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Conserved domains on  [gi|21396489|ref|NP_004784|]
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lon protease homolog, mitochondrial isoform 1 precursor [Homo sapiens]

Protein Classification

endopeptidase La( domain architecture ID 11489643)

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

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

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
lon TIGR00763
endopeptidase La; This protein, the ATP-dependent serine endopeptidase La, is induced by heat ...
 125-947 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: 1227.54  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21396489   125 PLIAITRNPVFPRFIKIIEVKNKKLVELLRRKVRLAQPYVGVFLKRDDSNESDvveSLDEIYHTGTFAQIHEMQDLGD-- 202
Cdd:TIGR00763   1 PLLPLRRRPLFPGMIKPIDVGREKSIKLIKEALRLKQPYLGLFLQKDDDNEEP---EEDDIYSVGVVAQILEMLPLPSsg 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21396489   203 --KLRMIVMGHRRVHISrqlevepeepeaenkhkprrkskrgkkeaedELSARHPaelameptpelpaeVLMVEVENVVH 280
Cdd:TIGR00763  78 taTYKVVVEGLRRIRIK-------------------------------ELSDKGG--------------YLVVRVDNLKE 112

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21396489   281 EDFQV-TEEVKALTAEIVKTIRDIIALNPLYRESVLQMMQAGQrvVDNPIYLSDMGAALTG-AESHELQDVLEETNIPKR 358
Cdd:TIGR00763 113 EPFDKdDEEIKALTREIKETFRELISLSKLFREQPALLSALED--IDEPGRLADFVAASLQlKEKDELQEVLETVNIEKR 190

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21396489   359 LYKALSLLKKEFELSKLQQRLGREVEEKIKQTHRKYLLQEQLKIIKKELGLEKDDKDAIEeKFRERLKELVVPKHVMDVV 438
Cdd:TIGR00763 191 LKKALELLKKELELLKLQNKITKKVEEKMEKTQREYYLREQLKAIKKELGIEKDDKDELE-KLKEKLEELKLPEEVKKVI 269

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21396489   439 DEELSKLGLLDNHSSEFNVTRNYLDWLTSIPWGKYSNENLDLARAQAVLEEDHYGMEDVKKRILEFIAVSQLRGSTQGKI 518
Cdd:TIGR00763 270 EKELTKLSLLEPSSSEFTVTRNYLDWLTDLPWGKYSKENLDLKRAKEILDEDHYGLKKVKERILEYLAVQKLRGKMKGPI 349

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21396489   519 LCFYGPPGVGKTSIARSIARALNREYFRFSVGGMTDVAEIKGHRRTYVGAMPGKIIQCLKKTKTENPLILIDEVDKIGRG 598
Cdd:TIGR00763 350 LCLVGPPGVGKTSLGKSIAKALNRKFVRFSLGGVRDEAEIRGHRRTYVGAMPGRIIQGLKKAKTKNPLFLLDEIDKIGSS 429

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21396489   599 YQGDPSSALLELLDPEQNANFLDHYLDVPVDLSKVLFICTANVTDTIPEPLRDRMEMINVSGYVAQEKLAIAERYLVPQA 678
Cdd:TIGR00763 430 FRGDPASALLEVLDPEQNNAFSDHYLDVPFDLSKVIFIATANSIDTIPRPLLDRMEVIELSGYTEEEKLEIAKKYLIPKA 509

                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21396489   679 RALCGLDESKAKLSSDVLTLLIKQYCRESGVRNLQKQVEKVLRKSAYKIVS------GEAESVEVTPENLQDFVGKPVFT 752
Cdd:TIGR00763 510 LEDHGLKPDELKITDEALLLLIKYYTREAGVRNLERQIEKICRKAAVKLVEqgekkkSEAESVVITPDNLKKYLGKPVFT 589

                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21396489   753 VERMYDVTPPGVVMGLAWTAMGGSTLFVETSLRRPqdkdakgdkDGSLEVTGQLGEVMKESARIAYTFARAFLMQHAPAN 832
Cdd:TIGR00763 590 YERAYEVTPPGVVMGLAWTPMGGDTLFIETTKVAG---------KGSLELTGQLGDVMKESAQIALTYVRSIAADLGISP 660

                         730       740       750       760       770       780       790       800
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21396489   833 DYLVTSHIHLHVPEGATPKDGPSAGCTIVTALLSLAMGRPVRQNLAMTGEVSLTGKILPVGGIKEKTIAAKRAGVTCIVL 912
Cdd:TIGR00763 661 NFFEKADIHLHVPEGATPKDGPSAGITMATALLSLATGKPVRPDVAMTGEITLRGKVLPIGGLKEKTIAAKRAGIKTIIL 740

                         810       820       830
                  ....*....|....*....|....*....|....*
gi 21396489   913 PAENKKDFYDLAAFITEGLEVHFVEHYREIFDIAF 947
Cdd:TIGR00763 741 PEKNRRDLEELPENVKEGLEIHFVKHYDEVLKKAF 775
 
Name Accession Description Interval E-value
lon TIGR00763
endopeptidase La; This protein, the ATP-dependent serine endopeptidase La, is induced by heat ...
 125-947 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: 1227.54  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21396489   125 PLIAITRNPVFPRFIKIIEVKNKKLVELLRRKVRLAQPYVGVFLKRDDSNESDvveSLDEIYHTGTFAQIHEMQDLGD-- 202
Cdd:TIGR00763   1 PLLPLRRRPLFPGMIKPIDVGREKSIKLIKEALRLKQPYLGLFLQKDDDNEEP---EEDDIYSVGVVAQILEMLPLPSsg 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21396489   203 --KLRMIVMGHRRVHISrqlevepeepeaenkhkprrkskrgkkeaedELSARHPaelameptpelpaeVLMVEVENVVH 280
Cdd:TIGR00763  78 taTYKVVVEGLRRIRIK-------------------------------ELSDKGG--------------YLVVRVDNLKE 112

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21396489   281 EDFQV-TEEVKALTAEIVKTIRDIIALNPLYRESVLQMMQAGQrvVDNPIYLSDMGAALTG-AESHELQDVLEETNIPKR 358
Cdd:TIGR00763 113 EPFDKdDEEIKALTREIKETFRELISLSKLFREQPALLSALED--IDEPGRLADFVAASLQlKEKDELQEVLETVNIEKR 190

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21396489   359 LYKALSLLKKEFELSKLQQRLGREVEEKIKQTHRKYLLQEQLKIIKKELGLEKDDKDAIEeKFRERLKELVVPKHVMDVV 438
Cdd:TIGR00763 191 LKKALELLKKELELLKLQNKITKKVEEKMEKTQREYYLREQLKAIKKELGIEKDDKDELE-KLKEKLEELKLPEEVKKVI 269

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21396489   439 DEELSKLGLLDNHSSEFNVTRNYLDWLTSIPWGKYSNENLDLARAQAVLEEDHYGMEDVKKRILEFIAVSQLRGSTQGKI 518
Cdd:TIGR00763 270 EKELTKLSLLEPSSSEFTVTRNYLDWLTDLPWGKYSKENLDLKRAKEILDEDHYGLKKVKERILEYLAVQKLRGKMKGPI 349

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21396489   519 LCFYGPPGVGKTSIARSIARALNREYFRFSVGGMTDVAEIKGHRRTYVGAMPGKIIQCLKKTKTENPLILIDEVDKIGRG 598
Cdd:TIGR00763 350 LCLVGPPGVGKTSLGKSIAKALNRKFVRFSLGGVRDEAEIRGHRRTYVGAMPGRIIQGLKKAKTKNPLFLLDEIDKIGSS 429

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21396489   599 YQGDPSSALLELLDPEQNANFLDHYLDVPVDLSKVLFICTANVTDTIPEPLRDRMEMINVSGYVAQEKLAIAERYLVPQA 678
Cdd:TIGR00763 430 FRGDPASALLEVLDPEQNNAFSDHYLDVPFDLSKVIFIATANSIDTIPRPLLDRMEVIELSGYTEEEKLEIAKKYLIPKA 509

                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21396489   679 RALCGLDESKAKLSSDVLTLLIKQYCRESGVRNLQKQVEKVLRKSAYKIVS------GEAESVEVTPENLQDFVGKPVFT 752
Cdd:TIGR00763 510 LEDHGLKPDELKITDEALLLLIKYYTREAGVRNLERQIEKICRKAAVKLVEqgekkkSEAESVVITPDNLKKYLGKPVFT 589

                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21396489   753 VERMYDVTPPGVVMGLAWTAMGGSTLFVETSLRRPqdkdakgdkDGSLEVTGQLGEVMKESARIAYTFARAFLMQHAPAN 832
Cdd:TIGR00763 590 YERAYEVTPPGVVMGLAWTPMGGDTLFIETTKVAG---------KGSLELTGQLGDVMKESAQIALTYVRSIAADLGISP 660

                         730       740       750       760       770       780       790       800
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21396489   833 DYLVTSHIHLHVPEGATPKDGPSAGCTIVTALLSLAMGRPVRQNLAMTGEVSLTGKILPVGGIKEKTIAAKRAGVTCIVL 912
Cdd:TIGR00763 661 NFFEKADIHLHVPEGATPKDGPSAGITMATALLSLATGKPVRPDVAMTGEITLRGKVLPIGGLKEKTIAAKRAGIKTIIL 740

                         810       820       830
                  ....*....|....*....|....*....|....*
gi 21396489   913 PAENKKDFYDLAAFITEGLEVHFVEHYREIFDIAF 947
Cdd:TIGR00763 741 PEKNRRDLEELPENVKEGLEIHFVKHYDEVLKKAF 775
Lon COG0466
ATP-dependent Lon protease, bacterial type [Posttranslational modification, protein turnover, ...
 116-950 0e+00

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


Pssm-ID: 440234 [Multi-domain]  Cd Length: 785  Bit Score: 1013.40  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21396489 116 TIPDVFPHLPLiaitRN-PVFPRFIKIIEVKNKKLVELLRrKVRLAQPYVGVFLKRDDSNESDvveSLDEIYHTGTFAQI 194
Cdd:COG0466   9 ELPETLPLLPL----RDvVVFPGMVIPLFVGREKSIKALE-EAMEGDKLIGLVAQKDAEVEDP---GPDDLYEVGTVAKI 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21396489 195 HEMQDLGD-KLRMIVMGHRRVHIsrqlevepeepeaenkhkprrkskrgkkeaeDELSARHPaelameptpelpaeVLMV 273
Cdd:COG0466  81 LQLLKLPDgTVKVLVEGLQRARI-------------------------------KEFVQEEP--------------YLEA 115

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21396489 274 EVEnVVHEDFQVTEEVKALTAEIVKTIRDIIALNPLYRESVLQMMQAgqrvVDNPIYLSDMGAALTGAESHELQDVLEET 353
Cdd:COG0466 116 EVE-PLEEEEEDDKELEALMRSLKEQFEEYVKLNPKIPPELLAALSN----IEDPGRLADFIASHLPLKIEEKQELLETL 190

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21396489 354 NIPKRLYKALSLLKKEFELSKLQQRLGREVEEKIKQTHRKYLLQEQLKIIKKELGlEKDDKDAIEEKFRERLKELVVPKH 433
Cdd:COG0466 191 DVKERLEKLLELLEKEIEVLELEKKIRSRVKEQMEKSQREYYLREQLKAIQKELG-EKDDGEDEIEELREKIEKAKLPEE 269

                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21396489 434 VMDVVDEELSKLGLLDNHSSEFNVTRNYLDWLTSIPWGKYSNENLDLARAQAVLEEDHYGMEDVKKRILEFIAVSQLRGS 513
Cdd:COG0466 270 VKEKAEKELKKLERMPPMSAEATVIRNYLDWLLDLPWGKRTKDNLDLKKAEKILDEDHYGLEKVKERILEYLAVRKLKKK 349

                       410       420       430       440       450       460       470       480
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21396489 514 TQGKILCFYGPPGVGKTSIARSIARALNREYFRFSVGGMTDVAEIKGHRRTYVGAMPGKIIQCLKKTKTENPLILIDEVD 593
Cdd:COG0466 350 LKGPILCLVGPPGVGKTSLGKSIARALGRKFVRISLGGVRDEAEIRGHRRTYIGAMPGRIIQGLKKAGTKNPVFLLDEID 429

                       490       500       510       520       530       540       550       560
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21396489 594 KIGRGYQGDPSSALLELLDPEQNANFLDHYLDVPVDLSKVLFICTANVTDTIPEPLRDRMEMINVSGYVAQEKLAIAERY 673
Cdd:COG0466 430 KMGSDFRGDPASALLEVLDPEQNNTFSDHYLEVPFDLSKVMFIATANSLDTIPAPLLDRMEIIELSGYTEEEKLEIAKRY 509

                       570       580       590       600       610       620       630       640
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21396489 674 LVPQARALCGLDESKAKLSSDVLTLLIKQYCRESGVRNLQKQVEKVLRKSAYKIVSGEAESVEVTPENLQDFVGKPVFTV 753
Cdd:COG0466 510 LIPKQLKEHGLKKEELKISDEALRKIIRGYTREAGVRNLEREIAKICRKVAKKIAEGKKKKVTITPKNLEKYLGVPRFRY 589

                       650       660       670       680       690       700       710       720
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21396489 754 ERMYDVTPPGVVMGLAWTAMGGSTLFVETSLrrpqdkdAKGdkDGSLEVTGQLGEVMKESARIAYTFARAFLMQHAPAND 833
Cdd:COG0466 590 EKAEEEDQVGVVTGLAWTEVGGDILFIEATL-------MPG--KGKLTLTGQLGDVMKESAQAALSYVRSRAEELGIDPD 660

                       730       740       750       760       770       780       790       800
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21396489 834 YLVTSHIHLHVPEGATPKDGPSAGCTIVTALLSLAMGRPVRQNLAMTGEVSLTGKILPVGGIKEKTIAAKRAGVTCIVLP 913
Cdd:COG0466 661 FFEKYDIHIHVPEGATPKDGPSAGITMATALVSALTGRPVRSDVAMTGEITLRGRVLPIGGLKEKLLAAHRAGIKTVILP 740

                       810       820       830
                ....*....|....*....|....*....|....*..
gi 21396489 914 AENKKDFYDLAAFITEGLEVHFVEHYREIFDIAFPDE 950
Cdd:COG0466 741 KENEKDLEEIPEEVKKGLEFHPVEHIDEVLKIALEKE 777
PRK10787 PRK10787
DNA-binding ATP-dependent protease La; Provisional
 325-947 3.03e-178

DNA-binding ATP-dependent protease La; Provisional


Pssm-ID: 182730 [Multi-domain]  Cd Length: 784  Bit Score: 536.83  E-value: 3.03e-178
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21396489  325 VDNPIYLSDMGAALTGAESHELQDVLEETNIPKRLYKALSLLKKEFELSKLQQRLGREVEEKIKQTHRKYLLQEQLKIIK 404
Cdd:PRK10787 159 IDDPARLADTIAAHMPLKLADKQSVLEMSDVNERLEYLMAMMESEIDLLQVEKRIRNRVKKQMEKSQREYYLNEQMKAIQ 238

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21396489  405 KELGlEKDDKDAIEEKFRERLKELVVPKHVMDVVDEELSKLGLLDNHSSEFNVTRNYLDWLTSIPWGKYSNENLDLARAQ 484
Cdd:PRK10787 239 KELG-EMDDAPDENEALKRKIDAAKMPKEAKEKAEAELQKLKMMSPMSAEATVVRGYIDWMVQVPWNARSKVKKDLRQAQ 317

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21396489  485 AVLEEDHYGMEDVKKRILEFIAVSQLRGSTQGKILCFYGPPGVGKTSIARSIARALNREYFRFSVGGMTDVAEIKGHRRT 564
Cdd:PRK10787 318 EILDTDHYGLERVKDRILEYLAVQSRVNKIKGPILCLVGPPGVGKTSLGQSIAKATGRKYVRMALGGVRDEAEIRGHRRT 397

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21396489  565 YVGAMPGKIIQCLKKTKTENPLILIDEVDKIGRGYQGDPSSALLELLDPEQNANFLDHYLDVPVDLSKVLFICTANVTDt 644
Cdd:PRK10787 398 YIGSMPGKLIQKMAKVGVKNPLFLLDEIDKMSSDMRGDPASALLEVLDPEQNVAFSDHYLEVDYDLSDVMFVATSNSMN- 476

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21396489  645 IPEPLRDRMEMINVSGYVAQEKLAIAERYLVPQARALCGLDESKAKLSSDVLTLLIKQYCRESGVRNLQKQVEKVLRKSA 724
Cdd:PRK10787 477 IPAPLLDRMEVIRLSGYTEDEKLNIAKRHLLPKQIERNALKKGELTVDDSAIIGIIRYYTREAGVRSLEREISKLCRKAV 556

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21396489  725 YKIVSGEA-ESVEVTPENLQDFVGKPVFTVERMYDVTPPGVVMGLAWTAMGGSTLFVETslrrpqdkdAKGDKDGSLEVT 803
Cdd:PRK10787 557 KQLLLDKSlKHIEINGDNLHDYLGVQRFDYGRADNENRVGQVTGLAWTEVGGDLLTIET---------ACVPGKGKLTYT 627

                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21396489  804 GQLGEVMKESARIAYTFARAFLMQHAPANDYLVTSHIHLHVPEGATPKDGPSAGCTIVTALLSLAMGRPVRQNLAMTGEV 883
Cdd:PRK10787 628 GSLGEVMQESIQAALTVVRARAEKLGINPDFYEKRDIHVHVPEGATPKDGPSAGIAMCTALVSCLTGNPVRADVAMTGEI 707

                        570       580       590       600       610       620
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 21396489  884 SLTGKILPVGGIKEKTIAAKRAGVTCIVLPAENKKDFYDLAAFITEGLEVHFVEHYREIFDIAF 947
Cdd:PRK10787 708 TLRGQVLPIGGLKEKLLAAHRGGIKTVLIPFENKRDLEEIPDNVIADLDIHPVKRIEEVLTLAL 771
RecA-like_Lon cd19500
lon protease homolog 2 peroxisomal; Lon protease (also known as Lon peptidase) is an ...
 480-661 3.83e-129

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


Pssm-ID: 410908 [Multi-domain]  Cd Length: 182  Bit Score: 386.91  E-value: 3.83e-129
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21396489 480 LARAQAVLEEDHYGMEDVKKRILEFIAVSQLRGSTQGKILCFYGPPGVGKTSIARSIARALNREYFRFSVGGMTDVAEIK 559
Cdd:cd19500   1 IKKARKVLDADHYGLEDVKERILEYLAVRKLKGSMKGPILCLVGPPGVGKTSLGKSIARALGRKFVRISLGGVRDEAEIR 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21396489 560 GHRRTYVGAMPGKIIQCLKKTKTENPLILIDEVDKIGRGYQGDPSSALLELLDPEQNANFLDHYLDVPVDLSKVLFICTA 639
Cdd:cd19500  81 GHRRTYVGAMPGRIIQALKKAGTNNPVFLLDEIDKIGSSFRGDPASALLEVLDPEQNSTFSDHYLDVPFDLSKVLFIATA 160

                       170       180
                ....*....|....*....|..
gi 21396489 640 NVTDTIPEPLRDRMEMINVSGY 661
Cdd:cd19500 161 NSLDTIPGPLLDRMEIIELSGY 182
Lon_C pfam05362
Lon protease (S16) C-terminal proteolytic domain; The Lon serine proteases must hydrolyse ATP ...
 737-948 1.20e-79

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: 257.17  E-value: 1.20e-79
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21396489   737 VTPENLQDFVGKPVFTVERMYDVTPPGVVMGLAWTAMGGSTLFVETSLrrpqdkdAKGDkdGSLEVTGQLGEVMKESARI 816
Cdd:pfam05362   2 VTAKNLEKYLGVPRFRYGEAEKEDQVGVVTGLAWTEVGGDLLTIEAVI-------MPGK--GKLTLTGQLGDVMKESAQA 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21396489   817 AYTFARAFLMQHAPANDYLVTSHIHLHVPEGATPKDGPSAGCTIVTALLSLAMGRPVRQNLAMTGEVSLTGKILPVGGIK 896
Cdd:pfam05362  73 ALSYVRSRAEELGIDPDFFEKKDIHIHVPEGATPKDGPSAGVTMATALVSALTGIPVRKDVAMTGEITLRGRVLPIGGLK 152

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 21396489   897 EKTIAAKRAGVTCIVLPAENKKDFYDLAAFITEGLEVHFVEHYREIFDIAFP 948
Cdd:pfam05362 153 EKLLAAHRAGIKTVIIPKENEKDLEDIPENVREGLEIIPVEHVDEVLKHALV 204
LON smart00464
Found in ATP-dependent protease La (LON); N-terminal domain of the ATP-dependent protease La ...
 123-200 4.92e-17

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: 77.09  E-value: 4.92e-17
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 21396489    123 HLPLIAITRNPVFPRFIKIIEVKNKKLVELLRRKVRLAQPYVGVFLKRDDSNESDVVESLDEIYHtgTFAQIHEMQDL 200
Cdd:smart00464   1 TLPLLPIRRRPLFPGFVLPIPVKRPKSVAAIKEALRRSQPYVIVFLLQDDPTETPEPLSDTIAAL--MPLELHEKQEL 76
 
Name Accession Description Interval E-value
lon TIGR00763
endopeptidase La; This protein, the ATP-dependent serine endopeptidase La, is induced by heat ...
 125-947 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: 1227.54  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21396489   125 PLIAITRNPVFPRFIKIIEVKNKKLVELLRRKVRLAQPYVGVFLKRDDSNESDvveSLDEIYHTGTFAQIHEMQDLGD-- 202
Cdd:TIGR00763   1 PLLPLRRRPLFPGMIKPIDVGREKSIKLIKEALRLKQPYLGLFLQKDDDNEEP---EEDDIYSVGVVAQILEMLPLPSsg 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21396489   203 --KLRMIVMGHRRVHISrqlevepeepeaenkhkprrkskrgkkeaedELSARHPaelameptpelpaeVLMVEVENVVH 280
Cdd:TIGR00763  78 taTYKVVVEGLRRIRIK-------------------------------ELSDKGG--------------YLVVRVDNLKE 112

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21396489   281 EDFQV-TEEVKALTAEIVKTIRDIIALNPLYRESVLQMMQAGQrvVDNPIYLSDMGAALTG-AESHELQDVLEETNIPKR 358
Cdd:TIGR00763 113 EPFDKdDEEIKALTREIKETFRELISLSKLFREQPALLSALED--IDEPGRLADFVAASLQlKEKDELQEVLETVNIEKR 190

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21396489   359 LYKALSLLKKEFELSKLQQRLGREVEEKIKQTHRKYLLQEQLKIIKKELGLEKDDKDAIEeKFRERLKELVVPKHVMDVV 438
Cdd:TIGR00763 191 LKKALELLKKELELLKLQNKITKKVEEKMEKTQREYYLREQLKAIKKELGIEKDDKDELE-KLKEKLEELKLPEEVKKVI 269

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21396489   439 DEELSKLGLLDNHSSEFNVTRNYLDWLTSIPWGKYSNENLDLARAQAVLEEDHYGMEDVKKRILEFIAVSQLRGSTQGKI 518
Cdd:TIGR00763 270 EKELTKLSLLEPSSSEFTVTRNYLDWLTDLPWGKYSKENLDLKRAKEILDEDHYGLKKVKERILEYLAVQKLRGKMKGPI 349

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21396489   519 LCFYGPPGVGKTSIARSIARALNREYFRFSVGGMTDVAEIKGHRRTYVGAMPGKIIQCLKKTKTENPLILIDEVDKIGRG 598
Cdd:TIGR00763 350 LCLVGPPGVGKTSLGKSIAKALNRKFVRFSLGGVRDEAEIRGHRRTYVGAMPGRIIQGLKKAKTKNPLFLLDEIDKIGSS 429

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21396489   599 YQGDPSSALLELLDPEQNANFLDHYLDVPVDLSKVLFICTANVTDTIPEPLRDRMEMINVSGYVAQEKLAIAERYLVPQA 678
Cdd:TIGR00763 430 FRGDPASALLEVLDPEQNNAFSDHYLDVPFDLSKVIFIATANSIDTIPRPLLDRMEVIELSGYTEEEKLEIAKKYLIPKA 509

                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21396489   679 RALCGLDESKAKLSSDVLTLLIKQYCRESGVRNLQKQVEKVLRKSAYKIVS------GEAESVEVTPENLQDFVGKPVFT 752
Cdd:TIGR00763 510 LEDHGLKPDELKITDEALLLLIKYYTREAGVRNLERQIEKICRKAAVKLVEqgekkkSEAESVVITPDNLKKYLGKPVFT 589

                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21396489   753 VERMYDVTPPGVVMGLAWTAMGGSTLFVETSLRRPqdkdakgdkDGSLEVTGQLGEVMKESARIAYTFARAFLMQHAPAN 832
Cdd:TIGR00763 590 YERAYEVTPPGVVMGLAWTPMGGDTLFIETTKVAG---------KGSLELTGQLGDVMKESAQIALTYVRSIAADLGISP 660

                         730       740       750       760       770       780       790       800
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21396489   833 DYLVTSHIHLHVPEGATPKDGPSAGCTIVTALLSLAMGRPVRQNLAMTGEVSLTGKILPVGGIKEKTIAAKRAGVTCIVL 912
Cdd:TIGR00763 661 NFFEKADIHLHVPEGATPKDGPSAGITMATALLSLATGKPVRPDVAMTGEITLRGKVLPIGGLKEKTIAAKRAGIKTIIL 740

                         810       820       830
                  ....*....|....*....|....*....|....*
gi 21396489   913 PAENKKDFYDLAAFITEGLEVHFVEHYREIFDIAF 947
Cdd:TIGR00763 741 PEKNRRDLEELPENVKEGLEIHFVKHYDEVLKKAF 775
Lon COG0466
ATP-dependent Lon protease, bacterial type [Posttranslational modification, protein turnover, ...
 116-950 0e+00

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


Pssm-ID: 440234 [Multi-domain]  Cd Length: 785  Bit Score: 1013.40  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21396489 116 TIPDVFPHLPLiaitRN-PVFPRFIKIIEVKNKKLVELLRrKVRLAQPYVGVFLKRDDSNESDvveSLDEIYHTGTFAQI 194
Cdd:COG0466   9 ELPETLPLLPL----RDvVVFPGMVIPLFVGREKSIKALE-EAMEGDKLIGLVAQKDAEVEDP---GPDDLYEVGTVAKI 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21396489 195 HEMQDLGD-KLRMIVMGHRRVHIsrqlevepeepeaenkhkprrkskrgkkeaeDELSARHPaelameptpelpaeVLMV 273
Cdd:COG0466  81 LQLLKLPDgTVKVLVEGLQRARI-------------------------------KEFVQEEP--------------YLEA 115

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21396489 274 EVEnVVHEDFQVTEEVKALTAEIVKTIRDIIALNPLYRESVLQMMQAgqrvVDNPIYLSDMGAALTGAESHELQDVLEET 353
Cdd:COG0466 116 EVE-PLEEEEEDDKELEALMRSLKEQFEEYVKLNPKIPPELLAALSN----IEDPGRLADFIASHLPLKIEEKQELLETL 190

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21396489 354 NIPKRLYKALSLLKKEFELSKLQQRLGREVEEKIKQTHRKYLLQEQLKIIKKELGlEKDDKDAIEEKFRERLKELVVPKH 433
Cdd:COG0466 191 DVKERLEKLLELLEKEIEVLELEKKIRSRVKEQMEKSQREYYLREQLKAIQKELG-EKDDGEDEIEELREKIEKAKLPEE 269

                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21396489 434 VMDVVDEELSKLGLLDNHSSEFNVTRNYLDWLTSIPWGKYSNENLDLARAQAVLEEDHYGMEDVKKRILEFIAVSQLRGS 513
Cdd:COG0466 270 VKEKAEKELKKLERMPPMSAEATVIRNYLDWLLDLPWGKRTKDNLDLKKAEKILDEDHYGLEKVKERILEYLAVRKLKKK 349

                       410       420       430       440       450       460       470       480
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21396489 514 TQGKILCFYGPPGVGKTSIARSIARALNREYFRFSVGGMTDVAEIKGHRRTYVGAMPGKIIQCLKKTKTENPLILIDEVD 593
Cdd:COG0466 350 LKGPILCLVGPPGVGKTSLGKSIARALGRKFVRISLGGVRDEAEIRGHRRTYIGAMPGRIIQGLKKAGTKNPVFLLDEID 429

                       490       500       510       520       530       540       550       560
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21396489 594 KIGRGYQGDPSSALLELLDPEQNANFLDHYLDVPVDLSKVLFICTANVTDTIPEPLRDRMEMINVSGYVAQEKLAIAERY 673
Cdd:COG0466 430 KMGSDFRGDPASALLEVLDPEQNNTFSDHYLEVPFDLSKVMFIATANSLDTIPAPLLDRMEIIELSGYTEEEKLEIAKRY 509

                       570       580       590       600       610       620       630       640
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21396489 674 LVPQARALCGLDESKAKLSSDVLTLLIKQYCRESGVRNLQKQVEKVLRKSAYKIVSGEAESVEVTPENLQDFVGKPVFTV 753
Cdd:COG0466 510 LIPKQLKEHGLKKEELKISDEALRKIIRGYTREAGVRNLEREIAKICRKVAKKIAEGKKKKVTITPKNLEKYLGVPRFRY 589

                       650       660       670       680       690       700       710       720
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21396489 754 ERMYDVTPPGVVMGLAWTAMGGSTLFVETSLrrpqdkdAKGdkDGSLEVTGQLGEVMKESARIAYTFARAFLMQHAPAND 833
Cdd:COG0466 590 EKAEEEDQVGVVTGLAWTEVGGDILFIEATL-------MPG--KGKLTLTGQLGDVMKESAQAALSYVRSRAEELGIDPD 660

                       730       740       750       760       770       780       790       800
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21396489 834 YLVTSHIHLHVPEGATPKDGPSAGCTIVTALLSLAMGRPVRQNLAMTGEVSLTGKILPVGGIKEKTIAAKRAGVTCIVLP 913
Cdd:COG0466 661 FFEKYDIHIHVPEGATPKDGPSAGITMATALVSALTGRPVRSDVAMTGEITLRGRVLPIGGLKEKLLAAHRAGIKTVILP 740

                       810       820       830
                ....*....|....*....|....*....|....*..
gi 21396489 914 AENKKDFYDLAAFITEGLEVHFVEHYREIFDIAFPDE 950
Cdd:COG0466 741 KENEKDLEEIPEEVKKGLEFHPVEHIDEVLKIALEKE 777
PRK10787 PRK10787
DNA-binding ATP-dependent protease La; Provisional
 325-947 3.03e-178

DNA-binding ATP-dependent protease La; Provisional


Pssm-ID: 182730 [Multi-domain]  Cd Length: 784  Bit Score: 536.83  E-value: 3.03e-178
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21396489  325 VDNPIYLSDMGAALTGAESHELQDVLEETNIPKRLYKALSLLKKEFELSKLQQRLGREVEEKIKQTHRKYLLQEQLKIIK 404
Cdd:PRK10787 159 IDDPARLADTIAAHMPLKLADKQSVLEMSDVNERLEYLMAMMESEIDLLQVEKRIRNRVKKQMEKSQREYYLNEQMKAIQ 238

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21396489  405 KELGlEKDDKDAIEEKFRERLKELVVPKHVMDVVDEELSKLGLLDNHSSEFNVTRNYLDWLTSIPWGKYSNENLDLARAQ 484
Cdd:PRK10787 239 KELG-EMDDAPDENEALKRKIDAAKMPKEAKEKAEAELQKLKMMSPMSAEATVVRGYIDWMVQVPWNARSKVKKDLRQAQ 317

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21396489  485 AVLEEDHYGMEDVKKRILEFIAVSQLRGSTQGKILCFYGPPGVGKTSIARSIARALNREYFRFSVGGMTDVAEIKGHRRT 564
Cdd:PRK10787 318 EILDTDHYGLERVKDRILEYLAVQSRVNKIKGPILCLVGPPGVGKTSLGQSIAKATGRKYVRMALGGVRDEAEIRGHRRT 397

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21396489  565 YVGAMPGKIIQCLKKTKTENPLILIDEVDKIGRGYQGDPSSALLELLDPEQNANFLDHYLDVPVDLSKVLFICTANVTDt 644
Cdd:PRK10787 398 YIGSMPGKLIQKMAKVGVKNPLFLLDEIDKMSSDMRGDPASALLEVLDPEQNVAFSDHYLEVDYDLSDVMFVATSNSMN- 476

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21396489  645 IPEPLRDRMEMINVSGYVAQEKLAIAERYLVPQARALCGLDESKAKLSSDVLTLLIKQYCRESGVRNLQKQVEKVLRKSA 724
Cdd:PRK10787 477 IPAPLLDRMEVIRLSGYTEDEKLNIAKRHLLPKQIERNALKKGELTVDDSAIIGIIRYYTREAGVRSLEREISKLCRKAV 556

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21396489  725 YKIVSGEA-ESVEVTPENLQDFVGKPVFTVERMYDVTPPGVVMGLAWTAMGGSTLFVETslrrpqdkdAKGDKDGSLEVT 803
Cdd:PRK10787 557 KQLLLDKSlKHIEINGDNLHDYLGVQRFDYGRADNENRVGQVTGLAWTEVGGDLLTIET---------ACVPGKGKLTYT 627

                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21396489  804 GQLGEVMKESARIAYTFARAFLMQHAPANDYLVTSHIHLHVPEGATPKDGPSAGCTIVTALLSLAMGRPVRQNLAMTGEV 883
Cdd:PRK10787 628 GSLGEVMQESIQAALTVVRARAEKLGINPDFYEKRDIHVHVPEGATPKDGPSAGIAMCTALVSCLTGNPVRADVAMTGEI 707

                        570       580       590       600       610       620
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 21396489  884 SLTGKILPVGGIKEKTIAAKRAGVTCIVLPAENKKDFYDLAAFITEGLEVHFVEHYREIFDIAF 947
Cdd:PRK10787 708 TLRGQVLPIGGLKEKLLAAHRGGIKTVLIPFENKRDLEEIPDNVIADLDIHPVKRIEEVLTLAL 771
RecA-like_Lon cd19500
lon protease homolog 2 peroxisomal; Lon protease (also known as Lon peptidase) is an ...
 480-661 3.83e-129

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


Pssm-ID: 410908 [Multi-domain]  Cd Length: 182  Bit Score: 386.91  E-value: 3.83e-129
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21396489 480 LARAQAVLEEDHYGMEDVKKRILEFIAVSQLRGSTQGKILCFYGPPGVGKTSIARSIARALNREYFRFSVGGMTDVAEIK 559
Cdd:cd19500   1 IKKARKVLDADHYGLEDVKERILEYLAVRKLKGSMKGPILCLVGPPGVGKTSLGKSIARALGRKFVRISLGGVRDEAEIR 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21396489 560 GHRRTYVGAMPGKIIQCLKKTKTENPLILIDEVDKIGRGYQGDPSSALLELLDPEQNANFLDHYLDVPVDLSKVLFICTA 639
Cdd:cd19500  81 GHRRTYVGAMPGRIIQALKKAGTNNPVFLLDEIDKIGSSFRGDPASALLEVLDPEQNSTFSDHYLDVPFDLSKVLFIATA 160

                       170       180
                ....*....|....*....|..
gi 21396489 640 NVTDTIPEPLRDRMEMINVSGY 661
Cdd:cd19500 161 NSLDTIPGPLLDRMEIIELSGY 182
Lon_C pfam05362
Lon protease (S16) C-terminal proteolytic domain; The Lon serine proteases must hydrolyse ATP ...
 737-948 1.20e-79

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: 257.17  E-value: 1.20e-79
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21396489   737 VTPENLQDFVGKPVFTVERMYDVTPPGVVMGLAWTAMGGSTLFVETSLrrpqdkdAKGDkdGSLEVTGQLGEVMKESARI 816
Cdd:pfam05362   2 VTAKNLEKYLGVPRFRYGEAEKEDQVGVVTGLAWTEVGGDLLTIEAVI-------MPGK--GKLTLTGQLGDVMKESAQA 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21396489   817 AYTFARAFLMQHAPANDYLVTSHIHLHVPEGATPKDGPSAGCTIVTALLSLAMGRPVRQNLAMTGEVSLTGKILPVGGIK 896
Cdd:pfam05362  73 ALSYVRSRAEELGIDPDFFEKKDIHIHVPEGATPKDGPSAGVTMATALVSALTGIPVRKDVAMTGEITLRGRVLPIGGLK 152

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 21396489   897 EKTIAAKRAGVTCIVLPAENKKDFYDLAAFITEGLEVHFVEHYREIFDIAFP 948
Cdd:pfam05362 153 EKLLAAHRAGIKTVIIPKENEKDLEDIPENVREGLEIIPVEHVDEVLKHALV 204
AAA pfam00004
ATPase family associated with various cellular activities (AAA); AAA family proteins often ...
 519-661 6.61e-32

ATPase family associated with various cellular activities (AAA); AAA family proteins often perform chaperone-like functions that assist in the assembly, operation, or disassembly of protein complexes.


Pssm-ID: 459627 [Multi-domain]  Cd Length: 130  Bit Score: 120.78  E-value: 6.61e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21396489   519 LCFYGPPGVGKTSIARSIARALNREYFRFSVGGMTDvaeikghrrTYVGAMPGKIIQCLKKTKTENP-LILIDEVDKIGR 597
Cdd:pfam00004   1 LLLYGPPGTGKTTLAKAVAKELGAPFIEISGSELVS---------KYVGESEKRLRELFEAAKKLAPcVIFIDEIDALAG 71

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 21396489   598 -------GYQGDPSSALLELLDPEQNANfldhyldvpvdlSKVLFICTANVTDTIPEPLRDRMEMINVSGY 661
Cdd:pfam00004  72 srgsggdSESRRVVNQLLTELDGFTSSN------------SKVIVIAATNRPDKLDPALLGRFDRIIEFPL 130
LON_substr_bdg pfam02190
ATP-dependent protease La (LON) substrate-binding domain; This domain has been shown to be ...
 124-368 8.50e-24

ATP-dependent protease La (LON) substrate-binding domain; This domain has been shown to be part of the PUA superfamily. This domain represents a general protein and polypeptide interaction domain for the ATP-dependent serine peptidase, LON, Peptidase_S16, pfam05362. ATP-dependent Lon proteases are conserved in all living organizms and catalyze rapid turnover of short-lived regulatory proteins and many damaged or denatured proteins.


Pssm-ID: 426647 [Multi-domain]  Cd Length: 195  Bit Score: 99.72  E-value: 8.50e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21396489   124 LPLIAITRNPVFPRFIKIIEVKNKKLVELLRRKVRLAQPYvGVFLKrDDSNESDVVESLDEIYHTGTFAQIHEMQDLGDK 203
Cdd:pfam02190   2 LPLLPLRNTVLFPGMVLPLFVGRPRSIAAIEAALNKDKLY-GVLLV-SQKDAEDEEPTPDDLYEVGTVAKIVQILKLPDG 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21396489   204 -LRMIVMGHRRVHIsrqlevepeepeaenkhkprrkskrgkkeaEDELSARHPaelameptpelpaeVLMVEVENVVHED 282
Cdd:pfam02190  80 tYKVLVEGLERVRI------------------------------VELVKKEEP--------------YLRAEVEDLPEDS 115

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21396489   283 FQVTEEVKALTAEIVKTIRDIIALNPLYrESVLQMMqagqrVVDNPIYLSDMGAALTGAESHELQDVLEETNIPKRLYKA 362
Cdd:pfam02190 116 DELSEALKALVKELIEKLRRLLKLLLPL-ELLLKIK-----DIENPGRLADLVAAILPLSPEEKQELLETLDVKERLEKV 189


                  ....*.
gi 21396489   363 LSLLKK 368
Cdd:pfam02190 190 LELLNR 195
RecA-like_protease cd19481
proteases similar to RecA; RecA-like NTPases. This family includes the NTP binding domain of ...
 497-658 2.51e-19

proteases similar to RecA; RecA-like NTPases. This family includes the NTP binding domain of F1 and V1 H(+)ATPases, DnaB and related helicases as well as bacterial RecA and related eukaryotic and archaeal recombinases. This group also includes bacterial conjugation proteins and related DNA transfer proteins involved in type II and type IV secretion.


Pssm-ID: 410889 [Multi-domain]  Cd Length: 158  Bit Score: 85.80  E-value: 2.51e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21396489 497 VKKRILEFIAV------SQLRGSTQGKILCFYGPPGVGKTSIARSIARALNREYFRFSVGGMTDVAeikghrRTYVGAMP 570
Cdd:cd19481   1 LKASLREAVEAprrgsrLRRYGLGLPKGILLYGPPGTGKTLLAKALAGELGLPLIVVKLSSLLSKY------VGESEKNL 74

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21396489 571 GKIIQCLKKTKteNPLILIDEVDKIG--RGYQGDPS------SALLELLDPEQNanfldhyldvpvdLSKVLFICTAN-V 641
Cdd:cd19481  75 RKIFERARRLA--PCILFIDEIDAIGrkRDSSGESGelrrvlNQLLTELDGVNS-------------RSKVLVIAATNrP 139

                       170
                ....*....|....*....
gi 21396489 642 TDTIPEPLR--DRMEMINV 658
Cdd:cd19481 140 DLLDPALLRpgRFDEVIEF 158
COG1750 COG1750
Predicted archaeal serine protease, S18 family [General function prediction only];
807-921 8.54e-18

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


Pssm-ID: 441356 [Multi-domain]  Cd Length: 213  Bit Score: 83.10  E-value: 8.54e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21396489 807 GEVMKESARIAytFARAFLMQHAPANDYLVTSHIhlhvpEGATPK-DGPSAGCTIVTALLSLAMGRPVRQNLAMTGEVSL 885
Cdd:COG1750  69 GPDTQASARIA--ALVASLLAGVDLSSYDVYISI-----ESDSPIvGGPSAGGAMTVATYAALLGLPLNKSVTMTGMINP 141

                        90       100       110
                ....*....|....*....|....*....|....*.
gi 21396489 886 TGKILPVGGIKEKTIAAKRAGVTCIVLPAENKKDFY 921
Cdd:COG1750 142 DGSIGPVGGVYEKLEAAASAGAKYFLIPKGQAILTG 177
LON smart00464
Found in ATP-dependent protease La (LON); N-terminal domain of the ATP-dependent protease La ...
 123-200 4.92e-17

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: 77.09  E-value: 4.92e-17
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 21396489    123 HLPLIAITRNPVFPRFIKIIEVKNKKLVELLRRKVRLAQPYVGVFLKRDDSNESDVVESLDEIYHtgTFAQIHEMQDL 200
Cdd:smart00464   1 TLPLLPIRRRPLFPGFVLPIPVKRPKSVAAIKEALRRSQPYVIVFLLQDDPTETPEPLSDTIAAL--MPLELHEKQEL 76
AAA cd00009
The AAA+ (ATPases Associated with a wide variety of cellular Activities) superfamily ...
 492-656 5.13e-16

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: 76.03  E-value: 5.13e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21396489 492 YGMEDVKKRILEFIAvsqlrgSTQGKILCFYGPPGVGKTSIARSIARALNREYFRF---SVGGMTDVAEIKGHRRTYVGA 568
Cdd:cd00009   1 VGQEEAIEALREALE------LPPPKNLLLYGPPGTGKTTLARAIANELFRPGAPFlylNASDLLEGLVVAELFGHFLVR 74

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21396489 569 MPGKIIQclkktKTENPLILIDEVDKIGRGYQgdpssallelldpEQNANFLDHYLDVPVDLSKVLFICTANVTD--TIP 646
Cdd:cd00009  75 LLFELAE-----KAKPGVLFIDEIDSLSRGAQ-------------NALLRVLETLNDLRIDRENVRVIGATNRPLlgDLD 136

                       170
                ....*....|
gi 21396489 647 EPLRDRMEMI 656
Cdd:cd00009 137 RALYDRLDIR 146
SpoVK COG0464
AAA+-type ATPase, SpoVK/Ycf46/Vps4 family [Cell wall/membrane/envelope biogenesis, Cell cycle ...
 493-674 4.23e-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: 78.41  E-value: 4.23e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21396489 493 GMEDVKKRILEFIA-------VSQLRGSTQGKILCFYGPPGVGKTSIARSIARALNREYFRFSVGGMTDvaeikghrrTY 565
Cdd:COG0464 161 GLEEVKEELRELVAlplkrpeLREEYGLPPPRGLLLYGPPGTGKTLLARALAGELGLPLIEVDLSDLVS---------KY 231

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21396489 566 VGAMPGKIIQCLKKTKTENPLIL-IDEVDKI--GRGYQGDPS-----SALLELLDpeqnanfldhylDVPvdlSKVLFIC 637
Cdd:COG0464 232 VGETEKNLREVFDKARGLAPCVLfIDEADALagKRGEVGDGVgrrvvNTLLTEME------------ELR---SDVVVIA 296

                       170       180       190
                ....*....|....*....|....*....|....*...
gi 21396489 638 TANVTDTIPEPLRDRM-EMINVSGYVAQEKLAIAERYL 674
Cdd:COG0464 297 ATNRPDLLDPALLRRFdEIIFFPLPDAEERLEIFRIHL 334
COG1223 COG1223
Predicted ATPase, AAA+ superfamily [General function prediction only];
489-674 1.89e-12

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


Pssm-ID: 440836 [Multi-domain]  Cd Length: 246  Bit Score: 68.37  E-value: 1.89e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21396489 489 EDHYGMEDVKKRILEFIA----VSQLRG---STQGKILcFYGPPGVGKTSIARSIARALNREYFRFSVGGMTDvaeikgh 561
Cdd:COG1223   2 DDVVGQEEAKKKLKLIIKelrrRENLRKfglWPPRKIL-FYGPPGTGKTMLAEALAGELKLPLLTVRLDSLIG------- 73

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21396489 562 rrTYVGAMPGKIIQCLKKTKTENPLILIDEVDKIG--RGYQ---GDPS---SALLELLDPEQnanfldhyldvpvdlSKV 633
Cdd:COG1223  74 --SYLGETARNLRKLFDFARRAPCVIFFDEFDAIAkdRGDQndvGEVKrvvNALLQELDGLP---------------SGS 136

                       170       180       190       200
                ....*....|....*....|....*....|....*....|..
gi 21396489 634 LFICTANVTDTIPEPLRDRMEM-INVSGYVAQEKLAIAERYL 674
Cdd:COG1223 137 VVIAATNHPELLDSALWRRFDEvIEFPLPDKEERKEILELNL 178
AAA smart00382
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ...
 515-652 1.65e-09

ATPases associated with a variety of cellular activities; AAA - ATPases associated with a variety of cellular activities. This profile/alignment only detects a fraction of this vast family. The poorly conserved N-terminal helix is missing from the alignment.


Pssm-ID: 214640 [Multi-domain]  Cd Length: 148  Bit Score: 57.38  E-value: 1.65e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21396489    515 QGKILCFYGPPGVGKTSIARSIARALNREYFRFSVGGMTDVAEIKGHRR-----------TYVGAMPGKIIQCLKKTKte 583
Cdd:smart00382   1 PGEVILIVGPPGSGKTTLARALARELGPPGGGVIYIDGEDILEEVLDQLlliivggkkasGSGELRLRLALALARKLK-- 78

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21396489    584 NPLILIDEVDKIGRgyqgDPSSALLELLDPEQNANFLDHYLDVPVdlskvlfICTAN-VTDTIPEPLRDR 652
Cdd:smart00382  79 PDVLILDEITSLLD----AEQEALLLLLEELRLLLLLKSEKNLTV-------ILTTNdEKDLGPALLRRR 137
PRK13342 PRK13342
recombination factor protein RarA; Reviewed
 521-592 2.99e-09

recombination factor protein RarA; Reviewed


Pssm-ID: 237355 [Multi-domain]  Cd Length: 413  Bit Score: 60.10  E-value: 2.99e-09
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 21396489  521 FYGPPGVGKTSIARSIARALNREYFRFSvGGMTDVAEIKghrrtyvgampgKIIQCLKKTKT--ENPLILIDEV 592
Cdd:PRK13342  41 LWGPPGTGKTTLARIIAGATDAPFEALS-AVTSGVKDLR------------EVIEEARQRRSagRRTILFIDEI 101
AAA_5 pfam07728
AAA domain (dynein-related subfamily); This Pfam entry includes some of the AAA proteins not ...
 519-653 3.73e-09

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: 55.76  E-value: 3.73e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21396489   519 LCFYGPPGVGKTSIARSIARAL-NREYFRFSVGGMTDVAEIKGHRRTYVGAmPGKIIQCLKKTKTENPLILIDEVDKIGR 597
Cdd:pfam07728   2 VLLVGPPGTGKTELAERLAAALsNRPVFYVQLTRDTTEEDLFGRRNIDPGG-ASWVDGPLVRAAREGEIAVLDEINRANP 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 21396489   598 GYQGdpssALLELLDPEQ----NANFLdhyldVPVDLSKVLFICTANVTDT----IPEPLRDRM 653
Cdd:pfam07728  81 DVLN----SLLSLLDERRlllpDGGEL-----VKAAPDGFRLIATMNPLDRglneLSPALRSRF 135
AAA_2 pfam07724
AAA domain (Cdc48 subfamily); This Pfam entry includes some of the AAA proteins not detected ...
 521-641 3.14e-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: 54.12  E-value: 3.14e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21396489   521 FYGPPGVGKTSIARSIARALNREYFRFSVGGMTDVAEikghrRTYV----GAMPGKI------IQCLKKTKTENPLILID 590
Cdd:pfam07724   8 FLGPTGVGKTELAKALAELLFGDERALIRIDMSEYME-----EHSVsrliGAPPGYVgyeeggQLTEAVRRKPYSIVLID 82

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 21396489   591 EVDKIGRGYQgdpsSALLELLDpeqNANFLDHYlDVPVDLSKVLFICTANV 641
Cdd:pfam07724  83 EIEKAHPGVQ----NDLLQILE---GGTLTDKQ-GRTVDFKNTLFIMTGNF 125
44 PHA02544
clamp loader, small subunit; Provisional
 495-703 3.49e-08

clamp loader, small subunit; Provisional


Pssm-ID: 222866 [Multi-domain]  Cd Length: 316  Bit Score: 56.15  E-value: 3.49e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21396489  495 EDVKKRILEFIavsqlrgsTQGKI--LCFYGP-PGVGKTSIARSIARALNREYFrFSVGGMTDVAEIKGHRRTYVGAM-- 569
Cdd:PHA02544  27 AADKETFKSIV--------KKGRIpnMLLHSPsPGTGKTTVAKALCNEVGAEVL-FVNGSDCRIDFVRNRLTRFASTVsl 97

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21396489  570 --PGKIiqclkktktenplILIDEVDKIGRgyqgdpSSALLELldpeqnANFLDHYldvpvdlSK-VLFICTANVTDTIP 646
Cdd:PHA02544  98 tgGGKV-------------IIIDEFDRLGL------ADAQRHL------RSFMEAY-------SKnCSFIITANNKNGII 145

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 21396489  647 EPLRDRMEMINVSGYVAQEKLAIAERYLVpqaRALCGLDESKAKLSSDVLTLLIKQY 703
Cdd:PHA02544 146 EPLRSRCRVIDFGVPTKEEQIEMMKQMIV---RCKGILEAEGVEVDMKVLAALVKKN 199
PRK04195 PRK04195
replication factor C large subunit; Provisional
 493-702 3.65e-08

replication factor C large subunit; Provisional


Pssm-ID: 235250 [Multi-domain]  Cd Length: 482  Bit Score: 56.85  E-value: 3.65e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21396489  493 GMEDVKKRILEFIAvSQLRGSTQgKILCFYGPPGVGKTSIARSIARALNREYF-------------RFSVGGMTDVAEIK 559
Cdd:PRK04195  18 GNEKAKEQLREWIE-SWLKGKPK-KALLLYGPPGVGKTSLAHALANDYGWEVIelnasdqrtadviERVAGEAATSGSLF 95

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21396489  560 GHRRTyvgampgkiiqclkktktenpLILIDEVDKI-GRGYQGDpSSALLELLDpeqNANfldhyldVPVdlskvlfICT 638
Cdd:PRK04195  96 GARRK---------------------LILLDEVDGIhGNEDRGG-ARAILELIK---KAK-------QPI-------ILT 136

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 21396489  639 AN-VTDTIPEPLRDRMEMINVSgyvaqeklAIAERYLVPQARALCGLDesKAKLSSDVLTLLIKQ 702
Cdd:PRK04195 137 ANdPYDPSLRELRNACLMIEFK--------RLSTRSIVPVLKRICRKE--GIECDDEALKEIAER 191
RecA-like_VPS4-like cd19509
ATPase domain of VPS4, ATAD1, K, KTNA1, Spastin, FIGL-1 and similar ATPase domains; This ...
 493-654 3.83e-08

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: 53.90  E-value: 3.83e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21396489 493 GMEDVKKRILEFI--------AVSQLRGSTQGKILcfYGPPGVGKTSIARSIARALNREYFRFSVGGMTDvaeikghrrT 564
Cdd:cd19509   3 GLDDAKEALKEAVilpslrpdLFPGLRGPPRGILL--YGPPGTGKTLLARAVASESGSTFFSISASSLVS---------K 71

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21396489 565 YVGAmPGKIIQCLKKTKTEN--PLILIDEVDKIGRGYQGDPSSA-------LLELLDPEQNAnfldhyldvpvDLSKVLF 635
Cdd:cd19509  72 WVGE-SEKIVRALFALARELqpSIIFIDEIDSLLSERGSGEHEAsrrvkteFLVQMDGVLNK-----------PEDRVLV 139

                       170
                ....*....|....*....
gi 21396489 636 ICTANVTDTIPEPLRDRME 654
Cdd:cd19509 140 LGATNRPWELDEAFLRRFE 158
RPT1 COG1222
ATP-dependent 26S proteasome regulatory subunit [Posttranslational modification, protein ...
 397-597 1.84e-07

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


Pssm-ID: 440835 [Multi-domain]  Cd Length: 326  Bit Score: 54.24  E-value: 1.84e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21396489 397 QEQLKIIKKELGLEKDDKDAIEEKFRERLKELVVPKHVMDvvdEELSKLGLLDNHSSEFNVTRNYLDWLTSipwgkysne 476
Cdd:COG1222   1 GNDLLTIDENIKALLALIDALQERLGVELALLLQPVKALE---LLEEAPALLLNDANLTQKRLGTPRGTAV--------- 68

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21396489 477 nldLARAQAVLEEDHYGMEDVKKRILEFIAVSQLR-------GSTQGKILCFYGPPGVGKTSIARSIARALNREYFRfsV 549
Cdd:COG1222  69 ---PAESPDVTFDDIGGLDEQIEEIREAVELPLKNpelfrkyGIEPPKGVLLYGPPGTGKTLLAKAVAGELGAPFIR--V 143

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*....
gi 21396489 550 GGmtdvAEIkghRRTYVGAMPGKIIQCLKKTKTENP-LILIDEVDKIGR 597
Cdd:COG1222 144 RG----SEL---VSKYIGEGARNVREVFELAREKAPsIIFIDEIDAIAA 185
RarA COG2256
Replication-associated recombination protein RarA (DNA-dependent ATPase) [Replication, ...
 521-592 2.52e-07

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


Pssm-ID: 441857 [Multi-domain]  Cd Length: 439  Bit Score: 54.29  E-value: 2.52e-07
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 21396489 521 FYGPPGVGKTSIARSIARALNREYFRFSvGGMTDVAEIKghrrtyvgampgKIIQCLKKTKTEN--PLILIDEV 592
Cdd:COG2256  54 LWGPPGTGKTTLARLIANATDAEFVALS-AVTSGVKDIR------------EVIEEARERRAYGrrTILFVDEI 114
LonB COG1067
Predicted ATP-dependent protease [Posttranslational modification, protein turnover, chaperones] ...
 852-898 7.45e-07

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


Pssm-ID: 440686 [Multi-domain]  Cd Length: 742  Bit Score: 53.03  E-value: 7.45e-07
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*...
gi 21396489 852 DGPSAGCTIVTALLSlAMGR-PVRQNLAMTGEVSLTGKILPVGGIKEK 898
Cdd:COG1067 592 DGDSASSAELYALLS-ALSGvPIRQDIAVTGSVNQHGEVQPIGGVNEK 638
ruvB TIGR00635
Holliday junction DNA helicase, RuvB subunit; All proteins in this family for which functions ...
 489-673 8.92e-07

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: 51.92  E-value: 8.92e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21396489   489 EDHYGMEDVKKRILEFIAVSQLRGSTQGKILcFYGPPGVGKTSIARSIARALNREyFRFSVGGMTDvaeikghrrtyvga 568
Cdd:TIGR00635   4 AEFIGQEKVKEQLQLFIEAAKMRQEALDHLL-LYGPPGLGKTTLAHIIANEMGVN-LKITSGPALE-------------- 67

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21396489   569 MPGKIIQCLKKTKtENPLILIDEVDKIGRgyqgdpssALLELLDPEQNANFLDHYLD-------VPVDLSKVLFICTANV 641
Cdd:TIGR00635  68 KPGDLAAILTNLE-EGDVLFIDEIHRLSP--------AVEELLYPAMEDFRLDIVIGkgpsarsVRLDLPPFTLVGATTR 138

                         170       180       190
                  ....*....|....*....|....*....|...
gi 21396489   642 TDTIPEPLRDRMEMI-NVSGYVAQEKLAIAERY 673
Cdd:TIGR00635 139 AGMLTSPLRDRFGIIlRLEFYTVEELAEIVSRS 171
ChlI pfam13541
Subunit ChlI of Mg-chelatase;
850-916 2.21e-06

Subunit ChlI of Mg-chelatase;


Pssm-ID: 433293 [Multi-domain]  Cd Length: 121  Bit Score: 47.44  E-value: 2.21e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 21396489   850 PKDGPSAGCTIVTALLSLAMGRPVRQNLAMTGEVSLTGKILPVGGIKEKTIAAKRAGVTCIVLPAEN 916
Cdd:pfam13541  55 KKEGSSFDLPIAIGILAAQGQIPVLEETIFLGELSLDGSLRPVRGALPIALAARKHGFRGLIVPKEN 121
RecA-like_CDC48_NLV2_r1-like cd19503
first of two ATPase domains of CDC48 and NLV2, and similar ATPase domains; CDC48 in yeast and ...
 493-650 3.75e-06

first of two ATPase domains of CDC48 and NLV2, and similar ATPase domains; CDC48 in yeast and p97 or VCP metazoans is an ATP-dependent molecular chaperone which plays an essential role in many cellular processes, by segregating polyubiquitinated proteins from complexes or membranes. Cdc48/p97 consists of an N-terminal domain and two ATPase domains; this subfamily represents the first of the two ATPase domains. This subfamily also includes the first of the two ATPase domains of NVL (nuclear VCP-like protein) 2, an isoform of NVL mainly present in the nucleolus, which is involved in ribosome biogenesis, in telomerase assembly and the regulation of telomerase activity, and in pre-rRNA processing. This subfamily belongs to the RecA-like NTPase family which includes the NTP binding domain of F1 and V1 H(+)ATPases, DnaB and related helicases as well as bacterial RecA and related eukaryotic and archaeal recombinases. The RecA-like NTPase family also includes bacterial conjugation proteins and related DNA transfer proteins involved in type II and type IV secretion.


Pssm-ID: 410911 [Multi-domain]  Cd Length: 165  Bit Score: 48.06  E-value: 3.75e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21396489 493 GMEDVKKRILEFIAvSQLRGSTQGKIL--------CFYGPPGVGKTSIARSIARALNREYFrfsvggmtdvaEIKGHrrT 564
Cdd:cd19503   4 GLDEQIASLKELIE-LPLKYPELFRALglkpprgvLLHGPPGTGKTLLARAVANEAGANFL-----------SISGP--S 69

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21396489 565 YVGAMPGKIIQCLKK-----TKTENPLILIDEVDKIG--RGY-QGDPS----SALLELLDPEQNANfldhyldvpvdlsK 632
Cdd:cd19503  70 IVSKYLGESEKNLREifeeaRSHAPSIIFIDEIDALApkREEdQREVErrvvAQLLTLMDGMSSRG-------------K 136

                       170
                ....*....|....*...
gi 21396489 633 VLFICTANVTDTIPEPLR 650
Cdd:cd19503 137 VVVIAATNRPDAIDPALR 154
ruvB PRK00080
Holliday junction branch migration DNA helicase RuvB;
489-541 5.38e-06

Holliday junction branch migration DNA helicase RuvB;


Pssm-ID: 234619 [Multi-domain]  Cd Length: 328  Bit Score: 49.36  E-value: 5.38e-06
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|...
gi 21396489  489 EDHYGMEDVKKRILEFIAVSQLRGSTQGKILcFYGPPGVGKTSIARSIARALN 541
Cdd:PRK00080  25 DEFIGQEKVKENLKIFIEAAKKRGEALDHVL-LYGPPGLGKTTLANIIANEMG 76
SdrC COG3480
Predicted secreted protein YlbL, contains PDZ domain [Signal transduction mechanisms];
853-933 5.63e-06

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


Pssm-ID: 442703 [Multi-domain]  Cd Length: 344  Bit Score: 49.42  E-value: 5.63e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21396489 853 GPSAGctivtaL-LSLAM-----------GRPVrqnlAMTGEVSLTGKILPVGGIKEKTIAAKRAGVTCIVLPAENkkdf 920
Cdd:COG3480 240 GPSAG------LmFALGIydqltpgdltgGKKI----AGTGTIDADGTVGPIGGIDQKVVAARRAGATIFLAPASN---- 305

                        90
                ....*....|....
gi 21396489 921 YDLA-AFITEGLEV 933
Cdd:COG3480 306 CAEAvGTIPTGLKV 319
RuvB_N pfam05496
Holliday junction DNA helicase RuvB P-loop domain; The RuvB protein makes up part of the ...
 489-541 6.88e-06

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


Pssm-ID: 398900 [Multi-domain]  Cd Length: 159  Bit Score: 47.11  E-value: 6.88e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 21396489   489 EDHYGMEDVKKRILEFIAVSQLRGSTQGKILcFYGPPGVGKTSIARSIARALN 541
Cdd:pfam05496   7 DEYIGQEKVKENLKIFIEAAKQRGEALDHVL-LYGPPGLGKTTLANIIANEMG 58
RecA-like_FtsH cd19501
ATP-dependent zinc metalloprotease FtsH; FtsH ATPase is a processive, ATP-dependent zinc ...
 493-597 7.26e-06

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: 47.23  E-value: 7.26e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21396489 493 GMEDVKKRILEFiaVSQLRGSTQ-----GKI---LCFYGPPGVGKTSIARSIARALNREYfrFSVGGmTDVAEIkghrrt 564
Cdd:cd19501   8 GCEEAKEELKEV--VEFLKNPEKftklgAKIpkgVLLVGPPGTGKTLLAKAVAGEAGVPF--FSISG-SDFVEM------ 76

                        90       100       110
                ....*....|....*....|....*....|....
gi 21396489 565 YVGAMPGKIIQCLKKTKTENP-LILIDEVDKIGR 597
Cdd:cd19501  77 FVGVGASRVRDLFEQAKKNAPcIVFIDEIDAVGR 110
MoxR COG0714
MoxR-like ATPase [General function prediction only]; MoxR-like ATPase is part of the Pathway ...
 523-612 9.85e-06

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: 48.63  E-value: 9.85e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21396489 523 GPPGVGKTSIARSIARALNREYFR--FSVGGM------TDVAEIKGHRRTYVgamPGKIIQclkktktenPLILIDEVDK 594
Cdd:COG0714  38 GVPGVGKTTLAKALARALGLPFIRiqFTPDLLpsdilgTYIYDQQTGEFEFR---PGPLFA---------NVLLADEINR 105

                        90       100
                ....*....|....*....|
gi 21396489 595 igrgyqGDP--SSALLELLD 612
Cdd:COG0714 106 ------APPktQSALLEAME 119
RecA-like_HslU cd19498
ATP-dependent protease ATPase subunit HslU; HslU is a component of the ATP-dependent protease ...
 523-650 1.94e-05

ATP-dependent protease ATPase subunit HslU; HslU is a component of the ATP-dependent protease HslVU. In HslVU, HslU ATPase serves to unfold and translocate protein substrate, and the HslV protease degrades the unfolded proteins. This RecA-like_HslU subfamily belongs to the RecA-like NTPase family which includes the NTP binding domain of F1 and V1 H(+)ATPases, DnaB and related helicases as well as bacterial RecA and related eukaryotic and archaeal recombinases. The RecA-like NTPase family also includes bacterial conjugation proteins and related DNA transfer proteins involved in type II and type IV secretion.


Pssm-ID: 410906 [Multi-domain]  Cd Length: 183  Bit Score: 46.22  E-value: 1.94e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21396489 523 GPPGVGKTSIARSIARALNREYFRFSVGGMTDVAeikghrrtYVGAMPGKIIQCLKKTktenpLILIDEVDKI---GRGY 599
Cdd:cd19498  53 GPTGVGKTEIARRLAKLAGAPFIKVEATKFTEVG--------YVGRDVESIIRDLVEG-----IVFIDEIDKIakrGGSS 119

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 21396489 600 QGDPSSALLE--LLDPEQNANFLDHYldVPVDLSKVLFICT-----ANVTDTIPE-----PLR 650
Cdd:cd19498 120 GPDVSREGVQrdLLPIVEGSTVSTKY--GPVKTDHILFIAAgafhvAKPSDLIPElqgrfPIR 180
ftsH CHL00176
cell division protein; Validated
 485-597 3.17e-05

cell division protein; Validated


Pssm-ID: 214386 [Multi-domain]  Cd Length: 638  Bit Score: 47.74  E-value: 3.17e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21396489  485 AVLEEDHYGMEDVKKRILEFiaVSQLR--------GSTQGKILCFYGPPGVGKTSIARSIARALNREYfrFSVGGMTDVA 556
Cdd:CHL00176 179 GITFRDIAGIEEAKEEFEEV--VSFLKkperftavGAKIPKGVLLVGPPGTGKTLLAKAIAGEAEVPF--FSISGSEFVE 254

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 21396489  557 EIKGhrrtyVGAmpGKIIQCLKKTKTENPLIL-IDEVDKIGR 597
Cdd:CHL00176 255 MFVG-----VGA--ARVRDLFKKAKENSPCIVfIDEIDAVGR 289
rfc PRK00440
replication factor C small subunit; Reviewed
 472-546 4.47e-05

replication factor C small subunit; Reviewed


Pssm-ID: 234763 [Multi-domain]  Cd Length: 319  Bit Score: 46.79  E-value: 4.47e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 21396489  472 KYSNENLDlaraqavleeDHYGMEDVKKRILEFIAvsqlrgstQGKI--LCFYGPPGVGKTSIARSIARALNREYFR 546
Cdd:PRK00440  10 KYRPRTLD----------EIVGQEEIVERLKSYVK--------EKNMphLLFAGPPGTGKTTAALALARELYGEDWR 68
RuvB COG2255
Holliday junction resolvasome RuvABC, ATP-dependent DNA helicase subunit RuvB [Replication, ...
 489-541 9.30e-05

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


Pssm-ID: 441856 [Multi-domain]  Cd Length: 337  Bit Score: 45.84  E-value: 9.30e-05
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|...
gi 21396489 489 EDHYGMEDVKKRILEFIAVSQLRGSTQGKILcFYGPPGVGKTSIARSIARALN 541
Cdd:COG2255  28 DEYIGQEKVKENLKIFIEAAKKRGEALDHVL-LYGPPGLGKTTLAHIIANEMG 79
RecA-like_Figl-1 cd19525
ATPase domain of Fidgetin-Like 1 (FIGL-1); FIGL-1 may participate in DNA repair in the nucleus; ...
 489-595 1.14e-04

ATPase domain of Fidgetin-Like 1 (FIGL-1); FIGL-1 may participate in DNA repair in the nucleus; it may be involved in DNA double-strand break repair via homologous recombination. Caenorhabditis elegans FIGL-1 is a nuclear protein and controls the mitotic progression in the germ line and mouse FIGL-1 may be involved in the control of male meiosis. human FIGL-1 has been shown to be a centrosome protein involved in ciliogenesis perhaps as a microtubule-severing protein. This subfamily belongs to the RecA-like NTPase family which includes the NTP binding domain of F1 and V1 H(+)ATPases, DnaB and related helicases as well as bacterial RecA and related eukaryotic and archaeal recombinases. The RecA-like NTPase family also includes bacterial conjugation proteins and related DNA transfer proteins involved in type II and type IV secretion.


Pssm-ID: 410933 [Multi-domain]  Cd Length: 186  Bit Score: 44.21  E-value: 1.14e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21396489 489 EDHYGMEDVKKRILEFIAV--------SQLRGSTQGKILcfYGPPGVGKTSIARSIARALNREYFRFSVGGMTDvaeikg 560
Cdd:cd19525  22 ADIAGLEFAKKTIKEIVVWpmlrpdifTGLRGPPKGILL--FGPPGTGKTLIGKCIASQSGATFFSISASSLTS------ 93

                        90       100       110
                ....*....|....*....|....*....|....*.
gi 21396489 561 hrrTYVGAMPGKIIQCLKKTKTENP-LILIDEVDKI 595
Cdd:cd19525  94 ---KWVGEGEKMVRALFSVARCKQPaVIFIDEIDSL 126
RecA-like_VCP_r2 cd19529
second of two ATPase domains of Valosin-containing protein-like ATPase (VAT) and similar ...
 522-650 1.36e-04

second of two ATPase domains of Valosin-containing protein-like ATPase (VAT) and similar ATPase domains; The Valosin-containing protein-like ATPase of Thermoplasma acidophilum (VAT), is an archaeal homolog of the ubiquitous Cdc48/p97. It is a protein unfoldase that functions in concert with the 20S proteasome by unfolding proteasome substrates and passing them on for degradation. VAT forms a homohexamer, each monomer contains two tandem ATPase domains, referred to as D1 and D2, and an N-terminal domain. This subfamily belongs to the RecA-like NTPase family which includes the NTP binding domain of F1 and V1 H(+)ATPases, DnaB and related helicases as well as bacterial RecA and related eukaryotic and archaeal recombinases. The RecA-like NTPase family also includes bacterial conjugation proteins and related DNA transfer proteins involved in type II and type IV secretion.


Pssm-ID: 410937 [Multi-domain]  Cd Length: 159  Bit Score: 43.25  E-value: 1.36e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21396489 522 YGPPGVGKTSIARSIARALNREYfrFSVGGMTDVAEikghrrtYVGAMPGKIIQCLKKTKTENP-LILIDEVDKI--GRG 598
Cdd:cd19529  33 YGPPGTGKTLLAKAVATESNANF--ISVKGPELLSK-------WVGESEKAIREIFRKARQVAPcVIFFDEIDSIapRRG 103

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|...
gi 21396489 599 YQGDPSSAllelldpEQNANFLDHYLDVPVDLSKVLFICTANVTDTI-PEPLR 650
Cdd:cd19529 104 TTGDSGVT-------ERVVNQLLTELDGLEEMNGVVVIAATNRPDIIdPALLR 149
RecA-like_ClpB_Hsp104-like cd19499
Chaperone protein ClpB/Hsp104 subfamily; Bacterial Caseinolytic peptidase B (ClpB) and ...
 519-656 1.44e-04

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: 43.71  E-value: 1.44e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21396489 519 LCFYGPPGVGKTSIARSIARAL---NREYFRFSVGG---MTDVAEIKGHRRTYVGA-MPGKIIQCLKKtkteNP--LILI 589
Cdd:cd19499  44 FLFLGPTGVGKTELAKALAELLfgdEDNLIRIDMSEymeKHSVSRLIGAPPGYVGYtEGGQLTEAVRR----KPysVVLL 119

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 21396489 590 DEVDKIGRGYQGdpssALLELLDpeqNANFLDHYLDVpVDLSKVLFICTANVtdtIPEPLRDRMEMI 656
Cdd:cd19499 120 DEIEKAHPDVQN----LLLQVLD---DGRLTDSHGRT-VDFKNTIIIMTSNH---FRPEFLNRIDEI 175
DnaX COG2812
DNA polymerase III, gamma/tau subunits [Replication, recombination and repair];
521-541 1.50e-04

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


Pssm-ID: 442061 [Multi-domain]  Cd Length: 340  Bit Score: 45.18  E-value: 1.50e-04
                        10        20
                ....*....|....*....|.
gi 21396489 521 FYGPPGVGKTSIARSIARALN 541
Cdd:COG2812  37 FTGPRGVGKTTLARILAKALN 57
RecA-like_Pch2-like cd19508
ATPase domain of Pachytene checkpoint 2 (Pch2) and similar ATPase domains; Pch2 (known as ...
 495-652 1.66e-04

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: 43.59  E-value: 1.66e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21396489 495 EDVKKRILEFIAVSqLRGSTQG---------KILCFYGPPGVGKTSIARSIARALN-REYFRFSVGGMTdvaEIKGHR-- 562
Cdd:cd19508  23 SNLKSRLLDYVTTT-LLFSDKNvntnlitwnRLVLLHGPPGTGKTSLCKALAQKLSiRLSSRYRYGQLI---EINSHSlf 98

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21396489 563 -------RTYVGAMPGKiIQCLKKTKTENPLILIDEVDKIgrGYQGDPSSALLELLDPEQNANFLDHYLDVPVDLSKVLF 635
Cdd:cd19508  99 skwfsesGKLVTKMFQK-IQELIDDKDALVFVLIDEVESL--AAARSASSSGTEPSDAIRVVNAVLTQIDRIKRYHNNVI 175

                       170
                ....*....|....*..
gi 21396489 636 ICTANVTDTIPEPLRDR 652
Cdd:cd19508 176 LLTSNLLEKIDVAFVDR 192
RecA-like_ATAD1 cd19520
ATPase domain of ATPase family AAA domain-containing protein 1 and similar ATPase domains; ...
 493-593 2.11e-04

ATPase domain of ATPase family AAA domain-containing protein 1 and similar ATPase domains; ATPase family AAA domain-containing protein 1 (ATAD1, also known as Thorase) is an ATPase that plays a critical role in regulating the surface expression of alpha-amino-3-hydroxy-5-methyl-4-isoxazolepropionic acid (AMPA) receptors, thereby regulating synaptic plasticity, learning and memory. This subfamily belongs to the RecA-like NTPase family which includes the NTP binding domain of F1 and V1 H(+)ATPases, DnaB and related helicases as well as bacterial RecA and related eukaryotic and archaeal recombinases. The RecA-like NTPase family also includes bacterial conjugation proteins and related DNA transfer proteins involved in type II and type IV secretion.


Pssm-ID: 410928 [Multi-domain]  Cd Length: 166  Bit Score: 42.80  E-value: 2.11e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21396489 493 GMEDVKKRILEFI----------AVSQLRGSTQGKILcfYGPPGVGKTSIARSIARALNREYFRFSVGGMTDvaEIKGHR 562
Cdd:cd19520   4 GLDEVITELKELVilplqrpelfDNSRLLQPPKGVLL--YGPPGCGKTMLAKATAKEAGARFINLQVSSLTD--KWYGES 79

                        90       100       110
                ....*....|....*....|....*....|.
gi 21396489 563 RTYVGAMPGKIIqclkktKTENPLILIDEVD 593
Cdd:cd19520  80 QKLVAAVFSLAS------KLQPSIIFIDEID 104
McrB COG1401
5-methylcytosine-specific restriction endonuclease McrBC, GTP-binding regulatory subunit McrB ...
 319-644 2.72e-04

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


Pssm-ID: 441011 [Multi-domain]  Cd Length: 477  Bit Score: 44.76  E-value: 2.72e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21396489 319 QAGQRVVDNPIYLSDMGAALTGAESHELQDVLEETNIPKRLYKALSLLKKEFELSKLQQRLGREVEEKIKQTHRKYLLQE 398
Cdd:COG1401  24 DAVRELGIRADDLRGAAELATRLAERLSEELLRADRAARATELVEELSAALEVVVLLLDLEKVELNEKLALSEAAVAIEE 103

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21396489 399 QLKIIKKELGLEKDDKDAIEEKFRERLKELVVPKHVMDVVDEELSKLGLLDNHSSEFNVTRNYLDWLTSIP-WGKYSNEN 477
Cdd:COG1401 104 LYELEADSEIEAVGLLLELAERSDALEALERARLLLELADLEERAALETEVLEALEAELEELLAAPEDLSAdALAAELSA 183

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21396489 478 LDLARAQAVLEEDHYGMEDVKKRILEFIA--VSQLRGSTQgKILcfYGPPGVGKTSIARSIARAL---NREYFRF----- 547
Cdd:COG1401 184 AEELYSEDLESEDDYLKDLLREKFEETLEafLAALKTKKN-VIL--AGPPGTGKTYLARRLAEALggeDNGRIEFvqfhp 260

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21396489 548 ------SVGGMTDVAEIKGHRRTyvgamPGKIIQCLKKTKtENP----LILIDEvdkIGRG----YQGDpssaLLELLDP 613
Cdd:COG1401 261 swsyedFLLGYRPSLDEGKYEPT-----PGIFLRFCLKAE-KNPdkpyVLIIDE---INRAnvekYFGE----LLSLLES 327

                       330       340       350
                ....*....|....*....|....*....|....*..
gi 21396489 614 EQNANFLD---HYLDVPVDLS---KVLFICTANVTDT 644
Cdd:COG1401 328 DKRGEELSielPYSGEGEEFSippNLYIIGTMNTDDR 364
hflB PRK10733
ATP-dependent zinc metalloprotease FtsH;
490-597 2.94e-04

ATP-dependent zinc metalloprotease FtsH;


Pssm-ID: 182683 [Multi-domain]  Cd Length: 644  Bit Score: 44.64  E-value: 2.94e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21396489  490 DHYGMEDVKKRILEFIAVSQLRGSTQ---GKI---LCFYGPPGVGKTSIARSIARALNREYFRFSvggMTDVAEIkghrr 563
Cdd:PRK10733 153 DVAGCDEAKEEVAELVEYLREPSRFQklgGKIpkgVLMVGPPGTGKTLLAKAIAGEAKVPFFTIS---GSDFVEM----- 224

                         90       100       110
                 ....*....|....*....|....*....|....*
gi 21396489  564 tYVGAMPGKIIQCLKKTKTENP-LILIDEVDKIGR 597
Cdd:PRK10733 225 -FVGVGASRVRDMFEQAKKAAPcIIFIDEIDAVGR 258
RecA-like_PEX6_r2 cd19527
second of two ATPase domains of Peroxisomal biogenesis factor 6 (PEX6); PEX6(also known as ...
 497-602 3.05e-04

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: 42.50  E-value: 3.05e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21396489 497 VKKRILEFIAVSQLR------GSTQGKILCFYGPPGVGKTSIARSIARALNREYfrFSVGGMTDVaeikghrRTYVGAMP 570
Cdd:cd19527   1 VKKEILDTIQLPLEHpelfssGLRKRSGILLYGPPGTGKTLLAKAIATECSLNF--LSVKGPELI-------NMYIGESE 71

                        90       100       110
                ....*....|....*....|....*....|....*
gi 21396489 571 GKIIQCLKKTKTENP-LILIDEVDKIG--RGYQGD 602
Cdd:cd19527  72 ANVREVFQKARDAKPcVIFFDELDSLApsRGNSGD 106
AAA_PrkA smart00763
PrkA AAA domain; This is a family of PrkA bacterial and archaeal serine kinases approximately ...
 488-550 3.36e-04

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


Pssm-ID: 214810  Cd Length: 361  Bit Score: 44.20  E-value: 3.36e-04
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 21396489    488 EEDHYGMEDVKKRILEFIAVSQLRGSTQGKILCFYGPPGVGKTSIARSIARALnREYFRFSVG 550
Cdd:smart00763  50 DHDFFGMEEAIERFVNYFKSAAQGLEERKQILYLLGPVGGGKSSLVECLKRGL-EEYSKTDEG 111
RecA-like_NVL_r1-like cd19518
first of two ATPase domains of NVL (nuclear VCP-like protein) and similar ATPase domains; NVL ...
 493-596 8.35e-04

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: 41.24  E-value: 8.35e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21396489 493 GMEDVKKRILEFIA-------VSQLRGSTQGKILCFYGPPGVGKTSIARSIARALNREYFRFS----VGGMTdvaeikgh 561
Cdd:cd19518   4 GMDSTLKELCELLIhpilppeYFQHLGVEPPRGVLLHGPPGCGKTMLANAIAGELKVPFLKISateiVSGVS-------- 75

                        90       100       110
                ....*....|....*....|....*....|....*.
gi 21396489 562 rrtyvGAMPGKIIQCLKKTKTENPLIL-IDEVDKIG 596
Cdd:cd19518  76 -----GESEEKIRELFDQAISNAPCIVfIDEIDAIT 106
RecA-like_CDC48_r1-like cd19519
first of two ATPase domains of CDC48 and similar ATPase domains; CDC48 in yeast and p97 or VCP ...
 522-595 8.86e-04

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: 40.88  E-value: 8.86e-04
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 21396489 522 YGPPGVGKTSIARSIARALNReyFRFSVGGmtdvAEIKGhrrTYVGAMPGKIIQCLKKTKTENP-LILIDEVDKI 595
Cdd:cd19519  40 YGPPGTGKTLIARAVANETGA--FFFLING----PEIMS---KLAGESESNLRKAFEEAEKNAPaIIFIDEIDAI 105
PRK15455 PRK15455
PrkA family serine protein kinase; Provisional
 489-533 2.53e-03

PrkA family serine protein kinase; Provisional


Pssm-ID: 185352 [Multi-domain]  Cd Length: 644  Bit Score: 41.51  E-value: 2.53e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|
gi 21396489  489 EDHYGMEDVKKRIlefiaVSQLRGSTQG-----KILCFYGPPGVGKTSIA 533
Cdd:PRK15455  76 EEFYGMEEAIEQI-----VSYFRHAAQGleekkQILYLLGPVGGGKSSLA 120
RNA_helicase pfam00910
RNA helicase; This family includes RNA helicases thought to be involved in duplex unwinding ...
 519-544 2.84e-03

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


Pssm-ID: 459992  Cd Length: 102  Bit Score: 37.97  E-value: 2.84e-03
                          10        20
                  ....*....|....*....|....*.
gi 21396489   519 LCFYGPPGVGKTSIARSIARALNREY 544
Cdd:pfam00910   1 IWLYGPPGCGKSTLAKYLARALLKKL 26
RecA-like_PAN_like cd19502
proteasome activating nucleotidase PAN and related proteasome subunits; This subfamily ...
 522-611 2.87e-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: 39.63  E-value: 2.87e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21396489 522 YGPPGVGKTSIARSIARALNREYFRfsVGGMTDVaeikghrRTYVGAMPGKIIQCLKKTKTENP-LILIDEVDKIGRGYQ 600
Cdd:cd19502  43 YGPPGTGKTLLAKAVANHTDATFIR--VVGSELV-------QKYIGEGARLVRELFEMAREKAPsIIFIDEIDAIGAKRF 113

                        90
                ....*....|....*...
gi 21396489 601 GDPSSA-------LLELL 611
Cdd:cd19502 114 DSGTGGdrevqrtMLELL 131
COG1373 COG1373
Predicted ATPase, AAA+ superfamily [General function prediction only];
494-592 2.94e-03

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


Pssm-ID: 440984 [Multi-domain]  Cd Length: 405  Bit Score: 41.08  E-value: 2.94e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21396489 494 MEDVKKRILEFIavsqLRGSTQGKILCFYGPPGVGKTSIARSIARAL-NREYFRFsvggmtDVAEIkghrRTYVGAMPGK 572
Cdd:COG1373   2 MIMIKRKILDKL----LKLLDNRKAVVITGPRQVGKTTLLKQLAKELeNILYINL------DDPRL----RALAEEDPDD 67

                        90       100
                ....*....|....*....|
gi 21396489 573 IIQCLKKTKTENPLILIDEV 592
Cdd:COG1373  68 LLEALKELYPGKTYLFLDEI 87
RecA-like_spastin cd19524
ATPase domain of spastin; Spastin is an ATP-dependent microtubule-severing protein involved in ...
 490-595 2.99e-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: 39.45  E-value: 2.99e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21396489 490 DHYGMEDVKKRILEFIAVSQLRGS------TQGKILCFYGPPGVGKTSIARSIARALNREYFRFSVGGMTDvaeikghrr 563
Cdd:cd19524   1 DIAGQDLAKQALQEMVILPSLRPElftglrAPARGLLLFGPPGNGKTMLAKAVAAESNATFFNISAASLTS--------- 71

                        90       100       110
                ....*....|....*....|....*....|....
gi 21396489 564 TYVGAMPgKIIQCLKKTKTE-NP-LILIDEVDKI 595
Cdd:cd19524  72 KYVGEGE-KLVRALFAVARElQPsIIFIDEVDSL 104
RecA-like_NSF-SEC18_r1-like cd19504
first of two ATPase domains of NSF and SEC18, and similar ATPase domains; ...
 500-649 3.11e-03

first of two ATPase domains of NSF and SEC18, and similar ATPase domains; N-ethylmaleimide-sensitive factor (NSF) and Saccharomyces cerevisiae Vesicular-fusion protein Sec18, key factors for eukaryotic trafficking, are ATPases and SNARE disassembly chaperones. NSF/Sec18 activate or prime SNAREs, the terminal catalysts of membrane fusion. Sec18/NSF associates with SNARE complexes through binding Sec17/alpha-SNAP. Sec18 has an N-terminal cap domain and two nucleotide-binding domains (D1 and D2) which form the two rings of the hexameric complex. The hydrolysis of ATP by D1 generates most of the energy necessary to disassemble inactive SNARE bundles, while the D2 ring binds ATP to stabilize the homohexamer. This subfamily includes the first (D1) ATPase domain of NSF/Sec18, 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: 410912 [Multi-domain]  Cd Length: 177  Bit Score: 39.78  E-value: 3.11e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21396489 500 RILEFIAVSQLrGSTQGKILCFYGPPGVGKTSIARSIARALNREYFRFSVGgmtdvAEIkghRRTYVGAMPGKIIQCLK- 578
Cdd:cd19504  20 RVFPPEIVEQL-GCKHVKGILLYGPPGTGKTLMARQIGKMLNAREPKIVNG-----PEI---LNKYVGESEANIRKLFAd 90

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21396489 579 -----KTKTENP---LILIDEVDKI--GRGYQGDPSSAllelldPEQNANFLDHYLDVPVDLSKVLFICTANVTDTIPEP 648
Cdd:cd19504  91 aeeeqRRLGANSglhIIIFDEIDAIckQRGSMAGSTGV------HDTVVNQLLSKIDGVEQLNNILVIGMTNRKDLIDEA 164


                .
gi 21396489 649 L 649
Cdd:cd19504 165 L 165
AAA_22 pfam13401
AAA domain;
511-611 3.14e-03

AAA domain;


Pssm-ID: 379165 [Multi-domain]  Cd Length: 129  Bit Score: 38.86  E-value: 3.14e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21396489   511 RGSTQGkILCFYGPPGVGKTSIARSIARAL---NREYFRFSVGGMTDVAEI----------KGHRRTYVGAMPGKIIQCL 577
Cdd:pfam13401   1 IRFGAG-ILVLTGESGTGKTTLLRRLLEQLpevRDSVVFVDLPSGTSPKDLlrallralglPLSGRLSKEELLAALQQLL 79

                          90       100       110
                  ....*....|....*....|....*....|....
gi 21396489   578 KKTKTEnPLILIDEVDKIgrgyqgdpSSALLELL 611
Cdd:pfam13401  80 LALAVA-VVLIIDEAQHL--------SLEALEEL 104
T7SS_EccA TIGR03922
type VII secretion AAA-ATPase EccA; This model represents the AAA family ATPase, EccA, of the ...
 480-540 3.17e-03

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


Pssm-ID: 188437 [Multi-domain]  Cd Length: 557  Bit Score: 41.37  E-value: 3.17e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21396489   480 LARAQAVLEEdHYGMEDVKKRI------LEFIAVSQLRG---STQGKILCFYGPPGVGKTSIARSIARAL 540
Cdd:TIGR03922 268 LAEAEAELAE-QIGLERVKRQVaalkssTAMALARAERGlpvAQTSNHMLFAGPPGTGKTTIARVVAKIY 336
PRK13341 PRK13341
AAA family ATPase;
519-538 3.20e-03

AAA family ATPase;


Pssm-ID: 237354 [Multi-domain]  Cd Length: 725  Bit Score: 41.19  E-value: 3.20e-03
                         10        20
                 ....*....|....*....|
gi 21396489  519 LCFYGPPGVGKTSIARSIAR 538
Cdd:PRK13341  55 LILYGPPGVGKTTLARIIAN 74
RecA-like_CDC48_r2-like cd19511
second of two ATPase domains of CDC48/p97, PEX1 and -6, VAT and NVL, and similar ATPase ...
 521-612 3.57e-03

second of two ATPase domains of CDC48/p97, PEX1 and -6, VAT and NVL, and similar ATPase domains; This subfamily includes the second of two ATPase domains of the molecular chaperone CDC48 in yeast and p97 or VCP in metazoans, Peroxisomal biogenesis factor 1 (PEX1) and -6 (PEX6), Valosin-containing protein-like ATPase (VAT), and nuclear VCP-like protein (NVL). 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: 410919 [Multi-domain]  Cd Length: 159  Bit Score: 39.19  E-value: 3.57e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21396489 521 FYGPPGVGKTSIARSIAralnreyfrfSVGGMTDVAeIKGHR--RTYVGAMPGKIIQCLKKTKTENP-LILIDEVDKIG- 596
Cdd:cd19511  32 LYGPPGCGKTLLAKALA----------SEAGLNFIS-VKGPElfSKYVGESERAVREIFQKARQAAPcIIFFDEIDSLAp 100

                        90       100
                ....*....|....*....|...
gi 21396489 597 -RGYQGDPS------SALLELLD 612
Cdd:cd19511 101 rRGQSDSSGvtdrvvSQLLTELD 123
AAA_16 pfam13191
AAA ATPase domain; This family of domains contain a P-loop motif that is characteriztic of the ...
 515-550 3.74e-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: 3.74e-03
                          10        20        30
                  ....*....|....*....|....*....|....*.
gi 21396489   515 QGKILCFYGPPGVGKTSIARSIARALNREYFRFSVG 550
Cdd:pfam13191  23 RPPSVLLTGEAGTGKTTLLRELLRALERDGGYFLRG 58
FlhF COG1419
Flagellar biosynthesis GTPase FlhF [Cell motility];
397-533 3.76e-03

Flagellar biosynthesis GTPase FlhF [Cell motility];


Pssm-ID: 441029 [Multi-domain]  Cd Length: 361  Bit Score: 40.62  E-value: 3.76e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21396489 397 QEQLKIIKKELgleKDDKDAIEEKFRERLKELVVPKHVMDVVDEELSKLGLLDNHSSEFnvtrnyldwltsipwgkysne 476
Cdd:COG1419  73 EEELEELRREL---AELKELLEEQLSGLAGESARLPPELAELLERLLEAGVSPELAREL--------------------- 128

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 21396489 477 nldLARAQAVLEEDhYGMEDVKKRILEFIAVSQLRGSTQGKILCFYGPPGVGKT-SIA 533
Cdd:COG1419 129 ---LEKLPEDLSAE-EAWRALLEALARRLPVAEDPLLDEGGVIALVGPTGVGKTtTIA 182
RecA-like_VPS4 cd19521
ATPase domain of vacuolar protein sorting-associated protein 4; Vacuolar protein ...
 489-654 4.16e-03

ATPase domain of vacuolar protein sorting-associated protein 4; Vacuolar protein sorting-associated protein 4 (Vps4) is believed to be involved in intracellular protein transport out of a prevacuolar endosomal compartment. 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: 410929 [Multi-domain]  Cd Length: 170  Bit Score: 39.07  E-value: 4.16e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21396489 489 EDHYGMEDVKKRILEF----IAVSQL----RGSTQGKILcfYGPPGVGKTSIARSIARALNREYFRFSVGGMTDvaeikg 560
Cdd:cd19521   7 EDVAGLEGAKEALKEAvilpVKFPHLftgnRKPWSGILL--YGPPGTGKSYLAKAVATEANSTFFSVSSSDLVS------ 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21396489 561 hrrTYVGAMPGKIIQCLKKTKTENP-LILIDEVDKIGrGYQGDPSSALLELLDPEqnanFLDHYLDVPVDLSKVLFICTA 639
Cdd:cd19521  79 ---KWMGESEKLVKQLFAMARENKPsIIFIDEVDSLC-GTRGEGESEASRRIKTE----LLVQMNGVGNDSQGVLVLGAT 150

                       170
                ....*....|....*
gi 21396489 640 NVTDTIPEPLRDRME 654
Cdd:cd19521 151 NIPWQLDSAIRRRFE 165
PRK06835 PRK06835
DNA replication protein DnaC; Validated
 494-540 5.05e-03

DNA replication protein DnaC; Validated


Pssm-ID: 235871 [Multi-domain]  Cd Length: 329  Bit Score: 40.27  E-value: 5.05e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*..
gi 21396489  494 MEDVKKRILEFIAVSqlrgSTQGKILCFYGPPGVGKTSIARSIARAL 540
Cdd:PRK06835 165 MEKILEKCKNFIENF----DKNNENLLFYGNTGTGKTFLSNCIAKEL 207
CDC48 TIGR01243
AAA family ATPase, CDC48 subfamily; This subfamily of the AAA family ATPases includes two ...
 486-595 9.43e-03

AAA family ATPase, CDC48 subfamily; This subfamily of the AAA family ATPases includes two members each from three archaeal species. It also includes yeast CDC48 (cell division control protein 48) and the human ortholog, transitional endoplasmic reticulum ATPase (valosin-containing protein). These proteins in eukaryotes are involved in the budding and transfer of membrane from the transitional endoplasmic reticulum to the Golgi apparatus.


Pssm-ID: 273521 [Multi-domain]  Cd Length: 733  Bit Score: 39.89  E-value: 9.43e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21396489   486 VLEEDHYGMEDVKKRILEFIAVS-------QLRGSTQGKILCFYGPPGVGKTSIARSIARALNrEYFrFSVGGmtdvAEI 558
Cdd:TIGR01243 175 VTYEDIGGLKEAKEKIREMVELPmkhpelfEHLGIEPPKGVLLYGPPGTGKTLLAKAVANEAG-AYF-ISING----PEI 248

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 21396489   559 KGhrrTYVGAMPGKIIQCLKKTKTENP-LILIDEVDKI 595
Cdd:TIGR01243 249 MS---KYYGESEERLREIFKEAEENAPsIIFIDEIDAI 283
 
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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