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Conserved domains on  [gi|17505831|ref|NP_492796|]
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Lon protease homolog, mitochondrial [Caenorhabditis elegans]

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
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 ...
90-970 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: 1143.57  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17505831    90 PMLAINRYPLFPGFIKKVDiVKDDNLKALIRRQLSLKQPYAGVFVKRDDENKEEtitSLSEVYPTGSFVQIIEVRDQGS- 168
Cdd:TIGR00763   1 PLLPLRRRPLFPGMIKPID-VGREKSIKLIKEALRLKQPYLGLFLQKDDDNEEP---EEDDIYSVGVVAQILEMLPLPSs 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17505831   169 ---VLELVLSAHRRIRALEPIDeitpknetplngrrargkraasatspltpppsppplapsvasvapeisateekeektt 245
Cdd:TIGR00763  77 gtaTYKVVVEGLRRIRIKELSD---------------------------------------------------------- 98
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17505831   246 ppsatgekqKKGIIMVRTENVVAEPVPKNNE-TKATMMAIVQTIRDVVQFNQLFGQQINLLLHPSQnvIDNPVYLCDLVA 324
Cdd:TIGR00763  99 ---------KGGYLVVRVDNLKEEPFDKDDEeIKALTREIKETFRELISLSKLFREQPALLSALED--IDEPGRLADFVA 167
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17505831   325 TLVQSAETKDLQEMMDEIDVSKRLKIALLLIQKEKAVAKLKYDINKDVEKKVQDHHRKYLLNEQLKVIKKELGIEKDEKT 404
Cdd:TIGR00763 168 ASLQLKEKDELQEVLETVNIEKRLKKALELLKKELELLKLQNKITKKVEEKMEKTQREYYLREQLKAIKKELGIEKDDKD 247
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17505831   405 TIiEKIDERIKTLAVPEYALKVINEEKTKLQFLDPHSSEFSVTRNYLEWLTSVPWGLTSPENRRLSVAKKALDEGHYGMK 484
Cdd:TIGR00763 248 EL-EKLKEKLEELKLPEEVKKVIEKELTKLSLLEPSSSEFTVTRNYLDWLTDLPWGKYSKENLDLKRAKEILDEDHYGLK 326
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17505831   485 DVKERIMEFIAVNLLRKSIGGKILCFHGPPGVGKTSIAKSIATALNREYFRFSVGGMTDVAEIKGHRRTYVGAMPGKMIQ 564
Cdd:TIGR00763 327 KVKERILEYLAVQKLRGKMKGPILCLVGPPGVGKTSLGKSIAKALNRKFVRFSLGGVRDEAEIRGHRRTYVGAMPGRIIQ 406
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17505831   565 CMKKVKTENPLVLIDEVDKIgGAGFHGDPASALLELLDPEQNANFNDHFLDVPVDLSRVLFICTANEISKIPGPLRDRME 644
Cdd:TIGR00763 407 GLKKAKTKNPLFLLDEIDKI-GSSFRGDPASALLEVLDPEQNNAFSDHYLDVPFDLSKVIFIATANSIDTIPRPLLDRME 485
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17505831   645 MIDVSGYLAEEKVEIAHQHLIPQLRKDTSLATEQLKIEDSALEELIKHYCRESGVRNLQQHIERIFRKAALQIAEqQNED 724
Cdd:TIGR00763 486 VIELSGYTEEEKLEIAKKYLIPKALEDHGLKPDELKITDEALLLLIKYYTREAGVRNLERQIEKICRKAAVKLVE-QGEK 564
                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17505831   725 EepaekattaitenseaepitstssadclKSSAEQIVVCTENLQKFVGRPKFTSDRMYEVTPPGVIMGLAWTAMGGSALY 804
Cdd:TIGR00763 565 K----------------------------KSEAESVVITPDNLKKYLGKPVFTYERAYEVTPPGVVMGLAWTPMGGDTLF 616
                         730       740       750       760       770       780       790       800
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17505831   805 IETVLKRPvdltndkDGSIETTGNLGDVMKESVRTALTVAKGILAREQPDNKFFDKAHIHIHVPEGATPKDGPSAGVTLV 884
Cdd:TIGR00763 617 IETTKVAG-------KGSLELTGQLGDVMKESAQIALTYVRSIAADLGISPNFFEKADIHLHVPEGATPKDGPSAGITMA 689
                         810       820       830       840       850       860       870       880
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17505831   885 SSLLSLALDRPVVQDMAMTGEISLTGKVLPVGGIREKVIAARRVGAKRVFLPNENRRDFDDLPEFMKSELDIRFVSHYDE 964
Cdd:TIGR00763 690 TALLSLATGKPVRPDVAMTGEITLRGKVLPIGGLKEKTIAAKRAGIKTIILPEKNRRDLEELPENVKEGLEIHFVKHYDE 769

                  ....*.
gi 17505831   965 LYEHLF 970
Cdd:TIGR00763 770 VLKKAF 775
 
Name Accession Description Interval E-value
lon TIGR00763
endopeptidase La; This protein, the ATP-dependent serine endopeptidase La, is induced by heat ...
90-970 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: 1143.57  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17505831    90 PMLAINRYPLFPGFIKKVDiVKDDNLKALIRRQLSLKQPYAGVFVKRDDENKEEtitSLSEVYPTGSFVQIIEVRDQGS- 168
Cdd:TIGR00763   1 PLLPLRRRPLFPGMIKPID-VGREKSIKLIKEALRLKQPYLGLFLQKDDDNEEP---EEDDIYSVGVVAQILEMLPLPSs 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17505831   169 ---VLELVLSAHRRIRALEPIDeitpknetplngrrargkraasatspltpppsppplapsvasvapeisateekeektt 245
Cdd:TIGR00763  77 gtaTYKVVVEGLRRIRIKELSD---------------------------------------------------------- 98
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17505831   246 ppsatgekqKKGIIMVRTENVVAEPVPKNNE-TKATMMAIVQTIRDVVQFNQLFGQQINLLLHPSQnvIDNPVYLCDLVA 324
Cdd:TIGR00763  99 ---------KGGYLVVRVDNLKEEPFDKDDEeIKALTREIKETFRELISLSKLFREQPALLSALED--IDEPGRLADFVA 167
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17505831   325 TLVQSAETKDLQEMMDEIDVSKRLKIALLLIQKEKAVAKLKYDINKDVEKKVQDHHRKYLLNEQLKVIKKELGIEKDEKT 404
Cdd:TIGR00763 168 ASLQLKEKDELQEVLETVNIEKRLKKALELLKKELELLKLQNKITKKVEEKMEKTQREYYLREQLKAIKKELGIEKDDKD 247
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17505831   405 TIiEKIDERIKTLAVPEYALKVINEEKTKLQFLDPHSSEFSVTRNYLEWLTSVPWGLTSPENRRLSVAKKALDEGHYGMK 484
Cdd:TIGR00763 248 EL-EKLKEKLEELKLPEEVKKVIEKELTKLSLLEPSSSEFTVTRNYLDWLTDLPWGKYSKENLDLKRAKEILDEDHYGLK 326
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17505831   485 DVKERIMEFIAVNLLRKSIGGKILCFHGPPGVGKTSIAKSIATALNREYFRFSVGGMTDVAEIKGHRRTYVGAMPGKMIQ 564
Cdd:TIGR00763 327 KVKERILEYLAVQKLRGKMKGPILCLVGPPGVGKTSLGKSIAKALNRKFVRFSLGGVRDEAEIRGHRRTYVGAMPGRIIQ 406
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17505831   565 CMKKVKTENPLVLIDEVDKIgGAGFHGDPASALLELLDPEQNANFNDHFLDVPVDLSRVLFICTANEISKIPGPLRDRME 644
Cdd:TIGR00763 407 GLKKAKTKNPLFLLDEIDKI-GSSFRGDPASALLEVLDPEQNNAFSDHYLDVPFDLSKVIFIATANSIDTIPRPLLDRME 485
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17505831   645 MIDVSGYLAEEKVEIAHQHLIPQLRKDTSLATEQLKIEDSALEELIKHYCRESGVRNLQQHIERIFRKAALQIAEqQNED 724
Cdd:TIGR00763 486 VIELSGYTEEEKLEIAKKYLIPKALEDHGLKPDELKITDEALLLLIKYYTREAGVRNLERQIEKICRKAAVKLVE-QGEK 564
                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17505831   725 EepaekattaitenseaepitstssadclKSSAEQIVVCTENLQKFVGRPKFTSDRMYEVTPPGVIMGLAWTAMGGSALY 804
Cdd:TIGR00763 565 K----------------------------KSEAESVVITPDNLKKYLGKPVFTYERAYEVTPPGVVMGLAWTPMGGDTLF 616
                         730       740       750       760       770       780       790       800
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17505831   805 IETVLKRPvdltndkDGSIETTGNLGDVMKESVRTALTVAKGILAREQPDNKFFDKAHIHIHVPEGATPKDGPSAGVTLV 884
Cdd:TIGR00763 617 IETTKVAG-------KGSLELTGQLGDVMKESAQIALTYVRSIAADLGISPNFFEKADIHLHVPEGATPKDGPSAGITMA 689
                         810       820       830       840       850       860       870       880
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17505831   885 SSLLSLALDRPVVQDMAMTGEISLTGKVLPVGGIREKVIAARRVGAKRVFLPNENRRDFDDLPEFMKSELDIRFVSHYDE 964
Cdd:TIGR00763 690 TALLSLATGKPVRPDVAMTGEITLRGKVLPIGGLKEKTIAAKRAGIKTIILPEKNRRDLEELPENVKEGLEIHFVKHYDE 769

                  ....*.
gi 17505831   965 LYEHLF 970
Cdd:TIGR00763 770 VLKKAF 775
Lon COG0466
ATP-dependent Lon protease, bacterial type [Posttranslational modification, protein turnover, ...
254-970 0e+00

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


Pssm-ID: 440234 [Multi-domain]  Cd Length: 785  Bit Score: 881.28  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17505831 254 QKKGIIMVRTEnVVAEPVPKNNETKATMMAIVQTIRDVVQFNQLFGQQINLLLhpsQNvIDNPVYLCDLVATLVqSAETK 333
Cdd:COG0466 108 QEEPYLEAEVE-PLEEEEEDDKELEALMRSLKEQFEEYVKLNPKIPPELLAAL---SN-IEDPGRLADFIASHL-PLKIE 181
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17505831 334 DLQEMMDEIDVSKRLKIALLLIQKEKAVAKLKYDINKDVEKKVQDHHRKYLLNEQLKVIKKELGiEKDEKTTIIEKIDER 413
Cdd:COG0466 182 EKQELLETLDVKERLEKLLELLEKEIEVLELEKKIRSRVKEQMEKSQREYYLREQLKAIQKELG-EKDDGEDEIEELREK 260
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17505831 414 IKTLAVPEYALKVINEEKTKLQFLDPHSSEFSVTRNYLEWLTSVPWGLTSPENRRLSVAKKALDEGHYGMKDVKERIMEF 493
Cdd:COG0466 261 IEKAKLPEEVKEKAEKELKKLERMPPMSAEATVIRNYLDWLLDLPWGKRTKDNLDLKKAEKILDEDHYGLEKVKERILEY 340
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17505831 494 IAVNLLRKSIGGKILCFHGPPGVGKTSIAKSIATALNREYFRFSVGGMTDVAEIKGHRRTYVGAMPGKMIQCMKKVKTEN 573
Cdd:COG0466 341 LAVRKLKKKLKGPILCLVGPPGVGKTSLGKSIARALGRKFVRISLGGVRDEAEIRGHRRTYIGAMPGRIIQGLKKAGTKN 420
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17505831 574 PLVLIDEVDKIGgAGFHGDPASALLELLDPEQNANFNDHFLDVPVDLSRVLFICTANEISKIPGPLRDRMEMIDVSGYLA 653
Cdd:COG0466 421 PVFLLDEIDKMG-SDFRGDPASALLEVLDPEQNNTFSDHYLEVPFDLSKVMFIATANSLDTIPAPLLDRMEIIELSGYTE 499
                       410       420       430       440       450       460       470       480
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17505831 654 EEKVEIAHQHLIPQLRKDTSLATEQLKIEDSALEELIKHYCRESGVRNLQQHIERIFRKAALQIAEqqnedeepaekatt 733
Cdd:COG0466 500 EEKLEIAKRYLIPKQLKEHGLKKEELKISDEALRKIIRGYTREAGVRNLEREIAKICRKVAKKIAE-------------- 565
                       490       500       510       520       530       540       550       560
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17505831 734 aitenseaepitstssadclkSSAEQIVVCTENLQKFVGRPKFTSDRMYEVTPPGVIMGLAWTAMGGSALYIETVL---K 810
Cdd:COG0466 566 ---------------------GKKKKVTITPKNLEKYLGVPRFRYEKAEEEDQVGVVTGLAWTEVGGDILFIEATLmpgK 624
                       570       580       590       600       610       620       630       640
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17505831 811 rpvdltndkdGSIETTGNLGDVMKESVRTALTVAKGILAREQPDNKFFDKAHIHIHVPEGATPKDGPSAGVTLVSSLLSL 890
Cdd:COG0466 625 ----------GKLTLTGQLGDVMKESAQAALSYVRSRAEELGIDPDFFEKYDIHIHVPEGATPKDGPSAGITMATALVSA 694
                       650       660       670       680       690       700       710       720
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17505831 891 ALDRPVVQDMAMTGEISLTGKVLPVGGIREKVIAARRVGAKRVFLPNENRRDFDDLPEFMKSELDIRFVSHYDELYEHLF 970
Cdd:COG0466 695 LTGRPVRSDVAMTGEITLRGRVLPIGGLKEKLLAAHRAGIKTVILPKENEKDLEEIPEEVKKGLEFHPVEHIDEVLKIAL 774
PRK10787 PRK10787
DNA-binding ATP-dependent protease La; Provisional
309-965 1.41e-171

DNA-binding ATP-dependent protease La; Provisional


Pssm-ID: 182730 [Multi-domain]  Cd Length: 784  Bit Score: 519.88  E-value: 1.41e-171
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17505831  309 SQNVIDNPVYLCDLVATLVqSAETKDLQEMMDEIDVSKRLKIALLLIQKEKAVAKLKYDINKDVEKKVQDHHRKYLLNEQ 388
Cdd:PRK10787 155 SLNSIDDPARLADTIAAHM-PLKLADKQSVLEMSDVNERLEYLMAMMESEIDLLQVEKRIRNRVKKQMEKSQREYYLNEQ 233
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17505831  389 LKVIKKELGiEKDEKTTIIEKIDERIKTLAVPEYALKVINEEKTKLQFLDPHSSEFSVTRNYLEWLTSVPWGLTSPENRR 468
Cdd:PRK10787 234 MKAIQKELG-EMDDAPDENEALKRKIDAAKMPKEAKEKAEAELQKLKMMSPMSAEATVVRGYIDWMVQVPWNARSKVKKD 312
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17505831  469 LSVAKKALDEGHYGMKDVKERIMEFIAVNLLRKSIGGKILCFHGPPGVGKTSIAKSIATALNREYFRFSVGGMTDVAEIK 548
Cdd:PRK10787 313 LRQAQEILDTDHYGLERVKDRILEYLAVQSRVNKIKGPILCLVGPPGVGKTSLGQSIAKATGRKYVRMALGGVRDEAEIR 392
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17505831  549 GHRRTYVGAMPGKMIQCMKKVKTENPLVLIDEVDKIgGAGFHGDPASALLELLDPEQNANFNDHFLDVPVDLSRVLFICT 628
Cdd:PRK10787 393 GHRRTYIGSMPGKLIQKMAKVGVKNPLFLLDEIDKM-SSDMRGDPASALLEVLDPEQNVAFSDHYLEVDYDLSDVMFVAT 471
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17505831  629 ANEISkIPGPLRDRMEMIDVSGYLAEEKVEIAHQHLIPQLRKDTSLATEQLKIEDSALEELIKHYCRESGVRNLQQHIER 708
Cdd:PRK10787 472 SNSMN-IPAPLLDRMEVIRLSGYTEDEKLNIAKRHLLPKQIERNALKKGELTVDDSAIIGIIRYYTREAGVRSLEREISK 550
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17505831  709 IFRKAALQIaeqqnedeepaekattaitenseaepitstssadCLKSSAEQIVVCTENLQKFVGRPKFTSDRMYEVTPPG 788
Cdd:PRK10787 551 LCRKAVKQL----------------------------------LLDKSLKHIEINGDNLHDYLGVQRFDYGRADNENRVG 596
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17505831  789 VIMGLAWTAMGGSALYIETVlkrpvdlTNDKDGSIETTGNLGDVMKESVRTALTVAKGILAREQPDNKFFDKAHIHIHVP 868
Cdd:PRK10787 597 QVTGLAWTEVGGDLLTIETA-------CVPGKGKLTYTGSLGEVMQESIQAALTVVRARAEKLGINPDFYEKRDIHVHVP 669
                        570       580       590       600       610       620       630       640
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17505831  869 EGATPKDGPSAGVTLVSSLLSLALDRPVVQDMAMTGEISLTGKVLPVGGIREKVIAARRVGAKRVFLPNENRRDFDDLPE 948
Cdd:PRK10787 670 EGATPKDGPSAGIAMCTALVSCLTGNPVRADVAMTGEITLRGQVLPIGGLKEKLLAAHRGGIKTVLIPFENKRDLEEIPD 749
                        650
                 ....*....|....*..
gi 17505831  949 FMKSELDIRFVSHYDEL 965
Cdd:PRK10787 750 NVIADLDIHPVKRIEEV 766
RecA-like_Lon cd19500
lon protease homolog 2 peroxisomal; Lon protease (also known as Lon peptidase) is an ...
469-651 9.52e-121

lon protease homolog 2 peroxisomal; Lon protease (also known as Lon peptidase) is an evolutionarily conserved ATP-dependent serine protease, present in bacteria and eukaryotic mitochondria and peroxisomes, which mediates the selective degradation of mutant and abnormal proteins as well as certain short-lived regulatory proteins. Lon protease is both an ATP-dependent peptidase and a protein-activated ATPase. This RecA-like Lon domain subfamily belongs to the RecA-like NTPase family which includes the NTP binding domain of F1 and V1 H(+)ATPases, DnaB and related helicases as well as bacterial RecA and related eukaryotic and archaeal recombinases. The RecA-like NTPase family also includes bacterial conjugation proteins and related DNA transfer proteins involved in type II and type IV secretion.


Pssm-ID: 410908 [Multi-domain]  Cd Length: 182  Bit Score: 365.34  E-value: 9.52e-121
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17505831 469 LSVAKKALDEGHYGMKDVKERIMEFIAVNLLRKSIGGKILCFHGPPGVGKTSIAKSIATALNREYFRFSVGGMTDVAEIK 548
Cdd:cd19500   1 IKKARKVLDADHYGLEDVKERILEYLAVRKLKGSMKGPILCLVGPPGVGKTSLGKSIARALGRKFVRISLGGVRDEAEIR 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17505831 549 GHRRTYVGAMPGKMIQCMKKVKTENPLVLIDEVDKIgGAGFHGDPASALLELLDPEQNANFNDHFLDVPVDLSRVLFICT 628
Cdd:cd19500  81 GHRRTYVGAMPGRIIQALKKAGTNNPVFLLDEIDKI-GSSFRGDPASALLEVLDPEQNSTFSDHYLDVPFDLSKVLFIAT 159
                       170       180
                ....*....|....*....|...
gi 17505831 629 ANEISKIPGPLRDRMEMIDVSGY 651
Cdd:cd19500 160 ANSLDTIPGPLLDRMEIIELSGY 182
Lon_C pfam05362
Lon protease (S16) C-terminal proteolytic domain; The Lon serine proteases must hydrolyse ATP ...
761-970 1.16e-75

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: 246.77  E-value: 1.16e-75
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17505831   761 VVCTENLQKFVGRPKFTSDRMYEVTPPGVIMGLAWTAMGGSALYIETVLKrpvdltnDKDGSIETTGNLGDVMKESVRTA 840
Cdd:pfam05362   1 KVTAKNLEKYLGVPRFRYGEAEKEDQVGVVTGLAWTEVGGDLLTIEAVIM-------PGKGKLTLTGQLGDVMKESAQAA 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17505831   841 LTVAKGILAREQPDNKFFDKAHIHIHVPEGATPKDGPSAGVTLVSSLLSLALDRPVVQDMAMTGEISLTGKVLPVGGIRE 920
Cdd:pfam05362  74 LSYVRSRAEELGIDPDFFEKKDIHIHVPEGATPKDGPSAGVTMATALVSALTGIPVRKDVAMTGEITLRGRVLPIGGLKE 153
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 17505831   921 KVIAARRVGAKRVFLPNENRRDFDDLPEFMKSELDIRFVSHYDELYEHLF 970
Cdd:pfam05362 154 KLLAAHRAGIKTVIIPKENEKDLEDIPENVREGLEIIPVEHVDEVLKHAL 203
AAA smart00382
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ...
505-642 1.50e-07

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: 51.61  E-value: 1.50e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17505831    505 GKILCFHGPPGVGKTSIAKSIATALNREYFRFSVGGMTDVAEIKGHRRTYVGAMPGKM----IQCMKKV-----KTENPL 575
Cdd:smart00382   2 GEVILIVGPPGSGKTTLARALARELGPPGGGVIYIDGEDILEEVLDQLLLIIVGGKKAsgsgELRLRLAlalarKLKPDV 81
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 17505831    576 VLIDEVDKiggagfHGDPASALLELLDPEqnanfnDHFLDVPVDLSRVLFICTANEIS-KIPGPLRDR 642
Cdd:smart00382  82 LILDEITS------LLDAEQEALLLLLEE------LRLLLLLKSEKNLTVILTTNDEKdLGPALLRRR 137
 
Name Accession Description Interval E-value
lon TIGR00763
endopeptidase La; This protein, the ATP-dependent serine endopeptidase La, is induced by heat ...
90-970 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: 1143.57  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17505831    90 PMLAINRYPLFPGFIKKVDiVKDDNLKALIRRQLSLKQPYAGVFVKRDDENKEEtitSLSEVYPTGSFVQIIEVRDQGS- 168
Cdd:TIGR00763   1 PLLPLRRRPLFPGMIKPID-VGREKSIKLIKEALRLKQPYLGLFLQKDDDNEEP---EEDDIYSVGVVAQILEMLPLPSs 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17505831   169 ---VLELVLSAHRRIRALEPIDeitpknetplngrrargkraasatspltpppsppplapsvasvapeisateekeektt 245
Cdd:TIGR00763  77 gtaTYKVVVEGLRRIRIKELSD---------------------------------------------------------- 98
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17505831   246 ppsatgekqKKGIIMVRTENVVAEPVPKNNE-TKATMMAIVQTIRDVVQFNQLFGQQINLLLHPSQnvIDNPVYLCDLVA 324
Cdd:TIGR00763  99 ---------KGGYLVVRVDNLKEEPFDKDDEeIKALTREIKETFRELISLSKLFREQPALLSALED--IDEPGRLADFVA 167
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17505831   325 TLVQSAETKDLQEMMDEIDVSKRLKIALLLIQKEKAVAKLKYDINKDVEKKVQDHHRKYLLNEQLKVIKKELGIEKDEKT 404
Cdd:TIGR00763 168 ASLQLKEKDELQEVLETVNIEKRLKKALELLKKELELLKLQNKITKKVEEKMEKTQREYYLREQLKAIKKELGIEKDDKD 247
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17505831   405 TIiEKIDERIKTLAVPEYALKVINEEKTKLQFLDPHSSEFSVTRNYLEWLTSVPWGLTSPENRRLSVAKKALDEGHYGMK 484
Cdd:TIGR00763 248 EL-EKLKEKLEELKLPEEVKKVIEKELTKLSLLEPSSSEFTVTRNYLDWLTDLPWGKYSKENLDLKRAKEILDEDHYGLK 326
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17505831   485 DVKERIMEFIAVNLLRKSIGGKILCFHGPPGVGKTSIAKSIATALNREYFRFSVGGMTDVAEIKGHRRTYVGAMPGKMIQ 564
Cdd:TIGR00763 327 KVKERILEYLAVQKLRGKMKGPILCLVGPPGVGKTSLGKSIAKALNRKFVRFSLGGVRDEAEIRGHRRTYVGAMPGRIIQ 406
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17505831   565 CMKKVKTENPLVLIDEVDKIgGAGFHGDPASALLELLDPEQNANFNDHFLDVPVDLSRVLFICTANEISKIPGPLRDRME 644
Cdd:TIGR00763 407 GLKKAKTKNPLFLLDEIDKI-GSSFRGDPASALLEVLDPEQNNAFSDHYLDVPFDLSKVIFIATANSIDTIPRPLLDRME 485
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17505831   645 MIDVSGYLAEEKVEIAHQHLIPQLRKDTSLATEQLKIEDSALEELIKHYCRESGVRNLQQHIERIFRKAALQIAEqQNED 724
Cdd:TIGR00763 486 VIELSGYTEEEKLEIAKKYLIPKALEDHGLKPDELKITDEALLLLIKYYTREAGVRNLERQIEKICRKAAVKLVE-QGEK 564
                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17505831   725 EepaekattaitenseaepitstssadclKSSAEQIVVCTENLQKFVGRPKFTSDRMYEVTPPGVIMGLAWTAMGGSALY 804
Cdd:TIGR00763 565 K----------------------------KSEAESVVITPDNLKKYLGKPVFTYERAYEVTPPGVVMGLAWTPMGGDTLF 616
                         730       740       750       760       770       780       790       800
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17505831   805 IETVLKRPvdltndkDGSIETTGNLGDVMKESVRTALTVAKGILAREQPDNKFFDKAHIHIHVPEGATPKDGPSAGVTLV 884
Cdd:TIGR00763 617 IETTKVAG-------KGSLELTGQLGDVMKESAQIALTYVRSIAADLGISPNFFEKADIHLHVPEGATPKDGPSAGITMA 689
                         810       820       830       840       850       860       870       880
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17505831   885 SSLLSLALDRPVVQDMAMTGEISLTGKVLPVGGIREKVIAARRVGAKRVFLPNENRRDFDDLPEFMKSELDIRFVSHYDE 964
Cdd:TIGR00763 690 TALLSLATGKPVRPDVAMTGEITLRGKVLPIGGLKEKTIAAKRAGIKTIILPEKNRRDLEELPENVKEGLEIHFVKHYDE 769

                  ....*.
gi 17505831   965 LYEHLF 970
Cdd:TIGR00763 770 VLKKAF 775
Lon COG0466
ATP-dependent Lon protease, bacterial type [Posttranslational modification, protein turnover, ...
254-970 0e+00

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


Pssm-ID: 440234 [Multi-domain]  Cd Length: 785  Bit Score: 881.28  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17505831 254 QKKGIIMVRTEnVVAEPVPKNNETKATMMAIVQTIRDVVQFNQLFGQQINLLLhpsQNvIDNPVYLCDLVATLVqSAETK 333
Cdd:COG0466 108 QEEPYLEAEVE-PLEEEEEDDKELEALMRSLKEQFEEYVKLNPKIPPELLAAL---SN-IEDPGRLADFIASHL-PLKIE 181
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17505831 334 DLQEMMDEIDVSKRLKIALLLIQKEKAVAKLKYDINKDVEKKVQDHHRKYLLNEQLKVIKKELGiEKDEKTTIIEKIDER 413
Cdd:COG0466 182 EKQELLETLDVKERLEKLLELLEKEIEVLELEKKIRSRVKEQMEKSQREYYLREQLKAIQKELG-EKDDGEDEIEELREK 260
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17505831 414 IKTLAVPEYALKVINEEKTKLQFLDPHSSEFSVTRNYLEWLTSVPWGLTSPENRRLSVAKKALDEGHYGMKDVKERIMEF 493
Cdd:COG0466 261 IEKAKLPEEVKEKAEKELKKLERMPPMSAEATVIRNYLDWLLDLPWGKRTKDNLDLKKAEKILDEDHYGLEKVKERILEY 340
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17505831 494 IAVNLLRKSIGGKILCFHGPPGVGKTSIAKSIATALNREYFRFSVGGMTDVAEIKGHRRTYVGAMPGKMIQCMKKVKTEN 573
Cdd:COG0466 341 LAVRKLKKKLKGPILCLVGPPGVGKTSLGKSIARALGRKFVRISLGGVRDEAEIRGHRRTYIGAMPGRIIQGLKKAGTKN 420
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17505831 574 PLVLIDEVDKIGgAGFHGDPASALLELLDPEQNANFNDHFLDVPVDLSRVLFICTANEISKIPGPLRDRMEMIDVSGYLA 653
Cdd:COG0466 421 PVFLLDEIDKMG-SDFRGDPASALLEVLDPEQNNTFSDHYLEVPFDLSKVMFIATANSLDTIPAPLLDRMEIIELSGYTE 499
                       410       420       430       440       450       460       470       480
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17505831 654 EEKVEIAHQHLIPQLRKDTSLATEQLKIEDSALEELIKHYCRESGVRNLQQHIERIFRKAALQIAEqqnedeepaekatt 733
Cdd:COG0466 500 EEKLEIAKRYLIPKQLKEHGLKKEELKISDEALRKIIRGYTREAGVRNLEREIAKICRKVAKKIAE-------------- 565
                       490       500       510       520       530       540       550       560
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17505831 734 aitenseaepitstssadclkSSAEQIVVCTENLQKFVGRPKFTSDRMYEVTPPGVIMGLAWTAMGGSALYIETVL---K 810
Cdd:COG0466 566 ---------------------GKKKKVTITPKNLEKYLGVPRFRYEKAEEEDQVGVVTGLAWTEVGGDILFIEATLmpgK 624
                       570       580       590       600       610       620       630       640
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17505831 811 rpvdltndkdGSIETTGNLGDVMKESVRTALTVAKGILAREQPDNKFFDKAHIHIHVPEGATPKDGPSAGVTLVSSLLSL 890
Cdd:COG0466 625 ----------GKLTLTGQLGDVMKESAQAALSYVRSRAEELGIDPDFFEKYDIHIHVPEGATPKDGPSAGITMATALVSA 694
                       650       660       670       680       690       700       710       720
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17505831 891 ALDRPVVQDMAMTGEISLTGKVLPVGGIREKVIAARRVGAKRVFLPNENRRDFDDLPEFMKSELDIRFVSHYDELYEHLF 970
Cdd:COG0466 695 LTGRPVRSDVAMTGEITLRGRVLPIGGLKEKLLAAHRAGIKTVILPKENEKDLEEIPEEVKKGLEFHPVEHIDEVLKIAL 774
PRK10787 PRK10787
DNA-binding ATP-dependent protease La; Provisional
309-965 1.41e-171

DNA-binding ATP-dependent protease La; Provisional


Pssm-ID: 182730 [Multi-domain]  Cd Length: 784  Bit Score: 519.88  E-value: 1.41e-171
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17505831  309 SQNVIDNPVYLCDLVATLVqSAETKDLQEMMDEIDVSKRLKIALLLIQKEKAVAKLKYDINKDVEKKVQDHHRKYLLNEQ 388
Cdd:PRK10787 155 SLNSIDDPARLADTIAAHM-PLKLADKQSVLEMSDVNERLEYLMAMMESEIDLLQVEKRIRNRVKKQMEKSQREYYLNEQ 233
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17505831  389 LKVIKKELGiEKDEKTTIIEKIDERIKTLAVPEYALKVINEEKTKLQFLDPHSSEFSVTRNYLEWLTSVPWGLTSPENRR 468
Cdd:PRK10787 234 MKAIQKELG-EMDDAPDENEALKRKIDAAKMPKEAKEKAEAELQKLKMMSPMSAEATVVRGYIDWMVQVPWNARSKVKKD 312
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17505831  469 LSVAKKALDEGHYGMKDVKERIMEFIAVNLLRKSIGGKILCFHGPPGVGKTSIAKSIATALNREYFRFSVGGMTDVAEIK 548
Cdd:PRK10787 313 LRQAQEILDTDHYGLERVKDRILEYLAVQSRVNKIKGPILCLVGPPGVGKTSLGQSIAKATGRKYVRMALGGVRDEAEIR 392
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17505831  549 GHRRTYVGAMPGKMIQCMKKVKTENPLVLIDEVDKIgGAGFHGDPASALLELLDPEQNANFNDHFLDVPVDLSRVLFICT 628
Cdd:PRK10787 393 GHRRTYIGSMPGKLIQKMAKVGVKNPLFLLDEIDKM-SSDMRGDPASALLEVLDPEQNVAFSDHYLEVDYDLSDVMFVAT 471
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17505831  629 ANEISkIPGPLRDRMEMIDVSGYLAEEKVEIAHQHLIPQLRKDTSLATEQLKIEDSALEELIKHYCRESGVRNLQQHIER 708
Cdd:PRK10787 472 SNSMN-IPAPLLDRMEVIRLSGYTEDEKLNIAKRHLLPKQIERNALKKGELTVDDSAIIGIIRYYTREAGVRSLEREISK 550
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17505831  709 IFRKAALQIaeqqnedeepaekattaitenseaepitstssadCLKSSAEQIVVCTENLQKFVGRPKFTSDRMYEVTPPG 788
Cdd:PRK10787 551 LCRKAVKQL----------------------------------LLDKSLKHIEINGDNLHDYLGVQRFDYGRADNENRVG 596
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17505831  789 VIMGLAWTAMGGSALYIETVlkrpvdlTNDKDGSIETTGNLGDVMKESVRTALTVAKGILAREQPDNKFFDKAHIHIHVP 868
Cdd:PRK10787 597 QVTGLAWTEVGGDLLTIETA-------CVPGKGKLTYTGSLGEVMQESIQAALTVVRARAEKLGINPDFYEKRDIHVHVP 669
                        570       580       590       600       610       620       630       640
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17505831  869 EGATPKDGPSAGVTLVSSLLSLALDRPVVQDMAMTGEISLTGKVLPVGGIREKVIAARRVGAKRVFLPNENRRDFDDLPE 948
Cdd:PRK10787 670 EGATPKDGPSAGIAMCTALVSCLTGNPVRADVAMTGEITLRGQVLPIGGLKEKLLAAHRGGIKTVLIPFENKRDLEEIPD 749
                        650
                 ....*....|....*..
gi 17505831  949 FMKSELDIRFVSHYDEL 965
Cdd:PRK10787 750 NVIADLDIHPVKRIEEV 766
RecA-like_Lon cd19500
lon protease homolog 2 peroxisomal; Lon protease (also known as Lon peptidase) is an ...
469-651 9.52e-121

lon protease homolog 2 peroxisomal; Lon protease (also known as Lon peptidase) is an evolutionarily conserved ATP-dependent serine protease, present in bacteria and eukaryotic mitochondria and peroxisomes, which mediates the selective degradation of mutant and abnormal proteins as well as certain short-lived regulatory proteins. Lon protease is both an ATP-dependent peptidase and a protein-activated ATPase. This RecA-like Lon domain subfamily belongs to the RecA-like NTPase family which includes the NTP binding domain of F1 and V1 H(+)ATPases, DnaB and related helicases as well as bacterial RecA and related eukaryotic and archaeal recombinases. The RecA-like NTPase family also includes bacterial conjugation proteins and related DNA transfer proteins involved in type II and type IV secretion.


Pssm-ID: 410908 [Multi-domain]  Cd Length: 182  Bit Score: 365.34  E-value: 9.52e-121
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17505831 469 LSVAKKALDEGHYGMKDVKERIMEFIAVNLLRKSIGGKILCFHGPPGVGKTSIAKSIATALNREYFRFSVGGMTDVAEIK 548
Cdd:cd19500   1 IKKARKVLDADHYGLEDVKERILEYLAVRKLKGSMKGPILCLVGPPGVGKTSLGKSIARALGRKFVRISLGGVRDEAEIR 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17505831 549 GHRRTYVGAMPGKMIQCMKKVKTENPLVLIDEVDKIgGAGFHGDPASALLELLDPEQNANFNDHFLDVPVDLSRVLFICT 628
Cdd:cd19500  81 GHRRTYVGAMPGRIIQALKKAGTNNPVFLLDEIDKI-GSSFRGDPASALLEVLDPEQNSTFSDHYLDVPFDLSKVLFIAT 159
                       170       180
                ....*....|....*....|...
gi 17505831 629 ANEISKIPGPLRDRMEMIDVSGY 651
Cdd:cd19500 160 ANSLDTIPGPLLDRMEIIELSGY 182
Lon_C pfam05362
Lon protease (S16) C-terminal proteolytic domain; The Lon serine proteases must hydrolyse ATP ...
761-970 1.16e-75

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: 246.77  E-value: 1.16e-75
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17505831   761 VVCTENLQKFVGRPKFTSDRMYEVTPPGVIMGLAWTAMGGSALYIETVLKrpvdltnDKDGSIETTGNLGDVMKESVRTA 840
Cdd:pfam05362   1 KVTAKNLEKYLGVPRFRYGEAEKEDQVGVVTGLAWTEVGGDLLTIEAVIM-------PGKGKLTLTGQLGDVMKESAQAA 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17505831   841 LTVAKGILAREQPDNKFFDKAHIHIHVPEGATPKDGPSAGVTLVSSLLSLALDRPVVQDMAMTGEISLTGKVLPVGGIRE 920
Cdd:pfam05362  74 LSYVRSRAEELGIDPDFFEKKDIHIHVPEGATPKDGPSAGVTMATALVSALTGIPVRKDVAMTGEITLRGRVLPIGGLKE 153
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 17505831   921 KVIAARRVGAKRVFLPNENRRDFDDLPEFMKSELDIRFVSHYDELYEHLF 970
Cdd:pfam05362 154 KLLAAHRAGIKTVIIPKENEKDLEDIPENVREGLEIIPVEHVDEVLKHAL 203
AAA pfam00004
ATPase family associated with various cellular activities (AAA); AAA family proteins often ...
508-646 2.32e-31

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: 119.24  E-value: 2.32e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17505831   508 LCFHGPPGVGKTSIAKSIATALNREYFRFSVGGMTDvaeikghrrTYVGAMPGKMIQCMKKVKTENPLVL-IDEVDKIGG 586
Cdd:pfam00004   1 LLLYGPPGTGKTTLAKAVAKELGAPFIEISGSELVS---------KYVGESEKRLRELFEAAKKLAPCVIfIDEIDALAG 71
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 17505831   587 AGFHG------DPASALLELLDPEQNANfndhfldvpvdlSRVLFICTANEISKIPGPLRDRMEMI 646
Cdd:pfam00004  72 SRGSGgdsesrRVVNQLLTELDGFTSSN------------SKVIVIAATNRPDKLDPALLGRFDRI 125
LON_substr_bdg pfam02190
ATP-dependent protease La (LON) substrate-binding domain; This domain has been shown to be ...
88-357 4.97e-19

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: 86.24  E-value: 4.97e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17505831    88 NVPMLAINRYPLFPGFIKKVDiVKDDNLKALIRRQLSLKQPYAGVFVKRDDENKEEtiTSLSEVYPTGSFVQIIEVRDQG 167
Cdd:pfam02190   1 ELPLLPLRNTVLFPGMVLPLF-VGRPRSIAAIEAALNKDKLYGVLLVSQKDAEDEE--PTPDDLYEVGTVAKIVQILKLP 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17505831   168 S-VLELVLSAHRRIRalepIDEItpknetplngrrargkraasatspltpppsppplapsvasvapeisateekeekttp 246
Cdd:pfam02190  78 DgTYKVLVEGLERVR----IVEL--------------------------------------------------------- 96
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17505831   247 psatgEKQKKGIIMVRTENVVAEPVPKNNETKATMMAIVQTIRDVVQfnqlfgQQINLLLHPSQNVIDNPVYLCDLVATL 326
Cdd:pfam02190  97 -----VKKEEPYLRAEVEDLPEDSDELSEALKALVKELIEKLRRLLK------LLLPLELLLKIKDIENPGRLADLVAAI 165
                         250       260       270
                  ....*....|....*....|....*....|.
gi 17505831   327 VqSAETKDLQEMMDEIDVSKRLKIALLLIQK 357
Cdd:pfam02190 166 L-PLSPEEKQELLETLDVKERLEKVLELLNR 195
RecA-like_protease cd19481
proteases similar to RecA; RecA-like NTPases. This family includes the NTP binding domain of ...
486-640 4.64e-16

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: 76.55  E-value: 4.64e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17505831 486 VKERIMEFIAV------NLLRKSIGGKILCFHGPPGVGKTSIAKSIATALNREYFRFSVGGMTDVAeikghrRTYVGAMP 559
Cdd:cd19481   1 LKASLREAVEAprrgsrLRRYGLGLPKGILLYGPPGTGKTLLAKALAGELGLPLIVVKLSSLLSKY------VGESEKNL 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17505831 560 GKMIQCMKkvKTENPLVLIDEVDKIGG-AGFHGDPA------SALLELLDPEQNanfndhfldvpvdLSRVLFICTANEI 632
Cdd:cd19481  75 RKIFERAR--RLAPCILFIDEIDAIGRkRDSSGESGelrrvlNQLLTELDGVNS-------------RSKVLVIAATNRP 139

                ....*....
gi 17505831 633 SKI-PGPLR 640
Cdd:cd19481 140 DLLdPALLR 148
SpoVK COG0464
AAA+-type ATPase, SpoVK/Ycf46/Vps4 family [Cell wall/membrane/envelope biogenesis, Cell cycle ...
340-724 7.92e-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: 77.64  E-value: 7.92e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17505831 340 DEIDVSKRLKIALLLIQKEKAVAKLKYDINKDVEKKVQDHHRKYLLNEQLKVIKKELGIEKDEKTTIIEKIDERIKTLAV 419
Cdd:COG0464  15 LLLLDDAALRLLLLLLLALAAALLLLLLLLLLLLLALLLVELLLLLLSGALAALLLLALLLLALLALLAALLSALELLLL 94
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17505831 420 PEYALKVINEEKTKLQFLDPHSSEFSVTRNYLEWLTSVPWGLTSPENRRLSVAKKALDEGHY----GMKDVKERIMEFIA 495
Cdd:COG0464  95 GELLLLLLLLLLLLLLLLDLERALLELLRESAEALALAAPLVTYEDIGGLEEELLELREAILddlgGLEEVKEELRELVA 174
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17505831 496 VNL----LRKSIG---GKILCFHGPPGVGKTSIAKSIATALNREYFRFSVGGMTDvaeikghrrTYVGAMPGKMIQCMKK 568
Cdd:COG0464 175 LPLkrpeLREEYGlppPRGLLLYGPPGTGKTLLARALAGELGLPLIEVDLSDLVS---------KYVGETEKNLREVFDK 245
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17505831 569 VKTENPLVL-IDEVDKIGGA-GFHGDPA-----SALLELLDpeqnaNFNDhfldvpvdlsRVLFICTANEISKIPGPLRD 641
Cdd:COG0464 246 ARGLAPCVLfIDEADALAGKrGEVGDGVgrrvvNTLLTEME-----ELRS----------DVVVIAATNRPDLLDPALLR 310
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17505831 642 RM-EMIDVSGYLAEEKVEIAHQHLipqlrKDTSLAteqlkiEDSALEELIKHYCRESGvRNlqqhIERIFRKAALQIAEQ 720
Cdd:COG0464 311 RFdEIIFFPLPDAEERLEIFRIHL-----RKRPLD------EDVDLEELAEATEGLSG-AD----IRNVVRRAALQALRL 374

                ....
gi 17505831 721 QNED 724
Cdd:COG0464 375 GREP 378
AAA cd00009
The AAA+ (ATPases Associated with a wide variety of cellular Activities) superfamily ...
487-646 8.95e-13

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: 66.79  E-value: 8.95e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17505831 487 KERIMEFIAVNLLRKSIGGKILCFHGPPGVGKTSIAKSIATALNREYFRF---SVGGMTDVAEIKGHRRTYVGAMPGKMI 563
Cdd:cd00009   1 VGQEEAIEALREALELPPPKNLLLYGPPGTGKTTLARAIANELFRPGAPFlylNASDLLEGLVVAELFGHFLVRLLFELA 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17505831 564 QCMKkvkteNPLVLIDEVDKIgGAGFHgdpaSALLELLdpeqnanfnDHFLDVPVDLSRVLFICTAN--EISKIPGPLRD 641
Cdd:cd00009  81 EKAK-----PGVLFIDEIDSL-SRGAQ----NALLRVL---------ETLNDLRIDRENVRVIGATNrpLLGDLDRALYD 141

                ....*
gi 17505831 642 RMEMI 646
Cdd:cd00009 142 RLDIR 146
COG1750 COG1750
Predicted archaeal serine protease, S18 family [General function prediction only];
823-970 6.42e-12

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


Pssm-ID: 441356 [Multi-domain]  Cd Length: 213  Bit Score: 65.77  E-value: 6.42e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17505831 823 IETTGNLGDVMKESVRTALTVAkGILAreqpdNKFFDKAHIHIHVPEGATPKDGPSAGVTLVSSLLSLALDRPVVQDMAM 902
Cdd:COG1750  62 VSTSPLTGPDTQASARIAALVA-SLLA-----GVDLSSYDVYISIESDSPIVGGPSAGGAMTVATYAALLGLPLNKSVTM 135
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 17505831 903 TGEISLTGKVLPVGGIREKVIAARRVGAKRVFLPNENRRDFD---------DLPEFMKsELDIRF--VSHYDELYEHLF 970
Cdd:COG1750 136 TGMINPDGSIGPVGGVYEKLEAAASAGAKYFLIPKGQAILTGyntqvgetvDLVEYGK-ELGVKVieVSTIADALQYFT 213
SdrC COG3480
Predicted secreted protein YlbL, contains PDZ domain [Signal transduction mechanisms];
812-939 3.98e-09

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


Pssm-ID: 442703 [Multi-domain]  Cd Length: 344  Bit Score: 59.44  E-value: 3.98e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17505831 812 PVDLTNDKDG-SIETTGNLGDVMKESVRTALtvakGILAREQPDNKFfdkaHIHIHVPE-GatpkdGPSAG-------Vt 882
Cdd:COG3480 187 TVTLTVTRDGkEKTVTVTLVKLPDDDGRAGI----GISLVTKVDFPF----DVDIDLGDiG-----GPSAGlmfalgiY- 252
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 17505831 883 lvssllslalDRPVVQDM------AMTGEISLTGKVLPVGGIREKVIAARRVGAKrVFL-PNEN 939
Cdd:COG3480 253 ----------DQLTPGDLtggkkiAGTGTIDADGTVGPIGGIDQKVVAARRAGAT-IFLaPASN 305
RecA-like_FtsH cd19501
ATP-dependent zinc metalloprotease FtsH; FtsH ATPase is a processive, ATP-dependent zinc ...
482-591 1.30e-08

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: 55.32  E-value: 1.30e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17505831 482 GMKDVKERIMEFiaVNLLRK-----SIGGKI---LCFHGPPGVGKTSIAKSIATALNREYfrFSVGGmTDVAEIkghrrt 553
Cdd:cd19501   8 GCEEAKEELKEV--VEFLKNpekftKLGAKIpkgVLLVGPPGTGKTLLAKAVAGEAGVPF--FSISG-SDFVEM------ 76
                        90       100       110       120
                ....*....|....*....|....*....|....*....|..
gi 17505831 554 YVGAMPGKMIQCMKKVKTENP-LVLIDEVDKIG---GAGFHG 591
Cdd:cd19501  77 FVGVGASRVRDLFEQAKKNAPcIVFIDEIDAVGrkrGAGLGG 118
AAA_2 pfam07724
AAA domain (Cdc48 subfamily); This Pfam entry includes some of the AAA proteins not detected ...
510-669 4.41e-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: 4.41e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17505831   510 FHGPPGVGKTSIAKSIATALNREYFRFSVGGMTD------VAEIKGHRRTYVGAmpGKMIQCMKKV-KTENPLVLIDEVD 582
Cdd:pfam07724   8 FLGPTGVGKTELAKALAELLFGDERALIRIDMSEymeehsVSRLIGAPPGYVGY--EEGGQLTEAVrRKPYSIVLIDEIE 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17505831   583 KIggagfHGDPASALLELLDpeqNANFNDHFlDVPVDLSRVLFICTAN-EISKIPGPLRDRMEMIDVSgyLAEEKVEIAH 661
Cdd:pfam07724  86 KA-----HPGVQNDLLQILE---GGTLTDKQ-GRTVDFKNTLFIMTGNfGSEKISDASRLGDSPDYEL--LKEEVMDLLK 154

                  ....*...
gi 17505831   662 QHLIPQLR 669
Cdd:pfam07724 155 KGFIPEFL 162
44 PHA02544
clamp loader, small subunit; Provisional
505-693 9.40e-08

clamp loader, small subunit; Provisional


Pssm-ID: 222866 [Multi-domain]  Cd Length: 316  Bit Score: 55.00  E-value: 9.40e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17505831  505 GKI--LCFHGP-PGVGKTSIAKSIATALNREYFrFSVGGMTDVAEIKGHRRTYVGAM----PGKMIqcmkkvktenplvL 577
Cdd:PHA02544  40 GRIpnMLLHSPsPGTGKTTVAKALCNEVGAEVL-FVNGSDCRIDFVRNRLTRFASTVsltgGGKVI-------------I 105
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17505831  578 IDEVDKIGGAgfhgdPASALLELLDPEQNANfndhfldvpvdlsrVLFICTANEISKIPGPLRDRMEMIDVSGYLAEEKV 657
Cdd:PHA02544 106 IDEFDRLGLA-----DAQRHLRSFMEAYSKN--------------CSFIITANNKNGIIEPLRSRCRVIDFGVPTKEEQI 166
                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 17505831  658 EIAHQHLIpqlRKDTSLATEQLKIEDSALEELIKHY 693
Cdd:PHA02544 167 EMMKQMIV---RCKGILEAEGVEVDMKVLAALVKKN 199
AAA smart00382
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ...
505-642 1.50e-07

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: 51.61  E-value: 1.50e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17505831    505 GKILCFHGPPGVGKTSIAKSIATALNREYFRFSVGGMTDVAEIKGHRRTYVGAMPGKM----IQCMKKV-----KTENPL 575
Cdd:smart00382   2 GEVILIVGPPGSGKTTLARALARELGPPGGGVIYIDGEDILEEVLDQLLLIIVGGKKAsgsgELRLRLAlalarKLKPDV 81
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 17505831    576 VLIDEVDKiggagfHGDPASALLELLDPEqnanfnDHFLDVPVDLSRVLFICTANEIS-KIPGPLRDR 642
Cdd:smart00382  82 LILDEITS------LLDAEQEALLLLLEE------LRLLLLLKSEKNLTVILTTNDEKdLGPALLRRR 137
LON smart00464
Found in ATP-dependent protease La (LON); N-terminal domain of the ATP-dependent protease La ...
89-151 1.85e-07

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: 49.74  E-value: 1.85e-07
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 17505831     89 VPMLAINRYPLFPGFIKKVDiVKDDNLKALIRRQLSLKQPYAGVFVKRDDENKEETITSLSEV 151
Cdd:smart00464   2 LPLLPIRRRPLFPGFVLPIP-VKRPKSVAAIKEALRRSQPYVIVFLLQDDPTETPEPLSDTIA 63
PRK04195 PRK04195
replication factor C large subunit; Provisional
482-692 2.80e-07

replication factor C large subunit; Provisional


Pssm-ID: 235250 [Multi-domain]  Cd Length: 482  Bit Score: 54.16  E-value: 2.80e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17505831  482 GMKDVKERIMEFIAvNLLRKSIGgKILCFHGPPGVGKTSIAKSIATALNREYF-------------RFSVGGMTDVAEIK 548
Cdd:PRK04195  18 GNEKAKEQLREWIE-SWLKGKPK-KALLLYGPPGVGKTSLAHALANDYGWEVIelnasdqrtadviERVAGEAATSGSLF 95
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17505831  549 GHRRTyvgampgkmiqcmkkvktenpLVLIDEVDKI-GGAGFHGdpASALLELLDpeqNANfndhfldVPVdlsrvlfIC 627
Cdd:PRK04195  96 GARRK---------------------LILLDEVDGIhGNEDRGG--ARAILELIK---KAK-------QPI-------IL 135
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 17505831  628 TANEI-SKIPGPLRDRMEMIDVSgylaeekvEIAHQHLIPQLRKdtSLATEQLKIEDSALEELIKH 692
Cdd:PRK04195 136 TANDPyDPSLRELRNACLMIEFK--------RLSTRSIVPVLKR--ICRKEGIECDDEALKEIAER 191
PRK13342 PRK13342
recombination factor protein RarA; Reviewed
498-581 3.87e-07

recombination factor protein RarA; Reviewed


Pssm-ID: 237355 [Multi-domain]  Cd Length: 413  Bit Score: 53.55  E-value: 3.87e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17505831  498 LLRKSIGGKILC---FHGPPGVGKTSIAKSIATALNREYFRFSvGGMTDVAEIKghrrtyvgampgKMIQCMKKVKT--E 572
Cdd:PRK13342  26 PLRRMIEAGRLSsmiLWGPPGTGKTTLARIIAGATDAPFEALS-AVTSGVKDLR------------EVIEEARQRRSagR 92

                 ....*....
gi 17505831  573 NPLVLIDEV 581
Cdd:PRK13342  93 RTILFIDEI 101
AAA_5 pfam07728
AAA domain (dynein-related subfamily); This Pfam entry includes some of the AAA proteins not ...
508-643 5.75e-07

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: 49.60  E-value: 5.75e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17505831   508 LCFHGPPGVGKTSIAKSIATAL-NREYFRFSVGGMTDVAEIKGHRRtyvgampgkmIQCMKKVKTENPLV---------L 577
Cdd:pfam07728   2 VLLVGPPGTGKTELAERLAAALsNRPVFYVQLTRDTTEEDLFGRRN----------IDPGGASWVDGPLVraaregeiaV 71
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17505831   578 IDEVDKIggagfHGDPASALLELLDPEQNANFNDHFLdVPVDLSRVLFICTANEI----SKIPGPLRDRM 643
Cdd:pfam07728  72 LDEINRA-----NPDVLNSLLSLLDERRLLLPDGGEL-VKAAPDGFRLIATMNPLdrglNELSPALRSRF 135
RPT1 COG1222
ATP-dependent 26S proteasome regulatory subunit [Posttranslational modification, protein ...
482-586 7.09e-07

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


Pssm-ID: 440835 [Multi-domain]  Cd Length: 326  Bit Score: 52.32  E-value: 7.09e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17505831 482 GMKDVKERIMEFIAVNLLR----KSIG----GKILcFHGPPGVGKTSIAKSIATALNREYFRfsVGGmtdvAEIkghRRT 553
Cdd:COG1222  82 GLDEQIEEIREAVELPLKNpelfRKYGieppKGVL-LYGPPGTGKTLLAKAVAGELGAPFIR--VRG----SEL---VSK 151
                        90       100       110
                ....*....|....*....|....*....|....
gi 17505831 554 YVGAMPGKMIQCMKKVKTENPLVL-IDEVDKIGG 586
Cdd:COG1222 152 YIGEGARNVREVFELAREKAPSIIfIDEIDAIAA 185
COG1223 COG1223
Predicted ATPase, AAA+ superfamily [General function prediction only];
481-585 1.95e-06

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


Pssm-ID: 440836 [Multi-domain]  Cd Length: 246  Bit Score: 50.27  E-value: 1.95e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17505831 481 YGMKDVKER----IMEFIAVNLLRK---SIGGKILcFHGPPGVGKTSIAKSIATALNREYFRFSVGGMTDvaeikghrrT 553
Cdd:COG1223   5 VGQEEAKKKlkliIKELRRRENLRKfglWPPRKIL-FYGPPGTGKTMLAEALAGELKLPLLTVRLDSLIG---------S 74
                        90       100       110
                ....*....|....*....|....*....|..
gi 17505831 554 YVGAMPGKMIQCMKKVKTENPLVLIDEVDKIG 585
Cdd:COG1223  75 YLGETARNLRKLFDFARRAPCVIFFDEFDAIA 106
RarA COG2256
Replication-associated recombination protein RarA (DNA-dependent ATPase) [Replication, ...
498-548 4.06e-06

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


Pssm-ID: 441857 [Multi-domain]  Cd Length: 439  Bit Score: 50.44  E-value: 4.06e-06
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....
gi 17505831 498 LLRKSI-GGKI--LCFHGPPGVGKTSIAKSIATALNREYFRFSvGGMTDVAEIK 548
Cdd:COG2256  39 PLRRAIeAGRLssMILWGPPGTGKTTLARLIANATDAEFVALS-AVTSGVKDIR 91
RecA-like_VPS4-like cd19509
ATPase domain of VPS4, ATAD1, K, KTNA1, Spastin, FIGL-1 and similar ATPase domains; This ...
482-644 4.59e-06

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: 47.73  E-value: 4.59e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17505831 482 GMKDVKERIMEFIAVNLLRKSI--GG----KILCFHGPPGVGKTSIAKSIATALNREYFRFSVGGMTDvaeikghrrTYV 555
Cdd:cd19509   3 GLDDAKEALKEAVILPSLRPDLfpGLrgppRGILLYGPPGTGKTLLARAVASESGSTFFSISASSLVS---------KWV 73
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17505831 556 GAmPGKMIQCMKKVKTEN--PLVLIDEVDKIG---GAGFHGDPA---SALLELLDPEQNAnfndhfldvpvDLSRVLFIC 627
Cdd:cd19509  74 GE-SEKIVRALFALARELqpSIIFIDEIDSLLserGSGEHEASRrvkTEFLVQMDGVLNK-----------PEDRVLVLG 141
                       170
                ....*....|....*..
gi 17505831 628 TANEISKIPGPLRDRME 644
Cdd:cd19509 142 ATNRPWELDEAFLRRFE 158
RecA-like_Pch2-like cd19508
ATPase domain of Pachytene checkpoint 2 (Pch2) and similar ATPase domains; Pch2 (known as ...
486-642 5.44e-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: 48.21  E-value: 5.44e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17505831 486 VKERIMEFIAVNLLRKSIG--------GKILCFHGPPGVGKTSIAKSIATALN-REYFRFSVGGMTdvaEIKGHRR---- 552
Cdd:cd19508  25 LKSRLLDYVTTTLLFSDKNvntnlitwNRLVLLHGPPGTGKTSLCKALAQKLSiRLSSRYRYGQLI---EINSHSLfskw 101
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17505831 553 -TYVGAMPGKM---IQCMKKVKTENPLVLIDEVDKIGGAgfhGDPASALLELLDPEQNANFNDHFLDVPVDLSRVLFICT 628
Cdd:cd19508 102 fSESGKLVTKMfqkIQELIDDKDALVFVLIDEVESLAAA---RSASSSGTEPSDAIRVVNAVLTQIDRIKRYHNNVILLT 178
                       170
                ....*....|....
gi 17505831 629 ANEISKIPGPLRDR 642
Cdd:cd19508 179 SNLLEKIDVAFVDR 192
hflB PRK10733
ATP-dependent zinc metalloprotease FtsH;
482-591 3.21e-05

ATP-dependent zinc metalloprotease FtsH;


Pssm-ID: 182683 [Multi-domain]  Cd Length: 644  Bit Score: 47.72  E-value: 3.21e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17505831  482 GMKDVKERIMEFiaVNLLR-----KSIGGKI---LCFHGPPGVGKTSIAKSIATALNREYFRFSvggMTDVAEIkghrrt 553
Cdd:PRK10733 156 GCDEAKEEVAEL--VEYLRepsrfQKLGGKIpkgVLMVGPPGTGKTLLAKAIAGEAKVPFFTIS---GSDFVEM------ 224
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 17505831  554 YVGAMPGKMIQCMKKVKTENP-LVLIDEVDKIG---GAGFHG 591
Cdd:PRK10733 225 FVGVGASRVRDMFEQAKKAAPcIIFIDEIDAVGrqrGAGLGG 266
MoxR COG0714
MoxR-like ATPase [General function prediction only]; MoxR-like ATPase is part of the Pathway ...
512-694 3.51e-05

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: 46.70  E-value: 3.51e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17505831 512 GPPGVGKTSIAKSIATALNREYFR--FSVGGM------TDVAEIKGHRRTYVgamPGKMIQcmkkvktenPLVLIDEVDK 583
Cdd:COG0714  38 GVPGVGKTTLAKALARALGLPFIRiqFTPDLLpsdilgTYIYDQQTGEFEFR---PGPLFA---------NVLLADEINR 105
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17505831 584 iggagfhGDPA--SALLELLDpeqnanfnDHFLDVP---VDLSRVLF-ICTANEISKI-----PGPLRDRMEM-IDVsGY 651
Cdd:COG0714 106 -------APPKtqSALLEAME--------ERQVTIPggtYKLPEPFLvIATQNPIEQEgtyplPEAQLDRFLLkLYI-GY 169
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|.
gi 17505831 652 L-AEEKVEIAHQH-------LIPQLRKDTSLATEQLkIEDSALEELIKHYC 694
Cdd:COG0714 170 PdAEEEREILRRHtgrhlaeVEPVLSPEELLALQEL-VRQVHVSEAVLDYI 219
RecA-like_NVL_r1-like cd19518
first of two ATPase domains of NVL (nuclear VCP-like protein) and similar ATPase domains; NVL ...
482-586 3.93e-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: 45.09  E-value: 3.93e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17505831 482 GMKDVKERIMEFIAVNLLRKSIGGKI-------LCFHGPPGVGKTSIAKSIATALNREYFRFS----VGGMTdvaeikgh 550
Cdd:cd19518   4 GMDSTLKELCELLIHPILPPEYFQHLgvepprgVLLHGPPGCGKTMLANAIAGELKVPFLKISateiVSGVS-------- 75
                        90       100       110
                ....*....|....*....|....*....|....*..
gi 17505831 551 rrtyvGAMPGKMIQCMKKVKTENP-LVLIDEVDKIGG 586
Cdd:cd19518  76 -----GESEEKIRELFDQAISNAPcIVFIDEIDAITP 107
ftsH CHL00176
cell division protein; Validated
482-592 4.86e-05

cell division protein; Validated


Pssm-ID: 214386 [Multi-domain]  Cd Length: 638  Bit Score: 47.35  E-value: 4.86e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17505831  482 GMKDVKERIMEFiaVNLLRK-----SIGGKI---LCFHGPPGVGKTSIAKSIATALNREYfrFSVGGMTDVAEIKGhrrt 553
Cdd:CHL00176 187 GIEEAKEEFEEV--VSFLKKperftAVGAKIpkgVLLVGPPGTGKTLLAKAIAGEAEVPF--FSISGSEFVEMFVG---- 258
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 17505831  554 yVGAmpGKMIQCMKKVKTENP-LVLIDEVDKIG---GAGFHGD 592
Cdd:CHL00176 259 -VGA--ARVRDLFKKAKENSPcIVFIDEIDAVGrqrGAGIGGG 298
T7SS_EccA TIGR03922
type VII secretion AAA-ATPase EccA; This model represents the AAA family ATPase, EccA, of the ...
469-693 5.64e-05

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: 46.76  E-value: 5.64e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17505831   469 LSVAKKALDEgHYGMKDVKERIMEF---IAVNLLRKSIGGKI------LCFHGPPGVGKTSIAKSIATALnreyfrfsvG 539
Cdd:TIGR03922 268 LAEAEAELAE-QIGLERVKRQVAALkssTAMALARAERGLPVaqtsnhMLFAGPPGTGKTTIARVVAKIY---------C 337
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17505831   540 GMTDVAE---IKGHRRTYVGAMPGKmiqcmKKVKTENplvLIDEVdkIGGAGFHgDPASALLELL----DPEQNANFNDH 612
Cdd:TIGR03922 338 GLGVLRKplvREVSRADLIGQYIGE-----SEAKTNE---IIDSA--LGGVLFL-DEAYTLVETGygqkDPFGLEAIDTL 406
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17505831   613 FLDVPVDLSRVLFICT--ANEISKI----PGpLRDRM-EMIDVSGYLAEEKVEIAhqHLIPQLRKDTslateqlkIEDSA 685
Cdd:TIGR03922 407 LARMENDRDRLVVIGAgyRKDLDKFlevnEG-LRSRFtRVIEFPSYSPDELVEIA--RRMATERDSV--------LDDAA 475

                  ....*...
gi 17505831   686 LEELIKHY 693
Cdd:TIGR03922 476 ADALLEAA 483
RecA-like_CDC48_NLV2_r1-like cd19503
first of two ATPase domains of CDC48 and NLV2, and similar ATPase domains; CDC48 in yeast and ...
482-602 1.30e-04

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: 43.43  E-value: 1.30e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17505831 482 GMKDVKERIMEFIAVNL----LRKSIGGK----ILcFHGPPGVGKTSIAKSIATALNREYFrfsvggmtdvaEIKGHrrT 553
Cdd:cd19503   4 GLDEQIASLKELIELPLkypeLFRALGLKpprgVL-LHGPPGTGKTLLARAVANEAGANFL-----------SISGP--S 69
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 17505831 554 YVGAMPGKMIQCMKKV-----KTENPLVLIDEVDKI------GGAGFHGDPASALLELLD 602
Cdd:cd19503  70 IVSKYLGESEKNLREIfeearSHAPSIIFIDEIDALapkreeDQREVERRVVAQLLTLMD 129
RecA-like_Ycf46-like cd19507
ATPase domain of Ycf46 and similar ATPase domains; Ycf46 may play a role in the regulation of ...
512-592 1.53e-04

ATPase domain of Ycf46 and similar ATPase domains; Ycf46 may play a role in the regulation of photosynthesis in cyanobacteria, especially in CO2 uptake and utilization. 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: 410915 [Multi-domain]  Cd Length: 161  Bit Score: 43.13  E-value: 1.53e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17505831 512 GPPGVGKTSIAKSIATALNREYFRFSVGGMTDvaeikghrrTYVGAMPGKMIQCMKKVKTENPLVL-IDEVDK-IGGAGF 589
Cdd:cd19507  38 GIQGTGKSLTAKAIAGVWQLPLLRLDMGRLFG---------GLVGESESRLRQMIQTAEAIAPCVLwIDEIEKgFSNADS 108

                ...
gi 17505831 590 HGD 592
Cdd:cd19507 109 KGD 111
ChlI pfam13541
Subunit ChlI of Mg-chelatase;
895-939 2.03e-04

Subunit ChlI of Mg-chelatase;


Pssm-ID: 433293 [Multi-domain]  Cd Length: 121  Bit Score: 42.05  E-value: 2.03e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 17505831   895 PVVQDMAMTGEISLTGKVLPVGGIREKVIAARRVGAKRVFLPNEN 939
Cdd:pfam13541  77 PVLEETIFLGELSLDGSLRPVRGALPIALAARKHGFRGLIVPKEN 121
DnaX COG2812
DNA polymerase III, gamma/tau subunits [Replication, recombination and repair];
495-689 5.90e-04

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


Pssm-ID: 442061 [Multi-domain]  Cd Length: 340  Bit Score: 43.26  E-value: 5.90e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17505831 495 AVNLLRKSI-GGKI----LcFHGPPGVGKTSIAKSIATALN----------------REyfrFSVGGMTDVAEI---KGH 550
Cdd:COG2812  18 VVRTLKNALaSGRLahayL-FTGPRGVGKTTLARILAKALNcengptgepcgecescRA---IAAGSHPDVIEIdaeASN 93
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17505831 551 R--------RTYVGAMPgkmIQCMKKVktenplVLIDEVDKIGGAGFhgdpaSALLELLD--PEqnanfndhfldvpvdl 620
Cdd:COG2812  94 IgvddirelIEKVSYAP---VEGRYKV------YIIDEAHMLTTEAF-----NALLKTLEepPP---------------- 143
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 17505831 621 sRVLFICTANEISKIPGPLRDRMEMIDVSgYLAEEKVEiahQHLIPQLRKdtslatEQLKIEDSALEEL 689
Cdd:COG2812 144 -HVVFILATTEPQKLLPTILSRCQRFDFR-RLPPEEIA---EHLAKIAER------EGIEIEPEALALI 201
RecA-like_PEX6_r2 cd19527
second of two ATPase domains of Peroxisomal biogenesis factor 6 (PEX6); PEX6(also known as ...
486-592 1.21e-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: 40.57  E-value: 1.21e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17505831 486 VKERIMEFIAVNLLRK---SIGGKI---LCFHGPPGVGKTSIAKSIATALNREYfrFSVGGMTDVaeikghrRTYVGAMP 559
Cdd:cd19527   1 VKKEILDTIQLPLEHPelfSSGLRKrsgILLYGPPGTGKTLLAKAIATECSLNF--LSVKGPELI-------NMYIGESE 71
                        90       100       110
                ....*....|....*....|....*....|....*
gi 17505831 560 GKMIQCMKKVKTENP-LVLIDEVDKIGGA-GFHGD 592
Cdd:cd19527  72 ANVREVFQKARDAKPcVIFFDELDSLAPSrGNSGD 106
rfc PRK00440
replication factor C small subunit; Reviewed
474-535 1.33e-03

replication factor C small subunit; Reviewed


Pssm-ID: 234763 [Multi-domain]  Cd Length: 319  Bit Score: 42.17  E-value: 1.33e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 17505831  474 KALDEgHYGMKDVKERIMEFIAvnllRKSIGGkiLCFHGPPGVGKTSIAKSIATALNREYFR 535
Cdd:PRK00440  14 RTLDE-IVGQEEIVERLKSYVK----EKNMPH--LLFAGPPGTGKTTAALALARELYGEDWR 68
RecA-like_CDC48_r1-like cd19519
first of two ATPase domains of CDC48 and similar ATPase domains; CDC48 in yeast and p97 or VCP ...
482-584 1.38e-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: 40.50  E-value: 1.38e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17505831 482 GMKDVKERIMEFIAVNL----LRKSIG---GKILCFHGPPGVGKTSIAKSIATALNReyFRFSVGGmtdvAEIKGhrrTY 554
Cdd:cd19519   4 GCRKQLAQIREMVELPLrhpeLFKAIGikpPRGILLYGPPGTGKTLIARAVANETGA--FFFLING----PEIMS---KL 74
                        90       100       110
                ....*....|....*....|....*....|.
gi 17505831 555 VGAMPGKMIQCMKKVKTENP-LVLIDEVDKI 584
Cdd:cd19519  75 AGESESNLRKAFEEAEKNAPaIIFIDEIDAI 105
ruvB PRK00080
Holliday junction branch migration DNA helicase RuvB;
474-530 2.23e-03

Holliday junction branch migration DNA helicase RuvB;


Pssm-ID: 234619 [Multi-domain]  Cd Length: 328  Bit Score: 41.27  E-value: 2.23e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 17505831  474 KALDEghY-GMKDVKERIMEFIAVNLLRKSIGGKILcFHGPPGVGKTSIAKSIATALN 530
Cdd:PRK00080  22 KSLDE--FiGQEKVKENLKIFIEAAKKRGEALDHVL-LYGPPGLGKTTLANIIANEMG 76
PRK06647 PRK06647
DNA polymerase III subunits gamma and tau; Validated
492-642 2.84e-03

DNA polymerase III subunits gamma and tau; Validated


Pssm-ID: 235845 [Multi-domain]  Cd Length: 563  Bit Score: 41.29  E-value: 2.84e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17505831  492 EFIaVNLLRKSI-GGKI---LCFHGPPGVGKTSIAKSIATALN----------------REyfrFSVGGMTDVAEIKGHR 551
Cdd:PRK06647  22 DFV-VETLKHSIeSNKIanaYIFSGPRGVGKTSSARAFARCLNcvngptpmpcgecsscKS---IDNDNSLDVIEIDGAS 97
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17505831  552 RTYVgampgkmiQCMKKVKTE---NP------LVLIDEVDKIGGAGFhgdpaSALLELLdpEQNANFndhfldvpvdlsr 622
Cdd:PRK06647  98 NTSV--------QDVRQIKEEimfPPassryrVYIIDEVHMLSNSAF-----NALLKTI--EEPPPY------------- 149
                        170       180
                 ....*....|....*....|
gi 17505831  623 VLFICTANEISKIPGPLRDR 642
Cdd:PRK06647 150 IVFIFATTEVHKLPATIKSR 169
ruvB TIGR00635
Holliday junction DNA helicase, RuvB subunit; All proteins in this family for which functions ...
482-530 2.84e-03

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: 40.75  E-value: 2.84e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 17505831   482 GMKDVKERIMEFIAVNLLRKSIGGKILcFHGPPGVGKTSIAKSIATALN 530
Cdd:TIGR00635   8 GQEKVKEQLQLFIEAAKMRQEALDHLL-LYGPPGLGKTTLAHIIANEMG 55
RecA-like_ClpB_Hsp104-like cd19499
Chaperone protein ClpB/Hsp104 subfamily; Bacterial Caseinolytic peptidase B (ClpB) and ...
508-630 3.29e-03

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: 39.47  E-value: 3.29e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17505831 508 LCFHGPPGVGKTSIAKSIATAL---NREYFRFSVGG---MTDVAEIKGHRRTYVGAmpGKMIQCMKKVKtENP--LVLID 579
Cdd:cd19499  44 FLFLGPTGVGKTELAKALAELLfgdEDNLIRIDMSEymeKHSVSRLIGAPPGYVGY--TEGGQLTEAVR-RKPysVVLLD 120
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....
gi 17505831 580 EVDKIggagfHGDPASALLELLDpeqnanfNDHFLD---VPVDLSRVLFICTAN 630
Cdd:cd19499 121 EIEKA-----HPDVQNLLLQVLD-------DGRLTDshgRTVDFKNTIIIMTSN 162
AAA_16 pfam13191
AAA ATPase domain; This family of domains contain a P-loop motif that is characteriztic of the ...
488-539 3.59e-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: 39.41  E-value: 3.59e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 17505831   488 ERIMEFIAVNLLRKSIG-GKILCFHGPPGVGKTSIAKSIATALNREYFRFSVG 539
Cdd:pfam13191   6 EEELEQLLDALDRVRSGrPPSVLLTGEAGTGKTTLLRELLRALERDGGYFLRG 58
RecA-like_spastin cd19524
ATPase domain of spastin; Spastin is an ATP-dependent microtubule-severing protein involved in ...
482-584 3.90e-03

ATPase domain of spastin; Spastin is an ATP-dependent microtubule-severing protein involved in microtubule dynamics; it specifically recognizes and cuts microtubules that are polyglutamylated. 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: 410932 [Multi-domain]  Cd Length: 164  Bit Score: 39.06  E-value: 3.90e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17505831 482 GMKDVKERIMEFIAVNLLRKSI------GGKILCFHGPPGVGKTSIAKSIATALNREYFRFSVGGMTDvaeikghrrTYV 555
Cdd:cd19524   4 GQDLAKQALQEMVILPSLRPELftglraPARGLLLFGPPGNGKTMLAKAVAAESNATFFNISAASLTS---------KYV 74
                        90       100       110
                ....*....|....*....|....*....|.
gi 17505831 556 GAMPgKMIQCMKKVKTE-NP-LVLIDEVDKI 584
Cdd:cd19524  75 GEGE-KLVRALFAVARElQPsIIFIDEVDSL 104
RecA-like_ATAD1 cd19520
ATPase domain of ATPase family AAA domain-containing protein 1 and similar ATPase domains; ...
482-582 4.15e-03

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: 38.94  E-value: 4.15e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17505831 482 GMKDVKERIMEFIAVNLLRKSI--GGKIL------CFHGPPGVGKTSIAKSIATALNREYFRFSVGGMTDvaEIKGHRRT 553
Cdd:cd19520   4 GLDEVITELKELVILPLQRPELfdNSRLLqppkgvLLYGPPGCGKTMLAKATAKEAGARFINLQVSSLTD--KWYGESQK 81
                        90       100
                ....*....|....*....|....*....
gi 17505831 554 YVGAMpgkmiqCMKKVKTENPLVLIDEVD 582
Cdd:cd19520  82 LVAAV------FSLASKLQPSIIFIDEID 104
RuvB_N pfam05496
Holliday junction DNA helicase RuvB P-loop domain; The RuvB protein makes up part of the ...
482-530 5.14e-03

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: 38.64  E-value: 5.14e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 17505831   482 GMKDVKERIMEFIAVNLLRKSIGGKILcFHGPPGVGKTSIAKSIATALN 530
Cdd:pfam05496  11 GQEKVKENLKIFIEAAKQRGEALDHVL-LYGPPGLGKTTLANIIANEMG 58
cbbX CHL00181
CbbX; Provisional
465-531 5.23e-03

CbbX; Provisional


Pssm-ID: 177083 [Multi-domain]  Cd Length: 287  Bit Score: 40.09  E-value: 5.23e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 17505831  465 ENRRLSVAKKALDEGHYGMKDVKERIMEFIA---VNLLRKSIG------GKILCFHGPPGVGKTSIAKSIATALNR 531
Cdd:CHL00181  10 EKTQIQEVLDILDEELVGLAPVKTRIREIAAlllIDRLRKNLGltssnpGLHMSFTGSPGTGKTTVALKMADILYK 85
RNA_helicase pfam00910
RNA helicase; This family includes RNA helicases thought to be involved in duplex unwinding ...
508-533 5.73e-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: 37.20  E-value: 5.73e-03
                          10        20
                  ....*....|....*....|....*.
gi 17505831   508 LCFHGPPGVGKTSIAKSIATALNREY 533
Cdd:pfam00910   1 IWLYGPPGCGKSTLAKYLARALLKKL 26
RecA-like_PAN_like cd19502
proteasome activating nucleotidase PAN and related proteasome subunits; This subfamily ...
511-601 5.81e-03

proteasome activating nucleotidase PAN and related proteasome subunits; This subfamily contains ATPase subunits of the eukaryotic 26S proteasome, and of the archaeal proteasome which carry out ATP-dependent degradation of substrates of the ubiquitin-proteasome pathway. The eukaryotic 26S proteasome consists of a proteolytic 20S core particle (CP), and a 19S regulatory particle (RP) which provides the ATP-dependence and the specificity for ubiquitinated proteins. In the archaea the RP is a homohexameric complex of proteasome-activating nucleotidase (PAN). This subfamily also includes various eukaryotic 26S subunits including, proteasome 26S subunit, ATPase 2 (PSMC2, also known as S7 and MSS1) which is a member of the 19S RP and has a chaperone like activity; and proteasome 20S subunit alpha 6 (PSMA6, also known as IOTA, p27K, and PROS27) which is a member of the 20S CP. This RecA-like_PAN 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: 410910 [Multi-domain]  Cd Length: 171  Bit Score: 38.86  E-value: 5.81e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17505831 511 HGPPGVGKTSIAKSIATALNREYFRfsVGGMTDVaeikghrRTYVGAMPgKMIQCMKKVKTENP--LVLIDEVDKIGGAG 588
Cdd:cd19502  43 YGPPGTGKTLLAKAVANHTDATFIR--VVGSELV-------QKYIGEGA-RLVRELFEMAREKApsIIFIDEIDAIGAKR 112
                        90
                ....*....|....*....
gi 17505831 589 FHGDPAS------ALLELL 601
Cdd:cd19502 113 FDSGTGGdrevqrTMLELL 131
clpA PRK11034
ATP-dependent Clp protease ATP-binding subunit; Provisional
500-712 8.62e-03

ATP-dependent Clp protease ATP-binding subunit; Provisional


Pssm-ID: 236828 [Multi-domain]  Cd Length: 758  Bit Score: 39.82  E-value: 8.62e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17505831  500 RKSIGGkiLCFHGPPGVGKTSIAKSIATALNREYFRFSV---GGMTDVAEIKGHRRTYVGAMPGKMIQcMKKVKTENPLV 576
Cdd:PRK11034 485 HKPVGS--FLFAGPTGVGKTEVTVQLSKALGIELLRFDMseyMERHTVSRLIGAPPGYVGFDQGGLLT-DAVIKHPHAVL 561
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17505831  577 LIDEVDKIggagfHGDPASALLELLDpeqNANFNDHFlDVPVDLSRVLFICTAN------------------------EI 632
Cdd:PRK11034 562 LLDEIEKA-----HPDVFNLLLQVMD---NGTLTDNN-GRKADFRNVVLVMTTNagvreterksiglihqdnstdameEI 632
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17505831  633 SKIPGP-LRDRMEMIDVSGYLAEEKVEIAHQHLIPQLRKDTSLATEQLKIEDSALEELI-KHYCRESGVRNLQQHIERIF 710
Cdd:PRK11034 633 KKIFTPeFRNRLDNIIWFDHLSTDVIHQVVDKFIVELQAQLDQKGVSLEVSQEARDWLAeKGYDRAMGARPMARVIQDNL 712

                 ..
gi 17505831  711 RK 712
Cdd:PRK11034 713 KK 714
PRK13341 PRK13341
AAA family ATPase;
498-527 8.71e-03

AAA family ATPase;


Pssm-ID: 237354 [Multi-domain]  Cd Length: 725  Bit Score: 40.04  E-value: 8.71e-03
                         10        20        30
                 ....*....|....*....|....*....|...
gi 17505831  498 LLRKSI-GGKI--LCFHGPPGVGKTSIAKSIAT 527
Cdd:PRK13341  42 LLRRAIkADRVgsLILYGPPGVGKTTLARIIAN 74
 
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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