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Conserved domains on  [gi|118573575|sp|Q8CGK3|]
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RecName: Full=Lon protease homolog, mitochondrial; AltName: Full=Lon protease-like protein; Short=LONP; AltName: Full=Mitochondrial ATP-dependent protease Lon; AltName: Full=Serine protease 15; Flags: Precursor

Protein Classification

endopeptidase La( domain architecture ID 11489643)

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 TIGR00763
endopeptidase La; This protein, the ATP-dependent serine endopeptidase La, is induced by heat ...
 113-936 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: 1196.34  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118573575  113 PLIAITRNPVFPRFIKIVEVKNKKLVELLRRKVRLAQPYVGVFLKRDDNNESDvveSLDEIYHTGTFAQIHEMQDLGD-- 190
Cdd:TIGR00763   1 PLLPLRRRPLFPGMIKPIDVGREKSIKLIKEALRLKQPYLGLFLQKDDDNEEP---EEDDIYSVGVVAQILEMLPLPSsg 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118573575  191 --KLRMIVTGHRRIHIsrqlevepeglepeaekqksrrklkrgkKEVEDElgpkpqlemvteaatdtsKEVLMVEVENVA 268
Cdd:TIGR00763  78 taTYKVVVEGLRRIRI----------------------------KELSDK------------------GGYLVVRVDNLK 111

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118573575  269 HEDFQV-TEEVKALTAEIVKTIRDIIALNPLYRESVLQMMQAGQrvVDNPIYLSDMGAALTG-AESHELQDVLEETNILK 346
Cdd:TIGR00763 112 EEPFDKdDEEIKALTREIKETFRELISLSKLFREQPALLSALED--IDEPGRLADFVAASLQlKEKDELQEVLETVNIEK 189

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118573575  347 RLYKALSLLKKEFELSKLQQRLGREVEEKIKQTHRKYLLQEQLKIIKKELGLEKDDKDAIEeKFRERLRELVVPKHVMDV 426
Cdd:TIGR00763 190 RLKKALELLKKELELLKLQNKITKKVEEKMEKTQREYYLREQLKAIKKELGIEKDDKDELE-KLKEKLEELKLPEEVKKV 268

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118573575  427 VDEELSKLALLDNHSSEFNVTRNYLDWLTSIPWGRQSDENLDLARAQAVLEEDHYGMEDVKKRVLEFIAVSQLRGSTQGK 506
Cdd:TIGR00763 269 IEKELTKLSLLEPSSSEFTVTRNYLDWLTDLPWGKYSKENLDLKRAKEILDEDHYGLKKVKERILEYLAVQKLRGKMKGP 348

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118573575  507 ILCFHGPPGVGKTSIARSIARALGREYFRFSVGGMTDVAEIKGHRRTYVGAMPGKIIQCLKKTKTENPLVLIDEVDKIGR 586
Cdd:TIGR00763 349 ILCLVGPPGVGKTSLGKSIAKALNRKFVRFSLGGVRDEAEIRGHRRTYVGAMPGRIIQGLKKAKTKNPLFLLDEIDKIGS 428

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118573575  587 GYQGDPSSALLELLDPEQNANFLDHYLDVPVDLSKVLFICTANVIDTIPEPLRDRMEMINVSGYVAQEKLAIAERYLVPQ 666
Cdd:TIGR00763 429 SFRGDPASALLEVLDPEQNNAFSDHYLDVPFDLSKVIFIATANSIDTIPRPLLDRMEVIELSGYTEEEKLEIAKKYLIPK 508

                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118573575  667 ARTLCGLDESKAQLSAAVLTLLIKQYCRESGVRNLQKQVEKVLRKAAYKIVS------GEAQTVQVTPENLQDFVGKPVF 740
Cdd:TIGR00763 509 ALEDHGLKPDELKITDEALLLLIKYYTREAGVRNLERQIEKICRKAAVKLVEqgekkkSEAESVVITPDNLKKYLGKPVF 588

                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118573575  741 TVERMYEVTPPGVVMGLAWTAMGGSTLFVETSLRRPqpsgskedkDGSLEVTGQLGDVMKESARIAYTYARAFLMEQDPE 820
Cdd:TIGR00763 589 TYERAYEVTPPGVVMGLAWTPMGGDTLFIETTKVAG---------KGSLELTGQLGDVMKESAQIALTYVRSIAADLGIS 659

                         730       740       750       760       770       780       790       800
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118573575  821 NDFLVTSHIHLHVPEGATPKDGPSAGCTIVTALLSLALGQPVLQNLAMTGEVSLTGKVLPVGGIKEKTIAAKRAGVTCII 900
Cdd:TIGR00763 660 PNFFEKADIHLHVPEGATPKDGPSAGITMATALLSLATGKPVRPDVAMTGEITLRGKVLPIGGLKEKTIAAKRAGIKTII 739

                         810       820       830
                  ....*....|....*....|....*....|....*.
gi 118573575  901 LPAENRKDYSDLAPFITEGLEVHFVEHYRDIFPIAF 936
Cdd:TIGR00763 740 LPEKNRRDLEELPENVKEGLEIHFVKHYDEVLKKAF 775
 
Name Accession Description Interval E-value
lon TIGR00763
endopeptidase La; This protein, the ATP-dependent serine endopeptidase La, is induced by heat ...
 113-936 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: 1196.34  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118573575  113 PLIAITRNPVFPRFIKIVEVKNKKLVELLRRKVRLAQPYVGVFLKRDDNNESDvveSLDEIYHTGTFAQIHEMQDLGD-- 190
Cdd:TIGR00763   1 PLLPLRRRPLFPGMIKPIDVGREKSIKLIKEALRLKQPYLGLFLQKDDDNEEP---EEDDIYSVGVVAQILEMLPLPSsg 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118573575  191 --KLRMIVTGHRRIHIsrqlevepeglepeaekqksrrklkrgkKEVEDElgpkpqlemvteaatdtsKEVLMVEVENVA 268
Cdd:TIGR00763  78 taTYKVVVEGLRRIRI----------------------------KELSDK------------------GGYLVVRVDNLK 111

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118573575  269 HEDFQV-TEEVKALTAEIVKTIRDIIALNPLYRESVLQMMQAGQrvVDNPIYLSDMGAALTG-AESHELQDVLEETNILK 346
Cdd:TIGR00763 112 EEPFDKdDEEIKALTREIKETFRELISLSKLFREQPALLSALED--IDEPGRLADFVAASLQlKEKDELQEVLETVNIEK 189

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118573575  347 RLYKALSLLKKEFELSKLQQRLGREVEEKIKQTHRKYLLQEQLKIIKKELGLEKDDKDAIEeKFRERLRELVVPKHVMDV 426
Cdd:TIGR00763 190 RLKKALELLKKELELLKLQNKITKKVEEKMEKTQREYYLREQLKAIKKELGIEKDDKDELE-KLKEKLEELKLPEEVKKV 268

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118573575  427 VDEELSKLALLDNHSSEFNVTRNYLDWLTSIPWGRQSDENLDLARAQAVLEEDHYGMEDVKKRVLEFIAVSQLRGSTQGK 506
Cdd:TIGR00763 269 IEKELTKLSLLEPSSSEFTVTRNYLDWLTDLPWGKYSKENLDLKRAKEILDEDHYGLKKVKERILEYLAVQKLRGKMKGP 348

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118573575  507 ILCFHGPPGVGKTSIARSIARALGREYFRFSVGGMTDVAEIKGHRRTYVGAMPGKIIQCLKKTKTENPLVLIDEVDKIGR 586
Cdd:TIGR00763 349 ILCLVGPPGVGKTSLGKSIAKALNRKFVRFSLGGVRDEAEIRGHRRTYVGAMPGRIIQGLKKAKTKNPLFLLDEIDKIGS 428

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118573575  587 GYQGDPSSALLELLDPEQNANFLDHYLDVPVDLSKVLFICTANVIDTIPEPLRDRMEMINVSGYVAQEKLAIAERYLVPQ 666
Cdd:TIGR00763 429 SFRGDPASALLEVLDPEQNNAFSDHYLDVPFDLSKVIFIATANSIDTIPRPLLDRMEVIELSGYTEEEKLEIAKKYLIPK 508

                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118573575  667 ARTLCGLDESKAQLSAAVLTLLIKQYCRESGVRNLQKQVEKVLRKAAYKIVS------GEAQTVQVTPENLQDFVGKPVF 740
Cdd:TIGR00763 509 ALEDHGLKPDELKITDEALLLLIKYYTREAGVRNLERQIEKICRKAAVKLVEqgekkkSEAESVVITPDNLKKYLGKPVF 588

                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118573575  741 TVERMYEVTPPGVVMGLAWTAMGGSTLFVETSLRRPqpsgskedkDGSLEVTGQLGDVMKESARIAYTYARAFLMEQDPE 820
Cdd:TIGR00763 589 TYERAYEVTPPGVVMGLAWTPMGGDTLFIETTKVAG---------KGSLELTGQLGDVMKESAQIALTYVRSIAADLGIS 659

                         730       740       750       760       770       780       790       800
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118573575  821 NDFLVTSHIHLHVPEGATPKDGPSAGCTIVTALLSLALGQPVLQNLAMTGEVSLTGKVLPVGGIKEKTIAAKRAGVTCII 900
Cdd:TIGR00763 660 PNFFEKADIHLHVPEGATPKDGPSAGITMATALLSLATGKPVRPDVAMTGEITLRGKVLPIGGLKEKTIAAKRAGIKTII 739

                         810       820       830
                  ....*....|....*....|....*....|....*.
gi 118573575  901 LPAENRKDYSDLAPFITEGLEVHFVEHYRDIFPIAF 936
Cdd:TIGR00763 740 LPEKNRRDLEELPENVKEGLEIHFVKHYDEVLKKAF 775
Lon COG0466
ATP-dependent Lon protease, bacterial type [Posttranslational modification, protein turnover, ...
 112-940 0e+00

ATP-dependent Lon protease, bacterial type [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 440234 [Multi-domain]  Cd Length: 785  Bit Score: 1005.31  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118573575 112 LPLIAITRNPVFPRFIKIVEVKNKKLVELLrRKVRLAQPYVGVFLKRDDNNESDvveSLDEIYHTGTFAQIHEMQDLGD- 190
Cdd:COG0466   14 LPLLPLRDVVVFPGMVIPLFVGREKSIKAL-EEAMEGDKLIGLVAQKDAEVEDP---GPDDLYEVGTVAKILQLLKLPDg 89

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118573575 191 KLRMIVTGHRRIHISRQLEVEPeglepeaekqksrrklkrgkkevedelgpkpqlemvteaatdtskeVLMVEVEnVAHE 270
Cdd:COG0466   90 TVKVLVEGLQRARIKEFVQEEP----------------------------------------------YLEAEVE-PLEE 122

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118573575 271 DFQVTEEVKALTAEIVKTIRDIIALNPLYRESVLQMMQAgqrvVDNPIYLSDMGAALTGAESHELQDVLEETNILKRLYK 350
Cdd:COG0466  123 EEEDDKELEALMRSLKEQFEEYVKLNPKIPPELLAALSN----IEDPGRLADFIASHLPLKIEEKQELLETLDVKERLEK 198

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118573575 351 ALSLLKKEFELSKLQQRLGREVEEKIKQTHRKYLLQEQLKIIKKELGlEKDDKDAIEEKFRERLRELVVPKHVMDVVDEE 430
Cdd:COG0466  199 LLELLEKEIEVLELEKKIRSRVKEQMEKSQREYYLREQLKAIQKELG-EKDDGEDEIEELREKIEKAKLPEEVKEKAEKE 277

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118573575 431 LSKLALLDNHSSEFNVTRNYLDWLTSIPWGRQSDENLDLARAQAVLEEDHYGMEDVKKRVLEFIAVSQLRGSTQGKILCF 510
Cdd:COG0466  278 LKKLERMPPMSAEATVIRNYLDWLLDLPWGKRTKDNLDLKKAEKILDEDHYGLEKVKERILEYLAVRKLKKKLKGPILCL 357

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118573575 511 HGPPGVGKTSIARSIARALGREYFRFSVGGMTDVAEIKGHRRTYVGAMPGKIIQCLKKTKTENPLVLIDEVDKIGRGYQG 590
Cdd:COG0466  358 VGPPGVGKTSLGKSIARALGRKFVRISLGGVRDEAEIRGHRRTYIGAMPGRIIQGLKKAGTKNPVFLLDEIDKMGSDFRG 437

                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118573575 591 DPSSALLELLDPEQNANFLDHYLDVPVDLSKVLFICTANVIDTIPEPLRDRMEMINVSGYVAQEKLAIAERYLVPQARTL 670
Cdd:COG0466  438 DPASALLEVLDPEQNNTFSDHYLEVPFDLSKVMFIATANSLDTIPAPLLDRMEIIELSGYTEEEKLEIAKRYLIPKQLKE 517

                        570       580       590       600       610       620       630       640
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118573575 671 CGLDESKAQLSAAVLTLLIKQYCRESGVRNLQKQVEKVLRKAAYKIVSGEAQTVQVTPENLQDFVGKPVFTVERMYEVTP 750
Cdd:COG0466  518 HGLKKEELKISDEALRKIIRGYTREAGVRNLEREIAKICRKVAKKIAEGKKKKVTITPKNLEKYLGVPRFRYEKAEEEDQ 597

                        650       660       670       680       690       700       710       720
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118573575 751 PGVVMGLAWTAMGGSTLFVETSLRRpqpsGSkedkdGSLEVTGQLGDVMKESARIAYTYARAFLMEQDPENDFLVTSHIH 830
Cdd:COG0466  598 VGVVTGLAWTEVGGDILFIEATLMP----GK-----GKLTLTGQLGDVMKESAQAALSYVRSRAEELGIDPDFFEKYDIH 668

                        730       740       750       760       770       780       790       800
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118573575 831 LHVPEGATPKDGPSAGCTIVTALLSLALGQPVLQNLAMTGEVSLTGKVLPVGGIKEKTIAAKRAGVTCIILPAENRKDYS 910
Cdd:COG0466  669 IHVPEGATPKDGPSAGITMATALVSALTGRPVRSDVAMTGEITLRGRVLPIGGLKEKLLAAHRAGIKTVILPKENEKDLE 748

                        810       820       830
                 ....*....|....*....|....*....|
gi 118573575 911 DLAPFITEGLEVHFVEHYRDIFPIAFPRRE 940
Cdd:COG0466  749 EIPEEVKKGLEFHPVEHIDEVLKIALEKEP 778
PRK10787 PRK10787
DNA-binding ATP-dependent protease La; Provisional
 314-936 2.98e-175

DNA-binding ATP-dependent protease La; Provisional


Pssm-ID: 182730 [Multi-domain]  Cd Length: 784  Bit Score: 528.74  E-value: 2.98e-175
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118573575 314 VDNPIYLSDMGAALTGAESHELQDVLEETNILKRLYKALSLLKKEFELSKLQQRLGREVEEKIKQTHRKYLLQEQLKIIK 393
Cdd:PRK10787 159 IDDPARLADTIAAHMPLKLADKQSVLEMSDVNERLEYLMAMMESEIDLLQVEKRIRNRVKKQMEKSQREYYLNEQMKAIQ 238

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118573575 394 KELGlEKDDKDAIEEKFRERLRELVVPKHVMDVVDEELSKLALLDNHSSEFNVTRNYLDWLTSIPWGRQSDENLDLARAQ 473
Cdd:PRK10787 239 KELG-EMDDAPDENEALKRKIDAAKMPKEAKEKAEAELQKLKMMSPMSAEATVVRGYIDWMVQVPWNARSKVKKDLRQAQ 317

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118573575 474 AVLEEDHYGMEDVKKRVLEFIAVSQLRGSTQGKILCFHGPPGVGKTSIARSIARALGREYFRFSVGGMTDVAEIKGHRRT 553
Cdd:PRK10787 318 EILDTDHYGLERVKDRILEYLAVQSRVNKIKGPILCLVGPPGVGKTSLGQSIAKATGRKYVRMALGGVRDEAEIRGHRRT 397

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118573575 554 YVGAMPGKIIQCLKKTKTENPLVLIDEVDKIGRGYQGDPSSALLELLDPEQNANFLDHYLDVPVDLSKVLFICTANVIDt 633
Cdd:PRK10787 398 YIGSMPGKLIQKMAKVGVKNPLFLLDEIDKMSSDMRGDPASALLEVLDPEQNVAFSDHYLEVDYDLSDVMFVATSNSMN- 476

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118573575 634 IPEPLRDRMEMINVSGYVAQEKLAIAERYLVPQARTLCGLDESKAQLSAAVLTLLIKQYCRESGVRNLQKQVEKVLRKAA 713
Cdd:PRK10787 477 IPAPLLDRMEVIRLSGYTEDEKLNIAKRHLLPKQIERNALKKGELTVDDSAIIGIIRYYTREAGVRSLEREISKLCRKAV 556

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118573575 714 YKIVSGEA-QTVQVTPENLQDFVGKPVFTVERMYEVTPPGVVMGLAWTAMGGSTLFVETSLRRPQpsgskedkdGSLEVT 792
Cdd:PRK10787 557 KQLLLDKSlKHIEINGDNLHDYLGVQRFDYGRADNENRVGQVTGLAWTEVGGDLLTIETACVPGK---------GKLTYT 627

                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118573575 793 GQLGDVMKESARIAYTYARAFLMEQDPENDFLVTSHIHLHVPEGATPKDGPSAGCTIVTALLSLALGQPVLQNLAMTGEV 872
Cdd:PRK10787 628 GSLGEVMQESIQAALTVVRARAEKLGINPDFYEKRDIHVHVPEGATPKDGPSAGIAMCTALVSCLTGNPVRADVAMTGEI 707

                        570       580       590       600       610       620
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 118573575 873 SLTGKVLPVGGIKEKTIAAKRAGVTCIILPAENRKDYSDLAPFITEGLEVHFVEHYRDIFPIAF 936
Cdd:PRK10787 708 TLRGQVLPIGGLKEKLLAAHRGGIKTVLIPFENKRDLEEIPDNVIADLDIHPVKRIEEVLTLAL 771
RecA-like_Lon cd19500
lon protease homolog 2 peroxisomal; Lon protease (also known as Lon peptidase) is an ...
 469-650 8.76e-129

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: 385.76  E-value: 8.76e-129
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118573575 469 LARAQAVLEEDHYGMEDVKKRVLEFIAVSQLRGSTQGKILCFHGPPGVGKTSIARSIARALGREYFRFSVGGMTDVAEIK 548
Cdd:cd19500    1 IKKARKVLDADHYGLEDVKERILEYLAVRKLKGSMKGPILCLVGPPGVGKTSLGKSIARALGRKFVRISLGGVRDEAEIR 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118573575 549 GHRRTYVGAMPGKIIQCLKKTKTENPLVLIDEVDKIGRGYQGDPSSALLELLDPEQNANFLDHYLDVPVDLSKVLFICTA 628
Cdd:cd19500   81 GHRRTYVGAMPGRIIQALKKAGTNNPVFLLDEIDKIGSSFRGDPASALLEVLDPEQNSTFSDHYLDVPFDLSKVLFIATA 160

                        170       180
                 ....*....|....*....|..
gi 118573575 629 NVIDTIPEPLRDRMEMINVSGY 650
Cdd:cd19500  161 NSLDTIPGPLLDRMEIIELSGY 182
Lon_C pfam05362
Lon protease (S16) C-terminal proteolytic domain; The Lon serine proteases must hydrolyse ATP ...
 725-938 7.54e-83

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: 265.64  E-value: 7.54e-83
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118573575  725 QVTPENLQDFVGKPVFTVERMYEVTPPGVVMGLAWTAMGGSTLFVETSLRrpqpSGSkedkdGSLEVTGQLGDVMKESAR 804
Cdd:pfam05362   1 KVTAKNLEKYLGVPRFRYGEAEKEDQVGVVTGLAWTEVGGDLLTIEAVIM----PGK-----GKLTLTGQLGDVMKESAQ 71

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118573575  805 IAYTYARAFLMEQDPENDFLVTSHIHLHVPEGATPKDGPSAGCTIVTALLSLALGQPVLQNLAMTGEVSLTGKVLPVGGI 884
Cdd:pfam05362  72 AALSYVRSRAEELGIDPDFFEKKDIHIHVPEGATPKDGPSAGVTMATALVSALTGIPVRKDVAMTGEITLRGRVLPIGGL 151

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 118573575  885 KEKTIAAKRAGVTCIILPAENRKDYSDLAPFITEGLEVHFVEHYRDIFPIAFPR 938
Cdd:pfam05362 152 KEKLLAAHRAGIKTVIIPKENEKDLEDIPENVREGLEIIPVEHVDEVLKHALVG 205
LON smart00464
Found in ATP-dependent protease La (LON); N-terminal domain of the ATP-dependent protease La ...
 111-188 2.67e-16

Found in ATP-dependent protease La (LON); N-terminal domain of the ATP-dependent protease La (LON), present also in other bacterial ORFs.


Pssm-ID: 197740 [Multi-domain]  Cd Length: 92  Bit Score: 74.78  E-value: 2.67e-16
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 118573575   111 HLPLIAITRNPVFPRFIKIVEVKNKKLVELLRRKVRLAQPYVGVFLKRDDNNESDVVESLDEIYHtgTFAQIHEMQDL 188
Cdd:smart00464   1 TLPLLPIRRRPLFPGFVLPIPVKRPKSVAAIKEALRRSQPYVIVFLLQDDPTETPEPLSDTIAAL--MPLELHEKQEL 76
 
Name Accession Description Interval E-value
lon TIGR00763
endopeptidase La; This protein, the ATP-dependent serine endopeptidase La, is induced by heat ...
 113-936 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: 1196.34  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118573575  113 PLIAITRNPVFPRFIKIVEVKNKKLVELLRRKVRLAQPYVGVFLKRDDNNESDvveSLDEIYHTGTFAQIHEMQDLGD-- 190
Cdd:TIGR00763   1 PLLPLRRRPLFPGMIKPIDVGREKSIKLIKEALRLKQPYLGLFLQKDDDNEEP---EEDDIYSVGVVAQILEMLPLPSsg 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118573575  191 --KLRMIVTGHRRIHIsrqlevepeglepeaekqksrrklkrgkKEVEDElgpkpqlemvteaatdtsKEVLMVEVENVA 268
Cdd:TIGR00763  78 taTYKVVVEGLRRIRI----------------------------KELSDK------------------GGYLVVRVDNLK 111

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118573575  269 HEDFQV-TEEVKALTAEIVKTIRDIIALNPLYRESVLQMMQAGQrvVDNPIYLSDMGAALTG-AESHELQDVLEETNILK 346
Cdd:TIGR00763 112 EEPFDKdDEEIKALTREIKETFRELISLSKLFREQPALLSALED--IDEPGRLADFVAASLQlKEKDELQEVLETVNIEK 189

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118573575  347 RLYKALSLLKKEFELSKLQQRLGREVEEKIKQTHRKYLLQEQLKIIKKELGLEKDDKDAIEeKFRERLRELVVPKHVMDV 426
Cdd:TIGR00763 190 RLKKALELLKKELELLKLQNKITKKVEEKMEKTQREYYLREQLKAIKKELGIEKDDKDELE-KLKEKLEELKLPEEVKKV 268

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118573575  427 VDEELSKLALLDNHSSEFNVTRNYLDWLTSIPWGRQSDENLDLARAQAVLEEDHYGMEDVKKRVLEFIAVSQLRGSTQGK 506
Cdd:TIGR00763 269 IEKELTKLSLLEPSSSEFTVTRNYLDWLTDLPWGKYSKENLDLKRAKEILDEDHYGLKKVKERILEYLAVQKLRGKMKGP 348

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118573575  507 ILCFHGPPGVGKTSIARSIARALGREYFRFSVGGMTDVAEIKGHRRTYVGAMPGKIIQCLKKTKTENPLVLIDEVDKIGR 586
Cdd:TIGR00763 349 ILCLVGPPGVGKTSLGKSIAKALNRKFVRFSLGGVRDEAEIRGHRRTYVGAMPGRIIQGLKKAKTKNPLFLLDEIDKIGS 428

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118573575  587 GYQGDPSSALLELLDPEQNANFLDHYLDVPVDLSKVLFICTANVIDTIPEPLRDRMEMINVSGYVAQEKLAIAERYLVPQ 666
Cdd:TIGR00763 429 SFRGDPASALLEVLDPEQNNAFSDHYLDVPFDLSKVIFIATANSIDTIPRPLLDRMEVIELSGYTEEEKLEIAKKYLIPK 508

                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118573575  667 ARTLCGLDESKAQLSAAVLTLLIKQYCRESGVRNLQKQVEKVLRKAAYKIVS------GEAQTVQVTPENLQDFVGKPVF 740
Cdd:TIGR00763 509 ALEDHGLKPDELKITDEALLLLIKYYTREAGVRNLERQIEKICRKAAVKLVEqgekkkSEAESVVITPDNLKKYLGKPVF 588

                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118573575  741 TVERMYEVTPPGVVMGLAWTAMGGSTLFVETSLRRPqpsgskedkDGSLEVTGQLGDVMKESARIAYTYARAFLMEQDPE 820
Cdd:TIGR00763 589 TYERAYEVTPPGVVMGLAWTPMGGDTLFIETTKVAG---------KGSLELTGQLGDVMKESAQIALTYVRSIAADLGIS 659

                         730       740       750       760       770       780       790       800
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118573575  821 NDFLVTSHIHLHVPEGATPKDGPSAGCTIVTALLSLALGQPVLQNLAMTGEVSLTGKVLPVGGIKEKTIAAKRAGVTCII 900
Cdd:TIGR00763 660 PNFFEKADIHLHVPEGATPKDGPSAGITMATALLSLATGKPVRPDVAMTGEITLRGKVLPIGGLKEKTIAAKRAGIKTII 739

                         810       820       830
                  ....*....|....*....|....*....|....*.
gi 118573575  901 LPAENRKDYSDLAPFITEGLEVHFVEHYRDIFPIAF 936
Cdd:TIGR00763 740 LPEKNRRDLEELPENVKEGLEIHFVKHYDEVLKKAF 775
Lon COG0466
ATP-dependent Lon protease, bacterial type [Posttranslational modification, protein turnover, ...
 112-940 0e+00

ATP-dependent Lon protease, bacterial type [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 440234 [Multi-domain]  Cd Length: 785  Bit Score: 1005.31  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118573575 112 LPLIAITRNPVFPRFIKIVEVKNKKLVELLrRKVRLAQPYVGVFLKRDDNNESDvveSLDEIYHTGTFAQIHEMQDLGD- 190
Cdd:COG0466   14 LPLLPLRDVVVFPGMVIPLFVGREKSIKAL-EEAMEGDKLIGLVAQKDAEVEDP---GPDDLYEVGTVAKILQLLKLPDg 89

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118573575 191 KLRMIVTGHRRIHISRQLEVEPeglepeaekqksrrklkrgkkevedelgpkpqlemvteaatdtskeVLMVEVEnVAHE 270
Cdd:COG0466   90 TVKVLVEGLQRARIKEFVQEEP----------------------------------------------YLEAEVE-PLEE 122

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118573575 271 DFQVTEEVKALTAEIVKTIRDIIALNPLYRESVLQMMQAgqrvVDNPIYLSDMGAALTGAESHELQDVLEETNILKRLYK 350
Cdd:COG0466  123 EEEDDKELEALMRSLKEQFEEYVKLNPKIPPELLAALSN----IEDPGRLADFIASHLPLKIEEKQELLETLDVKERLEK 198

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118573575 351 ALSLLKKEFELSKLQQRLGREVEEKIKQTHRKYLLQEQLKIIKKELGlEKDDKDAIEEKFRERLRELVVPKHVMDVVDEE 430
Cdd:COG0466  199 LLELLEKEIEVLELEKKIRSRVKEQMEKSQREYYLREQLKAIQKELG-EKDDGEDEIEELREKIEKAKLPEEVKEKAEKE 277

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118573575 431 LSKLALLDNHSSEFNVTRNYLDWLTSIPWGRQSDENLDLARAQAVLEEDHYGMEDVKKRVLEFIAVSQLRGSTQGKILCF 510
Cdd:COG0466  278 LKKLERMPPMSAEATVIRNYLDWLLDLPWGKRTKDNLDLKKAEKILDEDHYGLEKVKERILEYLAVRKLKKKLKGPILCL 357

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118573575 511 HGPPGVGKTSIARSIARALGREYFRFSVGGMTDVAEIKGHRRTYVGAMPGKIIQCLKKTKTENPLVLIDEVDKIGRGYQG 590
Cdd:COG0466  358 VGPPGVGKTSLGKSIARALGRKFVRISLGGVRDEAEIRGHRRTYIGAMPGRIIQGLKKAGTKNPVFLLDEIDKMGSDFRG 437

                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118573575 591 DPSSALLELLDPEQNANFLDHYLDVPVDLSKVLFICTANVIDTIPEPLRDRMEMINVSGYVAQEKLAIAERYLVPQARTL 670
Cdd:COG0466  438 DPASALLEVLDPEQNNTFSDHYLEVPFDLSKVMFIATANSLDTIPAPLLDRMEIIELSGYTEEEKLEIAKRYLIPKQLKE 517

                        570       580       590       600       610       620       630       640
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118573575 671 CGLDESKAQLSAAVLTLLIKQYCRESGVRNLQKQVEKVLRKAAYKIVSGEAQTVQVTPENLQDFVGKPVFTVERMYEVTP 750
Cdd:COG0466  518 HGLKKEELKISDEALRKIIRGYTREAGVRNLEREIAKICRKVAKKIAEGKKKKVTITPKNLEKYLGVPRFRYEKAEEEDQ 597

                        650       660       670       680       690       700       710       720
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118573575 751 PGVVMGLAWTAMGGSTLFVETSLRRpqpsGSkedkdGSLEVTGQLGDVMKESARIAYTYARAFLMEQDPENDFLVTSHIH 830
Cdd:COG0466  598 VGVVTGLAWTEVGGDILFIEATLMP----GK-----GKLTLTGQLGDVMKESAQAALSYVRSRAEELGIDPDFFEKYDIH 668

                        730       740       750       760       770       780       790       800
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118573575 831 LHVPEGATPKDGPSAGCTIVTALLSLALGQPVLQNLAMTGEVSLTGKVLPVGGIKEKTIAAKRAGVTCIILPAENRKDYS 910
Cdd:COG0466  669 IHVPEGATPKDGPSAGITMATALVSALTGRPVRSDVAMTGEITLRGRVLPIGGLKEKLLAAHRAGIKTVILPKENEKDLE 748

                        810       820       830
                 ....*....|....*....|....*....|
gi 118573575 911 DLAPFITEGLEVHFVEHYRDIFPIAFPRRE 940
Cdd:COG0466  749 EIPEEVKKGLEFHPVEHIDEVLKIALEKEP 778
PRK10787 PRK10787
DNA-binding ATP-dependent protease La; Provisional
 314-936 2.98e-175

DNA-binding ATP-dependent protease La; Provisional


Pssm-ID: 182730 [Multi-domain]  Cd Length: 784  Bit Score: 528.74  E-value: 2.98e-175
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118573575 314 VDNPIYLSDMGAALTGAESHELQDVLEETNILKRLYKALSLLKKEFELSKLQQRLGREVEEKIKQTHRKYLLQEQLKIIK 393
Cdd:PRK10787 159 IDDPARLADTIAAHMPLKLADKQSVLEMSDVNERLEYLMAMMESEIDLLQVEKRIRNRVKKQMEKSQREYYLNEQMKAIQ 238

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118573575 394 KELGlEKDDKDAIEEKFRERLRELVVPKHVMDVVDEELSKLALLDNHSSEFNVTRNYLDWLTSIPWGRQSDENLDLARAQ 473
Cdd:PRK10787 239 KELG-EMDDAPDENEALKRKIDAAKMPKEAKEKAEAELQKLKMMSPMSAEATVVRGYIDWMVQVPWNARSKVKKDLRQAQ 317

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118573575 474 AVLEEDHYGMEDVKKRVLEFIAVSQLRGSTQGKILCFHGPPGVGKTSIARSIARALGREYFRFSVGGMTDVAEIKGHRRT 553
Cdd:PRK10787 318 EILDTDHYGLERVKDRILEYLAVQSRVNKIKGPILCLVGPPGVGKTSLGQSIAKATGRKYVRMALGGVRDEAEIRGHRRT 397

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118573575 554 YVGAMPGKIIQCLKKTKTENPLVLIDEVDKIGRGYQGDPSSALLELLDPEQNANFLDHYLDVPVDLSKVLFICTANVIDt 633
Cdd:PRK10787 398 YIGSMPGKLIQKMAKVGVKNPLFLLDEIDKMSSDMRGDPASALLEVLDPEQNVAFSDHYLEVDYDLSDVMFVATSNSMN- 476

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118573575 634 IPEPLRDRMEMINVSGYVAQEKLAIAERYLVPQARTLCGLDESKAQLSAAVLTLLIKQYCRESGVRNLQKQVEKVLRKAA 713
Cdd:PRK10787 477 IPAPLLDRMEVIRLSGYTEDEKLNIAKRHLLPKQIERNALKKGELTVDDSAIIGIIRYYTREAGVRSLEREISKLCRKAV 556

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118573575 714 YKIVSGEA-QTVQVTPENLQDFVGKPVFTVERMYEVTPPGVVMGLAWTAMGGSTLFVETSLRRPQpsgskedkdGSLEVT 792
Cdd:PRK10787 557 KQLLLDKSlKHIEINGDNLHDYLGVQRFDYGRADNENRVGQVTGLAWTEVGGDLLTIETACVPGK---------GKLTYT 627

                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118573575 793 GQLGDVMKESARIAYTYARAFLMEQDPENDFLVTSHIHLHVPEGATPKDGPSAGCTIVTALLSLALGQPVLQNLAMTGEV 872
Cdd:PRK10787 628 GSLGEVMQESIQAALTVVRARAEKLGINPDFYEKRDIHVHVPEGATPKDGPSAGIAMCTALVSCLTGNPVRADVAMTGEI 707

                        570       580       590       600       610       620
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 118573575 873 SLTGKVLPVGGIKEKTIAAKRAGVTCIILPAENRKDYSDLAPFITEGLEVHFVEHYRDIFPIAF 936
Cdd:PRK10787 708 TLRGQVLPIGGLKEKLLAAHRGGIKTVLIPFENKRDLEEIPDNVIADLDIHPVKRIEEVLTLAL 771
RecA-like_Lon cd19500
lon protease homolog 2 peroxisomal; Lon protease (also known as Lon peptidase) is an ...
 469-650 8.76e-129

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: 385.76  E-value: 8.76e-129
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118573575 469 LARAQAVLEEDHYGMEDVKKRVLEFIAVSQLRGSTQGKILCFHGPPGVGKTSIARSIARALGREYFRFSVGGMTDVAEIK 548
Cdd:cd19500    1 IKKARKVLDADHYGLEDVKERILEYLAVRKLKGSMKGPILCLVGPPGVGKTSLGKSIARALGRKFVRISLGGVRDEAEIR 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118573575 549 GHRRTYVGAMPGKIIQCLKKTKTENPLVLIDEVDKIGRGYQGDPSSALLELLDPEQNANFLDHYLDVPVDLSKVLFICTA 628
Cdd:cd19500   81 GHRRTYVGAMPGRIIQALKKAGTNNPVFLLDEIDKIGSSFRGDPASALLEVLDPEQNSTFSDHYLDVPFDLSKVLFIATA 160

                        170       180
                 ....*....|....*....|..
gi 118573575 629 NVIDTIPEPLRDRMEMINVSGY 650
Cdd:cd19500  161 NSLDTIPGPLLDRMEIIELSGY 182
Lon_C pfam05362
Lon protease (S16) C-terminal proteolytic domain; The Lon serine proteases must hydrolyse ATP ...
 725-938 7.54e-83

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: 265.64  E-value: 7.54e-83
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118573575  725 QVTPENLQDFVGKPVFTVERMYEVTPPGVVMGLAWTAMGGSTLFVETSLRrpqpSGSkedkdGSLEVTGQLGDVMKESAR 804
Cdd:pfam05362   1 KVTAKNLEKYLGVPRFRYGEAEKEDQVGVVTGLAWTEVGGDLLTIEAVIM----PGK-----GKLTLTGQLGDVMKESAQ 71

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118573575  805 IAYTYARAFLMEQDPENDFLVTSHIHLHVPEGATPKDGPSAGCTIVTALLSLALGQPVLQNLAMTGEVSLTGKVLPVGGI 884
Cdd:pfam05362  72 AALSYVRSRAEELGIDPDFFEKKDIHIHVPEGATPKDGPSAGVTMATALVSALTGIPVRKDVAMTGEITLRGRVLPIGGL 151

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 118573575  885 KEKTIAAKRAGVTCIILPAENRKDYSDLAPFITEGLEVHFVEHYRDIFPIAFPR 938
Cdd:pfam05362 152 KEKLLAAHRAGIKTVIIPKENEKDLEDIPENVREGLEIIPVEHVDEVLKHALVG 205
AAA pfam00004
ATPase family associated with various cellular activities (AAA); AAA family proteins often ...
 508-650 3.13e-32

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: 121.55  E-value: 3.13e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118573575  508 LCFHGPPGVGKTSIARSIARALGREYFRFSVGGMTDvaeikghrrTYVGAMPGKIIQCLKKTKTENPLVL-IDEVDKIGR 586
Cdd:pfam00004   1 LLLYGPPGTGKTTLAKAVAKELGAPFIEISGSELVS---------KYVGESEKRLRELFEAAKKLAPCVIfIDEIDALAG 71

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 118573575  587 -------GYQGDPSSALLELLDPEQNANfldhyldvpvdlSKVLFICTANVIDTIPEPLRDRMEMINVSGY 650
Cdd:pfam00004  72 srgsggdSESRRVVNQLLTELDGFTSSN------------SKVIVIAATNRPDKLDPALLGRFDRIIEFPL 130
LON_substr_bdg pfam02190
ATP-dependent protease La (LON) substrate-binding domain; This domain has been shown to be ...
 112-357 1.10e-24

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: 102.41  E-value: 1.10e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118573575  112 LPLIAITRNPVFPRFIKIVEVKNKKLVELLRRKVRLAQPYvGVFLKrDDNNESDVVESLDEIYHTGTFAQIHEMQDLGDK 191
Cdd:pfam02190   2 LPLLPLRNTVLFPGMVLPLFVGRPRSIAAIEAALNKDKLY-GVLLV-SQKDAEDEEPTPDDLYEVGTVAKIVQILKLPDG 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118573575  192 -LRMIVTGHRRIHIsrqlevepeglepeaekqksrrklkrgkKEVEDELGPkpqlemvteaatdtskeVLMVEVENVAHE 270
Cdd:pfam02190  80 tYKVLVEGLERVRI----------------------------VELVKKEEP-----------------YLRAEVEDLPED 114

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118573575  271 DFQVTEEVKALTAEIVKTIRDIIALNPLYrESVLQMMqagqrVVDNPIYLSDMGAALTGAESHELQDVLEETNILKRLYK 350
Cdd:pfam02190 115 SDELSEALKALVKELIEKLRRLLKLLLPL-ELLLKIK-----DIENPGRLADLVAAILPLSPEEKQELLETLDVKERLEK 188


                  ....*..
gi 118573575  351 ALSLLKK 357
Cdd:pfam02190 189 VLELLNR 195
RecA-like_protease cd19481
proteases similar to RecA; RecA-like NTPases. This family includes the NTP binding domain of ...
 486-647 1.82e-19

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: 86.18  E-value: 1.82e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118573575 486 VKKRVLEFIAV------SQLRGSTQGKILCFHGPPGVGKTSIARSIARALGREYFRFSVGGMTDVAeikghrRTYVGAMP 559
Cdd:cd19481    1 LKASLREAVEAprrgsrLRRYGLGLPKGILLYGPPGTGKTLLAKALAGELGLPLIVVKLSSLLSKY------VGESEKNL 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118573575 560 GKIIQCLKKTKteNPLVLIDEVDKIG--RGYQGDPS------SALLELLDPEQNanfldhyldvpvdLSKVLFICTANVI 631
Cdd:cd19481   75 RKIFERARRLA--PCILFIDEIDAIGrkRDSSGESGelrrvlNQLLTELDGVNS-------------RSKVLVIAATNRP 139

                        170
                 ....*....|....*....
gi 118573575 632 DTIPEPLRDR---MEMINV 647
Cdd:cd19481  140 DLLDPALLRPgrfDEVIEF 158
COG1750 COG1750
Predicted archaeal serine protease, S18 family [General function prediction only];
802-906 5.68e-17

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


Pssm-ID: 441356 [Multi-domain]  Cd Length: 213  Bit Score: 80.79  E-value: 5.68e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118573575 802 SARIAYTYArAFLMEQDPEN-DFLVtshihlHVPEGATPKDGPSAGCTIVTALLSLALGQPVLQNLAMTGEVSLTGKVLP 880
Cdd:COG1750   75 SARIAALVA-SLLAGVDLSSyDVYI------SIESDSPIVGGPSAGGAMTVATYAALLGLPLNKSVTMTGMINPDGSIGP 147

                         90       100
                 ....*....|....*....|....*.
gi 118573575 881 VGGIKEKTIAAKRAGVTCIILPAENR 906
Cdd:COG1750  148 VGGVYEKLEAAASAGAKYFLIPKGQA 173
LON smart00464
Found in ATP-dependent protease La (LON); N-terminal domain of the ATP-dependent protease La ...
 111-188 2.67e-16

Found in ATP-dependent protease La (LON); N-terminal domain of the ATP-dependent protease La (LON), present also in other bacterial ORFs.


Pssm-ID: 197740 [Multi-domain]  Cd Length: 92  Bit Score: 74.78  E-value: 2.67e-16
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 118573575   111 HLPLIAITRNPVFPRFIKIVEVKNKKLVELLRRKVRLAQPYVGVFLKRDDNNESDVVESLDEIYHtgTFAQIHEMQDL 188
Cdd:smart00464   1 TLPLLPIRRRPLFPGFVLPIPVKRPKSVAAIKEALRRSQPYVIVFLLQDDPTETPEPLSDTIAAL--MPLELHEKQEL 76
SpoVK COG0464
AAA+-type ATPase, SpoVK/Ycf46/Vps4 family [Cell wall/membrane/envelope biogenesis, Cell cycle ...
 325-663 1.05e-15

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: 80.34  E-value: 1.05e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118573575 325 AALTGAESHELQDVLEETNILKRLYKALSLLKKEFELSKLQQRLGREVEEKIKQTHRKYLLQEQLKIIKKELGLEKDDKD 404
Cdd:COG0464    9 VALALALLLLDDAALRLLLLLLLALAAALLLLLLLLLLLLLALLLVELLLLLLSGALAALLLLALLLLALLALLAALLSA 88

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118573575 405 AIEEKFRERLRELVVPKHVMDVVDEELSKLALLDNHSSEfnvtrNYLDWLTSIPWGRQSDENLDLARAQAVLEEDHYGME 484
Cdd:COG0464   89 LELLLLGELLLLLLLLLLLLLLLLDLERALLELLRESAE-----ALALAAPLVTYEDIGGLEEELLELREAILDDLGGLE 163

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118573575 485 DVKKRVLEFIA-------VSQLRGSTQGKILCFHGPPGVGKTSIARSIARALGREYFRFSVGGMTDvaeikghrrTYVGA 557
Cdd:COG0464  164 EVKEELRELVAlplkrpeLREEYGLPPPRGLLLYGPPGTGKTLLARALAGELGLPLIEVDLSDLVS---------KYVGE 234

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118573575 558 MPGKIIQCLKKTKTENPLVL-IDEVDKI--GRGYQGDPS-----SALLELLDpeqnanfldhylDVPvdlSKVLFICTAN 629
Cdd:COG0464  235 TEKNLREVFDKARGLAPCVLfIDEADALagKRGEVGDGVgrrvvNTLLTEME------------ELR---SDVVVIAATN 299

                        330       340       350
                 ....*....|....*....|....*....|....*
gi 118573575 630 VIDTIPEPLRDRM-EMINVSGYVAQEKLAIAERYL 663
Cdd:COG0464  300 RPDLLDPALLRRFdEIIFFPLPDAEERLEIFRIHL 334
AAA cd00009
The AAA+ (ATPases Associated with a wide variety of cellular Activities) superfamily ...
 481-645 1.54e-15

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: 74.88  E-value: 1.54e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118573575 481 YGMEDVKKRVLEFIAvsqlrgSTQGKILCFHGPPGVGKTSIARSIARALGREYFRF---SVGGMTDVAEIKGHRRTYVGA 557
Cdd:cd00009    1 VGQEEAIEALREALE------LPPPKNLLLYGPPGTGKTTLARAIANELFRPGAPFlylNASDLLEGLVVAELFGHFLVR 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118573575 558 MPGKIIQclkktKTENPLVLIDEVDKIGRGYQgdpssallelldpEQNANFLDHYLDVPVDLSKVLFICTANVID--TIP 635
Cdd:cd00009   75 LLFELAE-----KAKPGVLFIDEIDSLSRGAQ-------------NALLRVLETLNDLRIDRENVRVIGATNRPLlgDLD 136

                        170
                 ....*....|
gi 118573575 636 EPLRDRMEMI 645
Cdd:cd00009  137 RALYDRLDIR 146
COG1223 COG1223
Predicted ATPase, AAA+ superfamily [General function prediction only];
478-663 2.65e-11

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


Pssm-ID: 440836 [Multi-domain]  Cd Length: 246  Bit Score: 64.91  E-value: 2.65e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118573575 478 EDHYGMEDVKKRVLEFIA----VSQLRG---STQGKILcFHGPPGVGKTSIARSIARALGREYFRFSVGGMTDvaeikgh 550
Cdd:COG1223    2 DDVVGQEEAKKKLKLIIKelrrRENLRKfglWPPRKIL-FYGPPGTGKTMLAEALAGELKLPLLTVRLDSLIG------- 73

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118573575 551 rrTYVGAMPGKIIQCLKKTKTENPLVLIDEVDKIG--RGYQ---GDPS---SALLELLDPEQnanfldhyldvpvdlSKV 622
Cdd:COG1223   74 --SYLGETARNLRKLFDFARRAPCVIFFDEFDAIAkdRGDQndvGEVKrvvNALLQELDGLP---------------SGS 136

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 118573575 623 LFICTANVIDTIPEPLRDRMEM-INVSGYVAQEKLAIAERYL 663
Cdd:COG1223  137 VVIAATNHPELLDSALWRRFDEvIEFPLPDKEERKEILELNL 178
44 PHA02544
clamp loader, small subunit; Provisional
 484-692 4.11e-09

clamp loader, small subunit; Provisional


Pssm-ID: 222866 [Multi-domain]  Cd Length: 316  Bit Score: 59.23  E-value: 4.11e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118573575 484 EDVKKRVLEFIavsqlrgsTQGKI--LCFHGP-PGVGKTSIARSIARALGREYFrFSVGGMTDVAEIKGHRRTYVGAM-- 558
Cdd:PHA02544  27 AADKETFKSIV--------KKGRIpnMLLHSPsPGTGKTTVAKALCNEVGAEVL-FVNGSDCRIDFVRNRLTRFASTVsl 97

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118573575 559 --PGKIIqclkktktenplvLIDEVDKIGRgyqgdpSSALLELldpeqnANFLDHYldvpvdlSK-VLFICTANVIDTIP 635
Cdd:PHA02544  98 tgGGKVI-------------IIDEFDRLGL------ADAQRHL------RSFMEAY-------SKnCSFIITANNKNGII 145

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 118573575 636 EPLRDRMEMINVSGYVAQEKLAIAERYLVpQARTLCglDESKAQLSAAVLTLLIKQY 692
Cdd:PHA02544 146 EPLRSRCRVIDFGVPTKEEQIEMMKQMIV-RCKGIL--EAEGVEVDMKVLAALVKKN 199
AAA smart00382
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ...
 504-641 6.17e-09

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: 55.84  E-value: 6.17e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118573575   504 QGKILCFHGPPGVGKTSIARSIARALGREYFRFSVGGMTDVAEIKGHRR-----------TYVGAMPGKIIQCLKKTKte 572
Cdd:smart00382   1 PGEVILIVGPPGSGKTTLARALARELGPPGGGVIYIDGEDILEEVLDQLlliivggkkasGSGELRLRLALALARKLK-- 78

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118573575   573 NPLVLIDEVDKIGRgyqgDPSSALLELLDPEQNANFLDHYLDVPVdlskvlfICTAN-VIDTIPEPLRDR 641
Cdd:smart00382  79 PDVLILDEITSLLD----AEQEALLLLLEELRLLLLLKSEKNLTV-------ILTTNdEKDLGPALLRRR 137
PRK13342 PRK13342
recombination factor protein RarA; Reviewed
 510-581 2.84e-08

recombination factor protein RarA; Reviewed


Pssm-ID: 237355 [Multi-domain]  Cd Length: 413  Bit Score: 57.02  E-value: 2.84e-08
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 118573575 510 FHGPPGVGKTSIARSIARALGREYFRFSvGGMTDVAEIKghrrtyvgampgKIIQCLKKTKT--ENPLVLIDEV 581
Cdd:PRK13342  41 LWGPPGTGKTTLARIIAGATDAPFEALS-AVTSGVKDLR------------EVIEEARQRRSagRRTILFIDEI 101
SdrC COG3480
Predicted secreted protein YlbL, contains PDZ domain [Signal transduction mechanisms];
842-922 2.89e-08

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


Pssm-ID: 442703 [Multi-domain]  Cd Length: 344  Bit Score: 56.74  E-value: 2.89e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118573575 842 GPSAGctivtalLSLALGqpVLQNL-----------AMTGEVSLTGKVLPVGGIKEKTIAAKRAGVTCIILPAENrkdYS 910
Cdd:COG3480  240 GPSAG-------LMFALG--IYDQLtpgdltggkkiAGTGTIDADGTVGPIGGIDQKVVAARRAGATIFLAPASN---CA 307

                         90
                 ....*....|..
gi 118573575 911 DLAPFITEGLEV 922
Cdd:COG3480  308 EAVGTIPTGLKV 319
AAA_5 pfam07728
AAA domain (dynein-related subfamily); This Pfam entry includes some of the AAA proteins not ...
 508-642 4.16e-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: 53.07  E-value: 4.16e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118573575  508 LCFHGPPGVGKTSIARSIARAL-GREYFRFSVGGMTDVAEIKGHRRTYVGAmPGKIIQCLKKTKTENPLVLIDEVDKIGR 586
Cdd:pfam07728   2 VLLVGPPGTGKTELAERLAAALsNRPVFYVQLTRDTTEEDLFGRRNIDPGG-ASWVDGPLVRAAREGEIAVLDEINRANP 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 118573575  587 GYQGdpssALLELLDPEQ----NANFLdhyldVPVDLSKVLFICTANVIDT----IPEPLRDRM 642
Cdd:pfam07728  81 DVLN----SLLSLLDERRlllpDGGEL-----VKAAPDGFRLIATMNPLDRglneLSPALRSRF 135
AAA_2 pfam07724
AAA domain (Cdc48 subfamily); This Pfam entry includes some of the AAA proteins not detected ...
 510-630 4.30e-08

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: 53.74  E-value: 4.30e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118573575  510 FHGPPGVGKTSIARSIARALGREYFRFSVGGMTDVAEikghrRTYV----GAMPGKI------IQCLKKTKTENPLVLID 579
Cdd:pfam07724   8 FLGPTGVGKTELAKALAELLFGDERALIRIDMSEYME-----EHSVsrliGAPPGYVgyeeggQLTEAVRRKPYSIVLID 82

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 118573575  580 EVDKIGRGYQgdpsSALLELLDpeqNANFLDHYlDVPVDLSKVLFICTANV 630
Cdd:pfam07724  83 EIEKAHPGVQ----NDLLQILE---GGTLTDKQ-GRTVDFKNTLFIMTGNF 125
RecA-like_VPS4-like cd19509
ATPase domain of VPS4, ATAD1, K, KTNA1, Spastin, FIGL-1 and similar ATPase domains; This ...
 482-643 2.55e-07

ATPase domain of VPS4, ATAD1, K, KTNA1, Spastin, FIGL-1 and similar ATPase domains; This subfamily includes the ATPase domains of vacuolar protein sorting-associated protein 4 (VPS4), ATPase family AAA domain-containing protein 1 (ATAD1, also known as Thorase), Katanin p60 ATPase-containing subunit A1 (KTNA1), Spastin, and Fidgetin-Like 1 (FIGL-1). This 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: 410917 [Multi-domain]  Cd Length: 163  Bit Score: 51.20  E-value: 2.55e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118573575 482 GMEDVKKRVLEFI--------AVSQLRGSTQGKILcfHGPPGVGKTSIARSIARALGREYFRFSVGGMTDvaeikghrrT 553
Cdd:cd19509    3 GLDDAKEALKEAVilpslrpdLFPGLRGPPRGILL--YGPPGTGKTLLARAVASESGSTFFSISASSLVS---------K 71

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118573575 554 YVGAmPGKIIQCLKKTKTEN--PLVLIDEVDKIGRGYQGDPSSA-------LLELLDPEQNAnfldhyldvpvDLSKVLF 624
Cdd:cd19509   72 WVGE-SEKIVRALFALARELqpSIIFIDEIDSLLSERGSGEHEAsrrvkteFLVQMDGVLNK-----------PEDRVLV 139

                        170
                 ....*....|....*....
gi 118573575 625 ICTANVIDTIPEPLRDRME 643
Cdd:cd19509  140 LGATNRPWELDEAFLRRFE 158
MoxR COG0714
MoxR-like ATPase [General function prediction only]; MoxR-like ATPase is part of the Pathway ...
 512-644 2.89e-07

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: 53.25  E-value: 2.89e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118573575 512 GPPGVGKTSIARSIARALGREYFR--FSVGGM------TDVAEIKGHRRTYVgamPGKIIQclkktktenPLVLIDEVDK 583
Cdd:COG0714   38 GVPGVGKTTLAKALARALGLPFIRiqFTPDLLpsdilgTYIYDQQTGEFEFR---PGPLFA---------NVLLADEINR 105

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 118573575 584 igrgyqGDP--SSALLELLDpeqnanflDHYLDVP---VDLSKVLF-ICTANVIDTI-----PEPLRDRMEM 644
Cdd:COG0714  106 ------APPktQSALLEAME--------ERQVTIPggtYKLPEPFLvIATQNPIEQEgtyplPEAQLDRFLL 163
RPT1 COG1222
ATP-dependent 26S proteasome regulatory subunit [Posttranslational modification, protein ...
 386-586 4.12e-07

ATP-dependent 26S proteasome regulatory subunit [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 440835 [Multi-domain]  Cd Length: 326  Bit Score: 53.09  E-value: 4.12e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118573575 386 QEQLKIIKKELGLEKDDKDAIEEKFRERLRELVVPKHVMDvvdEELSKLALLDNHSSEFNVTRNYLDWLTSipwgrqsde 465
Cdd:COG1222    1 GNDLLTIDENIKALLALIDALQERLGVELALLLQPVKALE---LLEEAPALLLNDANLTQKRLGTPRGTAV--------- 68

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118573575 466 nldLARAQAVLEEDHYGMEDVKKRVLEFIAVSQLR-------GSTQGKILCFHGPPGVGKTSIARSIARALGREYFRfsV 538
Cdd:COG1222   69 ---PAESPDVTFDDIGGLDEQIEEIREAVELPLKNpelfrkyGIEPPKGVLLYGPPGTGKTLLAKAVAGELGAPFIR--V 143

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 118573575 539 GGmtdvAEIkghRRTYVGAMPGKIIQCLKKTKTENPLVL-IDEVDKIGR 586
Cdd:COG1222  144 RG----SEL---VSKYIGEGARNVREVFELAREKAPSIIfIDEIDAIAA 185
LonB COG1067
Predicted ATP-dependent protease [Posttranslational modification, protein turnover, chaperones] ...
 841-887 9.33e-07

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


Pssm-ID: 440686 [Multi-domain]  Cd Length: 742  Bit Score: 52.64  E-value: 9.33e-07
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*...
gi 118573575 841 DGPSAGCTIVTALLSlAL-GQPVLQNLAMTGEVSLTGKVLPVGGIKEK 887
Cdd:COG1067  592 DGDSASSAELYALLS-ALsGVPIRQDIAVTGSVNQHGEVQPIGGVNEK 638
ChlI pfam13541
Subunit ChlI of Mg-chelatase;
839-905 1.15e-06

Subunit ChlI of Mg-chelatase;


Pssm-ID: 433293 [Multi-domain]  Cd Length: 121  Bit Score: 48.21  E-value: 1.15e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 118573575  839 PKDGPSAGCTIVTALLSLALGQPVLQNLAMTGEVSLTGKVLPVGGIKEKTIAAKRAGVTCIILPAEN 905
Cdd:pfam13541  55 KKEGSSFDLPIAIGILAAQGQIPVLEETIFLGELSLDGSLRPVRGALPIALAARKHGFRGLIVPKEN 121
PRK04195 PRK04195
replication factor C large subunit; Provisional
 482-671 1.17e-06

replication factor C large subunit; Provisional


Pssm-ID: 235250 [Multi-domain]  Cd Length: 482  Bit Score: 52.23  E-value: 1.17e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118573575 482 GMEDVKKRVLEFIAvSQLRGSTQgKILCFHGPPGVGKTSIARSIARALGREYF-------------RFSVGGMTDVAEIK 548
Cdd:PRK04195  18 GNEKAKEQLREWIE-SWLKGKPK-KALLLYGPPGVGKTSLAHALANDYGWEVIelnasdqrtadviERVAGEAATSGSLF 95

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118573575 549 GHRRTyvgampgkiiqclkktktenpLVLIDEVDKI-GRGYQGDpSSALLELLDpeqNANfldhyldVPVdlskvlfICT 627
Cdd:PRK04195  96 GARRK---------------------LILLDEVDGIhGNEDRGG-ARAILELIK---KAK-------QPI-------ILT 136

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
gi 118573575 628 AN-VIDTIPEPLRDRMEMINVSgyvaqeklAIAERYLVPQARTLC 671
Cdd:PRK04195 137 ANdPYDPSLRELRNACLMIEFK--------RLSTRSIVPVLKRIC 173
RecA-like_Pch2-like cd19508
ATPase domain of Pachytene checkpoint 2 (Pch2) and similar ATPase domains; Pch2 (known as ...
 484-641 1.20e-06

ATPase domain of Pachytene checkpoint 2 (Pch2) and similar ATPase domains; Pch2 (known as Thyroid hormone receptor interactor 13 (TRIP13) and 16E1BP) is a key regulator of specific chromosomal events, like the control of G2/prophase processes such as DNA break formation and recombination, checkpoint signaling, and chromosome synapsis. This 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: 410916 [Multi-domain]  Cd Length: 199  Bit Score: 50.14  E-value: 1.20e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118573575 484 EDVKKRVLEFIAVSqLRGSTQG---------KILCFHGPPGVGKTSIARSIARALG-REYFRFSVGGMTdvaEIKGHR-- 551
Cdd:cd19508   23 SNLKSRLLDYVTTT-LLFSDKNvntnlitwnRLVLLHGPPGTGKTSLCKALAQKLSiRLSSRYRYGQLI---EINSHSlf 98

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118573575 552 -------RTYVGAMPGKiIQCLKKTKTENPLVLIDEVDKIgrGYQGDPSSALLELLDPEQNANFLDHYLDVPVDLSKVLF 624
Cdd:cd19508   99 skwfsesGKLVTKMFQK-IQELIDDKDALVFVLIDEVESL--AAARSASSSGTEPSDAIRVVNAVLTQIDRIKRYHNNVI 175

                        170
                 ....*....|....*..
gi 118573575 625 ICTANVIDTIPEPLRDR 641
Cdd:cd19508  176 LLTSNLLEKIDVAFVDR 192
RarA COG2256
Replication-associated recombination protein RarA (DNA-dependent ATPase) [Replication, ...
 510-581 1.23e-06

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


Pssm-ID: 441857 [Multi-domain]  Cd Length: 439  Bit Score: 51.98  E-value: 1.23e-06
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 118573575 510 FHGPPGVGKTSIARSIARALGREYFRFSvGGMTDVAEIKghrrtyvgampgKIIQCLKKTKTEN--PLVLIDEV 581
Cdd:COG2256   54 LWGPPGTGKTTLARLIANATDAEFVALS-AVTSGVKDIR------------EVIEEARERRAYGrrTILFVDEI 114
RecA-like_CDC48_NLV2_r1-like cd19503
first of two ATPase domains of CDC48 and NLV2, and similar ATPase domains; CDC48 in yeast and ...
 482-639 2.84e-06

first of two ATPase domains of CDC48 and NLV2, and similar ATPase domains; CDC48 in yeast and p97 or VCP metazoans is an ATP-dependent molecular chaperone which plays an essential role in many cellular processes, by segregating polyubiquitinated proteins from complexes or membranes. Cdc48/p97 consists of an N-terminal domain and two ATPase domains; this subfamily represents the first of the two ATPase domains. This subfamily also includes the first of the two ATPase domains of NVL (nuclear VCP-like protein) 2, an isoform of NVL mainly present in the nucleolus, which is involved in ribosome biogenesis, in telomerase assembly and the regulation of telomerase activity, and in pre-rRNA processing. This 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: 410911 [Multi-domain]  Cd Length: 165  Bit Score: 48.44  E-value: 2.84e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118573575 482 GMEDVKKRVLEFIAvSQLRGSTQGKIL--------CFHGPPGVGKTSIARSIARALGREYFrfsvggmtdvaEIKGHrrT 553
Cdd:cd19503    4 GLDEQIASLKELIE-LPLKYPELFRALglkpprgvLLHGPPGTGKTLLARAVANEAGANFL-----------SISGP--S 69

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118573575 554 YVGAMPGKIIQCLKK-----TKTENPLVLIDEVDKIG--RGY-QGDPS----SALLELLDPEQNANfldhyldvpvdlsK 621
Cdd:cd19503   70 IVSKYLGESEKNLREifeeaRSHAPSIIFIDEIDALApkREEdQREVErrvvAQLLTLMDGMSSRG-------------K 136

                        170
                 ....*....|....*...
gi 118573575 622 VLFICTANVIDTIPEPLR 639
Cdd:cd19503  137 VVVIAATNRPDAIDPALR 154
RuvB_N pfam05496
Holliday junction DNA helicase RuvB P-loop domain; The RuvB protein makes up part of the ...
 478-530 7.77e-06

Holliday junction DNA helicase RuvB P-loop domain; The RuvB protein makes up part of the RuvABC revolvasome which catalyzes the resolution of Holliday junctions that arise during genetic recombination and DNA repair. Branch migration is catalyzed by the RuvB protein that is targeted to the Holliday junction by the structure specific RuvA protein. This family contains the N-terminal region of the protein.


Pssm-ID: 398900 [Multi-domain]  Cd Length: 159  Bit Score: 46.72  E-value: 7.77e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 118573575  478 EDHYGMEDVKKRVLEFIAVSQLRGSTQGKILcFHGPPGVGKTSIARSIARALG 530
Cdd:pfam05496   7 DEYIGQEKVKENLKIFIEAAKQRGEALDHVL-LYGPPGLGKTTLANIIANEMG 58
ruvB PRK00080
Holliday junction branch migration DNA helicase RuvB;
478-530 1.24e-05

Holliday junction branch migration DNA helicase RuvB;


Pssm-ID: 234619 [Multi-domain]  Cd Length: 328  Bit Score: 48.20  E-value: 1.24e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|...
gi 118573575 478 EDHYGMEDVKKRVLEFIAVSQLRGSTQGKILcFHGPPGVGKTSIARSIARALG 530
Cdd:PRK00080  25 DEFIGQEKVKENLKIFIEAAKKRGEALDHVL-LYGPPGLGKTTLANIIANEMG 76
RecA-like_NVL_r1-like cd19518
first of two ATPase domains of NVL (nuclear VCP-like protein) and similar ATPase domains; NVL ...
 482-585 1.27e-05

first of two ATPase domains of NVL (nuclear VCP-like protein) and similar ATPase domains; NVL exists in two forms with N-terminal extensions of different lengths in mammalian cells. NVL has two alternatively spliced isoforms, a short form, NVL1, and a long form, NVL2. NVL2, the major species, is mainly present in the nucleolus, whereas NVL1 is nucleoplasmic. Each has an N-terminal domain, followed by two tandem ATPase domains; this subfamily includes the first of the two ATPase domains. NVL2 is involved in the biogenesis of the 60S ribosome subunit by associating specifically with ribosome protein L5 and modulating the function of DOB1. NVL2 is also required for telomerase assembly and the regulation of telomerase activity, and is involved in pre-rRNA processing. The role of NVL1 is unclear. This RecA-like_NVL_r1-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: 410926 [Multi-domain]  Cd Length: 169  Bit Score: 46.63  E-value: 1.27e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118573575 482 GMEDVKKRVLEFIA-------VSQLRGSTQGKILCFHGPPGVGKTSIARSIARALGREYFRFS----VGGMTdvaeikgh 550
Cdd:cd19518    4 GMDSTLKELCELLIhpilppeYFQHLGVEPPRGVLLHGPPGCGKTMLANAIAGELKVPFLKISateiVSGVS-------- 75

                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 118573575 551 rrtyvGAMPGKIIQCLKKTKTENP-LVLIDEVDKIG 585
Cdd:cd19518   76 -----GESEEKIRELFDQAISNAPcIVFIDEIDAIT 106
ruvB TIGR00635
Holliday junction DNA helicase, RuvB subunit; All proteins in this family for which functions ...
 478-662 1.37e-05

Holliday junction DNA helicase, RuvB subunit; All proteins in this family for which functions are known are 5'-3' DNA helicases that, as part of a complex with RuvA homologs serve as a 5'-3' Holliday junction helicase. RuvA specifically binds Holliday junctions as a sandwich of two tetramers and maintains the configuration of the junction. It forms a complex with two hexameric rings of RuvB, the subunit that contains helicase activity. The complex drives ATP-dependent branch migration of the Holliday junction recombination intermediate. The endonuclease RuvC resolves junctions. [DNA metabolism, DNA replication, recombination, and repair]


Pssm-ID: 129721 [Multi-domain]  Cd Length: 305  Bit Score: 48.07  E-value: 1.37e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118573575  478 EDHYGMEDVKKRVLEFIAVSQLRGSTQGKILcFHGPPGVGKTSIARSIARALGREyFRFSVGGMTDvaeikghrrtyvga 557
Cdd:TIGR00635   4 AEFIGQEKVKEQLQLFIEAAKMRQEALDHLL-LYGPPGLGKTTLAHIIANEMGVN-LKITSGPALE-------------- 67

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118573575  558 MPGKIIQCLKKTKtENPLVLIDEVDKIGRgyqgdpssALLELLDPEQNANFLDHYLD-------VPVDLSKVLFICTANV 630
Cdd:TIGR00635  68 KPGDLAAILTNLE-EGDVLFIDEIHRLSP--------AVEELLYPAMEDFRLDIVIGkgpsarsVRLDLPPFTLVGATTR 138

                         170       180       190
                  ....*....|....*....|....*....|...
gi 118573575  631 IDTIPEPLRDRMEMI-NVSGYVAQEKLAIAERY 662
Cdd:TIGR00635 139 AGMLTSPLRDRFGIIlRLEFYTVEELAEIVSRS 171
RecA-like_FtsH cd19501
ATP-dependent zinc metalloprotease FtsH; FtsH ATPase is a processive, ATP-dependent zinc ...
 482-586 2.85e-05

ATP-dependent zinc metalloprotease FtsH; FtsH ATPase is a processive, ATP-dependent zinc metallopeptidase for both cytoplasmic and membrane proteins. It is anchored to the cytoplasmic membrane such that the amino- and carboxy-termini are exposed to the cytoplasm. It presents a membrane-bound hexameric structure that is able to unfold and degrade protein substrates. It is comprised of an N-terminal transmembrane region and the larger C-terminal cytoplasmic region, which consists of an ATPase domain and a protease domain. This RecA-Like FTsH subfamily represents the ATPase domain, and 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: 410909 [Multi-domain]  Cd Length: 171  Bit Score: 45.69  E-value: 2.85e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118573575 482 GMEDVKKRVLEFiaVSQLRGSTQ-----GKI---LCFHGPPGVGKTSIARSIARALGREYfrFSVGGmTDVAEIkghrrt 553
Cdd:cd19501    8 GCEEAKEELKEV--VEFLKNPEKftklgAKIpkgVLLVGPPGTGKTLLAKAVAGEAGVPF--FSISG-SDFVEM------ 76

                         90       100       110
                 ....*....|....*....|....*....|....
gi 118573575 554 YVGAMPGKIIQCLKKTKTENP-LVLIDEVDKIGR 586
Cdd:cd19501   77 FVGVGASRVRDLFEQAKKNAPcIVFIDEIDAVGR 110
RecA-like_HslU cd19498
ATP-dependent protease ATPase subunit HslU; HslU is a component of the ATP-dependent protease ...
 512-639 4.91e-05

ATP-dependent protease ATPase subunit HslU; HslU is a component of the ATP-dependent protease HslVU. In HslVU, HslU ATPase serves to unfold and translocate protein substrate, and the HslV protease degrades the unfolded proteins. This RecA-like_HslU 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: 410906 [Multi-domain]  Cd Length: 183  Bit Score: 45.06  E-value: 4.91e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118573575 512 GPPGVGKTSIARSIARALGREYFRFSVGGMTDVAeikghrrtYVGAMPGKIIQCLKKTktenpLVLIDEVDKI---GRGY 588
Cdd:cd19498   53 GPTGVGKTEIARRLAKLAGAPFIKVEATKFTEVG--------YVGRDVESIIRDLVEG-----IVFIDEIDKIakrGGSS 119

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 118573575 589 QGDPSSALLE--LLDPEQNANFLDHYldVPVDLSKVLFICT-----ANVIDTIPE-----PLR 639
Cdd:cd19498  120 GPDVSREGVQrdLLPIVEGSTVSTKY--GPVKTDHILFIAAgafhvAKPSDLIPElqgrfPIR 180
ftsH CHL00176
cell division protein; Validated
 474-586 7.24e-05

cell division protein; Validated


Pssm-ID: 214386 [Multi-domain]  Cd Length: 638  Bit Score: 46.58  E-value: 7.24e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118573575 474 AVLEEDHYGMEDVKKRVLEFiaVSQLR--------GSTQGKILCFHGPPGVGKTSIARSIARALGREYfrFSVGGMTDVA 545
Cdd:CHL00176 179 GITFRDIAGIEEAKEEFEEV--VSFLKkperftavGAKIPKGVLLVGPPGTGKTLLAKAIAGEAEVPF--FSISGSEFVE 254

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 118573575 546 EIKGhrrtyVGAmpGKIIQCLKKTKTENP-LVLIDEVDKIGR 586
Cdd:CHL00176 255 MFVG-----VGA--ARVRDLFKKAKENSPcIVFIDEIDAVGR 289
RuvB COG2255
Holliday junction resolvasome RuvABC, ATP-dependent DNA helicase subunit RuvB [Replication, ...
 478-530 7.44e-05

Holliday junction resolvasome RuvABC, ATP-dependent DNA helicase subunit RuvB [Replication, recombination and repair];


Pssm-ID: 441856 [Multi-domain]  Cd Length: 337  Bit Score: 45.84  E-value: 7.44e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|...
gi 118573575 478 EDHYGMEDVKKRVLEFIAVSQLRGSTQGKILcFHGPPGVGKTSIARSIARALG 530
Cdd:COG2255   28 DEYIGQEKVKENLKIFIEAAKKRGEALDHVL-LYGPPGLGKTTLAHIIANEMG 79
RecA-like_ClpB_Hsp104-like cd19499
Chaperone protein ClpB/Hsp104 subfamily; Bacterial Caseinolytic peptidase B (ClpB) and ...
 508-646 8.83e-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: 44.09  E-value: 8.83e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118573575 508 LCFHGPPGVGKTSIARSIARAL--GREYF-RFSVGG---MTDVAEIKGHRRTYVGA-MPGKIIQCLKKtkteNP--LVLI 578
Cdd:cd19499   44 FLFLGPTGVGKTELAKALAELLfgDEDNLiRIDMSEymeKHSVSRLIGAPPGYVGYtEGGQLTEAVRR----KPysVVLL 119

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 118573575 579 DEVDKIGRGYQGdpssALLELLDpeqNANFLDHYLDVpVDLSKVLFICTANVIdtipeplrdRMEMIN 646
Cdd:cd19499  120 DEIEKAHPDVQN----LLLQVLD---DGRLTDSHGRT-VDFKNTIIIMTSNHF---------RPEFLN 170
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
208-445 9.25e-05

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 46.60  E-value: 9.25e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118573575 208 LEVEPEGLE---PEAEKQKSR-RKLKRGKKEVEDELGP--------------KPQLEMVTEAATDTSKEVLMVEVENVAH 269
Cdd:PRK03918 319 LEEEINGIEeriKELEEKEERlEELKKKLKELEKRLEEleerhelyeeakakKEELERLKKRLTGLTPEKLEKELEELEK 398

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118573575 270 EDFQVTEEVKALTAEIvKTIRDIIALnplYRESVLQMMQAGQRVvdnPIylsdMGAALTgaESHELQDVLEETNILKRLY 349
Cdd:PRK03918 399 AKEEIEEEISKITARI-GELKKEIKE---LKKAIEELKKAKGKC---PV----CGRELT--EEHRKELLEEYTAELKRIE 465

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118573575 350 KALSLLKKEfeLSKLQQRLgREVEEKIKQTHR---KYLLQEQLKIIKKEL---GLEKDDKDAIE-EKFRERLRELvvpKH 422
Cdd:PRK03918 466 KELKEIEEK--ERKLRKEL-RELEKVLKKESElikLKELAEQLKELEEKLkkyNLEELEKKAEEyEKLKEKLIKL---KG 539

                        250       260
                 ....*....|....*....|...
gi 118573575 423 VMDVVDEELSKLALLDNHSSEFN 445
Cdd:PRK03918 540 EIKSLKKELEKLEELKKKLAELE 562
RecA-like_ATAD1 cd19520
ATPase domain of ATPase family AAA domain-containing protein 1 and similar ATPase domains; ...
 482-543 2.45e-04

ATPase domain of ATPase family AAA domain-containing protein 1 and similar ATPase domains; ATPase family AAA domain-containing protein 1 (ATAD1, also known as Thorase) is an ATPase that plays a critical role in regulating the surface expression of alpha-amino-3-hydroxy-5-methyl-4-isoxazolepropionic acid (AMPA) receptors, thereby regulating synaptic plasticity, learning and memory. This 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: 410928 [Multi-domain]  Cd Length: 166  Bit Score: 42.80  E-value: 2.45e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 118573575 482 GMEDVKKRVLEFI----------AVSQLRGSTQGKILcfHGPPGVGKTSIARSIARALGREYFRFSVGGMTD 543
Cdd:cd19520    4 GLDEVITELKELVilplqrpelfDNSRLLQPPKGVLL--YGPPGCGKTMLAKATAKEAGARFINLQVSSLTD 73
AAA_PrkA smart00763
PrkA AAA domain; This is a family of PrkA bacterial and archaeal serine kinases approximately ...
 477-539 2.49e-04

PrkA AAA domain; This is a family of PrkA bacterial and archaeal serine kinases approximately 630 residues long. This is the N-terminal AAA domain.


Pssm-ID: 214810  Cd Length: 361  Bit Score: 44.59  E-value: 2.49e-04
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 118573575   477 EEDHYGMEDVKKRVLEFIAVSQLRGSTQGKILCFHGPPGVGKTSIARSIARALgREYFRFSVG 539
Cdd:smart00763  50 DHDFFGMEEAIERFVNYFKSAAQGLEERKQILYLLGPVGGGKSSLVECLKRGL-EEYSKTDEG 111
RecA-like_Figl-1 cd19525
ATPase domain of Fidgetin-Like 1 (FIGL-1); FIGL-1 may participate in DNA repair in the nucleus; ...
 478-584 2.89e-04

ATPase domain of Fidgetin-Like 1 (FIGL-1); FIGL-1 may participate in DNA repair in the nucleus; it may be involved in DNA double-strand break repair via homologous recombination. Caenorhabditis elegans FIGL-1 is a nuclear protein and controls the mitotic progression in the germ line and mouse FIGL-1 may be involved in the control of male meiosis. human FIGL-1 has been shown to be a centrosome protein involved in ciliogenesis perhaps as a microtubule-severing protein. This 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: 410933 [Multi-domain]  Cd Length: 186  Bit Score: 42.67  E-value: 2.89e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118573575 478 EDHYGMEDVKKRVLEFIAV--------SQLRGSTQGkILCFhGPPGVGKTSIARSIARALGREYFRFSVGGMTDvaeikg 549
Cdd:cd19525   22 ADIAGLEFAKKTIKEIVVWpmlrpdifTGLRGPPKG-ILLF-GPPGTGKTLIGKCIASQSGATFFSISASSLTS------ 93

                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 118573575 550 hrrTYVGAMPGKIIQCLKKTKTENPLVL-IDEVDKI 584
Cdd:cd19525   94 ---KWVGEGEKMVRALFSVARCKQPAVIfIDEIDSL 126
rfc PRK00440
replication factor C small subunit; Reviewed
 478-535 4.84e-04

replication factor C small subunit; Reviewed


Pssm-ID: 234763 [Multi-domain]  Cd Length: 319  Bit Score: 43.32  E-value: 4.84e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 118573575 478 EDHYGMEDVKKRVLEFIAvsqlrgstQGKI--LCFHGPPGVGKTSIARSIARALGREYFR 535
Cdd:PRK00440  17 DEIVGQEEIVERLKSYVK--------EKNMphLLFAGPPGTGKTTAALALARELYGEDWR 68
HolB COG0470
DNA polymerase III, delta prime subunit [Replication, recombination and repair];
510-648 5.49e-04

DNA polymerase III, delta prime subunit [Replication, recombination and repair];


Pssm-ID: 440238 [Multi-domain]  Cd Length: 289  Bit Score: 43.04  E-value: 5.49e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118573575 510 FHGPPGVGKTSIARSIARALGREY------------FRFSVGGMTDVAEIkghRRTYVGAMPGK-----IIQCLKKTKTE 572
Cdd:COG0470   23 LHGPPGIGKTTLALALARDLLCENpeggkacgqchsRLMAAGNHPDLLEL---NPEEKSDQIGIdqireLGEFLSLTPLE 99

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 118573575 573 NP--LVLIDEVDKIGRGYQgdpsSALLELL-DPEQNAnfldhyldvpvdlskvLFICTANVIDTIPEPLRDRMEMINVS 648
Cdd:COG0470  100 GGrkVVIIDEADAMNEAAA----NALLKTLeEPPKNT----------------PFILIANDPSRLLPTIRSRCQVIRFR 158
McrB COG1401
5-methylcytosine-specific restriction endonuclease McrBC, GTP-binding regulatory subunit McrB ...
 308-633 6.23e-04

5-methylcytosine-specific restriction endonuclease McrBC, GTP-binding regulatory subunit McrB [Defense mechanisms];


Pssm-ID: 441011 [Multi-domain]  Cd Length: 477  Bit Score: 43.60  E-value: 6.23e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118573575 308 QAGQRVVDNPIYLSDMGAALTGAESHELQDVLEETNILKRLYKALSLLKKEFELSKLQQRLGREVEEKIKQTHRKYLLQE 387
Cdd:COG1401   24 DAVRELGIRADDLRGAAELATRLAERLSEELLRADRAARATELVEELSAALEVVVLLLDLEKVELNEKLALSEAAVAIEE 103

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118573575 388 QLKIIKKELGLEKDDKDAIEEKFRERLRELVVPKHVMDVVDEELSKLALLDNHSSEFNVTRNYLDWLTSIP-WGRQSDEN 466
Cdd:COG1401  104 LYELEADSEIEAVGLLLELAERSDALEALERARLLLELADLEERAALETEVLEALEAELEELLAAPEDLSAdALAAELSA 183

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118573575 467 LDLARAQAVLEEDHYGMEDVKKRVLEFIA--VSQLRGSTQgKILcfHGPPGVGKTSIARSIARALG---REYFRF----- 536
Cdd:COG1401  184 AEELYSEDLESEDDYLKDLLREKFEETLEafLAALKTKKN-VIL--AGPPGTGKTYLARRLAEALGgedNGRIEFvqfhp 260

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118573575 537 ------SVGGMTDVAEIKGHRRTyvgamPGKIIQ-CLK-KTKTENPLVL-IDEvdkIGRG----YQGDpssaLLELLDPE 603
Cdd:COG1401  261 swsyedFLLGYRPSLDEGKYEPT-----PGIFLRfCLKaEKNPDKPYVLiIDE---INRAnvekYFGE----LLSLLESD 328

                        330       340       350
                 ....*....|....*....|....*....|....*.
gi 118573575 604 QNANFLD---HYLDVPVDLS---KVLFICTANVIDT 633
Cdd:COG1401  329 KRGEELSielPYSGEGEEFSippNLYIIGTMNTDDR 364
hflB PRK10733
ATP-dependent zinc metalloprotease FtsH;
479-586 1.11e-03

ATP-dependent zinc metalloprotease FtsH;


Pssm-ID: 182683 [Multi-domain]  Cd Length: 644  Bit Score: 42.71  E-value: 1.11e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118573575 479 DHYGMEDVKKRVLEFIAVSQLRGSTQ---GKI---LCFHGPPGVGKTSIARSIARALGREYFRFSvggMTDVAEIkghrr 552
Cdd:PRK10733 153 DVAGCDEAKEEVAELVEYLREPSRFQklgGKIpkgVLMVGPPGTGKTLLAKAIAGEAKVPFFTIS---GSDFVEM----- 224

                         90       100       110
                 ....*....|....*....|....*....|....*
gi 118573575 553 tYVGAMPGKIIQCLKKTKTENP-LVLIDEVDKIGR 586
Cdd:PRK10733 225 -FVGVGASRVRDMFEQAKKAAPcIIFIDEIDAVGR 258
DnaX COG2812
DNA polymerase III, gamma/tau subunits [Replication, recombination and repair];
510-529 1.15e-03

DNA polymerase III, gamma/tau subunits [Replication, recombination and repair];


Pssm-ID: 442061 [Multi-domain]  Cd Length: 340  Bit Score: 42.10  E-value: 1.15e-03
                         10        20
                 ....*....|....*....|
gi 118573575 510 FHGPPGVGKTSIARSIARAL 529
Cdd:COG2812   37 FTGPRGVGKTTLARILAKAL 56
RecA-like_CDC48_r1-like cd19519
first of two ATPase domains of CDC48 and similar ATPase domains; CDC48 in yeast and p97 or VCP ...
 511-584 1.77e-03

first of two ATPase domains of CDC48 and similar ATPase domains; CDC48 in yeast and p97 or VCP metazoans is an ATP-dependent molecular chaperone which plays an essential role in many cellular processes, by segregating polyubiquitinated proteins from complexes or membranes. Cdc48/p97 consists of an N-terminal domain and two ATPase domains; this subfamily represents the first of the two ATPase domains. CDC48's roles include in the fragmentation of Golgi stacks during mitosis and for their reassembly after mitosis, and in the formation of the nuclear envelope, and of the transitional endoplasmic reticulum (tER). This RecA-like_cdc48_r1-like subfamily belongs to the RecA-like 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: 410927 [Multi-domain]  Cd Length: 166  Bit Score: 40.11  E-value: 1.77e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 118573575 511 HGPPGVGKTSIARSIARALGReyFRFSVGGmtdvAEIKGhrrTYVGAMPGKIIQCLKKTKTENP-LVLIDEVDKI 584
Cdd:cd19519   40 YGPPGTGKTLIARAVANETGA--FFFLING----PEIMS---KLAGESESNLRKAFEEAEKNAPaIIFIDEIDAI 105
TsaE pfam02367
Threonylcarbamoyl adenosine biosynthesis protein TsaE; This family of proteins is involved in ...
 505-530 2.07e-03

Threonylcarbamoyl adenosine biosynthesis protein TsaE; This family of proteins is involved in the synthesis of threonylcarbamoyl adenosine (t(6)A).


Pssm-ID: 460540  Cd Length: 127  Bit Score: 38.95  E-value: 2.07e-03
                          10        20
                  ....*....|....*....|....*.
gi 118573575  505 GKILCFHGPPGVGKTSIARSIARALG 530
Cdd:pfam02367  21 GDVILLSGDLGAGKTTFTRGLARGLG 46
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
 242-417 2.45e-03

Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];


Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 41.35  E-value: 2.45e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118573575 242 KPQLEMVTEAATDTSKEV--LMVEVENVAHEDFQVTEEVKALTAEIVKTIRDIIALNplyRESVLQMMQAGQRVVDnpIY 319
Cdd:COG3883   22 QKELSELQAELEAAQAELdaLQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAE---AEIEERREELGERARA--LY 96

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118573575 320 LSDMG----AALTGAESheLQDVLEETNILKRLYKA-LSLLKkefELSKLQQRL---GREVEEKIKQTHRKyllQEQLKI 391
Cdd:COG3883   97 RSGGSvsylDVLLGSES--FSDFLDRLSALSKIADAdADLLE---ELKADKAELeakKAELEAKLAELEAL---KAELEA 168

                        170       180
                 ....*....|....*....|....*.
gi 118573575 392 IKKELGLEKDDKDAIEEKFRERLREL 417
Cdd:COG3883  169 AKAELEAQQAEQEALLAQLSAEEAAA 194
RecA-like_ATAD3-like cd19512
ATPase domains of ATPase AAA-domain protein 3A (ATAD3A), -3B, and -3C, and similar ATPase ...
 510-582 2.99e-03

ATPase domains of ATPase AAA-domain protein 3A (ATAD3A), -3B, and -3C, and similar ATPase domains; ATPase AAA-domain protein 3 (ATAD3) is a ubiquitously expressed mitochondrial protein involved in mitochondrial dynamics, DNA-nucleoid structural organization, cholesterol transport and steroidogenesis. The ATAD3 gene family in human comprises three paralog genes: ATAD3A, ATAD3B and ATAD3C. This 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: 410920 [Multi-domain]  Cd Length: 150  Bit Score: 39.05  E-value: 2.99e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 118573575 510 FHGPPGVGKTSIARSIARALGREYFRFSVGgmtDVAEIKghrRTYVGAMpGKIIQCLKKTKtENPLVLIDEVD 582
Cdd:cd19512   27 FYGPPGTGKTLFAKKLALHSGMDYAIMTGG---DVAPMG---REGVTAI-HKVFDWANTSR-RGLLLFVDEAD 91
RecA-like_PEX6_r2 cd19527
second of two ATPase domains of Peroxisomal biogenesis factor 6 (PEX6); PEX6(also known as ...
 486-591 3.45e-03

second of two ATPase domains of Peroxisomal biogenesis factor 6 (PEX6); PEX6(also known as Peroxin61)/PEX1 is a protein unfoldase; PEX6 and PEX1 form a heterohexameric Type-2 AAA-ATPase complex and are essential for peroxisome biogenesis as they are required for the import of folded proteins into the peroxisomal matrix. This subfamily represents the second ATPase domain of PEX6. This 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: 410935 [Multi-domain]  Cd Length: 160  Bit Score: 39.03  E-value: 3.45e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118573575 486 VKKRVLEFIAVSQLR------GSTQGKILCFHGPPGVGKTSIARSIARALGREYfrFSVGGMTDVaeikghrRTYVGAMP 559
Cdd:cd19527    1 VKKEILDTIQLPLEHpelfssGLRKRSGILLYGPPGTGKTLLAKAIATECSLNF--LSVKGPELI-------NMYIGESE 71

                         90       100       110
                 ....*....|....*....|....*....|....*
gi 118573575 560 GKIIQCLKKTKTENP-LVLIDEVDKIG--RGYQGD 591
Cdd:cd19527   72 ANVREVFQKARDAKPcVIFFDELDSLApsRGNSGD 106
RNA_helicase pfam00910
RNA helicase; This family includes RNA helicases thought to be involved in duplex unwinding ...
 508-533 3.79e-03

RNA helicase; This family includes RNA helicases thought to be involved in duplex unwinding during viral RNA replication. Members of this family are found in a variety of single stranded RNA viruses.


Pssm-ID: 459992  Cd Length: 102  Bit Score: 37.97  E-value: 3.79e-03
                          10        20
                  ....*....|....*....|....*.
gi 118573575  508 LCFHGPPGVGKTSIARSIARALGREY 533
Cdd:pfam00910   1 IWLYGPPGCGKSTLAKYLARALLKKL 26
PRK13341 PRK13341
AAA family ATPase;
508-527 4.04e-03

AAA family ATPase;


Pssm-ID: 237354 [Multi-domain]  Cd Length: 725  Bit Score: 40.81  E-value: 4.04e-03
                         10        20
                 ....*....|....*....|
gi 118573575 508 LCFHGPPGVGKTSIARSIAR 527
Cdd:PRK13341  55 LILYGPPGVGKTTLARIIAN 74
PrkA COG2766
Predicted Ser/Thr protein kinase [Signal transduction mechanisms];
481-535 4.34e-03

Predicted Ser/Thr protein kinase [Signal transduction mechanisms];


Pssm-ID: 442049 [Multi-domain]  Cd Length: 675  Bit Score: 40.98  E-value: 4.34e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 118573575 481 YGMEDVKKRVLEFiavsqLRGSTQG-----KILCFHGPPGVGKTSIARSIARALgREYFR 535
Cdd:COG2766   84 FGLEETLERIVDY-----LRSAARGlgerkRILLLHGPVGSGKSTLARCLKRGL-EEYSR 137
T7SS_EccA TIGR03922
type VII secretion AAA-ATPase EccA; This model represents the AAA family ATPase, EccA, of the ...
 469-529 4.68e-03

type VII secretion AAA-ATPase EccA; This model represents the AAA family ATPase, EccA, of the actinobacterial flavor of type VII secretion systems. Species such as Mycobacterium tuberculosis have several instances of this system per genome, designated EccA1, EccA2, etc. [Protein fate, Protein and peptide secretion and trafficking]


Pssm-ID: 188437 [Multi-domain]  Cd Length: 557  Bit Score: 40.60  E-value: 4.68e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118573575  469 LARAQAVLEEdHYGMEDVKKRV------LEFIAVSQLRG---STQGKILCFHGPPGVGKTSIARSIARAL 529
Cdd:TIGR03922 268 LAEAEAELAE-QIGLERVKRQVaalkssTAMALARAERGlpvAQTSNHMLFAGPPGTGKTTIARVVAKIY 336
RecA-like_VCP_r2 cd19529
second of two ATPase domains of Valosin-containing protein-like ATPase (VAT) and similar ...
 507-639 4.87e-03

second of two ATPase domains of Valosin-containing protein-like ATPase (VAT) and similar ATPase domains; The Valosin-containing protein-like ATPase of Thermoplasma acidophilum (VAT), is an archaeal homolog of the ubiquitous Cdc48/p97. It is a protein unfoldase that functions in concert with the 20S proteasome by unfolding proteasome substrates and passing them on for degradation. VAT forms a homohexamer, each monomer contains two tandem ATPase domains, referred to as D1 and D2, and an N-terminal domain. This 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: 410937 [Multi-domain]  Cd Length: 159  Bit Score: 38.63  E-value: 4.87e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118573575 507 ILCFhGPPGVGKTSIARSIARALGREYfrFSVGGMTDVAEikghrrtYVGAMPGKIIQCLKKTKTENPLVL-IDEVDKI- 584
Cdd:cd19529   30 ILLY-GPPGTGKTLLAKAVATESNANF--ISVKGPELLSK-------WVGESEKAIREIFRKARQVAPCVIfFDEIDSIa 99

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 118573575 585 -GRGYQGDPSSAllelldpEQNANFLDHYLDVPVDLSKVLFICTANVIDTI-PEPLR 639
Cdd:cd19529  100 pRRGTTGDSGVT-------ERVVNQLLTELDGLEEMNGVVVIAATNRPDIIdPALLR 149
AAA_16 pfam13191
AAA ATPase domain; This family of domains contain a P-loop motif that is characteriztic of the ...
 504-539 5.04e-03

AAA ATPase domain; This family of domains contain a P-loop motif that is characteriztic of the AAA superfamily.


Pssm-ID: 433025 [Multi-domain]  Cd Length: 167  Bit Score: 39.02  E-value: 5.04e-03
                          10        20        30
                  ....*....|....*....|....*....|....*.
gi 118573575  504 QGKILCFHGPPGVGKTSIARSIARALGREYFRFSVG 539
Cdd:pfam13191  23 RPPSVLLTGEAGTGKTTLLRELLRALERDGGYFLRG 58
 
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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