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Conserved domains on  [gi|19173766|ref|NP_596895|]
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lon protease homolog, mitochondrial precursor [Rattus norvegicus]

Protein Classification

endopeptidase La( domain architecture ID 11489643)

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

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

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
lon TIGR00763
endopeptidase La; This protein, the ATP-dependent serine endopeptidase La, is induced by heat ...
 113-937 0e+00

endopeptidase La; This protein, the ATP-dependent serine endopeptidase La, is induced by heat shock and other stresses in E. coli, B. subtilis, and other species. The yeast member, designated PIM1, is located in the mitochondrial matrix, required for mitochondrial function, and also induced by heat shock. [Protein fate, Degradation of proteins, peptides, and glycopeptides]


:

Pssm-ID: 273258 [Multi-domain]  Cd Length: 775  Bit Score: 1196.34  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19173766   113 PLIAISRNPVFPRFIKIVEVKNKKLVELLRRKVRLAQPYVGVFLKRDDNNESDvveSLDEIYHTGTFAQIHEMQDLGD-- 190
Cdd:TIGR00763   1 PLLPLRRRPLFPGMIKPIDVGREKSIKLIKEALRLKQPYLGLFLQKDDDNEEP---EEDDIYSVGVVAQILEMLPLPSsg 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19173766   191 --KLRMIVTGHRRIHISrqlEVEPEGlepeaenkqksrrklkrgkkevgdelgakpqlemvteatsdtskEVLMVEVENV 268
Cdd:TIGR00763  78 taTYKVVVEGLRRIRIK---ELSDKG--------------------------------------------GYLVVRVDNL 110

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19173766   269 AHEDFQV-TEEVKALTAEIVKTIRDIIALNPLYRESVLQMMQAGQrvVDNPIYLSDMGAALTG-AESHELQDVLEETNIL 346
Cdd:TIGR00763 111 KEEPFDKdDEEIKALTREIKETFRELISLSKLFREQPALLSALED--IDEPGRLADFVAASLQlKEKDELQEVLETVNIE 188

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19173766   347 KRLYKALSLLKKEFELSKLQQRLGREVEEKIKQTHRKYLLQEQLKIIKKELGLEKDDKDAIEeKFRERLKELVVPKHVMD 426
Cdd:TIGR00763 189 KRLKKALELLKKELELLKLQNKITKKVEEKMEKTQREYYLREQLKAIKKELGIEKDDKDELE-KLKEKLEELKLPEEVKK 267

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19173766   427 VVDEELSKLALLDNHSSEFNVTRNYLDWLTSIPWGRQSDENLDLARAQSVLEEDHYGMEDVKKRVLEFIAVSQLRGSTQG 506
Cdd:TIGR00763 268 VIEKELTKLSLLEPSSSEFTVTRNYLDWLTDLPWGKYSKENLDLKRAKEILDEDHYGLKKVKERILEYLAVQKLRGKMKG 347

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19173766   507 KILCFHGPPGVGKTSIARSIARALGREYFRFSVGGMTDVAEIKGHRRTYVGAMPGKIIQCLKKTKTENPLVLIDEVDKIG 586
Cdd:TIGR00763 348 PILCLVGPPGVGKTSLGKSIAKALNRKFVRFSLGGVRDEAEIRGHRRTYVGAMPGRIIQGLKKAKTKNPLFLLDEIDKIG 427

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19173766   587 RGYQGDPSSALLELLDPEQNANFLDHYLDVPVDLSKVLFICTANVTDTIPEPLRDRMEMINVSGYVAQEKLAIAERYLVP 666
Cdd:TIGR00763 428 SSFRGDPASALLEVLDPEQNNAFSDHYLDVPFDLSKVIFIATANSIDTIPRPLLDRMEVIELSGYTEEEKLEIAKKYLIP 507

                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19173766   667 QARTLCGLDESKAQLSATVLTLLIKQYCRESGVRNLQKQVEKVLRKAAYKIVS------GEAQTVHVTPENLQDFVGKPV 740
Cdd:TIGR00763 508 KALEDHGLKPDELKITDEALLLLIKYYTREAGVRNLERQIEKICRKAAVKLVEqgekkkSEAESVVITPDNLKKYLGKPV 587

                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19173766   741 FTVERMYDVTPPGVVMGLAWTAMGGSTLFVETSLRRPqpsgskedkDGSLEVTGQLGDVMKESARIAYTFARAFLMEQDP 820
Cdd:TIGR00763 588 FTYERAYEVTPPGVVMGLAWTPMGGDTLFIETTKVAG---------KGSLELTGQLGDVMKESAQIALTYVRSIAADLGI 658

                         730       740       750       760       770       780       790       800
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19173766   821 ENDFLVTSHIHLHVPEGATPKDGPSAGCTIVTALLSLALGQPVLQNLAMTGEVSLTGKVLPVGGIKEKTIAAKRAGVTCI 900
Cdd:TIGR00763 659 SPNFFEKADIHLHVPEGATPKDGPSAGITMATALLSLATGKPVRPDVAMTGEITLRGKVLPIGGLKEKTIAAKRAGIKTI 738

                         810       820       830
                  ....*....|....*....|....*....|....*..
gi 19173766   901 ILPAENRKDFSDLAPFITEGLEVHFVEHYRDIFRIAF 937
Cdd:TIGR00763 739 ILPEKNRRDLEELPENVKEGLEIHFVKHYDEVLKKAF 775
 
Name Accession Description Interval E-value
lon TIGR00763
endopeptidase La; This protein, the ATP-dependent serine endopeptidase La, is induced by heat ...
 113-937 0e+00

endopeptidase La; This protein, the ATP-dependent serine endopeptidase La, is induced by heat shock and other stresses in E. coli, B. subtilis, and other species. The yeast member, designated PIM1, is located in the mitochondrial matrix, required for mitochondrial function, and also induced by heat shock. [Protein fate, Degradation of proteins, peptides, and glycopeptides]


Pssm-ID: 273258 [Multi-domain]  Cd Length: 775  Bit Score: 1196.34  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19173766   113 PLIAISRNPVFPRFIKIVEVKNKKLVELLRRKVRLAQPYVGVFLKRDDNNESDvveSLDEIYHTGTFAQIHEMQDLGD-- 190
Cdd:TIGR00763   1 PLLPLRRRPLFPGMIKPIDVGREKSIKLIKEALRLKQPYLGLFLQKDDDNEEP---EEDDIYSVGVVAQILEMLPLPSsg 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19173766   191 --KLRMIVTGHRRIHISrqlEVEPEGlepeaenkqksrrklkrgkkevgdelgakpqlemvteatsdtskEVLMVEVENV 268
Cdd:TIGR00763  78 taTYKVVVEGLRRIRIK---ELSDKG--------------------------------------------GYLVVRVDNL 110

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19173766   269 AHEDFQV-TEEVKALTAEIVKTIRDIIALNPLYRESVLQMMQAGQrvVDNPIYLSDMGAALTG-AESHELQDVLEETNIL 346
Cdd:TIGR00763 111 KEEPFDKdDEEIKALTREIKETFRELISLSKLFREQPALLSALED--IDEPGRLADFVAASLQlKEKDELQEVLETVNIE 188

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19173766   347 KRLYKALSLLKKEFELSKLQQRLGREVEEKIKQTHRKYLLQEQLKIIKKELGLEKDDKDAIEeKFRERLKELVVPKHVMD 426
Cdd:TIGR00763 189 KRLKKALELLKKELELLKLQNKITKKVEEKMEKTQREYYLREQLKAIKKELGIEKDDKDELE-KLKEKLEELKLPEEVKK 267

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19173766   427 VVDEELSKLALLDNHSSEFNVTRNYLDWLTSIPWGRQSDENLDLARAQSVLEEDHYGMEDVKKRVLEFIAVSQLRGSTQG 506
Cdd:TIGR00763 268 VIEKELTKLSLLEPSSSEFTVTRNYLDWLTDLPWGKYSKENLDLKRAKEILDEDHYGLKKVKERILEYLAVQKLRGKMKG 347

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19173766   507 KILCFHGPPGVGKTSIARSIARALGREYFRFSVGGMTDVAEIKGHRRTYVGAMPGKIIQCLKKTKTENPLVLIDEVDKIG 586
Cdd:TIGR00763 348 PILCLVGPPGVGKTSLGKSIAKALNRKFVRFSLGGVRDEAEIRGHRRTYVGAMPGRIIQGLKKAKTKNPLFLLDEIDKIG 427

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19173766   587 RGYQGDPSSALLELLDPEQNANFLDHYLDVPVDLSKVLFICTANVTDTIPEPLRDRMEMINVSGYVAQEKLAIAERYLVP 666
Cdd:TIGR00763 428 SSFRGDPASALLEVLDPEQNNAFSDHYLDVPFDLSKVIFIATANSIDTIPRPLLDRMEVIELSGYTEEEKLEIAKKYLIP 507

                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19173766   667 QARTLCGLDESKAQLSATVLTLLIKQYCRESGVRNLQKQVEKVLRKAAYKIVS------GEAQTVHVTPENLQDFVGKPV 740
Cdd:TIGR00763 508 KALEDHGLKPDELKITDEALLLLIKYYTREAGVRNLERQIEKICRKAAVKLVEqgekkkSEAESVVITPDNLKKYLGKPV 587

                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19173766   741 FTVERMYDVTPPGVVMGLAWTAMGGSTLFVETSLRRPqpsgskedkDGSLEVTGQLGDVMKESARIAYTFARAFLMEQDP 820
Cdd:TIGR00763 588 FTYERAYEVTPPGVVMGLAWTPMGGDTLFIETTKVAG---------KGSLELTGQLGDVMKESAQIALTYVRSIAADLGI 658

                         730       740       750       760       770       780       790       800
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19173766   821 ENDFLVTSHIHLHVPEGATPKDGPSAGCTIVTALLSLALGQPVLQNLAMTGEVSLTGKVLPVGGIKEKTIAAKRAGVTCI 900
Cdd:TIGR00763 659 SPNFFEKADIHLHVPEGATPKDGPSAGITMATALLSLATGKPVRPDVAMTGEITLRGKVLPIGGLKEKTIAAKRAGIKTI 738

                         810       820       830
                  ....*....|....*....|....*....|....*..
gi 19173766   901 ILPAENRKDFSDLAPFITEGLEVHFVEHYRDIFRIAF 937
Cdd:TIGR00763 739 ILPEKNRRDLEELPENVKEGLEIHFVKHYDEVLKKAF 775
Lon COG0466
ATP-dependent Lon protease, bacterial type [Posttranslational modification, protein turnover, ...
 112-937 0e+00

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


Pssm-ID: 440234 [Multi-domain]  Cd Length: 785  Bit Score: 1004.54  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19173766 112 LPLIAISRNPVFPRFIKIVEVKNKKLVELLRrKVRLAQPYVGVFLKRDDNNESDvveSLDEIYHTGTFAQIHEMQDLGD- 190
Cdd:COG0466  14 LPLLPLRDVVVFPGMVIPLFVGREKSIKALE-EAMEGDKLIGLVAQKDAEVEDP---GPDDLYEVGTVAKILQLLKLPDg 89

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19173766 191 KLRMIVTGHRRIHISRQLEVEPeglepeaenkqksrrklkrgkkevgdelgakpqlemvteatsdtskeVLMVEVEnVAH 270
Cdd:COG0466  90 TVKVLVEGLQRARIKEFVQEEP-----------------------------------------------YLEAEVE-PLE 121

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19173766 271 EDFQVTEEVKALTAEIVKTIRDIIALNPLYRESVLQMMQAgqrvVDNPIYLSDMGAALTGAESHELQDVLEETNILKRLY 350
Cdd:COG0466 122 EEEEDDKELEALMRSLKEQFEEYVKLNPKIPPELLAALSN----IEDPGRLADFIASHLPLKIEEKQELLETLDVKERLE 197

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19173766 351 KALSLLKKEFELSKLQQRLGREVEEKIKQTHRKYLLQEQLKIIKKELGlEKDDKDAIEEKFRERLKELVVPKHVMDVVDE 430
Cdd:COG0466 198 KLLELLEKEIEVLELEKKIRSRVKEQMEKSQREYYLREQLKAIQKELG-EKDDGEDEIEELREKIEKAKLPEEVKEKAEK 276

                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19173766 431 ELSKLALLDNHSSEFNVTRNYLDWLTSIPWGRQSDENLDLARAQSVLEEDHYGMEDVKKRVLEFIAVSQLRGSTQGKILC 510
Cdd:COG0466 277 ELKKLERMPPMSAEATVIRNYLDWLLDLPWGKRTKDNLDLKKAEKILDEDHYGLEKVKERILEYLAVRKLKKKLKGPILC 356

                       410       420       430       440       450       460       470       480
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19173766 511 FHGPPGVGKTSIARSIARALGREYFRFSVGGMTDVAEIKGHRRTYVGAMPGKIIQCLKKTKTENPLVLIDEVDKIGRGYQ 590
Cdd:COG0466 357 LVGPPGVGKTSLGKSIARALGRKFVRISLGGVRDEAEIRGHRRTYIGAMPGRIIQGLKKAGTKNPVFLLDEIDKMGSDFR 436

                       490       500       510       520       530       540       550       560
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19173766 591 GDPSSALLELLDPEQNANFLDHYLDVPVDLSKVLFICTANVTDTIPEPLRDRMEMINVSGYVAQEKLAIAERYLVPQART 670
Cdd:COG0466 437 GDPASALLEVLDPEQNNTFSDHYLEVPFDLSKVMFIATANSLDTIPAPLLDRMEIIELSGYTEEEKLEIAKRYLIPKQLK 516

                       570       580       590       600       610       620       630       640
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19173766 671 LCGLDESKAQLSATVLTLLIKQYCRESGVRNLQKQVEKVLRKAAYKIVSGEAQTVHVTPENLQDFVGKPVFTVERMYDVT 750
Cdd:COG0466 517 EHGLKKEELKISDEALRKIIRGYTREAGVRNLEREIAKICRKVAKKIAEGKKKKVTITPKNLEKYLGVPRFRYEKAEEED 596

                       650       660       670       680       690       700       710       720
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19173766 751 PPGVVMGLAWTAMGGSTLFVETSLRRpqpsGSkedkdGSLEVTGQLGDVMKESARIAYTFARAFLMEQDPENDFLVTSHI 830
Cdd:COG0466 597 QVGVVTGLAWTEVGGDILFIEATLMP----GK-----GKLTLTGQLGDVMKESAQAALSYVRSRAEELGIDPDFFEKYDI 667

                       730       740       750       760       770       780       790       800
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19173766 831 HLHVPEGATPKDGPSAGCTIVTALLSLALGQPVLQNLAMTGEVSLTGKVLPVGGIKEKTIAAKRAGVTCIILPAENRKDF 910
Cdd:COG0466 668 HIHVPEGATPKDGPSAGITMATALVSALTGRPVRSDVAMTGEITLRGRVLPIGGLKEKLLAAHRAGIKTVILPKENEKDL 747

                       810       820
                ....*....|....*....|....*..
gi 19173766 911 SDLAPFITEGLEVHFVEHYRDIFRIAF 937
Cdd:COG0466 748 EEIPEEVKKGLEFHPVEHIDEVLKIAL 774
PRK10787 PRK10787
DNA-binding ATP-dependent protease La; Provisional
 315-937 5.41e-176

DNA-binding ATP-dependent protease La; Provisional


Pssm-ID: 182730 [Multi-domain]  Cd Length: 784  Bit Score: 530.67  E-value: 5.41e-176
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19173766  315 VDNPIYLSDMGAALTGAESHELQDVLEETNILKRLYKALSLLKKEFELSKLQQRLGREVEEKIKQTHRKYLLQEQLKIIK 394
Cdd:PRK10787 159 IDDPARLADTIAAHMPLKLADKQSVLEMSDVNERLEYLMAMMESEIDLLQVEKRIRNRVKKQMEKSQREYYLNEQMKAIQ 238

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19173766  395 KELGlEKDDKDAIEEKFRERLKELVVPKHVMDVVDEELSKLALLDNHSSEFNVTRNYLDWLTSIPWGRQSDENLDLARAQ 474
Cdd:PRK10787 239 KELG-EMDDAPDENEALKRKIDAAKMPKEAKEKAEAELQKLKMMSPMSAEATVVRGYIDWMVQVPWNARSKVKKDLRQAQ 317

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19173766  475 SVLEEDHYGMEDVKKRVLEFIAVSQLRGSTQGKILCFHGPPGVGKTSIARSIARALGREYFRFSVGGMTDVAEIKGHRRT 554
Cdd:PRK10787 318 EILDTDHYGLERVKDRILEYLAVQSRVNKIKGPILCLVGPPGVGKTSLGQSIAKATGRKYVRMALGGVRDEAEIRGHRRT 397

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19173766  555 YVGAMPGKIIQCLKKTKTENPLVLIDEVDKIGRGYQGDPSSALLELLDPEQNANFLDHYLDVPVDLSKVLFICTANVTDt 634
Cdd:PRK10787 398 YIGSMPGKLIQKMAKVGVKNPLFLLDEIDKMSSDMRGDPASALLEVLDPEQNVAFSDHYLEVDYDLSDVMFVATSNSMN- 476

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19173766  635 IPEPLRDRMEMINVSGYVAQEKLAIAERYLVPQARTLCGLDESKAQLSATVLTLLIKQYCRESGVRNLQKQVEKVLRKAA 714
Cdd:PRK10787 477 IPAPLLDRMEVIRLSGYTEDEKLNIAKRHLLPKQIERNALKKGELTVDDSAIIGIIRYYTREAGVRSLEREISKLCRKAV 556

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19173766  715 YKIVSGEA-QTVHVTPENLQDFVGKPVFTVERMYDVTPPGVVMGLAWTAMGGSTLFVETSLRRPQpsgskedkdGSLEVT 793
Cdd:PRK10787 557 KQLLLDKSlKHIEINGDNLHDYLGVQRFDYGRADNENRVGQVTGLAWTEVGGDLLTIETACVPGK---------GKLTYT 627

                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19173766  794 GQLGDVMKESARIAYTFARAFLMEQDPENDFLVTSHIHLHVPEGATPKDGPSAGCTIVTALLSLALGQPVLQNLAMTGEV 873
Cdd:PRK10787 628 GSLGEVMQESIQAALTVVRARAEKLGINPDFYEKRDIHVHVPEGATPKDGPSAGIAMCTALVSCLTGNPVRADVAMTGEI 707

                        570       580       590       600       610       620
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 19173766  874 SLTGKVLPVGGIKEKTIAAKRAGVTCIILPAENRKDFSDLAPFITEGLEVHFVEHYRDIFRIAF 937
Cdd:PRK10787 708 TLRGQVLPIGGLKEKLLAAHRGGIKTVLIPFENKRDLEEIPDNVIADLDIHPVKRIEEVLTLAL 771
RecA-like_Lon cd19500
lon protease homolog 2 peroxisomal; Lon protease (also known as Lon peptidase) is an ...
 470-651 1.05e-128

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


Pssm-ID: 410908 [Multi-domain]  Cd Length: 182  Bit Score: 385.37  E-value: 1.05e-128
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19173766 470 LARAQSVLEEDHYGMEDVKKRVLEFIAVSQLRGSTQGKILCFHGPPGVGKTSIARSIARALGREYFRFSVGGMTDVAEIK 549
Cdd:cd19500   1 IKKARKVLDADHYGLEDVKERILEYLAVRKLKGSMKGPILCLVGPPGVGKTSLGKSIARALGRKFVRISLGGVRDEAEIR 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19173766 550 GHRRTYVGAMPGKIIQCLKKTKTENPLVLIDEVDKIGRGYQGDPSSALLELLDPEQNANFLDHYLDVPVDLSKVLFICTA 629
Cdd:cd19500  81 GHRRTYVGAMPGRIIQALKKAGTNNPVFLLDEIDKIGSSFRGDPASALLEVLDPEQNSTFSDHYLDVPFDLSKVLFIATA 160

                       170       180
                ....*....|....*....|..
gi 19173766 630 NVTDTIPEPLRDRMEMINVSGY 651
Cdd:cd19500 161 NSLDTIPGPLLDRMEIIELSGY 182
Lon_C pfam05362
Lon protease (S16) C-terminal proteolytic domain; The Lon serine proteases must hydrolyse ATP ...
 727-938 6.54e-82

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: 263.33  E-value: 6.54e-82
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19173766   727 VTPENLQDFVGKPVFTVERMYDVTPPGVVMGLAWTAMGGSTLFVETSLRrpqpSGSkedkdGSLEVTGQLGDVMKESARI 806
Cdd:pfam05362   2 VTAKNLEKYLGVPRFRYGEAEKEDQVGVVTGLAWTEVGGDLLTIEAVIM----PGK-----GKLTLTGQLGDVMKESAQA 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19173766   807 AYTFARAFLMEQDPENDFLVTSHIHLHVPEGATPKDGPSAGCTIVTALLSLALGQPVLQNLAMTGEVSLTGKVLPVGGIK 886
Cdd:pfam05362  73 ALSYVRSRAEELGIDPDFFEKKDIHIHVPEGATPKDGPSAGVTMATALVSALTGIPVRKDVAMTGEITLRGRVLPIGGLK 152

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 19173766   887 EKTIAAKRAGVTCIILPAENRKDFSDLAPFITEGLEVHFVEHYRDIFRIAFP 938
Cdd:pfam05362 153 EKLLAAHRAGIKTVIIPKENEKDLEDIPENVREGLEIIPVEHVDEVLKHALV 204
LON smart00464
Found in ATP-dependent protease La (LON); N-terminal domain of the ATP-dependent protease La ...
 111-188 7.36e-16

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


Pssm-ID: 197740 [Multi-domain]  Cd Length: 92  Bit Score: 73.63  E-value: 7.36e-16
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 19173766    111 HLPLIAISRNPVFPRFIKIVEVKNKKLVELLRRKVRLAQPYVGVFLKRDDNNESDVVESLDEIYHtgTFAQIHEMQDL 188
Cdd:smart00464   1 TLPLLPIRRRPLFPGFVLPIPVKRPKSVAAIKEALRRSQPYVIVFLLQDDPTETPEPLSDTIAAL--MPLELHEKQEL 76
 
Name Accession Description Interval E-value
lon TIGR00763
endopeptidase La; This protein, the ATP-dependent serine endopeptidase La, is induced by heat ...
 113-937 0e+00

endopeptidase La; This protein, the ATP-dependent serine endopeptidase La, is induced by heat shock and other stresses in E. coli, B. subtilis, and other species. The yeast member, designated PIM1, is located in the mitochondrial matrix, required for mitochondrial function, and also induced by heat shock. [Protein fate, Degradation of proteins, peptides, and glycopeptides]


Pssm-ID: 273258 [Multi-domain]  Cd Length: 775  Bit Score: 1196.34  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19173766   113 PLIAISRNPVFPRFIKIVEVKNKKLVELLRRKVRLAQPYVGVFLKRDDNNESDvveSLDEIYHTGTFAQIHEMQDLGD-- 190
Cdd:TIGR00763   1 PLLPLRRRPLFPGMIKPIDVGREKSIKLIKEALRLKQPYLGLFLQKDDDNEEP---EEDDIYSVGVVAQILEMLPLPSsg 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19173766   191 --KLRMIVTGHRRIHISrqlEVEPEGlepeaenkqksrrklkrgkkevgdelgakpqlemvteatsdtskEVLMVEVENV 268
Cdd:TIGR00763  78 taTYKVVVEGLRRIRIK---ELSDKG--------------------------------------------GYLVVRVDNL 110

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19173766   269 AHEDFQV-TEEVKALTAEIVKTIRDIIALNPLYRESVLQMMQAGQrvVDNPIYLSDMGAALTG-AESHELQDVLEETNIL 346
Cdd:TIGR00763 111 KEEPFDKdDEEIKALTREIKETFRELISLSKLFREQPALLSALED--IDEPGRLADFVAASLQlKEKDELQEVLETVNIE 188

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19173766   347 KRLYKALSLLKKEFELSKLQQRLGREVEEKIKQTHRKYLLQEQLKIIKKELGLEKDDKDAIEeKFRERLKELVVPKHVMD 426
Cdd:TIGR00763 189 KRLKKALELLKKELELLKLQNKITKKVEEKMEKTQREYYLREQLKAIKKELGIEKDDKDELE-KLKEKLEELKLPEEVKK 267

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19173766   427 VVDEELSKLALLDNHSSEFNVTRNYLDWLTSIPWGRQSDENLDLARAQSVLEEDHYGMEDVKKRVLEFIAVSQLRGSTQG 506
Cdd:TIGR00763 268 VIEKELTKLSLLEPSSSEFTVTRNYLDWLTDLPWGKYSKENLDLKRAKEILDEDHYGLKKVKERILEYLAVQKLRGKMKG 347

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19173766   507 KILCFHGPPGVGKTSIARSIARALGREYFRFSVGGMTDVAEIKGHRRTYVGAMPGKIIQCLKKTKTENPLVLIDEVDKIG 586
Cdd:TIGR00763 348 PILCLVGPPGVGKTSLGKSIAKALNRKFVRFSLGGVRDEAEIRGHRRTYVGAMPGRIIQGLKKAKTKNPLFLLDEIDKIG 427

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19173766   587 RGYQGDPSSALLELLDPEQNANFLDHYLDVPVDLSKVLFICTANVTDTIPEPLRDRMEMINVSGYVAQEKLAIAERYLVP 666
Cdd:TIGR00763 428 SSFRGDPASALLEVLDPEQNNAFSDHYLDVPFDLSKVIFIATANSIDTIPRPLLDRMEVIELSGYTEEEKLEIAKKYLIP 507

                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19173766   667 QARTLCGLDESKAQLSATVLTLLIKQYCRESGVRNLQKQVEKVLRKAAYKIVS------GEAQTVHVTPENLQDFVGKPV 740
Cdd:TIGR00763 508 KALEDHGLKPDELKITDEALLLLIKYYTREAGVRNLERQIEKICRKAAVKLVEqgekkkSEAESVVITPDNLKKYLGKPV 587

                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19173766   741 FTVERMYDVTPPGVVMGLAWTAMGGSTLFVETSLRRPqpsgskedkDGSLEVTGQLGDVMKESARIAYTFARAFLMEQDP 820
Cdd:TIGR00763 588 FTYERAYEVTPPGVVMGLAWTPMGGDTLFIETTKVAG---------KGSLELTGQLGDVMKESAQIALTYVRSIAADLGI 658

                         730       740       750       760       770       780       790       800
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19173766   821 ENDFLVTSHIHLHVPEGATPKDGPSAGCTIVTALLSLALGQPVLQNLAMTGEVSLTGKVLPVGGIKEKTIAAKRAGVTCI 900
Cdd:TIGR00763 659 SPNFFEKADIHLHVPEGATPKDGPSAGITMATALLSLATGKPVRPDVAMTGEITLRGKVLPIGGLKEKTIAAKRAGIKTI 738

                         810       820       830
                  ....*....|....*....|....*....|....*..
gi 19173766   901 ILPAENRKDFSDLAPFITEGLEVHFVEHYRDIFRIAF 937
Cdd:TIGR00763 739 ILPEKNRRDLEELPENVKEGLEIHFVKHYDEVLKKAF 775
Lon COG0466
ATP-dependent Lon protease, bacterial type [Posttranslational modification, protein turnover, ...
 112-937 0e+00

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


Pssm-ID: 440234 [Multi-domain]  Cd Length: 785  Bit Score: 1004.54  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19173766 112 LPLIAISRNPVFPRFIKIVEVKNKKLVELLRrKVRLAQPYVGVFLKRDDNNESDvveSLDEIYHTGTFAQIHEMQDLGD- 190
Cdd:COG0466  14 LPLLPLRDVVVFPGMVIPLFVGREKSIKALE-EAMEGDKLIGLVAQKDAEVEDP---GPDDLYEVGTVAKILQLLKLPDg 89

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19173766 191 KLRMIVTGHRRIHISRQLEVEPeglepeaenkqksrrklkrgkkevgdelgakpqlemvteatsdtskeVLMVEVEnVAH 270
Cdd:COG0466  90 TVKVLVEGLQRARIKEFVQEEP-----------------------------------------------YLEAEVE-PLE 121

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19173766 271 EDFQVTEEVKALTAEIVKTIRDIIALNPLYRESVLQMMQAgqrvVDNPIYLSDMGAALTGAESHELQDVLEETNILKRLY 350
Cdd:COG0466 122 EEEEDDKELEALMRSLKEQFEEYVKLNPKIPPELLAALSN----IEDPGRLADFIASHLPLKIEEKQELLETLDVKERLE 197

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19173766 351 KALSLLKKEFELSKLQQRLGREVEEKIKQTHRKYLLQEQLKIIKKELGlEKDDKDAIEEKFRERLKELVVPKHVMDVVDE 430
Cdd:COG0466 198 KLLELLEKEIEVLELEKKIRSRVKEQMEKSQREYYLREQLKAIQKELG-EKDDGEDEIEELREKIEKAKLPEEVKEKAEK 276

                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19173766 431 ELSKLALLDNHSSEFNVTRNYLDWLTSIPWGRQSDENLDLARAQSVLEEDHYGMEDVKKRVLEFIAVSQLRGSTQGKILC 510
Cdd:COG0466 277 ELKKLERMPPMSAEATVIRNYLDWLLDLPWGKRTKDNLDLKKAEKILDEDHYGLEKVKERILEYLAVRKLKKKLKGPILC 356

                       410       420       430       440       450       460       470       480
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19173766 511 FHGPPGVGKTSIARSIARALGREYFRFSVGGMTDVAEIKGHRRTYVGAMPGKIIQCLKKTKTENPLVLIDEVDKIGRGYQ 590
Cdd:COG0466 357 LVGPPGVGKTSLGKSIARALGRKFVRISLGGVRDEAEIRGHRRTYIGAMPGRIIQGLKKAGTKNPVFLLDEIDKMGSDFR 436

                       490       500       510       520       530       540       550       560
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19173766 591 GDPSSALLELLDPEQNANFLDHYLDVPVDLSKVLFICTANVTDTIPEPLRDRMEMINVSGYVAQEKLAIAERYLVPQART 670
Cdd:COG0466 437 GDPASALLEVLDPEQNNTFSDHYLEVPFDLSKVMFIATANSLDTIPAPLLDRMEIIELSGYTEEEKLEIAKRYLIPKQLK 516

                       570       580       590       600       610       620       630       640
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19173766 671 LCGLDESKAQLSATVLTLLIKQYCRESGVRNLQKQVEKVLRKAAYKIVSGEAQTVHVTPENLQDFVGKPVFTVERMYDVT 750
Cdd:COG0466 517 EHGLKKEELKISDEALRKIIRGYTREAGVRNLEREIAKICRKVAKKIAEGKKKKVTITPKNLEKYLGVPRFRYEKAEEED 596

                       650       660       670       680       690       700       710       720
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19173766 751 PPGVVMGLAWTAMGGSTLFVETSLRRpqpsGSkedkdGSLEVTGQLGDVMKESARIAYTFARAFLMEQDPENDFLVTSHI 830
Cdd:COG0466 597 QVGVVTGLAWTEVGGDILFIEATLMP----GK-----GKLTLTGQLGDVMKESAQAALSYVRSRAEELGIDPDFFEKYDI 667

                       730       740       750       760       770       780       790       800
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19173766 831 HLHVPEGATPKDGPSAGCTIVTALLSLALGQPVLQNLAMTGEVSLTGKVLPVGGIKEKTIAAKRAGVTCIILPAENRKDF 910
Cdd:COG0466 668 HIHVPEGATPKDGPSAGITMATALVSALTGRPVRSDVAMTGEITLRGRVLPIGGLKEKLLAAHRAGIKTVILPKENEKDL 747

                       810       820
                ....*....|....*....|....*..
gi 19173766 911 SDLAPFITEGLEVHFVEHYRDIFRIAF 937
Cdd:COG0466 748 EEIPEEVKKGLEFHPVEHIDEVLKIAL 774
PRK10787 PRK10787
DNA-binding ATP-dependent protease La; Provisional
 315-937 5.41e-176

DNA-binding ATP-dependent protease La; Provisional


Pssm-ID: 182730 [Multi-domain]  Cd Length: 784  Bit Score: 530.67  E-value: 5.41e-176
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19173766  315 VDNPIYLSDMGAALTGAESHELQDVLEETNILKRLYKALSLLKKEFELSKLQQRLGREVEEKIKQTHRKYLLQEQLKIIK 394
Cdd:PRK10787 159 IDDPARLADTIAAHMPLKLADKQSVLEMSDVNERLEYLMAMMESEIDLLQVEKRIRNRVKKQMEKSQREYYLNEQMKAIQ 238

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19173766  395 KELGlEKDDKDAIEEKFRERLKELVVPKHVMDVVDEELSKLALLDNHSSEFNVTRNYLDWLTSIPWGRQSDENLDLARAQ 474
Cdd:PRK10787 239 KELG-EMDDAPDENEALKRKIDAAKMPKEAKEKAEAELQKLKMMSPMSAEATVVRGYIDWMVQVPWNARSKVKKDLRQAQ 317

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19173766  475 SVLEEDHYGMEDVKKRVLEFIAVSQLRGSTQGKILCFHGPPGVGKTSIARSIARALGREYFRFSVGGMTDVAEIKGHRRT 554
Cdd:PRK10787 318 EILDTDHYGLERVKDRILEYLAVQSRVNKIKGPILCLVGPPGVGKTSLGQSIAKATGRKYVRMALGGVRDEAEIRGHRRT 397

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19173766  555 YVGAMPGKIIQCLKKTKTENPLVLIDEVDKIGRGYQGDPSSALLELLDPEQNANFLDHYLDVPVDLSKVLFICTANVTDt 634
Cdd:PRK10787 398 YIGSMPGKLIQKMAKVGVKNPLFLLDEIDKMSSDMRGDPASALLEVLDPEQNVAFSDHYLEVDYDLSDVMFVATSNSMN- 476

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19173766  635 IPEPLRDRMEMINVSGYVAQEKLAIAERYLVPQARTLCGLDESKAQLSATVLTLLIKQYCRESGVRNLQKQVEKVLRKAA 714
Cdd:PRK10787 477 IPAPLLDRMEVIRLSGYTEDEKLNIAKRHLLPKQIERNALKKGELTVDDSAIIGIIRYYTREAGVRSLEREISKLCRKAV 556

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19173766  715 YKIVSGEA-QTVHVTPENLQDFVGKPVFTVERMYDVTPPGVVMGLAWTAMGGSTLFVETSLRRPQpsgskedkdGSLEVT 793
Cdd:PRK10787 557 KQLLLDKSlKHIEINGDNLHDYLGVQRFDYGRADNENRVGQVTGLAWTEVGGDLLTIETACVPGK---------GKLTYT 627

                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19173766  794 GQLGDVMKESARIAYTFARAFLMEQDPENDFLVTSHIHLHVPEGATPKDGPSAGCTIVTALLSLALGQPVLQNLAMTGEV 873
Cdd:PRK10787 628 GSLGEVMQESIQAALTVVRARAEKLGINPDFYEKRDIHVHVPEGATPKDGPSAGIAMCTALVSCLTGNPVRADVAMTGEI 707

                        570       580       590       600       610       620
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 19173766  874 SLTGKVLPVGGIKEKTIAAKRAGVTCIILPAENRKDFSDLAPFITEGLEVHFVEHYRDIFRIAF 937
Cdd:PRK10787 708 TLRGQVLPIGGLKEKLLAAHRGGIKTVLIPFENKRDLEEIPDNVIADLDIHPVKRIEEVLTLAL 771
RecA-like_Lon cd19500
lon protease homolog 2 peroxisomal; Lon protease (also known as Lon peptidase) is an ...
 470-651 1.05e-128

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


Pssm-ID: 410908 [Multi-domain]  Cd Length: 182  Bit Score: 385.37  E-value: 1.05e-128
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19173766 470 LARAQSVLEEDHYGMEDVKKRVLEFIAVSQLRGSTQGKILCFHGPPGVGKTSIARSIARALGREYFRFSVGGMTDVAEIK 549
Cdd:cd19500   1 IKKARKVLDADHYGLEDVKERILEYLAVRKLKGSMKGPILCLVGPPGVGKTSLGKSIARALGRKFVRISLGGVRDEAEIR 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19173766 550 GHRRTYVGAMPGKIIQCLKKTKTENPLVLIDEVDKIGRGYQGDPSSALLELLDPEQNANFLDHYLDVPVDLSKVLFICTA 629
Cdd:cd19500  81 GHRRTYVGAMPGRIIQALKKAGTNNPVFLLDEIDKIGSSFRGDPASALLEVLDPEQNSTFSDHYLDVPFDLSKVLFIATA 160

                       170       180
                ....*....|....*....|..
gi 19173766 630 NVTDTIPEPLRDRMEMINVSGY 651
Cdd:cd19500 161 NSLDTIPGPLLDRMEIIELSGY 182
Lon_C pfam05362
Lon protease (S16) C-terminal proteolytic domain; The Lon serine proteases must hydrolyse ATP ...
 727-938 6.54e-82

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: 263.33  E-value: 6.54e-82
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19173766   727 VTPENLQDFVGKPVFTVERMYDVTPPGVVMGLAWTAMGGSTLFVETSLRrpqpSGSkedkdGSLEVTGQLGDVMKESARI 806
Cdd:pfam05362   2 VTAKNLEKYLGVPRFRYGEAEKEDQVGVVTGLAWTEVGGDLLTIEAVIM----PGK-----GKLTLTGQLGDVMKESAQA 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19173766   807 AYTFARAFLMEQDPENDFLVTSHIHLHVPEGATPKDGPSAGCTIVTALLSLALGQPVLQNLAMTGEVSLTGKVLPVGGIK 886
Cdd:pfam05362  73 ALSYVRSRAEELGIDPDFFEKKDIHIHVPEGATPKDGPSAGVTMATALVSALTGIPVRKDVAMTGEITLRGRVLPIGGLK 152

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 19173766   887 EKTIAAKRAGVTCIILPAENRKDFSDLAPFITEGLEVHFVEHYRDIFRIAFP 938
Cdd:pfam05362 153 EKLLAAHRAGIKTVIIPKENEKDLEDIPENVREGLEIIPVEHVDEVLKHALV 204
AAA pfam00004
ATPase family associated with various cellular activities (AAA); AAA family proteins often ...
 509-651 1.41e-31

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


Pssm-ID: 459627 [Multi-domain]  Cd Length: 130  Bit Score: 120.01  E-value: 1.41e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19173766   509 LCFHGPPGVGKTSIARSIARALGREYFRFSVGGMTDvaeikghrrTYVGAMPGKIIQCLKKTKTENPLVL-IDEVDKIGR 587
Cdd:pfam00004   1 LLLYGPPGTGKTTLAKAVAKELGAPFIEISGSELVS---------KYVGESEKRLRELFEAAKKLAPCVIfIDEIDALAG 71

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 19173766   588 -------GYQGDPSSALLELLDPEQNANfldhyldvpvdlSKVLFICTANVTDTIPEPLRDRMEMINVSGY 651
Cdd:pfam00004  72 srgsggdSESRRVVNQLLTELDGFTSSN------------SKVIVIAATNRPDKLDPALLGRFDRIIEFPL 130
LON_substr_bdg pfam02190
ATP-dependent protease La (LON) substrate-binding domain; This domain has been shown to be ...
 112-358 9.46e-25

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


Pssm-ID: 426647 [Multi-domain]  Cd Length: 195  Bit Score: 102.80  E-value: 9.46e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19173766   112 LPLIAISRNPVFPRFIKIVEVKNKKLVELLRRKVRLAQPYvGVFLKrDDNNESDVVESLDEIYHTGTFAQIHEMQDLGDK 191
Cdd:pfam02190   2 LPLLPLRNTVLFPGMVLPLFVGRPRSIAAIEAALNKDKLY-GVLLV-SQKDAEDEEPTPDDLYEVGTVAKIVQILKLPDG 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19173766   192 -LRMIVTGHRRIHIsRQLEVEPEGLePEAEnkqksrrklkrgkkevgdelgakpqlemvteatsdtskevlmVEVENVAH 270
Cdd:pfam02190  80 tYKVLVEGLERVRI-VELVKKEEPY-LRAE------------------------------------------VEDLPEDS 115

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19173766   271 EDfqVTEEVKALTAEIVKTIRDIIALNPLYrESVLQMMqagqrVVDNPIYLSDMGAALTGAESHELQDVLEETNILKRLY 350
Cdd:pfam02190 116 DE--LSEALKALVKELIEKLRRLLKLLLPL-ELLLKIK-----DIENPGRLADLVAAILPLSPEEKQELLETLDVKERLE 187


                  ....*...
gi 19173766   351 KALSLLKK 358
Cdd:pfam02190 188 KVLELLNR 195
RecA-like_protease cd19481
proteases similar to RecA; RecA-like NTPases. This family includes the NTP binding domain of ...
 487-648 4.22e-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: 85.03  E-value: 4.22e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19173766 487 VKKRVLEFIAV------SQLRGSTQGKILCFHGPPGVGKTSIARSIARALGREYFRFSVGGMTDVAeikghrRTYVGAMP 560
Cdd:cd19481   1 LKASLREAVEAprrgsrLRRYGLGLPKGILLYGPPGTGKTLLAKALAGELGLPLIVVKLSSLLSKY------VGESEKNL 74

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19173766 561 GKIIQCLKKTKteNPLVLIDEVDKIG--RGYQGDPS------SALLELLDPEQNanfldhyldvpvdLSKVLFICTAN-V 631
Cdd:cd19481  75 RKIFERARRLA--PCILFIDEIDAIGrkRDSSGESGelrrvlNQLLTELDGVNS-------------RSKVLVIAATNrP 139

                       170
                ....*....|....*....
gi 19173766 632 TDTIPEPLR--DRMEMINV 648
Cdd:cd19481 140 DLLDPALLRpgRFDEVIEF 158
COG1750 COG1750
Predicted archaeal serine protease, S18 family [General function prediction only];
842-907 1.80e-16

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


Pssm-ID: 441356 [Multi-domain]  Cd Length: 213  Bit Score: 79.25  E-value: 1.80e-16
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 19173766 842 DGPSAGCTIVTALLSLALGQPVLQNLAMTGEVSLTGKVLPVGGIKEKTIAAKRAGVTCIILPAENR 907
Cdd:COG1750 108 GGPSAGGAMTVATYAALLGLPLNKSVTMTGMINPDGSIGPVGGVYEKLEAAASAGAKYFLIPKGQA 173
LON smart00464
Found in ATP-dependent protease La (LON); N-terminal domain of the ATP-dependent protease La ...
 111-188 7.36e-16

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


Pssm-ID: 197740 [Multi-domain]  Cd Length: 92  Bit Score: 73.63  E-value: 7.36e-16
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 19173766    111 HLPLIAISRNPVFPRFIKIVEVKNKKLVELLRRKVRLAQPYVGVFLKRDDNNESDVVESLDEIYHtgTFAQIHEMQDL 188
Cdd:smart00464   1 TLPLLPIRRRPLFPGFVLPIPVKRPKSVAAIKEALRRSQPYVIVFLLQDDPTETPEPLSDTIAAL--MPLELHEKQEL 76
AAA cd00009
The AAA+ (ATPases Associated with a wide variety of cellular Activities) superfamily ...
 482-646 1.54e-15

The AAA+ (ATPases Associated with a wide variety of cellular Activities) superfamily represents an ancient group of ATPases belonging to the ASCE (for additional strand, catalytic E) division of the P-loop NTPase fold. The ASCE division also includes ABC, RecA-like, VirD4-like, PilT-like, and SF1/2 helicases. Members of the AAA+ ATPases function as molecular chaperons, ATPase subunits of proteases, helicases, or nucleic-acid stimulated ATPases. The AAA+ proteins contain several distinct features in addition to the conserved alpha-beta-alpha core domain structure and the Walker A and B motifs of the P-loop NTPases.


Pssm-ID: 99707 [Multi-domain]  Cd Length: 151  Bit Score: 74.88  E-value: 1.54e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19173766 482 YGMEDVKKRVLEFIAvsqlrgSTQGKILCFHGPPGVGKTSIARSIARALGREYFRF---SVGGMTDVAEIKGHRRTYVGA 558
Cdd:cd00009   1 VGQEEAIEALREALE------LPPPKNLLLYGPPGTGKTTLARAIANELFRPGAPFlylNASDLLEGLVVAELFGHFLVR 74

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19173766 559 MPGKIIQclkktKTENPLVLIDEVDKIGRGYQgdpssallelldpEQNANFLDHYLDVPVDLSKVLFICTANVTD--TIP 636
Cdd:cd00009  75 LLFELAE-----KAKPGVLFIDEIDSLSRGAQ-------------NALLRVLETLNDLRIDRENVRVIGATNRPLlgDLD 136

                       170
                ....*....|
gi 19173766 637 EPLRDRMEMI 646
Cdd:cd00009 137 RALYDRLDIR 146
SpoVK COG0464
AAA+-type ATPase, SpoVK/Ycf46/Vps4 family [Cell wall/membrane/envelope biogenesis, Cell cycle ...
 483-664 6.66e-15

AAA+-type ATPase, SpoVK/Ycf46/Vps4 family [Cell wall/membrane/envelope biogenesis, Cell cycle control, cell division, chromosome partitioning, Signal transduction mechanisms];


Pssm-ID: 440232 [Multi-domain]  Cd Length: 397  Bit Score: 77.64  E-value: 6.66e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19173766 483 GMEDVKKRVLEFIA-------VSQLRGSTQGKILCFHGPPGVGKTSIARSIARALGREYFRFSVGGMTDvaeikghrrTY 555
Cdd:COG0464 161 GLEEVKEELRELVAlplkrpeLREEYGLPPPRGLLLYGPPGTGKTLLARALAGELGLPLIEVDLSDLVS---------KY 231

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19173766 556 VGAMPGKIIQCLKKTKTENPLVL-IDEVDKI--GRGYQGDPS-----SALLELLDpeqnanfldhylDVPvdlSKVLFIC 627
Cdd:COG0464 232 VGETEKNLREVFDKARGLAPCVLfIDEADALagKRGEVGDGVgrrvvNTLLTEME------------ELR---SDVVVIA 296

                       170       180       190
                ....*....|....*....|....*....|....*...
gi 19173766 628 TANVTDTIPEPLRDRM-EMINVSGYVAQEKLAIAERYL 664
Cdd:COG0464 297 ATNRPDLLDPALLRRFdEIIFFPLPDAEERLEIFRIHL 334
COG1223 COG1223
Predicted ATPase, AAA+ superfamily [General function prediction only];
479-664 2.41e-11

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


Pssm-ID: 440836 [Multi-domain]  Cd Length: 246  Bit Score: 64.91  E-value: 2.41e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19173766 479 EDHYGMEDVKKRVLEFIA----VSQLRG---STQGKILcFHGPPGVGKTSIARSIARALGREYFRFSVGGMTDvaeikgh 551
Cdd:COG1223   2 DDVVGQEEAKKKLKLIIKelrrRENLRKfglWPPRKIL-FYGPPGTGKTMLAEALAGELKLPLLTVRLDSLIG------- 73

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19173766 552 rrTYVGAMPGKIIQCLKKTKTENPLVLIDEVDKIG--RGYQ---GDPS---SALLELLDPEQnanfldhyldvpvdlSKV 623
Cdd:COG1223  74 --SYLGETARNLRKLFDFARRAPCVIFFDEFDAIAkdRGDQndvGEVKrvvNALLQELDGLP---------------SGS 136

                       170       180       190       200
                ....*....|....*....|....*....|....*....|..
gi 19173766 624 LFICTANVTDTIPEPLRDRMEM-INVSGYVAQEKLAIAERYL 664
Cdd:COG1223 137 VVIAATNHPELLDSALWRRFDEvIEFPLPDKEERKEILELNL 178
AAA smart00382
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ...
 505-642 3.93e-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: 56.23  E-value: 3.93e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19173766    505 QGKILCFHGPPGVGKTSIARSIARALGREYFRFSVGGMTDVAEIKGHRR-----------TYVGAMPGKIIQCLKKTKte 573
Cdd:smart00382   1 PGEVILIVGPPGSGKTTLARALARELGPPGGGVIYIDGEDILEEVLDQLlliivggkkasGSGELRLRLALALARKLK-- 78

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19173766    574 NPLVLIDEVDKIGRgyqgDPSSALLELLDPEQNANFLDHYLDVPVdlskvlfICTAN-VTDTIPEPLRDR 642
Cdd:smart00382  79 PDVLILDEITSLLD----AEQEALLLLLEELRLLLLLKSEKNLTV-------ILTTNdEKDLGPALLRRR 137
PRK13342 PRK13342
recombination factor protein RarA; Reviewed
 511-582 2.35e-08

recombination factor protein RarA; Reviewed


Pssm-ID: 237355 [Multi-domain]  Cd Length: 413  Bit Score: 57.40  E-value: 2.35e-08
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 19173766  511 FHGPPGVGKTSIARSIARALGREYFRFSvGGMTDVAEIKghrrtyvgampgKIIQCLKKTKT--ENPLVLIDEV 582
Cdd:PRK13342  41 LWGPPGTGKTTLARIIAGATDAPFEALS-AVTSGVKDLR------------EVIEEARQRRSagRRTILFIDEI 101
44 PHA02544
clamp loader, small subunit; Provisional
 485-693 4.32e-08

clamp loader, small subunit; Provisional


Pssm-ID: 222866 [Multi-domain]  Cd Length: 316  Bit Score: 56.15  E-value: 4.32e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19173766  485 EDVKKRVLEFIavsqlrgsTQGKI--LCFHGP-PGVGKTSIARSIARALGREYFrFSVGGMTDVAEIKGHRRTYVGAM-- 559
Cdd:PHA02544  27 AADKETFKSIV--------KKGRIpnMLLHSPsPGTGKTTVAKALCNEVGAEVL-FVNGSDCRIDFVRNRLTRFASTVsl 97

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19173766  560 --PGKIIqclkktktenplvLIDEVDKIGRgyqgdpSSALLELldpeqnANFLDHYldvpvdlSK-VLFICTANVTDTIP 636
Cdd:PHA02544  98 tgGGKVI-------------IIDEFDRLGL------ADAQRHL------RSFMEAY-------SKnCSFIITANNKNGII 145

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 19173766  637 EPLRDRMEMINVSGYVAQEKLAIAERYLVpQARTLCglDESKAQLSATVLTLLIKQY 693
Cdd:PHA02544 146 EPLRSRCRVIDFGVPTKEEQIEMMKQMIV-RCKGIL--EAEGVEVDMKVLAALVKKN 199
AAA_5 pfam07728
AAA domain (dynein-related subfamily); This Pfam entry includes some of the AAA proteins not ...
 509-643 4.41e-08

AAA domain (dynein-related subfamily); This Pfam entry includes some of the AAA proteins not detected by the pfam00004 model.


Pssm-ID: 400191 [Multi-domain]  Cd Length: 135  Bit Score: 52.68  E-value: 4.41e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19173766   509 LCFHGPPGVGKTSIARSIARAL-GREYFRFSVGGMTDVAEIKGHRRTYVGAmPGKIIQCLKKTKTENPLVLIDEVDKIGR 587
Cdd:pfam07728   2 VLLVGPPGTGKTELAERLAAALsNRPVFYVQLTRDTTEEDLFGRRNIDPGG-ASWVDGPLVRAAREGEIAVLDEINRANP 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 19173766   588 GYQGdpssALLELLDPEQ----NANFLdhyldVPVDLSKVLFICTANVTDT----IPEPLRDRM 643
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 ...
 511-631 4.51e-08

AAA domain (Cdc48 subfamily); This Pfam entry includes some of the AAA proteins not detected by the pfam00004 model.


Pssm-ID: 400187 [Multi-domain]  Cd Length: 168  Bit Score: 53.74  E-value: 4.51e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19173766   511 FHGPPGVGKTSIARSIARALGREYFRFSVGGMTDVAEikghrRTYV----GAMPGKI------IQCLKKTKTENPLVLID 580
Cdd:pfam07724   8 FLGPTGVGKTELAKALAELLFGDERALIRIDMSEYME-----EHSVsrliGAPPGYVgyeeggQLTEAVRRKPYSIVLID 82

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 19173766   581 EVDKIGRGYQgdpsSALLELLDpeqNANFLDHYlDVPVDLSKVLFICTANV 631
Cdd:pfam07724  83 EIEKAHPGVQ----NDLLQILE---GGTLTDKQ-GRTVDFKNTLFIMTGNF 125
RPT1 COG1222
ATP-dependent 26S proteasome regulatory subunit [Posttranslational modification, protein ...
 387-587 2.42e-07

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


Pssm-ID: 440835 [Multi-domain]  Cd Length: 326  Bit Score: 53.86  E-value: 2.42e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19173766 387 QEQLKIIKKELGLEKDDKDAIEEKFRERLKELVVPKHVMDVvdeELSKLALLDNHSSEFNVTRNYLDWLTSipwgrqsde 466
Cdd:COG1222   1 GNDLLTIDENIKALLALIDALQERLGVELALLLQPVKALEL---LEEAPALLLNDANLTQKRLGTPRGTAV--------- 68

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19173766 467 nldLARAQSVLEEDHYGMEDVKKRVLEFIAVSQLR-------GSTQGKILCFHGPPGVGKTSIARSIARALGREYFRfsV 539
Cdd:COG1222  69 ---PAESPDVTFDDIGGLDEQIEEIREAVELPLKNpelfrkyGIEPPKGVLLYGPPGTGKTLLAKAVAGELGAPFIR--V 143

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*....
gi 19173766 540 GGmtdvAEIkghRRTYVGAMPGKIIQCLKKTKTENPLVL-IDEVDKIGR 587
Cdd:COG1222 144 RG----SEL---VSKYIGEGARNVREVFELAREKAPSIIfIDEIDAIAA 185
SdrC COG3480
Predicted secreted protein YlbL, contains PDZ domain [Signal transduction mechanisms];
843-923 2.54e-07

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


Pssm-ID: 442703 [Multi-domain]  Cd Length: 344  Bit Score: 53.66  E-value: 2.54e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19173766 843 GPSAGctivtalLSLALGqpVLQNL-----------AMTGEVSLTGKVLPVGGIKEKTIAAKRAGVTCIILPAENrkdFS 911
Cdd:COG3480 240 GPSAG-------LMFALG--IYDQLtpgdltggkkiAGTGTIDADGTVGPIGGIDQKVVAARRAGATIFLAPASN---CA 307

                        90
                ....*....|..
gi 19173766 912 DLAPFITEGLEV 923
Cdd:COG3480 308 EAVGTIPTGLKV 319
RecA-like_VPS4-like cd19509
ATPase domain of VPS4, ATAD1, K, KTNA1, Spastin, FIGL-1 and similar ATPase domains; This ...
 483-644 5.42e-07

ATPase domain of VPS4, ATAD1, K, KTNA1, Spastin, FIGL-1 and similar ATPase domains; This subfamily includes the ATPase domains of vacuolar protein sorting-associated protein 4 (VPS4), ATPase family AAA domain-containing protein 1 (ATAD1, also known as Thorase), Katanin p60 ATPase-containing subunit A1 (KTNA1), Spastin, and Fidgetin-Like 1 (FIGL-1). This subfamily belongs to the RecA-like NTPase family which includes the NTP binding domain of F1 and V1 H(+)ATPases, DnaB and related helicases as well as bacterial RecA and related eukaryotic and archaeal recombinases. The RecA-like NTPase family also includes bacterial conjugation proteins and related DNA transfer proteins involved in type II and type IV secretion.


Pssm-ID: 410917 [Multi-domain]  Cd Length: 163  Bit Score: 50.43  E-value: 5.42e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19173766 483 GMEDVKKRVLEFI--------AVSQLRGSTQGKILcfHGPPGVGKTSIARSIARALGREYFRFSVGGMTDvaeikghrrT 554
Cdd:cd19509   3 GLDDAKEALKEAVilpslrpdLFPGLRGPPRGILL--YGPPGTGKTLLARAVASESGSTFFSISASSLVS---------K 71

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19173766 555 YVGAmPGKIIQCLKKTKTEN--PLVLIDEVDKIGRGYQGDPSSA-------LLELLDPEQNAnfldhyldvpvDLSKVLF 625
Cdd:cd19509  72 WVGE-SEKIVRALFALARELqpSIIFIDEIDSLLSERGSGEHEAsrrvkteFLVQMDGVLNK-----------PEDRVLV 139

                       170
                ....*....|....*....
gi 19173766 626 ICTANVTDTIPEPLRDRME 644
Cdd:cd19509 140 LGATNRPWELDEAFLRRFE 158
LonB COG1067
Predicted ATP-dependent protease [Posttranslational modification, protein turnover, chaperones] ...
 842-888 8.08e-07

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


Pssm-ID: 440686 [Multi-domain]  Cd Length: 742  Bit Score: 53.03  E-value: 8.08e-07
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*...
gi 19173766 842 DGPSAGCTIVTALLSlAL-GQPVLQNLAMTGEVSLTGKVLPVGGIKEK 888
Cdd:COG1067 592 DGDSASSAELYALLS-ALsGVPIRQDIAVTGSVNQHGEVQPIGGVNEK 638
PRK04195 PRK04195
replication factor C large subunit; Provisional
 483-672 8.75e-07

replication factor C large subunit; Provisional


Pssm-ID: 235250 [Multi-domain]  Cd Length: 482  Bit Score: 52.62  E-value: 8.75e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19173766  483 GMEDVKKRVLEFIAvSQLRGSTQgKILCFHGPPGVGKTSIARSIARALGREYF-------------RFSVGGMTDVAEIK 549
Cdd:PRK04195  18 GNEKAKEQLREWIE-SWLKGKPK-KALLLYGPPGVGKTSLAHALANDYGWEVIelnasdqrtadviERVAGEAATSGSLF 95

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19173766  550 GHRRTyvgampgkiiqclkktktenpLVLIDEVDKI-GRGYQGDpSSALLELLDpeqNANfldhyldVPVdlskvlfICT 628
Cdd:PRK04195  96 GARRK---------------------LILLDEVDGIhGNEDRGG-ARAILELIK---KAK-------QPI-------ILT 136

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
gi 19173766  629 AN-VTDTIPEPLRDRMEMINVSgyvaqeklAIAERYLVPQARTLC 672
Cdd:PRK04195 137 ANdPYDPSLRELRNACLMIEFK--------RLSTRSIVPVLKRIC 173
RarA COG2256
Replication-associated recombination protein RarA (DNA-dependent ATPase) [Replication, ...
 511-582 9.55e-07

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


Pssm-ID: 441857 [Multi-domain]  Cd Length: 439  Bit Score: 52.37  E-value: 9.55e-07
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 19173766 511 FHGPPGVGKTSIARSIARALGREYFRFSvGGMTDVAEIKghrrtyvgampgKIIQCLKKTKTEN--PLVLIDEV 582
Cdd:COG2256  54 LWGPPGTGKTTLARLIANATDAEFVALS-AVTSGVKDIR------------EVIEEARERRAYGrrTILFVDEI 114
ChlI pfam13541
Subunit ChlI of Mg-chelatase;
840-906 1.07e-06

Subunit ChlI of Mg-chelatase;


Pssm-ID: 433293 [Multi-domain]  Cd Length: 121  Bit Score: 48.60  E-value: 1.07e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 19173766   840 PKDGPSAGCTIVTALLSLALGQPVLQNLAMTGEVSLTGKVLPVGGIKEKTIAAKRAGVTCIILPAEN 906
Cdd:pfam13541  55 KKEGSSFDLPIAIGILAAQGQIPVLEETIFLGELSLDGSLRPVRGALPIALAARKHGFRGLIVPKEN 121
MoxR COG0714
MoxR-like ATPase [General function prediction only]; MoxR-like ATPase is part of the Pathway ...
 513-602 1.12e-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: 51.32  E-value: 1.12e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19173766 513 GPPGVGKTSIARSIARALGREYFR--FSVGGM------TDVAEIKGHRRTYVgamPGKIIQclkktktenPLVLIDEVDK 584
Cdd:COG0714  38 GVPGVGKTTLAKALARALGLPFIRiqFTPDLLpsdilgTYIYDQQTGEFEFR---PGPLFA---------NVLLADEINR 105

                        90       100
                ....*....|....*....|
gi 19173766 585 igrgyqGDP--SSALLELLD 602
Cdd:COG0714 106 ------APPktQSALLEAME 119
RecA-like_Pch2-like cd19508
ATPase domain of Pachytene checkpoint 2 (Pch2) and similar ATPase domains; Pch2 (known as ...
 485-642 5.77e-06

ATPase domain of Pachytene checkpoint 2 (Pch2) and similar ATPase domains; Pch2 (known as Thyroid hormone receptor interactor 13 (TRIP13) and 16E1BP) is a key regulator of specific chromosomal events, like the control of G2/prophase processes such as DNA break formation and recombination, checkpoint signaling, and chromosome synapsis. This subfamily belongs to the RecA-like NTPase family which includes the NTP binding domain of F1 and V1 H(+)ATPases, DnaB and related helicases as well as bacterial RecA and related eukaryotic and archaeal recombinases. The RecA-like NTPase family also includes bacterial conjugation proteins and related DNA transfer proteins involved in type II and type IV secretion


Pssm-ID: 410916 [Multi-domain]  Cd Length: 199  Bit Score: 48.21  E-value: 5.77e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19173766 485 EDVKKRVLEFIAVSqLRGSTQG---------KILCFHGPPGVGKTSIARSIARALG-REYFRFSVGGMTdvaEIKGHR-- 552
Cdd:cd19508  23 SNLKSRLLDYVTTT-LLFSDKNvntnlitwnRLVLLHGPPGTGKTSLCKALAQKLSiRLSSRYRYGQLI---EINSHSlf 98

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19173766 553 -------RTYVGAMPGKiIQCLKKTKTENPLVLIDEVDKIgrGYQGDPSSALLELLDPEQNANFLDHYLDVPVDLSKVLF 625
Cdd:cd19508  99 skwfsesGKLVTKMFQK-IQELIDDKDALVFVLIDEVESL--AAARSASSSGTEPSDAIRVVNAVLTQIDRIKRYHNNVI 175

                       170
                ....*....|....*..
gi 19173766 626 ICTANVTDTIPEPLRDR 642
Cdd:cd19508 176 LLTSNLLEKIDVAFVDR 192
RuvB_N pfam05496
Holliday junction DNA helicase RuvB P-loop domain; The RuvB protein makes up part of the ...
 479-531 7.08e-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: 7.08e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 19173766   479 EDHYGMEDVKKRVLEFIAVSQLRGSTQGKILcFHGPPGVGKTSIARSIARALG 531
Cdd:pfam05496   7 DEYIGQEKVKENLKIFIEAAKQRGEALDHVL-LYGPPGLGKTTLANIIANEMG 58
RecA-like_CDC48_NLV2_r1-like cd19503
first of two ATPase domains of CDC48 and NLV2, and similar ATPase domains; CDC48 in yeast and ...
 483-640 7.85e-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: 46.90  E-value: 7.85e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19173766 483 GMEDVKKRVLEFIAvSQLRGSTQGKIL--------CFHGPPGVGKTSIARSIARALGREYFrfsvggmtdvaEIKGHrrT 554
Cdd:cd19503   4 GLDEQIASLKELIE-LPLKYPELFRALglkpprgvLLHGPPGTGKTLLARAVANEAGANFL-----------SISGP--S 69

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19173766 555 YVGAMPGKIIQCLKK-----TKTENPLVLIDEVDKIG--RGY-QGDPS----SALLELLDPEQNANfldhyldvpvdlsK 622
Cdd:cd19503  70 IVSKYLGESEKNLREifeeaRSHAPSIIFIDEIDALApkREEdQREVErrvvAQLLTLMDGMSSRG-------------K 136

                       170
                ....*....|....*...
gi 19173766 623 VLFICTANVTDTIPEPLR 640
Cdd:cd19503 137 VVVIAATNRPDAIDPALR 154
ruvB PRK00080
Holliday junction branch migration DNA helicase RuvB;
479-531 1.13e-05

Holliday junction branch migration DNA helicase RuvB;


Pssm-ID: 234619 [Multi-domain]  Cd Length: 328  Bit Score: 48.59  E-value: 1.13e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|...
gi 19173766  479 EDHYGMEDVKKRVLEFIAVSQLRGSTQGKILcFHGPPGVGKTSIARSIARALG 531
Cdd:PRK00080  25 DEFIGQEKVKENLKIFIEAAKKRGEALDHVL-LYGPPGLGKTTLANIIANEMG 76
RecA-like_NVL_r1-like cd19518
first of two ATPase domains of NVL (nuclear VCP-like protein) and similar ATPase domains; NVL ...
 483-586 1.18e-05

first of two ATPase domains of NVL (nuclear VCP-like protein) and similar ATPase domains; NVL exists in two forms with N-terminal extensions of different lengths in mammalian cells. NVL has two alternatively spliced isoforms, a short form, NVL1, and a long form, NVL2. NVL2, the major species, is mainly present in the nucleolus, whereas NVL1 is nucleoplasmic. Each has an N-terminal domain, followed by two tandem ATPase domains; this subfamily includes the first of the two ATPase domains. NVL2 is involved in the biogenesis of the 60S ribosome subunit by associating specifically with ribosome protein L5 and modulating the function of DOB1. NVL2 is also required for telomerase assembly and the regulation of telomerase activity, and is involved in pre-rRNA processing. The role of NVL1 is unclear. This RecA-like_NVL_r1-like subfamily belongs to the RecA-like NTPase family which includes the NTP binding domain of F1 and V1 H(+)ATPases, DnaB and related helicases as well as bacterial RecA and related eukaryotic and archaeal recombinases. The RecA-like NTPase family also includes bacterial conjugation proteins and related DNA transfer proteins involved in type II and type IV secretion.


Pssm-ID: 410926 [Multi-domain]  Cd Length: 169  Bit Score: 46.63  E-value: 1.18e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19173766 483 GMEDVKKRVLEFIA-------VSQLRGSTQGKILCFHGPPGVGKTSIARSIARALGREYFRFS----VGGMTdvaeikgh 551
Cdd:cd19518   4 GMDSTLKELCELLIhpilppeYFQHLGVEPPRGVLLHGPPGCGKTMLANAIAGELKVPFLKISateiVSGVS-------- 75

                        90       100       110
                ....*....|....*....|....*....|....*.
gi 19173766 552 rrtyvGAMPGKIIQCLKKTKTENP-LVLIDEVDKIG 586
Cdd:cd19518  76 -----GESEEKIRELFDQAISNAPcIVFIDEIDAIT 106
ruvB TIGR00635
Holliday junction DNA helicase, RuvB subunit; All proteins in this family for which functions ...
 479-663 1.19e-05

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


Pssm-ID: 129721 [Multi-domain]  Cd Length: 305  Bit Score: 48.45  E-value: 1.19e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19173766   479 EDHYGMEDVKKRVLEFIAVSQLRGSTQGKILcFHGPPGVGKTSIARSIARALGREyFRFSVGGMTDvaeikghrrtyvga 558
Cdd:TIGR00635   4 AEFIGQEKVKEQLQLFIEAAKMRQEALDHLL-LYGPPGLGKTTLAHIIANEMGVN-LKITSGPALE-------------- 67

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19173766   559 MPGKIIQCLKKTKtENPLVLIDEVDKIGRgyqgdpssALLELLDPEQNANFLDHYLD-------VPVDLSKVLFICTANV 631
Cdd:TIGR00635  68 KPGDLAAILTNLE-EGDVLFIDEIHRLSP--------AVEELLYPAMEDFRLDIVIGkgpsarsVRLDLPPFTLVGATTR 138

                         170       180       190
                  ....*....|....*....|....*....|...
gi 19173766   632 TDTIPEPLRDRMEMI-NVSGYVAQEKLAIAERY 663
Cdd:TIGR00635 139 AGMLTSPLRDRFGIIlRLEFYTVEELAEIVSRS 171
RecA-like_HslU cd19498
ATP-dependent protease ATPase subunit HslU; HslU is a component of the ATP-dependent protease ...
 513-640 1.20e-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: 46.99  E-value: 1.20e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19173766 513 GPPGVGKTSIARSIARALGREYFRFSVGGMTDVAeikghrrtYVGAMPGKIIQCLKKTktenpLVLIDEVDKI---GRGY 589
Cdd:cd19498  53 GPTGVGKTEIARRLAKLAGAPFIKVEATKFTEVG--------YVGRDVESIIRDLVEG-----IVFIDEIDKIakrGGSS 119

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 19173766 590 QGDPSSALLE--LLDPEQNANFLDHYldVPVDLSKVLFICT-----ANVTDTIPE-----PLR 640
Cdd:cd19498 120 GPDVSREGVQrdLLPIVEGSTVSTKY--GPVKTDHILFIAAgafhvAKPSDLIPElqgrfPIR 180
RecA-like_FtsH cd19501
ATP-dependent zinc metalloprotease FtsH; FtsH ATPase is a processive, ATP-dependent zinc ...
 483-587 2.80e-05

ATP-dependent zinc metalloprotease FtsH; FtsH ATPase is a processive, ATP-dependent zinc metallopeptidase for both cytoplasmic and membrane proteins. It is anchored to the cytoplasmic membrane such that the amino- and carboxy-termini are exposed to the cytoplasm. It presents a membrane-bound hexameric structure that is able to unfold and degrade protein substrates. It is comprised of an N-terminal transmembrane region and the larger C-terminal cytoplasmic region, which consists of an ATPase domain and a protease domain. This RecA-Like FTsH subfamily represents the ATPase domain, and belongs to the RecA-like NTPase family which includes the NTP binding domain of F1 and V1 H(+)ATPases, DnaB and related helicases as well as bacterial RecA and related eukaryotic and archaeal recombinases. The RecA-like NTPase family also includes bacterial conjugation proteins and related DNA transfer proteins involved in type II and type IV secretion.


Pssm-ID: 410909 [Multi-domain]  Cd Length: 171  Bit Score: 45.69  E-value: 2.80e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19173766 483 GMEDVKKRVLEFiaVSQLRGSTQ-----GKI---LCFHGPPGVGKTSIARSIARALGREYfrFSVGGmTDVAEIkghrrt 554
Cdd:cd19501   8 GCEEAKEELKEV--VEFLKNPEKftklgAKIpkgVLLVGPPGTGKTLLAKAVAGEAGVPF--FSISG-SDFVEM------ 76

                        90       100       110
                ....*....|....*....|....*....|....
gi 19173766 555 YVGAMPGKIIQCLKKTKTENP-LVLIDEVDKIGR 587
Cdd:cd19501  77 FVGVGASRVRDLFEQAKKNAPcIVFIDEIDAVGR 110
RuvB COG2255
Holliday junction resolvasome RuvABC, ATP-dependent DNA helicase subunit RuvB [Replication, ...
 458-531 3.47e-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: 47.00  E-value: 3.47e-05
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 19173766 458 IPWGRQSDENLDLA-RAQSVleEDHYGMEDVKKRVLEFIAVSQLRGSTQGKILcFHGPPGVGKTSIARSIARALG 531
Cdd:COG2255   8 SSSASEEEDALERSlRPKRL--DEYIGQEKVKENLKIFIEAAKKRGEALDHVL-LYGPPGLGKTTLAHIIANEMG 79
RecA-like_ClpB_Hsp104-like cd19499
Chaperone protein ClpB/Hsp104 subfamily; Bacterial Caseinolytic peptidase B (ClpB) and ...
 509-646 1.31e-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: 1.31e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19173766 509 LCFHGPPGVGKTSIARSIARAL--GREYF-RFSVGG---MTDVAEIKGHRRTYVGA-MPGKIIQCLKKtkteNP--LVLI 579
Cdd:cd19499  44 FLFLGPTGVGKTELAKALAELLfgDEDNLiRIDMSEymeKHSVSRLIGAPPGYVGYtEGGQLTEAVRR----KPysVVLL 119

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 19173766 580 DEVDKIGRGYQGdpssALLELLDpeqNANFLDHYLDVpVDLSKVLFICTANVtdtIPEPLRDRMEMI 646
Cdd:cd19499 120 DEIEKAHPDVQN----LLLQVLD---DGRLTDSHGRT-VDFKNTIIIMTSNH---FRPEFLNRIDEI 175
ftsH CHL00176
cell division protein; Validated
 479-587 1.41e-04

cell division protein; Validated


Pssm-ID: 214386 [Multi-domain]  Cd Length: 638  Bit Score: 45.81  E-value: 1.41e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19173766  479 EDHYGMEDVKKRVLEFiaVSQLR--------GSTQGKILCFHGPPGVGKTSIARSIARALGREYfrFSVGGMTDVAEIKG 550
Cdd:CHL00176 183 RDIAGIEEAKEEFEEV--VSFLKkperftavGAKIPKGVLLVGPPGTGKTLLAKAIAGEAEVPF--FSISGSEFVEMFVG 258

                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 19173766  551 hrrtyVGAmpGKIIQCLKKTKTENP-LVLIDEVDKIGR 587
Cdd:CHL00176 259 -----VGA--ARVRDLFKKAKENSPcIVFIDEIDAVGR 289
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
208-446 1.71e-04

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 45.44  E-value: 1.71e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19173766  208 LEVEPEGLE---PEAENKQKSRRKLKRGKKEVGDELGA--------------KPQLEMVTEATSDTSKEVLMVEVENVAH 270
Cdd:PRK03918 319 LEEEINGIEeriKELEEKEERLEELKKKLKELEKRLEEleerhelyeeakakKEELERLKKRLTGLTPEKLEKELEELEK 398

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19173766  271 EDFQVTEEVKALTAEIvKTIRDIIALnplYRESVLQMMQAGQRVvdnPIylsdMGAALTgaESHELQDVLEETNILKRLY 350
Cdd:PRK03918 399 AKEEIEEEISKITARI-GELKKEIKE---LKKAIEELKKAKGKC---PV----CGRELT--EEHRKELLEEYTAELKRIE 465

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19173766  351 KALSLLKKEfeLSKLQQRLgREVEEKIKQTHR---KYLLQEQLKIIKKEL---GLEKDDKDAIE-EKFRERLKELvvpKH 423
Cdd:PRK03918 466 KELKEIEEK--ERKLRKEL-RELEKVLKKESElikLKELAEQLKELEEKLkkyNLEELEKKAEEyEKLKEKLIKL---KG 539

                        250       260
                 ....*....|....*....|...
gi 19173766  424 VMDVVDEELSKLALLDNHSSEFN 446
Cdd:PRK03918 540 EIKSLKKELEKLEELKKKLAELE 562
McrB COG1401
5-methylcytosine-specific restriction endonuclease McrBC, GTP-binding regulatory subunit McrB ...
 309-634 2.28e-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: 2.28e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19173766 309 QAGQRVVDNPIYLSDMGAALTGAESHELQDVLEETNILKRLYKALSLLKKEFELSKLQQRLGREVEEKIKQTHRKYLLQE 388
Cdd:COG1401  24 DAVRELGIRADDLRGAAELATRLAERLSEELLRADRAARATELVEELSAALEVVVLLLDLEKVELNEKLALSEAAVAIEE 103

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19173766 389 QLKIIKKELGLEKDDKDAIEEKFRERLKELVVPKHVMDVVDEELSKLALLDNHSSEFNVTRNYLDWLTSIP-WGRQSDEN 467
Cdd:COG1401 104 LYELEADSEIEAVGLLLELAERSDALEALERARLLLELADLEERAALETEVLEALEAELEELLAAPEDLSAdALAAELSA 183

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19173766 468 LDLARAQSVLEEDHYGMEDVKKRVLEFIA--VSQLRGSTQgKILcfHGPPGVGKTSIARSIARALG---REYFRF----- 537
Cdd:COG1401 184 AEELYSEDLESEDDYLKDLLREKFEETLEafLAALKTKKN-VIL--AGPPGTGKTYLARRLAEALGgedNGRIEFvqfhp 260

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19173766 538 ------SVGGMTDVAEIKGHRRTyvgamPGKIIQ-CLK-KTKTENPLVL-IDEvdkIGRG----YQGDpssaLLELLDPE 604
Cdd:COG1401 261 swsyedFLLGYRPSLDEGKYEPT-----PGIFLRfCLKaEKNPDKPYVLiIDE---INRAnvekYFGE----LLSLLESD 328

                       330       340       350
                ....*....|....*....|....*....|....*.
gi 19173766 605 QNANFLD---HYLDVPVDLS---KVLFICTANVTDT 634
Cdd:COG1401 329 KRGEELSielPYSGEGEEFSippNLYIIGTMNTDDR 364
AAA_PrkA smart00763
PrkA AAA domain; This is a family of PrkA bacterial and archaeal serine kinases approximately ...
 478-540 2.30e-04

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


Pssm-ID: 214810  Cd Length: 361  Bit Score: 44.59  E-value: 2.30e-04
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 19173766    478 EEDHYGMEDVKKRVLEFIAVSQLRGSTQGKILCFHGPPGVGKTSIARSIARALgREYFRFSVG 540
Cdd:smart00763  50 DHDFFGMEEAIERFVNYFKSAAQGLEERKQILYLLGPVGGGKSSLVECLKRGL-EEYSKTDEG 111
RecA-like_ATAD1 cd19520
ATPase domain of ATPase family AAA domain-containing protein 1 and similar ATPase domains; ...
 483-544 2.36e-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: 2.36e-04
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 19173766 483 GMEDVKKRVLEFI----------AVSQLRGSTQGKILcfHGPPGVGKTSIARSIARALGREYFRFSVGGMTD 544
Cdd:cd19520   4 GLDEVITELKELVilplqrpelfDNSRLLQPPKGVLL--YGPPGCGKTMLAKATAKEAGARFINLQVSSLTD 73
RecA-like_Figl-1 cd19525
ATPase domain of Fidgetin-Like 1 (FIGL-1); FIGL-1 may participate in DNA repair in the nucleus; ...
 479-585 2.54e-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: 43.05  E-value: 2.54e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19173766 479 EDHYGMEDVKKRVLEFIAV--------SQLRGSTQGkILCFhGPPGVGKTSIARSIARALGREYFRFSVGGMTDvaeikg 550
Cdd:cd19525  22 ADIAGLEFAKKTIKEIVVWpmlrpdifTGLRGPPKG-ILLF-GPPGTGKTLIGKCIASQSGATFFSISASSLTS------ 93

                        90       100       110
                ....*....|....*....|....*....|....*.
gi 19173766 551 hrrTYVGAMPGKIIQCLKKTKTENPLVL-IDEVDKI 585
Cdd:cd19525  94 ---KWVGEGEKMVRALFSVARCKQPAVIfIDEIDSL 126
rfc PRK00440
replication factor C small subunit; Reviewed
 479-536 4.21e-04

replication factor C small subunit; Reviewed


Pssm-ID: 234763 [Multi-domain]  Cd Length: 319  Bit Score: 43.71  E-value: 4.21e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 19173766  479 EDHYGMEDVKKRVLEFIAvsqlrgstQGKI--LCFHGPPGVGKTSIARSIARALGREYFR 536
Cdd:PRK00440  17 DEIVGQEEIVERLKSYVK--------EKNMphLLFAGPPGTGKTTAALALARELYGEDWR 68
hflB PRK10733
ATP-dependent zinc metalloprotease FtsH;
480-587 1.05e-03

ATP-dependent zinc metalloprotease FtsH;


Pssm-ID: 182683 [Multi-domain]  Cd Length: 644  Bit Score: 42.71  E-value: 1.05e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19173766  480 DHYGMEDVKKRVLEFIAVSQLRGSTQ---GKI---LCFHGPPGVGKTSIARSIARALGREYFRFSvggMTDVAEIkghrr 553
Cdd:PRK10733 153 DVAGCDEAKEEVAELVEYLREPSRFQklgGKIpkgVLMVGPPGTGKTLLAKAIAGEAKVPFFTIS---GSDFVEM----- 224

                         90       100       110
                 ....*....|....*....|....*....|....*
gi 19173766  554 tYVGAMPGKIIQCLKKTKTENP-LVLIDEVDKIGR 587
Cdd:PRK10733 225 -FVGVGASRVRDMFEQAKKAAPcIIFIDEIDAVGR 258
DnaX COG2812
DNA polymerase III, gamma/tau subunits [Replication, recombination and repair];
511-530 1.05e-03

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


Pssm-ID: 442061 [Multi-domain]  Cd Length: 340  Bit Score: 42.49  E-value: 1.05e-03
                        10        20
                ....*....|....*....|
gi 19173766 511 FHGPPGVGKTSIARSIARAL 530
Cdd:COG2812  37 FTGPRGVGKTTLARILAKAL 56
HolB COG0470
DNA polymerase III, delta prime subunit [Replication, recombination and repair];
511-649 1.31e-03

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


Pssm-ID: 440238 [Multi-domain]  Cd Length: 289  Bit Score: 41.88  E-value: 1.31e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19173766 511 FHGPPGVGKTSIARSIARALGREY------------FRFSVGGMTDVAEIkghRRTYVGAMPGK-----IIQCLKKTKTE 573
Cdd:COG0470  23 LHGPPGIGKTTLALALARDLLCENpeggkacgqchsRLMAAGNHPDLLEL---NPEEKSDQIGIdqireLGEFLSLTPLE 99

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 19173766 574 NP--LVLIDEVDKIGRGYQgdpsSALLELL-DPEQNAnfldhyldvpvdlskvLFICTANVTDTIPEPLRDRMEMINVS 649
Cdd:COG0470 100 GGrkVVIIDEADAMNEAAA----NALLKTLeEPPKNT----------------PFILIANDPSRLLPTIRSRCQVIRFR 158
RecA-like_CDC48_r1-like cd19519
first of two ATPase domains of CDC48 and similar ATPase domains; CDC48 in yeast and p97 or VCP ...
 512-585 1.48e-03

first of two ATPase domains of CDC48 and similar ATPase domains; CDC48 in yeast and p97 or VCP metazoans is an ATP-dependent molecular chaperone which plays an essential role in many cellular processes, by segregating polyubiquitinated proteins from complexes or membranes. Cdc48/p97 consists of an N-terminal domain and two ATPase domains; this subfamily represents the first of the two ATPase domains. CDC48's roles include in the fragmentation of Golgi stacks during mitosis and for their reassembly after mitosis, and in the formation of the nuclear envelope, and of the transitional endoplasmic reticulum (tER). This RecA-like_cdc48_r1-like subfamily belongs to the RecA-like family which includes the NTP binding domain of F1 and V1 H(+)ATPases, DnaB and related helicases as well as bacterial RecA and related eukaryotic and archaeal recombinases. The RecA-like NTPase family also includes bacterial conjugation proteins and related DNA transfer proteins involved in type II and type IV secretion.


Pssm-ID: 410927 [Multi-domain]  Cd Length: 166  Bit Score: 40.50  E-value: 1.48e-03
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 19173766 512 HGPPGVGKTSIARSIARALGReyFRFSVGGmtdvAEIKGhrrTYVGAMPGKIIQCLKKTKTENP-LVLIDEVDKI 585
Cdd:cd19519  40 YGPPGTGKTLIARAVANETGA--FFFLING----PEIMS---KLAGESESNLRKAFEEAEKNAPaIIFIDEIDAI 105
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
 242-418 1.52e-03

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


Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 42.12  E-value: 1.52e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19173766 242 AKPQLEMVTEATSDTSKEV---------LMVEVENVAHEDFQVTEEVKALTAEIVKTIRDIIALNplyRESVLQMMQAGQ 312
Cdd:COG3883  14 ADPQIQAKQKELSELQAELeaaqaeldaLQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAE---AEIEERREELGE 90

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19173766 313 RVVDnpIYLSDMG----AALTGAESheLQDVLEETNILKRLYKA-LSLLKkefELSKLQQRL---GREVEEKIKQTHRKy 384
Cdd:COG3883  91 RARA--LYRSGGSvsylDVLLGSES--FSDFLDRLSALSKIADAdADLLE---ELKADKAELeakKAELEAKLAELEAL- 162

                       170       180       190
                ....*....|....*....|....*....|....
gi 19173766 385 llQEQLKIIKKELGLEKDDKDAIEEKFRERLKEL 418
Cdd:COG3883 163 --KAELEAAKAELEAQQAEQEALLAQLSAEEAAA 194
TsaE pfam02367
Threonylcarbamoyl adenosine biosynthesis protein TsaE; This family of proteins is involved in ...
 506-531 1.90e-03

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


Pssm-ID: 460540  Cd Length: 127  Bit Score: 39.34  E-value: 1.90e-03
                          10        20
                  ....*....|....*....|....*.
gi 19173766   506 GKILCFHGPPGVGKTSIARSIARALG 531
Cdd:pfam02367  21 GDVILLSGDLGAGKTTFTRGLARGLG 46
RecA-like_VCP_r2 cd19529
second of two ATPase domains of Valosin-containing protein-like ATPase (VAT) and similar ...
 508-640 2.32e-03

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


Pssm-ID: 410937 [Multi-domain]  Cd Length: 159  Bit Score: 39.79  E-value: 2.32e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19173766 508 ILCFhGPPGVGKTSIARSIARALGREYfrFSVGGMTDVAEikghrrtYVGAMPGKIIQCLKKTKTENPLVL-IDEVDKI- 585
Cdd:cd19529  30 ILLY-GPPGTGKTLLAKAVATESNANF--ISVKGPELLSK-------WVGESEKAIREIFRKARQVAPCVIfFDEIDSIa 99

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 19173766 586 -GRGYQGDPSSAllelldpEQNANFLDHYLDVPVDLSKVLFICTANVTDTI-PEPLR 640
Cdd:cd19529 100 pRRGTTGDSGVT-------ERVVNQLLTELDGLEEMNGVVVIAATNRPDIIdPALLR 149
RecA-like_ATAD3-like cd19512
ATPase domains of ATPase AAA-domain protein 3A (ATAD3A), -3B, and -3C, and similar ATPase ...
 511-583 2.99e-03

ATPase domains of ATPase AAA-domain protein 3A (ATAD3A), -3B, and -3C, and similar ATPase domains; ATPase AAA-domain protein 3 (ATAD3) is a ubiquitously expressed mitochondrial protein involved in mitochondrial dynamics, DNA-nucleoid structural organization, cholesterol transport and steroidogenesis. The ATAD3 gene family in human comprises three paralog genes: ATAD3A, ATAD3B and ATAD3C. This subfamily belongs to the RecA-like NTPase family which includes the NTP binding domain of F1 and V1 H(+)ATPases, DnaB and related helicases as well as bacterial RecA and related eukaryotic and archaeal recombinases. The RecA-like NTPase family also includes bacterial conjugation proteins and related DNA transfer proteins involved in type II and type IV secretion.


Pssm-ID: 410920 [Multi-domain]  Cd Length: 150  Bit Score: 39.05  E-value: 2.99e-03
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 19173766 511 FHGPPGVGKTSIARSIARALGREYFRFSVGgmtDVAEIKghrRTYVGAMpGKIIQCLKKTKtENPLVLIDEVD 583
Cdd:cd19512  27 FYGPPGTGKTLFAKKLALHSGMDYAIMTGG---DVAPMG---REGVTAI-HKVFDWANTSR-RGLLLFVDEAD 91
RecA-like_PEX6_r2 cd19527
second of two ATPase domains of Peroxisomal biogenesis factor 6 (PEX6); PEX6(also known as ...
 487-592 3.45e-03

second of two ATPase domains of Peroxisomal biogenesis factor 6 (PEX6); PEX6(also known as Peroxin61)/PEX1 is a protein unfoldase; PEX6 and PEX1 form a heterohexameric Type-2 AAA-ATPase complex and are essential for peroxisome biogenesis as they are required for the import of folded proteins into the peroxisomal matrix. This subfamily represents the second ATPase domain of PEX6. This subfamily belongs to the RecA-like NTPase family which includes the NTP binding domain of F1 and V1 H(+)ATPases, DnaB and related helicases as well as bacterial RecA and related eukaryotic and archaeal recombinases. The RecA-like NTPase family also includes bacterial conjugation proteins and related DNA transfer proteins involved in type II and type IV secretion.


Pssm-ID: 410935 [Multi-domain]  Cd Length: 160  Bit Score: 39.03  E-value: 3.45e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19173766 487 VKKRVLEFIAVSQLR------GSTQGKILCFHGPPGVGKTSIARSIARALGREYfrFSVGGMTDVaeikghrRTYVGAMP 560
Cdd:cd19527   1 VKKEILDTIQLPLEHpelfssGLRKRSGILLYGPPGTGKTLLAKAIATECSLNF--LSVKGPELI-------NMYIGESE 71

                        90       100       110
                ....*....|....*....|....*....|....*
gi 19173766 561 GKIIQCLKKTKTENP-LVLIDEVDKIG--RGYQGD 592
Cdd:cd19527  72 ANVREVFQKARDAKPcVIFFDELDSLApsRGNSGD 106
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
213-420 3.55e-03

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 41.20  E-value: 3.55e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19173766  213 EGLEPEAENKQKSRRKLKRGKKEVGDELGAKPQLEMVTEATSDTSKEVLMvEVENVAHEDFQVTEEVKALTAEI--VKTI 290
Cdd:PRK03918 158 DDYENAYKNLGEVIKEIKRRIERLEKFIKRTENIEELIKEKEKELEEVLR-EINEISSELPELREELEKLEKEVkeLEEL 236

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19173766  291 RDIIALNPLYRESVLQMMQAGQRVVDNpiyLSDMGAALTgAESHELQDVLEETNILK---RLYKALSLLKKEF--ELSKL 365
Cdd:PRK03918 237 KEEIEELEKELESLEGSKRKLEEKIRE---LEERIEELK-KEIEELEEKVKELKELKekaEEYIKLSEFYEEYldELREI 312

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 19173766  366 QQRLGR------EVEEKIKQTHRKyllQEQLKIIKKELGLEKDDKDAIEEKFR--ERLKELVV 420
Cdd:PRK03918 313 EKRLSRleeeinGIEERIKELEEK---EERLEELKKKLKELEKRLEELEERHElyEEAKAKKE 372
PRK13341 PRK13341
AAA family ATPase;
509-528 3.62e-03

AAA family ATPase;


Pssm-ID: 237354 [Multi-domain]  Cd Length: 725  Bit Score: 41.19  E-value: 3.62e-03
                         10        20
                 ....*....|....*....|
gi 19173766  509 LCFHGPPGVGKTSIARSIAR 528
Cdd:PRK13341  55 LILYGPPGVGKTTLARIIAN 74
PrkA COG2766
Predicted Ser/Thr protein kinase [Signal transduction mechanisms];
482-536 3.67e-03

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


Pssm-ID: 442049 [Multi-domain]  Cd Length: 675  Bit Score: 40.98  E-value: 3.67e-03
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 19173766 482 YGMEDVKKRVLEFiavsqLRGSTQG-----KILCFHGPPGVGKTSIARSIARALgREYFR 536
Cdd:COG2766  84 FGLEETLERIVDY-----LRSAARGlgerkRILLLHGPVGSGKSTLARCLKRGL-EEYSR 137
RNA_helicase pfam00910
RNA helicase; This family includes RNA helicases thought to be involved in duplex unwinding ...
 509-534 3.80e-03

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


Pssm-ID: 459992  Cd Length: 102  Bit Score: 37.97  E-value: 3.80e-03
                          10        20
                  ....*....|....*....|....*.
gi 19173766   509 LCFHGPPGVGKTSIARSIARALGREY 534
Cdd:pfam00910   1 IWLYGPPGCGKSTLAKYLARALLKKL 26
AAA_16 pfam13191
AAA ATPase domain; This family of domains contain a P-loop motif that is characteriztic of the ...
 505-540 4.42e-03

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


Pssm-ID: 433025 [Multi-domain]  Cd Length: 167  Bit Score: 39.02  E-value: 4.42e-03
                          10        20        30
                  ....*....|....*....|....*....|....*.
gi 19173766   505 QGKILCFHGPPGVGKTSIARSIARALGREYFRFSVG 540
Cdd:pfam13191  23 RPPSVLLTGEAGTGKTTLLRELLRALERDGGYFLRG 58
CMPK cd02020
Cytidine monophosphate kinase (CMPK) catalyzes the reversible phosphorylation of cytidine ...
 513-542 9.62e-03

Cytidine monophosphate kinase (CMPK) catalyzes the reversible phosphorylation of cytidine monophosphate (CMP) to produce cytidine diphosphate (CDP), using ATP as the preferred phosphoryl donor.


Pssm-ID: 238978 [Multi-domain]  Cd Length: 147  Bit Score: 37.47  E-value: 9.62e-03
                        10        20        30
                ....*....|....*....|....*....|
gi 19173766 513 GPPGVGKTSIARSIARALGREYfrFSVGGM 542
Cdd:cd02020   6 GPAGSGKSTVAKLLAKKLGLPY--LDTGGI 33
AroK COG0703
Shikimate kinase [Amino acid transport and metabolism]; Shikimate kinase is part of the ...
 513-535 9.70e-03

Shikimate kinase [Amino acid transport and metabolism]; Shikimate kinase is part of the Pathway/BioSystem: Aromatic amino acid biosynthesis


Pssm-ID: 440467 [Multi-domain]  Cd Length: 165  Bit Score: 37.80  E-value: 9.70e-03
                        10        20
                ....*....|....*....|...
gi 19173766 513 GPPGVGKTSIARSIARALGREYF 535
Cdd:COG0703   5 GMMGAGKSTVGRLLAKRLGLPFV 27
 
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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