEGVLLPGSTMRTSVDSARNLQLVRsRLLKGTSLqstiLGVI----PNTPDPASDAqdlpp 75
Cdd:COG0466     1 MSeEKEEEELPETLPLLPLRDVVVFPGMVIPLFVGREKSIKALE-EAMEGDKL----IGLVaqkdAEVEDPGPDD----- 70

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1128611449  76 LHRIGTAALAVQVVgsNWPKPHYTLLITGLCRFQIVQVLKEKPYPIAEVEQLDrlEEFPNTCKMREELGELSEQFYKYAv 155
Cdd:COG0466    71 LYEVGTVAKILQLL--KLPDGTVKVLVEGLQRARIKEFVQEEPYLEAEVEPLE--EEEEDDKELEALMRSLKEQFEEYV- 145

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1128611449 156 qlveMLDMSVP--AVAKLRRLLDSlprEALPDILTSIIRTSNKEKLQILDAVSLEERFKMTIPLLVRQIEGLKLLQKTR- 232
Cdd:COG0466   146 ----KLNPKIPpeLLAALSNIEDP---GRLADFIASHLPLKIEEKQELLETLDVKERLEKLLELLEKEIEVLELEKKIRs 218

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1128611449 233 KPKQDDDKR---------VIAIR-----------PIRRithisgtledededednddivmLEKKIRTSSMPEQAHKVCVK 292
Cdd:COG0466   219 RVKEQMEKSqreyylreqLKAIQkelgekddgedEIEE----------------------LREKIEKAKLPEEVKEKAEK 276

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1128611449 293 EIKRLKKMPQSMPEYALTRNYLELMVELPWNKSTTDRLDIRAARILLDNDHYAMEKLKKRVLEYLAVRQLKNNLKGPILC 372
Cdd:COG0466   277 ELKKLERMPPMSAEATVIRNYLDWLLDLPWGKRTKDNLDLKKAEKILDEDHYGLEKVKERILEYLAVRKLKKKLKGPILC 356

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1128611449 373 FVGPPGVGKTSVGRSVAKTLGREFHRIALGGVCDQSDIRGHRRTYVGSMPGRIINGLKTVGVNNPVFLLDEVDKLGKSLQ 452
Cdd:COG0466   357 LVGPPGVGKTSLGKSIARALGRKFVRISLGGVRDEAEIRGHRRTYIGAMPGRIIQGLKKAGTKNPVFLLDEIDKMGSDFR 436

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1128611449 453 GDPAAALLEVLDPEQNHNFTDHYLNVAFDLSQVLFIATANTTATIPAALLDRMEIIQVPGYTQEEKIEIAHRHLIPKQLE 532
Cdd:COG0466   437 GDPASALLEVLDPEQNNTFSDHYLEVPFDLSKVMFIATANSLDTIPAPLLDRMEIIELSGYTEEEKLEIAKRYLIPKQLK 516

                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1128611449 533 QHGLTPQQIQIPQVTTLDIITRYTREAGVRSLDRKLGAICRAVAVKVAEGQHKEAKLDRSDvteregcrehiledekpes 612
Cdd:COG0466   517 EHGLKKEELKISDEALRKIIRGYTREAGVRNLEREIAKICRKVAKKIAEGKKKKVTITPKN------------------- 577

                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1128611449 613 isdttdlalppempilidfhaLKDILGPPMYEMEVSQRLSQPGVAIGLAWTPLGGEIMFVEASRMDGEGQLTLTGQLGDV 692
Cdd:COG0466   578 ---------------------LEKYLGVPRFRYEKAEEEDQVGVVTGLAWTEVGGDILFIEATLMPGKGKLTLTGQLGDV 636

                         730       740       750       760       770       780       790       800
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1128611449 693 MKESAHLAISWLRSNAKKYQLtnafgSFDLLDNTDIHLHFPAGAVTKDGPSAGVTIVTCLASLFSGRLVRSDVAMTGEIT 772
Cdd:COG0466   637 MKESAQAALSYVRSRAEELGI-----DPDFFEKYDIHIHVPEGATPKDGPSAGITMATALVSALTGRPVRSDVAMTGEIT 711

                         810       820       830       840       850       860
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1128611449 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: 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 2.78e-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: 2.78e-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 hydrolyse ATP ...
 634-837 5.03e-94

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: 294.53  E-value: 5.03e-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 1.86e-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: 1.86e-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, ...
 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: 984.89  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1128611449   1 MS-SVSPIQIPSRLPLLLTHEGVLLPGSTMRTSVDSARNLQLVRsRLLKGTSLqstiLGVI----PNTPDPASDAqdlpp 75
Cdd:COG0466     1 MSeEKEEEELPETLPLLPLRDVVVFPGMVIPLFVGREKSIKALE-EAMEGDKL----IGLVaqkdAEVEDPGPDD----- 70

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1128611449  76 LHRIGTAALAVQVVgsNWPKPHYTLLITGLCRFQIVQVLKEKPYPIAEVEQLDrlEEFPNTCKMREELGELSEQFYKYAv 155
Cdd:COG0466    71 LYEVGTVAKILQLL--KLPDGTVKVLVEGLQRARIKEFVQEEPYLEAEVEPLE--EEEEDDKELEALMRSLKEQFEEYV- 145

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1128611449 156 qlveMLDMSVP--AVAKLRRLLDSlprEALPDILTSIIRTSNKEKLQILDAVSLEERFKMTIPLLVRQIEGLKLLQKTR- 232
Cdd:COG0466   146 ----KLNPKIPpeLLAALSNIEDP---GRLADFIASHLPLKIEEKQELLETLDVKERLEKLLELLEKEIEVLELEKKIRs 218

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1128611449 233 KPKQDDDKR---------VIAIR-----------PIRRithisgtledededednddivmLEKKIRTSSMPEQAHKVCVK 292
Cdd:COG0466   219 RVKEQMEKSqreyylreqLKAIQkelgekddgedEIEE----------------------LREKIEKAKLPEEVKEKAEK 276

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1128611449 293 EIKRLKKMPQSMPEYALTRNYLELMVELPWNKSTTDRLDIRAARILLDNDHYAMEKLKKRVLEYLAVRQLKNNLKGPILC 372
Cdd:COG0466   277 ELKKLERMPPMSAEATVIRNYLDWLLDLPWGKRTKDNLDLKKAEKILDEDHYGLEKVKERILEYLAVRKLKKKLKGPILC 356

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1128611449 373 FVGPPGVGKTSVGRSVAKTLGREFHRIALGGVCDQSDIRGHRRTYVGSMPGRIINGLKTVGVNNPVFLLDEVDKLGKSLQ 452
Cdd:COG0466   357 LVGPPGVGKTSLGKSIARALGRKFVRISLGGVRDEAEIRGHRRTYIGAMPGRIIQGLKKAGTKNPVFLLDEIDKMGSDFR 436

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1128611449 453 GDPAAALLEVLDPEQNHNFTDHYLNVAFDLSQVLFIATANTTATIPAALLDRMEIIQVPGYTQEEKIEIAHRHLIPKQLE 532
Cdd:COG0466   437 GDPASALLEVLDPEQNNTFSDHYLEVPFDLSKVMFIATANSLDTIPAPLLDRMEIIELSGYTEEEKLEIAKRYLIPKQLK 516

                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1128611449 533 QHGLTPQQIQIPQVTTLDIITRYTREAGVRSLDRKLGAICRAVAVKVAEGQHKEAKLDRSDvteregcrehiledekpes 612
Cdd:COG0466   517 EHGLKKEELKISDEALRKIIRGYTREAGVRNLEREIAKICRKVAKKIAEGKKKKVTITPKN------------------- 577

                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1128611449 613 isdttdlalppempilidfhaLKDILGPPMYEMEVSQRLSQPGVAIGLAWTPLGGEIMFVEASRMDGEGQLTLTGQLGDV 692
Cdd:COG0466   578 ---------------------LEKYLGVPRFRYEKAEEEDQVGVVTGLAWTEVGGDILFIEATLMPGKGKLTLTGQLGDV 636

                         730       740       750       760       770       780       790       800
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1128611449 693 MKESAHLAISWLRSNAKKYQLtnafgSFDLLDNTDIHLHFPAGAVTKDGPSAGVTIVTCLASLFSGRLVRSDVAMTGEIT 772
Cdd:COG0466   637 MKESAQAALSYVRSRAEELGI-----DPDFFEKYDIHIHVPEGATPKDGPSAGITMATALVSALTGRPVRSDVAMTGEIT 711

                         810       820       830       840       850       860
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1128611449 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: 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 2.78e-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: 2.78e-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 hydrolyse ATP ...
 634-837 5.03e-94

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: 294.53  E-value: 5.03e-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 6.35e-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 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: 111.66  E-value: 6.35e-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 1.10e-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: 105.75  E-value: 1.10e-26
                          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
COG1750 COG1750
Predicted archaeal serine protease, S18 family [General function prediction only];
723-805 7.12e-16

Predicted archaeal serine protease, S18 family [General function prediction only];


Pssm-ID: 441356 [Multi-domain]  Cd Length: 213  Bit Score: 77.33  E-value: 7.12e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1128611449 723 LDNTDIHLHFPAGAVTKDGPSAGVTIVTCLASLFSGRLVRSDVAMTGEITLRGLVLPVGGIKDKVLAAHRAGLKQVIIPR 802
Cdd:COG1750    91 LSSYDVYISIESDSPIVGGPSAGGAMTVATYAALLGLPLNKSVTMTGMINPDGSIGPVGGVYEKLEAAASAGAKYFLIPK 170


                  ...
gi 1128611449 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 1.78e-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: 76.49  E-value: 1.78e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1128611449 337 ILLDNdhyAMEKLKKRVLEYLAVRQLKNNLKGPI---LCFVGPPGVGKTSVGRSVAKTLGREFHRIALGGVCDQsdirgh 413
Cdd:COG0464   160 GGLEE---VKEELRELVALPLKRPELREEYGLPPprgLLLYGPPGTGKTLLARALAGELGLPLIEVDLSDLVSK------ 230

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1128611449 414 rrtYVGSMPGRIINGLKTV-GVNNPVFLLDEVDKLGKSLQGDpaaallevldpeqnhnfTDHYLNVAFD---------LS 483
Cdd:COG0464   231 ---YVGETEKNLREVFDKArGLAPCVLFIDEADALAGKRGEV-----------------GDGVGRRVVNtlltemeelRS 290

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 1128611449 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 3.55e-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: 3.55e-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 4.18e-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: 4.18e-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
MoxR COG0714
MoxR-like ATPase [General function prediction only]; MoxR-like ATPase is part of the Pathway ...
 366-570 2.99e-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: 62.11  E-value: 2.99e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1128611449 366 LKGPILcFVGPPGVGKTSVGRSVAKTLGREFHRIalggvcdQsdirghrrTYVGSMPGRIInglktvGVNN--------- 436
Cdd:COG0714    30 AGGHLL-LEGVPGVGKTTLAKALARALGLPFIRI-------Q--------FTPDLLPSDIL------GTYIydqqtgefe 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1128611449 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 1128611449 500 ALLDRMEI-IQVpGY-TQEEKIEIAHRHLIPKQLE-QHGLTPQQI-----QIPQVTTLDIITRY-------TREAGvrsl 564
Cdd:COG0714   156 AQLDRFLLkLYI-GYpDAEEEREILRRHTGRHLAEvEPVLSPEELlalqeLVRQVHVSEAVLDYivdlvraTREHP---- 230


                  ....*.
gi 1128611449 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 5.87e-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: 5.87e-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
COG1223 COG1223
Predicted ATPase, AAA+ superfamily [General function prediction only];
341-526 1.49e-07

Predicted ATPase, AAA+ superfamily [General function prediction only];


Pssm-ID: 440836 [Multi-domain]  Cd Length: 246  Bit Score: 53.35  E-value: 1.49e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1128611449 341 NDHYAMEKLK---KRVLEYLAVRQL--KNNLKGP--ILcFVGPPGVGKTSVGRSVAKTLGREFHRIALGGVCDQsdirgh 413
Cdd:COG1223     2 DDVVGQEEAKkklKLIIKELRRRENlrKFGLWPPrkIL-FYGPPGTGKTMLAEALAGELKLPLLTVRLDSLIGS------ 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1128611449 414 rrtYVGSMPGRI------INGLKTvgvnnpVFLLDEVDKLGK-----SLQGDPAA---ALLEVLDPEQNHnftdhylnva 479
Cdd:COG1223    75 ---YLGETARNLrklfdfARRAPC------VIFFDEFDAIAKdrgdqNDVGEVKRvvnALLQELDGLPSG---------- 135

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 1128611449 480 fdlsqVLFIATANTTATIPAALLDRM-EIIQVPGYTQEEKIEIAHRHL 526
Cdd:COG1223   136 -----SVVIAATNHPELLDSALWRRFdEVIEFPLPDKEERKEILELNL 178
aroK PRK00131
shikimate kinase; Reviewed
 366-396 2.25e-06

shikimate kinase; Reviewed


Pssm-ID: 234654 [Multi-domain]  Cd Length: 175  Bit Score: 48.65  E-value: 2.25e-06
                          10        20        30
                  ....*....|....*....|....*....|.
gi 1128611449 366 LKGPILCFVGPPGVGKTSVGRSVAKTLGREF 396
Cdd:PRK00131    2 LKGPNIVLIGFMGAGKSTIGRLLAKRLGYDF 32
PRK13342 PRK13342
recombination factor protein RarA; Reviewed
 373-524 1.13e-05

recombination factor protein RarA; Reviewed


Pssm-ID: 237355 [Multi-domain]  Cd Length: 413  Bit Score: 48.93  E-value: 1.13e-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 1.26e-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: 1.26e-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
44 PHA02544
clamp loader, small subunit; Provisional
 369-522 1.35e-05

clamp loader, small subunit; Provisional


Pssm-ID: 222866 [Multi-domain]  Cd Length: 316  Bit Score: 48.06  E-value: 1.35e-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 1.47e-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: 1.47e-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
AAA smart00382
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ...
 367-505 1.86e-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: 1.86e-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
SdrC COG3480
Predicted secreted protein YlbL, contains PDZ domain [Signal transduction mechanisms];
741-833 4.29e-05

Predicted secreted protein YlbL, contains PDZ domain [Signal transduction mechanisms];


Pssm-ID: 442703 [Multi-domain]  Cd Length: 344  Bit Score: 46.73  E-value: 4.29e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1128611449 741 GPSAGvTIVTcLA--------SLFSGRlvrsDVAMTGEITLRGLVLPVGGIKDKVLAAHRAGLKQVIIPRRNEKDLEgip 812
Cdd:COG3480   240 GPSAG-LMFA-LGiydqltpgDLTGGK----KIAGTGTIDADGTVGPIGGIDQKVVAARRAGATIFLAPASNCAEAV--- 310

                          90       100
                  ....*....|....*....|.
gi 1128611449 813 GNVRQDLSFVTASCLDEVLNA 833
Cdd:COG3480   311 GTIPTGLKVVPVDTLDDALDA 331
LonB COG1067
Predicted ATP-dependent protease [Posttranslational modification, protein turnover, chaperones] ...
 740-843 5.15e-05

Predicted ATP-dependent protease [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 440686 [Multi-domain]  Cd Length: 742  Bit Score: 47.25  E-value: 5.15e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1128611449 740 DGPSAGVTIVTCLASLFSGRLVRSDVAMTGEITLRGLVLPVGGIKDKV-----LAAHRaGL--KQ-VIIPRRNEKDLegi 811
Cdd:COG1067   592 DGDSASSAELYALLSALSGVPIRQDIAVTGSVNQHGEVQPIGGVNEKIegffdVCKAR-GLtgKQgVIIPAANVKNL--- 667

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 1128611449 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 6.94e-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: 44.35  E-value: 6.94e-05
                          10        20
                  ....*....|....*....|....*..
gi 1128611449 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 9.73e-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: 9.73e-05
                          10        20
                  ....*....|....*....|...
gi 1128611449 374 VGPPGVGKTSVGRSVAKTLGREF 396
Cdd:cd00464     5 IGMMGAGKTTVGRLLAKALGLPF 27
FlhF COG1419
Flagellar biosynthesis GTPase FlhF [Cell motility];
292-390 1.01e-04

Flagellar biosynthesis GTPase FlhF [Cell motility];


Pssm-ID: 441029 [Multi-domain]  Cd Length: 361  Bit Score: 45.63  E-value: 1.01e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1128611449 292 KEIKRLKKMPQSMpeyaLTRNYLELMVELPWNKSTTDRL-----DIRAARILLDN--DHYAMEKLKKRVLEYLAvRQLKN 364
Cdd:COG1419    81 RELAELKELLEEQ----LSGLAGESARLPPELAELLERLleagvSPELARELLEKlpEDLSAEEAWRALLEALA-RRLPV 155

                          90       100       110
                  ....*....|....*....|....*....|.
gi 1128611449 365 NL-----KGPILCFVGPPGVGKTSvgrSVAK 390
Cdd:COG1419   156 AEdplldEGGVIALVGPTGVGKTT---TIAK 183
RarA COG2256
Replication-associated recombination protein RarA (DNA-dependent ATPase) [Replication, ...
 375-411 2.14e-04

Replication-associated recombination protein RarA (DNA-dependent ATPase) [Replication, recombination and repair];


Pssm-ID: 441857 [Multi-domain]  Cd Length: 439  Bit Score: 44.66  E-value: 2.14e-04
                          10        20        30
                  ....*....|....*....|....*....|....*....
gi 1128611449 375 GPPGVGKTSVGRSVAKTLGREFHRI--ALGGVcdqSDIR 411
Cdd:COG2256    56 GPPGTGKTTLARLIANATDAEFVALsaVTSGV---KDIR 91
clpA PRK11034
ATP-dependent Clp protease ATP-binding subunit; Provisional
 373-492 4.86e-04

ATP-dependent Clp protease ATP-binding subunit; Provisional


Pssm-ID: 236828 [Multi-domain]  Cd Length: 758  Bit Score: 44.06  E-value: 4.86e-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
AAA_3 pfam07726
ATPase family associated with various cellular activities (AAA); This Pfam entry includes some ...
 375-504 2.35e-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: 2.35e-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
Kti12 COG4088
tRNA uridine 5-carbamoylmethylation protein Kti12 (Killer toxin insensitivity protein) ...
 366-413 4.07e-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: 39.32  E-value: 4.07e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 1128611449 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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