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Conserved domains on  [gi|16128424|ref|NP_414973|]
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Lon protease [Escherichia coli str. K-12 substr. MG1655]

Protein Classification

endopeptidase La( domain architecture ID 11484944)

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

 Zoom to residue level

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List of domain hits

 Name Accession Description Interval E-value
PRK10787 PRK10787
DNA-binding ATP-dependent protease La; Provisional
 1-784 0e+00

DNA-binding ATP-dependent protease La; Provisional


:

Pssm-ID: 182730 [Multi-domain]  Cd Length: 784  Bit Score: 1639.27  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128424    1 MNPERSERIEIPVLPLRDVVVYPHMVIPLFVGREKSIRCLEAAMDHDKKIMLVAQKEASTDEPGVNDLFTVGTVASILQM 80
Cdd:PRK10787   1 MNPERSERIEIPVLPLRDVVVYPHMVIPLFVGREKSIRCLEAAMDHDKKIMLVAQKEASTDEPGVNDLFTVGTVASILQM 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128424   81 LKLPDGTVKVLVEGLQRARISALSDNGEHFSAKAEYLESPTIDEREQEVLVRTAISQFEGYIKLNKKIPPEVLTSLNSID 160
Cdd:PRK10787  81 LKLPDGTVKVLVEGLQRARISALSDNGEHFSAKAEYLESPTIDEREQEVLVRTAISQFEGYIKLNKKIPPEVLTSLNSID 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128424  161 DPARLADTIAAHMPLKLADKQSVLEMSDVNERLEYLMAMMESEIDLLQVEKRIRNRVKKQMEKSQREYYLNEQMKAIQKE 240
Cdd:PRK10787 161 DPARLADTIAAHMPLKLADKQSVLEMSDVNERLEYLMAMMESEIDLLQVEKRIRNRVKKQMEKSQREYYLNEQMKAIQKE 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128424  241 LGEMDDAPDENEALKRKIDAAKMPKEAKEKAEAELQKLKMMSPMSAEATVVRGYIDWMVQVPWNARSKVKKDLRQAQEIL 320
Cdd:PRK10787 241 LGEMDDAPDENEALKRKIDAAKMPKEAKEKAEAELQKLKMMSPMSAEATVVRGYIDWMVQVPWNARSKVKKDLRQAQEIL 320

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128424  321 DTDHYGLERVKDRILEYLAVQSRVNKIKGPILCLVGPPGVGKTSLGQSIAKATGRKYVRMALGGVRDEAEIRGHRRTYIG 400
Cdd:PRK10787 321 DTDHYGLERVKDRILEYLAVQSRVNKIKGPILCLVGPPGVGKTSLGQSIAKATGRKYVRMALGGVRDEAEIRGHRRTYIG 400

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128424  401 SMPGKLIQKMAKVGVKNPLFLLDEIDKMSSDMRGDPASALLEVLDPEQNVAFSDHYLEVDYDLSDVMFVATSNSMNIPAP 480
Cdd:PRK10787 401 SMPGKLIQKMAKVGVKNPLFLLDEIDKMSSDMRGDPASALLEVLDPEQNVAFSDHYLEVDYDLSDVMFVATSNSMNIPAP 480

                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128424  481 LLDRMEVIRLSGYTEDEKLNIAKRHLLPKQIERNALKKGELTVDDSAIIGIIRYYTREAGVRGLEREISKLCRKAVKQLL 560
Cdd:PRK10787 481 LLDRMEVIRLSGYTEDEKLNIAKRHLLPKQIERNALKKGELTVDDSAIIGIIRYYTREAGVRSLEREISKLCRKAVKQLL 560

                        570       580       590       600       610       620       630       640
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128424  561 LDKSLKHIEINGDNLHDYLGVQRFDYGRADNENRVGQVTGLAWTEVGGDLLTIETACVPGKGKLTYTGSLGEVMQESIQA 640
Cdd:PRK10787 561 LDKSLKHIEINGDNLHDYLGVQRFDYGRADNENRVGQVTGLAWTEVGGDLLTIETACVPGKGKLTYTGSLGEVMQESIQA 640

                        650       660       670       680       690       700       710       720
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128424  641 ALTVVRARAEKLGINPDFYEKRDIHVHVPEGATPKDGPSAGIAMCTALVSCLTGNPVRADVAMTGEITLRGQVLPIGGLK 720
Cdd:PRK10787 641 ALTVVRARAEKLGINPDFYEKRDIHVHVPEGATPKDGPSAGIAMCTALVSCLTGNPVRADVAMTGEITLRGQVLPIGGLK 720

                        730       740       750       760       770       780
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 16128424  721 EKLLAAHRGGIKTVLIPFENKRDLEEIPDNVIADLDIHPVKRIEEVLTLALQNEPSGMQVVTAK 784
Cdd:PRK10787 721 EKLLAAHRGGIKTVLIPFENKRDLEEIPDNVIADLDIHPVKRIEEVLTLALQNEPSGMQVVTAK 784
 
Name Accession Description Interval E-value
PRK10787 PRK10787
DNA-binding ATP-dependent protease La; Provisional
 1-784 0e+00

DNA-binding ATP-dependent protease La; Provisional


Pssm-ID: 182730 [Multi-domain]  Cd Length: 784  Bit Score: 1639.27  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128424    1 MNPERSERIEIPVLPLRDVVVYPHMVIPLFVGREKSIRCLEAAMDHDKKIMLVAQKEASTDEPGVNDLFTVGTVASILQM 80
Cdd:PRK10787   1 MNPERSERIEIPVLPLRDVVVYPHMVIPLFVGREKSIRCLEAAMDHDKKIMLVAQKEASTDEPGVNDLFTVGTVASILQM 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128424   81 LKLPDGTVKVLVEGLQRARISALSDNGEHFSAKAEYLESPTIDEREQEVLVRTAISQFEGYIKLNKKIPPEVLTSLNSID 160
Cdd:PRK10787  81 LKLPDGTVKVLVEGLQRARISALSDNGEHFSAKAEYLESPTIDEREQEVLVRTAISQFEGYIKLNKKIPPEVLTSLNSID 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128424  161 DPARLADTIAAHMPLKLADKQSVLEMSDVNERLEYLMAMMESEIDLLQVEKRIRNRVKKQMEKSQREYYLNEQMKAIQKE 240
Cdd:PRK10787 161 DPARLADTIAAHMPLKLADKQSVLEMSDVNERLEYLMAMMESEIDLLQVEKRIRNRVKKQMEKSQREYYLNEQMKAIQKE 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128424  241 LGEMDDAPDENEALKRKIDAAKMPKEAKEKAEAELQKLKMMSPMSAEATVVRGYIDWMVQVPWNARSKVKKDLRQAQEIL 320
Cdd:PRK10787 241 LGEMDDAPDENEALKRKIDAAKMPKEAKEKAEAELQKLKMMSPMSAEATVVRGYIDWMVQVPWNARSKVKKDLRQAQEIL 320

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128424  321 DTDHYGLERVKDRILEYLAVQSRVNKIKGPILCLVGPPGVGKTSLGQSIAKATGRKYVRMALGGVRDEAEIRGHRRTYIG 400
Cdd:PRK10787 321 DTDHYGLERVKDRILEYLAVQSRVNKIKGPILCLVGPPGVGKTSLGQSIAKATGRKYVRMALGGVRDEAEIRGHRRTYIG 400

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128424  401 SMPGKLIQKMAKVGVKNPLFLLDEIDKMSSDMRGDPASALLEVLDPEQNVAFSDHYLEVDYDLSDVMFVATSNSMNIPAP 480
Cdd:PRK10787 401 SMPGKLIQKMAKVGVKNPLFLLDEIDKMSSDMRGDPASALLEVLDPEQNVAFSDHYLEVDYDLSDVMFVATSNSMNIPAP 480

                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128424  481 LLDRMEVIRLSGYTEDEKLNIAKRHLLPKQIERNALKKGELTVDDSAIIGIIRYYTREAGVRGLEREISKLCRKAVKQLL 560
Cdd:PRK10787 481 LLDRMEVIRLSGYTEDEKLNIAKRHLLPKQIERNALKKGELTVDDSAIIGIIRYYTREAGVRSLEREISKLCRKAVKQLL 560

                        570       580       590       600       610       620       630       640
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128424  561 LDKSLKHIEINGDNLHDYLGVQRFDYGRADNENRVGQVTGLAWTEVGGDLLTIETACVPGKGKLTYTGSLGEVMQESIQA 640
Cdd:PRK10787 561 LDKSLKHIEINGDNLHDYLGVQRFDYGRADNENRVGQVTGLAWTEVGGDLLTIETACVPGKGKLTYTGSLGEVMQESIQA 640

                        650       660       670       680       690       700       710       720
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128424  641 ALTVVRARAEKLGINPDFYEKRDIHVHVPEGATPKDGPSAGIAMCTALVSCLTGNPVRADVAMTGEITLRGQVLPIGGLK 720
Cdd:PRK10787 641 ALTVVRARAEKLGINPDFYEKRDIHVHVPEGATPKDGPSAGIAMCTALVSCLTGNPVRADVAMTGEITLRGQVLPIGGLK 720

                        730       740       750       760       770       780
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 16128424  721 EKLLAAHRGGIKTVLIPFENKRDLEEIPDNVIADLDIHPVKRIEEVLTLALQNEPSGMQVVTAK 784
Cdd:PRK10787 721 EKLLAAHRGGIKTVLIPFENKRDLEEIPDNVIADLDIHPVKRIEEVLTLALQNEPSGMQVVTAK 784
Lon COG0466
ATP-dependent Lon protease, bacterial type [Posttranslational modification, protein turnover, ...
 2-775 0e+00

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


Pssm-ID: 440234 [Multi-domain]  Cd Length: 785  Bit Score: 1502.60  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128424   2 NPERSERIEIPVLPLRDVVVYPHMVIPLFVGREKSIRCLEAAMDHDKKIMLVAQKEASTDEPGVNDLFTVGTVASILQML 81
Cdd:COG0466   5 KEEEELPETLPLLPLRDVVVFPGMVIPLFVGREKSIKALEEAMEGDKLIGLVAQKDAEVEDPGPDDLYEVGTVAKILQLL 84

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128424  82 KLPDGTVKVLVEGLQRARISALSDNGEHFSAKAEYLESPTIDEREQEVLVRTAISQFEGYIKLNKKIPPEVLTSLNSIDD 161
Cdd:COG0466  85 KLPDGTVKVLVEGLQRARIKEFVQEEPYLEAEVEPLEEEEEDDKELEALMRSLKEQFEEYVKLNPKIPPELLAALSNIED 164

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128424 162 PARLADTIAAHMPLKLADKQSVLEMSDVNERLEYLMAMMESEIDLLQVEKRIRNRVKKQMEKSQREYYLNEQMKAIQKEL 241
Cdd:COG0466 165 PGRLADFIASHLPLKIEEKQELLETLDVKERLEKLLELLEKEIEVLELEKKIRSRVKEQMEKSQREYYLREQLKAIQKEL 244

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128424 242 GEMDDAPDENEALKRKIDAAKMPKEAKEKAEAELQKLKMMSPMSAEATVVRGYIDWMVQVPWNARSKVKKDLRQAQEILD 321
Cdd:COG0466 245 GEKDDGEDEIEELREKIEKAKLPEEVKEKAEKELKKLERMPPMSAEATVIRNYLDWLLDLPWGKRTKDNLDLKKAEKILD 324

                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128424 322 TDHYGLERVKDRILEYLAVQSRVNKIKGPILCLVGPPGVGKTSLGQSIAKATGRKYVRMALGGVRDEAEIRGHRRTYIGS 401
Cdd:COG0466 325 EDHYGLEKVKERILEYLAVRKLKKKLKGPILCLVGPPGVGKTSLGKSIARALGRKFVRISLGGVRDEAEIRGHRRTYIGA 404

                       410       420       430       440       450       460       470       480
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128424 402 MPGKLIQKMAKVGVKNPLFLLDEIDKMSSDMRGDPASALLEVLDPEQNVAFSDHYLEVDYDLSDVMFVATSNSM-NIPAP 480
Cdd:COG0466 405 MPGRIIQGLKKAGTKNPVFLLDEIDKMGSDFRGDPASALLEVLDPEQNNTFSDHYLEVPFDLSKVMFIATANSLdTIPAP 484

                       490       500       510       520       530       540       550       560
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128424 481 LLDRMEVIRLSGYTEDEKLNIAKRHLLPKQIERNALKKGELTVDDSAIIGIIRYYTREAGVRGLEREISKLCRKAVKQLL 560
Cdd:COG0466 485 LLDRMEIIELSGYTEEEKLEIAKRYLIPKQLKEHGLKKEELKISDEALRKIIRGYTREAGVRNLEREIAKICRKVAKKIA 564

                       570       580       590       600       610       620       630       640
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128424 561 LDKSlKHIEINGDNLHDYLGVQRFDYGRADNENRVGQVTGLAWTEVGGDLLTIETACVPGKGKLTYTGSLGEVMQESIQA 640
Cdd:COG0466 565 EGKK-KKVTITPKNLEKYLGVPRFRYEKAEEEDQVGVVTGLAWTEVGGDILFIEATLMPGKGKLTLTGQLGDVMKESAQA 643

                       650       660       670       680       690       700       710       720
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128424 641 ALTVVRARAEKLGINPDFYEKRDIHVHVPEGATPKDGPSAGIAMCTALVSCLTGNPVRADVAMTGEITLRGQVLPIGGLK 720
Cdd:COG0466 644 ALSYVRSRAEELGIDPDFFEKYDIHIHVPEGATPKDGPSAGITMATALVSALTGRPVRSDVAMTGEITLRGRVLPIGGLK 723

                       730       740       750       760       770
                ....*....|....*....|....*....|....*....|....*....|....*
gi 16128424 721 EKLLAAHRGGIKTVLIPFENKRDLEEIPDNVIADLDIHPVKRIEEVLTLALQNEP 775
Cdd:COG0466 724 EKLLAAHRAGIKTVILPKENEKDLEEIPEEVKKGLEFHPVEHIDEVLKIALEKEP 778
lon TIGR00763
endopeptidase La; This protein, the ATP-dependent serine endopeptidase La, is induced by heat ...
 12-771 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: 1190.18  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128424    12 PVLPLRDVVVYPHMVIPLFVGREKSIRCLEAAMDHDKKIM-LVAQKEASTDEPGVNDLFTVGTVASILQMLKLPD---GT 87
Cdd:TIGR00763   1 PLLPLRRRPLFPGMIKPIDVGREKSIKLIKEALRLKQPYLgLFLQKDDDNEEPEEDDIYSVGVVAQILEMLPLPSsgtAT 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128424    88 VKVLVEGLQRARISALSDNGEHFSAKAEYLES--PTIDEREQEVLVRTAISQFEGYIKLNK--KIPPEVLTSLNSIDDPA 163
Cdd:TIGR00763  81 YKVVVEGLRRIRIKELSDKGGYLVVRVDNLKEepFDKDDEEIKALTREIKETFRELISLSKlfREQPALLSALEDIDEPG 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128424   164 RLADTIAAHMPLK-LADKQSVLEMSDVNERLEYLMAMMESEIDLLQVEKRIRNRVKKQMEKSQREYYLNEQMKAIQKELG 242
Cdd:TIGR00763 161 RLADFVAASLQLKeKDELQEVLETVNIEKRLKKALELLKKELELLKLQNKITKKVEEKMEKTQREYYLREQLKAIKKELG 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128424   243 EMDDAPDENEALKRKIDAAKMPKEAKEKAEAELQKLKMMSPMSAEATVVRGYIDWMVQVPWNARSKVKKDLRQAQEILDT 322
Cdd:TIGR00763 241 IEKDDKDELEKLKEKLEELKLPEEVKKVIEKELTKLSLLEPSSSEFTVTRNYLDWLTDLPWGKYSKENLDLKRAKEILDE 320

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128424   323 DHYGLERVKDRILEYLAVQSRVNKIKGPILCLVGPPGVGKTSLGQSIAKATGRKYVRMALGGVRDEAEIRGHRRTYIGSM 402
Cdd:TIGR00763 321 DHYGLKKVKERILEYLAVQKLRGKMKGPILCLVGPPGVGKTSLGKSIAKALNRKFVRFSLGGVRDEAEIRGHRRTYVGAM 400

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128424   403 PGKLIQKMAKVGVKNPLFLLDEIDKMSSDMRGDPASALLEVLDPEQNVAFSDHYLEVDYDLSDVMFVATSNSMN-IPAPL 481
Cdd:TIGR00763 401 PGRIIQGLKKAKTKNPLFLLDEIDKIGSSFRGDPASALLEVLDPEQNNAFSDHYLDVPFDLSKVIFIATANSIDtIPRPL 480

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128424   482 LDRMEVIRLSGYTEDEKLNIAKRHLLPKQIERNALKKGELTVDDSAIIGIIRYYTREAGVRGLEREISKLCRKAVKQLLL 561
Cdd:TIGR00763 481 LDRMEVIELSGYTEEEKLEIAKKYLIPKALEDHGLKPDELKITDEALLLLIKYYTREAGVRNLERQIEKICRKAAVKLVE 560

                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128424   562 DKSLKH-----IEINGDNLHDYLGVQRFDYGRADNENRVGQVTGLAWTEVGGDLLTIETACVPGKGKLTYTGSLGEVMQE 636
Cdd:TIGR00763 561 QGEKKKseaesVVITPDNLKKYLGKPVFTYERAYEVTPPGVVMGLAWTPMGGDTLFIETTKVAGKGSLELTGQLGDVMKE 640

                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128424   637 SIQAALTVVRARAEKLGINPDFYEKRDIHVHVPEGATPKDGPSAGIAMCTALVSCLTGNPVRADVAMTGEITLRGQVLPI 716
Cdd:TIGR00763 641 SAQIALTYVRSIAADLGISPNFFEKADIHLHVPEGATPKDGPSAGITMATALLSLATGKPVRPDVAMTGEITLRGKVLPI 720

                         730       740       750       760       770
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 16128424   717 GGLKEKLLAAHRGGIKTVLIPFENKRDLEEIPDNVIADLDIHPVKRIEEVLTLAL 771
Cdd:TIGR00763 721 GGLKEKTIAAKRAGIKTIILPEKNRRDLEELPENVKEGLEIHFVKHYDEVLKKAF 775
Lon_C pfam05362
Lon protease (S16) C-terminal proteolytic domain; The Lon serine proteases must hydrolyse ATP ...
 570-771 4.09e-125

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: 372.73  E-value: 4.09e-125
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128424   570 INGDNLHDYLGVQRFDYGRADNENRVGQVTGLAWTEVGGDLLTIETACVPGKGKLTYTGSLGEVMQESIQAALTVVRARA 649
Cdd:pfam05362   2 VTAKNLEKYLGVPRFRYGEAEKEDQVGVVTGLAWTEVGGDLLTIEAVIMPGKGKLTLTGQLGDVMKESAQAALSYVRSRA 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128424   650 EKLGINPDFYEKRDIHVHVPEGATPKDGPSAGIAMCTALVSCLTGNPVRADVAMTGEITLRGQVLPIGGLKEKLLAAHRG 729
Cdd:pfam05362  82 EELGIDPDFFEKKDIHIHVPEGATPKDGPSAGVTMATALVSALTGIPVRKDVAMTGEITLRGRVLPIGGLKEKLLAAHRA 161

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 16128424   730 GIKTVLIPFENKRDLEEIPDNVIADLDIHPVKRIEEVLTLAL 771
Cdd:pfam05362 162 GIKTVIIPKENEKDLEDIPENVREGLEIIPVEHVDEVLKHAL 203
RecA-like_Lon cd19500
lon protease homolog 2 peroxisomal; Lon protease (also known as Lon peptidase) is an ...
 313-493 7.08e-124

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: 368.42  E-value: 7.08e-124
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128424 313 LRQAQEILDTDHYGLERVKDRILEYLAVQSRVNKIKGPILCLVGPPGVGKTSLGQSIAKATGRKYVRMALGGVRDEAEIR 392
Cdd:cd19500   1 IKKARKVLDADHYGLEDVKERILEYLAVRKLKGSMKGPILCLVGPPGVGKTSLGKSIARALGRKFVRISLGGVRDEAEIR 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128424 393 GHRRTYIGSMPGKLIQKMAKVGVKNPLFLLDEIDKMSSDMRGDPASALLEVLDPEQNVAFSDHYLEVDYDLSDVMFVATS 472
Cdd:cd19500  81 GHRRTYVGAMPGRIIQALKKAGTNNPVFLLDEIDKIGSSFRGDPASALLEVLDPEQNSTFSDHYLDVPFDLSKVLFIATA 160

                       170       180
                ....*....|....*....|..
gi 16128424 473 NSM-NIPAPLLDRMEVIRLSGY 493
Cdd:cd19500 161 NSLdTIPGPLLDRMEIIELSGY 182
LON smart00464
Found in ATP-dependent protease La (LON); N-terminal domain of the ATP-dependent protease La ...
 10-62 6.33e-09

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: 53.60  E-value: 6.33e-09
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 16128424     10 EIPVLPLRDVVVYPHMVIPLFVGREKSIRCLEAAMDHDKK--IMLVAQKEASTDE 62
Cdd:smart00464   1 TLPLLPIRRRPLFPGFVLPIPVKRPKSVAAIKEALRRSQPyvIVFLLQDDPTETP 55
 
Name Accession Description Interval E-value
PRK10787 PRK10787
DNA-binding ATP-dependent protease La; Provisional
 1-784 0e+00

DNA-binding ATP-dependent protease La; Provisional


Pssm-ID: 182730 [Multi-domain]  Cd Length: 784  Bit Score: 1639.27  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128424    1 MNPERSERIEIPVLPLRDVVVYPHMVIPLFVGREKSIRCLEAAMDHDKKIMLVAQKEASTDEPGVNDLFTVGTVASILQM 80
Cdd:PRK10787   1 MNPERSERIEIPVLPLRDVVVYPHMVIPLFVGREKSIRCLEAAMDHDKKIMLVAQKEASTDEPGVNDLFTVGTVASILQM 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128424   81 LKLPDGTVKVLVEGLQRARISALSDNGEHFSAKAEYLESPTIDEREQEVLVRTAISQFEGYIKLNKKIPPEVLTSLNSID 160
Cdd:PRK10787  81 LKLPDGTVKVLVEGLQRARISALSDNGEHFSAKAEYLESPTIDEREQEVLVRTAISQFEGYIKLNKKIPPEVLTSLNSID 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128424  161 DPARLADTIAAHMPLKLADKQSVLEMSDVNERLEYLMAMMESEIDLLQVEKRIRNRVKKQMEKSQREYYLNEQMKAIQKE 240
Cdd:PRK10787 161 DPARLADTIAAHMPLKLADKQSVLEMSDVNERLEYLMAMMESEIDLLQVEKRIRNRVKKQMEKSQREYYLNEQMKAIQKE 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128424  241 LGEMDDAPDENEALKRKIDAAKMPKEAKEKAEAELQKLKMMSPMSAEATVVRGYIDWMVQVPWNARSKVKKDLRQAQEIL 320
Cdd:PRK10787 241 LGEMDDAPDENEALKRKIDAAKMPKEAKEKAEAELQKLKMMSPMSAEATVVRGYIDWMVQVPWNARSKVKKDLRQAQEIL 320

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128424  321 DTDHYGLERVKDRILEYLAVQSRVNKIKGPILCLVGPPGVGKTSLGQSIAKATGRKYVRMALGGVRDEAEIRGHRRTYIG 400
Cdd:PRK10787 321 DTDHYGLERVKDRILEYLAVQSRVNKIKGPILCLVGPPGVGKTSLGQSIAKATGRKYVRMALGGVRDEAEIRGHRRTYIG 400

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128424  401 SMPGKLIQKMAKVGVKNPLFLLDEIDKMSSDMRGDPASALLEVLDPEQNVAFSDHYLEVDYDLSDVMFVATSNSMNIPAP 480
Cdd:PRK10787 401 SMPGKLIQKMAKVGVKNPLFLLDEIDKMSSDMRGDPASALLEVLDPEQNVAFSDHYLEVDYDLSDVMFVATSNSMNIPAP 480

                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128424  481 LLDRMEVIRLSGYTEDEKLNIAKRHLLPKQIERNALKKGELTVDDSAIIGIIRYYTREAGVRGLEREISKLCRKAVKQLL 560
Cdd:PRK10787 481 LLDRMEVIRLSGYTEDEKLNIAKRHLLPKQIERNALKKGELTVDDSAIIGIIRYYTREAGVRSLEREISKLCRKAVKQLL 560

                        570       580       590       600       610       620       630       640
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128424  561 LDKSLKHIEINGDNLHDYLGVQRFDYGRADNENRVGQVTGLAWTEVGGDLLTIETACVPGKGKLTYTGSLGEVMQESIQA 640
Cdd:PRK10787 561 LDKSLKHIEINGDNLHDYLGVQRFDYGRADNENRVGQVTGLAWTEVGGDLLTIETACVPGKGKLTYTGSLGEVMQESIQA 640

                        650       660       670       680       690       700       710       720
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128424  641 ALTVVRARAEKLGINPDFYEKRDIHVHVPEGATPKDGPSAGIAMCTALVSCLTGNPVRADVAMTGEITLRGQVLPIGGLK 720
Cdd:PRK10787 641 ALTVVRARAEKLGINPDFYEKRDIHVHVPEGATPKDGPSAGIAMCTALVSCLTGNPVRADVAMTGEITLRGQVLPIGGLK 720

                        730       740       750       760       770       780
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 16128424  721 EKLLAAHRGGIKTVLIPFENKRDLEEIPDNVIADLDIHPVKRIEEVLTLALQNEPSGMQVVTAK 784
Cdd:PRK10787 721 EKLLAAHRGGIKTVLIPFENKRDLEEIPDNVIADLDIHPVKRIEEVLTLALQNEPSGMQVVTAK 784
Lon COG0466
ATP-dependent Lon protease, bacterial type [Posttranslational modification, protein turnover, ...
 2-775 0e+00

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


Pssm-ID: 440234 [Multi-domain]  Cd Length: 785  Bit Score: 1502.60  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128424   2 NPERSERIEIPVLPLRDVVVYPHMVIPLFVGREKSIRCLEAAMDHDKKIMLVAQKEASTDEPGVNDLFTVGTVASILQML 81
Cdd:COG0466   5 KEEEELPETLPLLPLRDVVVFPGMVIPLFVGREKSIKALEEAMEGDKLIGLVAQKDAEVEDPGPDDLYEVGTVAKILQLL 84

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128424  82 KLPDGTVKVLVEGLQRARISALSDNGEHFSAKAEYLESPTIDEREQEVLVRTAISQFEGYIKLNKKIPPEVLTSLNSIDD 161
Cdd:COG0466  85 KLPDGTVKVLVEGLQRARIKEFVQEEPYLEAEVEPLEEEEEDDKELEALMRSLKEQFEEYVKLNPKIPPELLAALSNIED 164

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128424 162 PARLADTIAAHMPLKLADKQSVLEMSDVNERLEYLMAMMESEIDLLQVEKRIRNRVKKQMEKSQREYYLNEQMKAIQKEL 241
Cdd:COG0466 165 PGRLADFIASHLPLKIEEKQELLETLDVKERLEKLLELLEKEIEVLELEKKIRSRVKEQMEKSQREYYLREQLKAIQKEL 244

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128424 242 GEMDDAPDENEALKRKIDAAKMPKEAKEKAEAELQKLKMMSPMSAEATVVRGYIDWMVQVPWNARSKVKKDLRQAQEILD 321
Cdd:COG0466 245 GEKDDGEDEIEELREKIEKAKLPEEVKEKAEKELKKLERMPPMSAEATVIRNYLDWLLDLPWGKRTKDNLDLKKAEKILD 324

                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128424 322 TDHYGLERVKDRILEYLAVQSRVNKIKGPILCLVGPPGVGKTSLGQSIAKATGRKYVRMALGGVRDEAEIRGHRRTYIGS 401
Cdd:COG0466 325 EDHYGLEKVKERILEYLAVRKLKKKLKGPILCLVGPPGVGKTSLGKSIARALGRKFVRISLGGVRDEAEIRGHRRTYIGA 404

                       410       420       430       440       450       460       470       480
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128424 402 MPGKLIQKMAKVGVKNPLFLLDEIDKMSSDMRGDPASALLEVLDPEQNVAFSDHYLEVDYDLSDVMFVATSNSM-NIPAP 480
Cdd:COG0466 405 MPGRIIQGLKKAGTKNPVFLLDEIDKMGSDFRGDPASALLEVLDPEQNNTFSDHYLEVPFDLSKVMFIATANSLdTIPAP 484

                       490       500       510       520       530       540       550       560
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128424 481 LLDRMEVIRLSGYTEDEKLNIAKRHLLPKQIERNALKKGELTVDDSAIIGIIRYYTREAGVRGLEREISKLCRKAVKQLL 560
Cdd:COG0466 485 LLDRMEIIELSGYTEEEKLEIAKRYLIPKQLKEHGLKKEELKISDEALRKIIRGYTREAGVRNLEREIAKICRKVAKKIA 564

                       570       580       590       600       610       620       630       640
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128424 561 LDKSlKHIEINGDNLHDYLGVQRFDYGRADNENRVGQVTGLAWTEVGGDLLTIETACVPGKGKLTYTGSLGEVMQESIQA 640
Cdd:COG0466 565 EGKK-KKVTITPKNLEKYLGVPRFRYEKAEEEDQVGVVTGLAWTEVGGDILFIEATLMPGKGKLTLTGQLGDVMKESAQA 643

                       650       660       670       680       690       700       710       720
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128424 641 ALTVVRARAEKLGINPDFYEKRDIHVHVPEGATPKDGPSAGIAMCTALVSCLTGNPVRADVAMTGEITLRGQVLPIGGLK 720
Cdd:COG0466 644 ALSYVRSRAEELGIDPDFFEKYDIHIHVPEGATPKDGPSAGITMATALVSALTGRPVRSDVAMTGEITLRGRVLPIGGLK 723

                       730       740       750       760       770
                ....*....|....*....|....*....|....*....|....*....|....*
gi 16128424 721 EKLLAAHRGGIKTVLIPFENKRDLEEIPDNVIADLDIHPVKRIEEVLTLALQNEP 775
Cdd:COG0466 724 EKLLAAHRAGIKTVILPKENEKDLEEIPEEVKKGLEFHPVEHIDEVLKIALEKEP 778
lon TIGR00763
endopeptidase La; This protein, the ATP-dependent serine endopeptidase La, is induced by heat ...
 12-771 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: 1190.18  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128424    12 PVLPLRDVVVYPHMVIPLFVGREKSIRCLEAAMDHDKKIM-LVAQKEASTDEPGVNDLFTVGTVASILQMLKLPD---GT 87
Cdd:TIGR00763   1 PLLPLRRRPLFPGMIKPIDVGREKSIKLIKEALRLKQPYLgLFLQKDDDNEEPEEDDIYSVGVVAQILEMLPLPSsgtAT 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128424    88 VKVLVEGLQRARISALSDNGEHFSAKAEYLES--PTIDEREQEVLVRTAISQFEGYIKLNK--KIPPEVLTSLNSIDDPA 163
Cdd:TIGR00763  81 YKVVVEGLRRIRIKELSDKGGYLVVRVDNLKEepFDKDDEEIKALTREIKETFRELISLSKlfREQPALLSALEDIDEPG 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128424   164 RLADTIAAHMPLK-LADKQSVLEMSDVNERLEYLMAMMESEIDLLQVEKRIRNRVKKQMEKSQREYYLNEQMKAIQKELG 242
Cdd:TIGR00763 161 RLADFVAASLQLKeKDELQEVLETVNIEKRLKKALELLKKELELLKLQNKITKKVEEKMEKTQREYYLREQLKAIKKELG 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128424   243 EMDDAPDENEALKRKIDAAKMPKEAKEKAEAELQKLKMMSPMSAEATVVRGYIDWMVQVPWNARSKVKKDLRQAQEILDT 322
Cdd:TIGR00763 241 IEKDDKDELEKLKEKLEELKLPEEVKKVIEKELTKLSLLEPSSSEFTVTRNYLDWLTDLPWGKYSKENLDLKRAKEILDE 320

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128424   323 DHYGLERVKDRILEYLAVQSRVNKIKGPILCLVGPPGVGKTSLGQSIAKATGRKYVRMALGGVRDEAEIRGHRRTYIGSM 402
Cdd:TIGR00763 321 DHYGLKKVKERILEYLAVQKLRGKMKGPILCLVGPPGVGKTSLGKSIAKALNRKFVRFSLGGVRDEAEIRGHRRTYVGAM 400

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128424   403 PGKLIQKMAKVGVKNPLFLLDEIDKMSSDMRGDPASALLEVLDPEQNVAFSDHYLEVDYDLSDVMFVATSNSMN-IPAPL 481
Cdd:TIGR00763 401 PGRIIQGLKKAKTKNPLFLLDEIDKIGSSFRGDPASALLEVLDPEQNNAFSDHYLDVPFDLSKVIFIATANSIDtIPRPL 480

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128424   482 LDRMEVIRLSGYTEDEKLNIAKRHLLPKQIERNALKKGELTVDDSAIIGIIRYYTREAGVRGLEREISKLCRKAVKQLLL 561
Cdd:TIGR00763 481 LDRMEVIELSGYTEEEKLEIAKKYLIPKALEDHGLKPDELKITDEALLLLIKYYTREAGVRNLERQIEKICRKAAVKLVE 560

                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128424   562 DKSLKH-----IEINGDNLHDYLGVQRFDYGRADNENRVGQVTGLAWTEVGGDLLTIETACVPGKGKLTYTGSLGEVMQE 636
Cdd:TIGR00763 561 QGEKKKseaesVVITPDNLKKYLGKPVFTYERAYEVTPPGVVMGLAWTPMGGDTLFIETTKVAGKGSLELTGQLGDVMKE 640

                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128424   637 SIQAALTVVRARAEKLGINPDFYEKRDIHVHVPEGATPKDGPSAGIAMCTALVSCLTGNPVRADVAMTGEITLRGQVLPI 716
Cdd:TIGR00763 641 SAQIALTYVRSIAADLGISPNFFEKADIHLHVPEGATPKDGPSAGITMATALLSLATGKPVRPDVAMTGEITLRGKVLPI 720

                         730       740       750       760       770
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 16128424   717 GGLKEKLLAAHRGGIKTVLIPFENKRDLEEIPDNVIADLDIHPVKRIEEVLTLAL 771
Cdd:TIGR00763 721 GGLKEKTIAAKRAGIKTIILPEKNRRDLEELPENVKEGLEIHFVKHYDEVLKKAF 775
Lon_C pfam05362
Lon protease (S16) C-terminal proteolytic domain; The Lon serine proteases must hydrolyse ATP ...
 570-771 4.09e-125

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: 372.73  E-value: 4.09e-125
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128424   570 INGDNLHDYLGVQRFDYGRADNENRVGQVTGLAWTEVGGDLLTIETACVPGKGKLTYTGSLGEVMQESIQAALTVVRARA 649
Cdd:pfam05362   2 VTAKNLEKYLGVPRFRYGEAEKEDQVGVVTGLAWTEVGGDLLTIEAVIMPGKGKLTLTGQLGDVMKESAQAALSYVRSRA 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128424   650 EKLGINPDFYEKRDIHVHVPEGATPKDGPSAGIAMCTALVSCLTGNPVRADVAMTGEITLRGQVLPIGGLKEKLLAAHRG 729
Cdd:pfam05362  82 EELGIDPDFFEKKDIHIHVPEGATPKDGPSAGVTMATALVSALTGIPVRKDVAMTGEITLRGRVLPIGGLKEKLLAAHRA 161

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 16128424   730 GIKTVLIPFENKRDLEEIPDNVIADLDIHPVKRIEEVLTLAL 771
Cdd:pfam05362 162 GIKTVIIPKENEKDLEDIPENVREGLEIIPVEHVDEVLKHAL 203
RecA-like_Lon cd19500
lon protease homolog 2 peroxisomal; Lon protease (also known as Lon peptidase) is an ...
 313-493 7.08e-124

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: 368.42  E-value: 7.08e-124
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128424 313 LRQAQEILDTDHYGLERVKDRILEYLAVQSRVNKIKGPILCLVGPPGVGKTSLGQSIAKATGRKYVRMALGGVRDEAEIR 392
Cdd:cd19500   1 IKKARKVLDADHYGLEDVKERILEYLAVRKLKGSMKGPILCLVGPPGVGKTSLGKSIARALGRKFVRISLGGVRDEAEIR 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128424 393 GHRRTYIGSMPGKLIQKMAKVGVKNPLFLLDEIDKMSSDMRGDPASALLEVLDPEQNVAFSDHYLEVDYDLSDVMFVATS 472
Cdd:cd19500  81 GHRRTYVGAMPGRIIQALKKAGTNNPVFLLDEIDKIGSSFRGDPASALLEVLDPEQNSTFSDHYLDVPFDLSKVLFIATA 160

                       170       180
                ....*....|....*....|..
gi 16128424 473 NSM-NIPAPLLDRMEVIRLSGY 493
Cdd:cd19500 161 NSLdTIPGPLLDRMEIIELSGY 182
LON_substr_bdg pfam02190
ATP-dependent protease La (LON) substrate-binding domain; This domain has been shown to be ...
 10-201 4.06e-55

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: 187.93  E-value: 4.06e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128424    10 EIPVLPLRDVVVYPHMVIPLFVGREKSIRCLEAAMDHDKK--IMLVAQKEASTDEPGVNDLFTVGTVASILQMLKLPDGT 87
Cdd:pfam02190   1 ELPLLPLRNTVLFPGMVLPLFVGRPRSIAAIEAALNKDKLygVLLVSQKDAEDEEPTPDDLYEVGTVAKIVQILKLPDGT 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128424    88 VKVLVEGLQRARISALSDNgEHFSAKAEYLESPTIDEREQEVLVRTAISQFEGYIKLNKKI-PPEVLTSLNSIDDPARLA 166
Cdd:pfam02190  81 YKVLVEGLERVRIVELVKK-EEPYLRAEVEDLPEDSDELSEALKALVKELIEKLRRLLKLLlPLELLLKIKDIENPGRLA 159

                         170       180       190
                  ....*....|....*....|....*....|....*
gi 16128424   167 DTIAAHMPLKLADKQSVLEMSDVNERLEYLMAMME 201
Cdd:pfam02190 160 DLVAAILPLSPEEKQELLETLDVKERLEKVLELLN 194
AAA pfam00004
ATPase family associated with various cellular activities (AAA); AAA family proteins often ...
 352-493 9.38e-25

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: 99.98  E-value: 9.38e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128424   352 LCLVGPPGVGKTSLGQSIAKATGRKYVRMALGGVRDeaeirghrrTYIGSMPGKLIQKMAKVGVKNP-LFLLDEIDKM-- 428
Cdd:pfam00004   1 LLLYGPPGTGKTTLAKAVAKELGAPFIEISGSELVS---------KYVGESEKRLRELFEAAKKLAPcVIFIDEIDALag 71

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 16128424   429 -----SSDMRGDPASALLEVLDPEQNvafsdhylevdyDLSDVMFVATSNSM-NIPAPLLDRMEVIRLSGY 493
Cdd:pfam00004  72 srgsgGDSESRRVVNQLLTELDGFTS------------SNSKVIVIAATNRPdKLDPALLGRFDRIIEFPL 130
LON/PUA COG2802
Uncharacterized conserved protein, LON_N-like domain, ASCH/PUA-like superfamily [Function ...
 10-203 1.70e-24

Uncharacterized conserved protein, LON_N-like domain, ASCH/PUA-like superfamily [Function unknown];


Pssm-ID: 442054 [Multi-domain]  Cd Length: 194  Bit Score: 101.49  E-value: 1.70e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128424  10 EIPVLPLrDVVVYPHMVIPL--FVGREKsiRCLEAAMDHDKKIMlVAQKEASTDEPGVNDLFTVGTVASILQMLKLPDGT 87
Cdd:COG2802   6 ELPLFPL-GAVLFPGGRLPLhiFEPRYL--DMVRDCLAGDRPFG-VVLIREGREVGGPPPLYDVGTLARITDFEELEDGR 81

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128424  88 VKVLVEGLQRARISALSDNGEHF-SAKAEYL-ESPTIDEREQEVLVRTAISQ-FEGYIKLNKkippevLTSLNSIDDPAR 164
Cdd:COG2802  82 LDITLRGVQRFRILEELQEDDPYrVAEVEWLpDEPDLPVPEELEALRERLLRlLRRYPELAG------LEADPDLDDPEW 155

                       170       180       190
                ....*....|....*....|....*....|....*....
gi 16128424 165 LADTIAAHMPLKLADKQSVLEMSDVNERLEYLMAMMESE 203
Cdd:COG2802 156 LSNRLAELLPLDPEEKQALLEAPDLLERLELLLALLERE 194
COG1750 COG1750
Predicted archaeal serine protease, S18 family [General function prediction only];
611-767 2.04e-22

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


Pssm-ID: 441356 [Multi-domain]  Cd Length: 213  Bit Score: 96.20  E-value: 2.04e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128424 611 LTIETACvPGKGKLTYTGS--LGEVMQESIQAALTVVRARAeklGINPDFYekrDIHVHVPEGATPKDGPSAGIAMCTAL 688
Cdd:COG1750  48 ITVTVTY-PGSGRVYVSTSplTGPDTQASARIAALVASLLA---GVDLSSY---DVYISIESDSPIVGGPSAGGAMTVAT 120

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128424 689 VSCLTGNPVRADVAMTGEITLRGQVLPIGGLKEKLLAAHRGGIKTVLIPFENKRDLEE-----IPDNVIA-----DLDIH 758
Cdd:COG1750 121 YAALLGLPLNKSVTMTGMINPDGSIGPVGGVYEKLEAAASAGAKYFLIPKGQAILTGYntqvgETVDLVEygkelGVKVI 200


                ....*....
gi 16128424 759 PVKRIEEVL 767
Cdd:COG1750 201 EVSTIADAL 209
RecA-like_protease cd19481
proteases similar to RecA; RecA-like NTPases. This family includes the NTP binding domain of ...
 330-481 2.53e-12

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: 65.38  E-value: 2.53e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128424 330 VKDRILEYLAVQ------SRVNKIKGPILCLVGPPGVGKTSLGQSIAKATGRKYVRMALGGVRDEAeirghrRTYIGSMP 403
Cdd:cd19481   1 LKASLREAVEAPrrgsrlRRYGLGLPKGILLYGPPGTGKTLLAKALAGELGLPLIVVKLSSLLSKY------VGESEKNL 74

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128424 404 GKLIQKMAKvgVKNPLFLLDEIDKMSSDmRGDPA---------SALLEVLDPEQNvafsdhylevdydLSDVMFVATSN- 473
Cdd:cd19481  75 RKIFERARR--LAPCILFIDEIDAIGRK-RDSSGesgelrrvlNQLLTELDGVNS-------------RSKVLVIAATNr 138


                ....*....
gi 16128424 474 -SMNIPAPL 481
Cdd:cd19481 139 pDLLDPALL 147
AAA cd00009
The AAA+ (ATPases Associated with a wide variety of cellular Activities) superfamily ...
 325-488 6.47e-12

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: 64.09  E-value: 6.47e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128424 325 YGLERVKDRILEYLAVQSRVNkikgpiLCLVGPPGVGKTSLGQSIAKATGRKYVRMA---LGGVRDEAEIRGHRRTYIgs 401
Cdd:cd00009   1 VGQEEAIEALREALELPPPKN------LLLYGPPGTGKTTLARAIANELFRPGAPFLylnASDLLEGLVVAELFGHFL-- 72

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128424 402 mpgKLIQKMAKVGVKNPLFLLDEIDKMSSDMRgdpaSALLEVLdpeqnvafsDHYLEVDYDLSDVMFVATSNSMN---IP 478
Cdd:cd00009  73 ---VRLLFELAEKAKPGVLFIDEIDSLSRGAQ----NALLRVL---------ETLNDLRIDRENVRVIGATNRPLlgdLD 136

                       170
                ....*....|
gi 16128424 479 APLLDRMEVI 488
Cdd:cd00009 137 RALYDRLDIR 146
MoxR COG0714
MoxR-like ATPase [General function prediction only]; MoxR-like ATPase is part of the Pathway ...
 326-505 7.64e-11

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: 63.65  E-value: 7.64e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128424 326 GLERVKDRILeyLAVQSRvnkikGPILcLVGPPGVGKTSLGQSIAKATGRKYVRMalggvrdeaeirghrRTYIGSMPGK 405
Cdd:COG0714  16 GQEELIELVL--IALLAG-----GHLL-LEGVPGVGKTTLAKALARALGLPFIRI---------------QFTPDLLPSD 72

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128424 406 LI-------QKMAKVGVKNPLF----LLDEIDkmssdmRGDPA--SALLEVLDpeqnvafsDHYLEVD---YDLSDVMFV 469
Cdd:COG0714  73 ILgtyiydqQTGEFEFRPGPLFanvlLADEIN------RAPPKtqSALLEAME--------ERQVTIPggtYKLPEPFLV 138

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*
gi 16128424 470 -ATSNSM------NIPAPLLDRMeVIRLS-GY-TEDEKLNIAKRH 505
Cdd:COG0714 139 iATQNPIeqegtyPLPEAQLDRF-LLKLYiGYpDAEEEREILRRH 182
SdrC COG3480
Predicted secreted protein YlbL, contains PDZ domain [Signal transduction mechanisms];
677-777 1.12e-10

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


Pssm-ID: 442703 [Multi-domain]  Cd Length: 344  Bit Score: 64.06  E-value: 1.12e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128424 677 GPSAGIAMCTALVSCLTGNPVR--ADVAMTGEITLRGQVLPIGGLKEKLLAAHRGGIKTVLIPFENKRDLEE-IPDnvia 753
Cdd:COG3480 240 GPSAGLMFALGIYDQLTPGDLTggKKIAGTGTIDADGTVGPIGGIDQKVVAARRAGATIFLAPASNCAEAVGtIPT---- 315

                        90       100
                ....*....|....*....|....
gi 16128424 754 DLDIHPVKRIEEVLTlALQNEPSG 777
Cdd:COG3480 316 GLKVVPVDTLDDALD-ALEALRAG 338
SpoVK COG0464
AAA+-type ATPase, SpoVK/Ycf46/Vps4 family [Cell wall/membrane/envelope biogenesis, Cell cycle ...
 326-515 1.58e-10

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: 63.78  E-value: 1.58e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128424 326 GLERVKDRILEYLAVQSRVNKIKGPI-------LCLVGPPGVGKTSLGQSIAKATGRKYVRMALGGVRDEaeirghrrtY 398
Cdd:COG0464 161 GLEEVKEELRELVALPLKRPELREEYglppprgLLLYGPPGTGKTLLARALAGELGLPLIEVDLSDLVSK---------Y 231

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128424 399 IGSMPGKL--IQKMAKvGVKNPLFLLDEIDKMSSDmRGdpasallEVLDPEQNVAFSdhYL--EVDYDLSDVMFVATSNS 474
Cdd:COG0464 232 VGETEKNLreVFDKAR-GLAPCVLFIDEADALAGK-RG-------EVGDGVGRRVVN--TLltEMEELRSDVVVIAATNR 300

                       170       180       190       200
                ....*....|....*....|....*....|....*....|...
gi 16128424 475 M-NIPAPLLDRM-EVIRLSGYTEDEKLNIAKRHLLPKQIERNA 515
Cdd:COG0464 301 PdLLDPALLRRFdEIIFFPLPDAEERLEIFRIHLRKRPLDEDV 343
LonB COG1067
Predicted ATP-dependent protease [Posttranslational modification, protein turnover, chaperones] ...
 676-769 2.90e-10

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


Pssm-ID: 440686 [Multi-domain]  Cd Length: 742  Bit Score: 63.81  E-value: 2.90e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128424 676 DGPSAGIAMCTALVSCLTGNPVRADVAMTGEITLRGQVLPIGGLKEKL-----LAAHRG--GIKTVLIPFENKRDLeEIP 748
Cdd:COG1067 592 DGDSASSAELYALLSALSGVPIRQDIAVTGSVNQHGEVQPIGGVNEKIegffdVCKARGltGKQGVIIPAANVKNL-MLR 670

                        90       100
                ....*....|....*....|....*.
gi 16128424 749 DNVIADLD-----IHPVKRIEEVLTL 769
Cdd:COG1067 671 DEVVEAVKagqfhIYAVEHVDEAIEL 696
AAA_5 pfam07728
AAA domain (dynein-related subfamily); This Pfam entry includes some of the AAA proteins not ...
 352-485 4.59e-10

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: 58.07  E-value: 4.59e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128424   352 LCLVGPPGVGKTSLGQSIAKAT-GRKYVRMALGgvRD--EAEIRGHRRtyIGSMPGKLIQKMAKVGVKNP-LFLLDEIDK 427
Cdd:pfam07728   2 VLLVGPPGTGKTELAERLAAALsNRPVFYVQLT--RDttEEDLFGRRN--IDPGGASWVDGPLVRAAREGeIAVLDEINR 77

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 16128424   428 MSSDMrgdpASALLEVLDpEQNVAFSDHYLEVDYDLSDVMFVATSNS-----MNIPAPLLDRM 485
Cdd:pfam07728  78 ANPDV----LNSLLSLLD-ERRLLLPDGGELVKAAPDGFRLIATMNPldrglNELSPALRSRF 135
LON smart00464
Found in ATP-dependent protease La (LON); N-terminal domain of the ATP-dependent protease La ...
 10-62 6.33e-09

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: 53.60  E-value: 6.33e-09
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 16128424     10 EIPVLPLRDVVVYPHMVIPLFVGREKSIRCLEAAMDHDKK--IMLVAQKEASTDE 62
Cdd:smart00464   1 TLPLLPIRRRPLFPGFVLPIPVKRPKSVAAIKEALRRSQPyvIVFLLQDDPTETP 55
PRK13342 PRK13342
recombination factor protein RarA; Reviewed
 356-534 9.93e-08

recombination factor protein RarA; Reviewed


Pssm-ID: 237355 [Multi-domain]  Cd Length: 413  Bit Score: 55.09  E-value: 9.93e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128424  356 GPPGVGKTSLGQSIAKATGRKYVRM--ALGGVrdeAEIRghrrtyigsmpgKLIQ--KMAKVGVKNPLFLLDEI---DKM 428
Cdd:PRK13342  43 GPPGTGKTTLARIIAGATDAPFEALsaVTSGV---KDLR------------EVIEeaRQRRSAGRRTILFIDEIhrfNKA 107

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128424  429 SSDmrgdpasALLEVLdpEQNvafsdhylevdydlsDVMFVA--TSN-SMNIPAPLLDRMEVIRLSGYTEDEKLNIAKRH 505
Cdd:PRK13342 108 QQD-------ALLPHV--EDG---------------TITLIGatTENpSFEVNPALLSRAQVFELKPLSEEDIEQLLKRA 163

                        170       180
                 ....*....|....*....|....*....
gi 16128424  506 LlpkqierNALKKGELTVDDSAIIGIIRY 534
Cdd:PRK13342 164 L-------EDKERGLVELDDEALDALARL 185
RarA COG2256
Replication-associated recombination protein RarA (DNA-dependent ATPase) [Replication, ...
 356-534 2.23e-07

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


Pssm-ID: 441857 [Multi-domain]  Cd Length: 439  Bit Score: 53.91  E-value: 2.23e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128424 356 GPPGVGKTSLGQSIAKATGRKYVRM--ALGGVrdeAEIRghrrtyigsmpgKLIQ--KMAKVGVKNPLFLLDEI---DKM 428
Cdd:COG2256  56 GPPGTGKTTLARLIANATDAEFVALsaVTSGV---KDIR------------EVIEeaRERRAYGRRTILFVDEIhrfNKA 120

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128424 429 SSDmrgdpasALLevldpeqnvafsdHYLEvdydlsD--VMFVA--TSN-SMNIPAPLLDRMEVIRLSGYTEDEKLNIAK 503
Cdd:COG2256 121 QQD-------ALL-------------PHVE------DgtITLIGatTENpSFEVNSALLSRCRVFVLKPLSEEDLEQLLE 174

                       170       180       190
                ....*....|....*....|....*....|.
gi 16128424 504 RHLlpKQIERNaLKKGELTVDDSAIIGIIRY 534
Cdd:COG2256 175 RAL--ADDERG-LGGYKLELDDEALEALARL 202
COG1223 COG1223
Predicted ATPase, AAA+ superfamily [General function prediction only];
323-563 1.57e-06

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


Pssm-ID: 440836 [Multi-domain]  Cd Length: 246  Bit Score: 50.27  E-value: 1.57e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128424 323 DHYGLERVKD---RILEYLAVQSRVNKIKGP----ILcLVGPPGVGKTSLGQSIAKATGRKYVRMALGGVRDEaeirghr 395
Cdd:COG1223   3 DVVGQEEAKKklkLIIKELRRRENLRKFGLWpprkIL-FYGPPGTGKTMLAEALAGELKLPLLTVRLDSLIGS------- 74

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128424 396 rtYIG---SMPGKLIQKMAKVGVknpLFLLDEIDKMSSDmRGDPA---------SALLevldpeqnvafsdhyLEVDYDL 463
Cdd:COG1223  75 --YLGetaRNLRKLFDFARRAPC---VIFFDEFDAIAKD-RGDQNdvgevkrvvNALL---------------QELDGLP 133

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128424 464 SDVMFVATSNSMNI--PApLLDRM-EVIRLSGYTEDEKLNIAKRHL--LPKQIERNALKKGELTVDDSAiigiiryytre 538
Cdd:COG1223 134 SGSVVIAATNHPELldSA-LWRRFdEVIEFPLPDKEERKEILELNLkkFPLPFELDLKKLAKKLEGLSG----------- 201

                       250       260
                ....*....|....*....|....*
gi 16128424 539 agvrgleREISKLCRKAVKQLLLDK 563
Cdd:COG1223 202 -------ADIEKVLKTALKKAILED 219
AAA smart00382
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ...
 348-485 8.35e-06

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: 46.21  E-value: 8.35e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128424    348 KGPILCLVGPPGVGKTSLGQSIAKATGRKYVRMALGGVRDEAEIRGHRRTYIGSMPGKL----IQKMAKV-----GVKNP 418
Cdd:smart00382   1 PGEVILIVGPPGSGKTTLARALARELGPPGGGVIYIDGEDILEEVLDQLLLIIVGGKKAsgsgELRLRLAlalarKLKPD 80

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 16128424    419 LFLLDEIDkmssdmrgdpaSALLEVLDPEQNVAFSDHYLEVDYDLSDVMFVATSNSMNIPAPLLDRM 485
Cdd:smart00382  81 VLILDEIT-----------SLLDAEQEALLLLLEELRLLLLLKSEKNLTVILTTNDEKDLGPALLRR 136
ABC_ATPase cd00267
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ...
 348-469 3.79e-05

ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.


Pssm-ID: 213179 [Multi-domain]  Cd Length: 157  Bit Score: 44.54  E-value: 3.79e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128424 348 KGPILCLVGPPGVGKTSLGQSIAKATGRKYVRMALGGVRDEAEIRGHRRTYIGSMPG------KLIQkMAKVGVKNP-LF 420
Cdd:cd00267  24 AGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIAKLPLEELRRRIGYVPQlsggqrQRVA-LARALLLNPdLL 102

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|
gi 16128424 421 LLDEIDK-MSSDMRGDPASALLEVLDPEQNVAFSDHYLEVDYDLSDVMFV 469
Cdd:cd00267 103 LLDEPTSgLDPASRERLLELLRELAEEGRTVIIVTHDPELAELAADRVIV 152
FlhF COG1419
Flagellar biosynthesis GTPase FlhF [Cell motility];
316-371 1.46e-03

Flagellar biosynthesis GTPase FlhF [Cell motility];


Pssm-ID: 441029 [Multi-domain]  Cd Length: 361  Bit Score: 41.77  E-value: 1.46e-03
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 16128424 316 AQEILDT--DHYGLERVKDRILEYLAvqSRVNKIKGPIL------CLVGPPGVGKTSlgqSIAK 371
Cdd:COG1419 125 ARELLEKlpEDLSAEEAWRALLEALA--RRLPVAEDPLLdeggviALVGPTGVGKTT---TIAK 183
aroK PRK00131
shikimate kinase; Reviewed
 347-378 2.25e-03

shikimate kinase; Reviewed


Pssm-ID: 234654 [Multi-domain]  Cd Length: 175  Bit Score: 39.79  E-value: 2.25e-03
                         10        20        30
                 ....*....|....*....|....*....|..
gi 16128424  347 IKGPILCLVGPPGVGKTSLGQSIAKATGRKYV 378
Cdd:PRK00131   2 LKGPNIVLIGFMGAGKSTIGRLLAKRLGYDFI 33
T7SS_EccA TIGR03922
type VII secretion AAA-ATPase EccA; This model represents the AAA family ATPase, EccA, of the ...
 305-504 2.34e-03

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


Pssm-ID: 188437 [Multi-domain]  Cd Length: 557  Bit Score: 41.37  E-value: 2.34e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128424   305 ARSKVKKDLRQAQEILDtDHYGLERVKDRILEY--------------LAVQSRVNKikgpiLCLVGPPGVGKTslgqSIA 370
Cdd:TIGR03922 260 AAERKAKLLAEAEAELA-EQIGLERVKRQVAALksstamalaraergLPVAQTSNH-----MLFAGPPGTGKT----TIA 329

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128424   371 KATGRKYVrmALGGVRDEAEIRGHRRTYIGSMPGKLIQKMAKV--GVKNPLFLLDEIDKMSSDMRGDPasallevlDPEQ 448
Cdd:TIGR03922 330 RVVAKIYC--GLGVLRKPLVREVSRADLIGQYIGESEAKTNEIidSALGGVLFLDEAYTLVETGYGQK--------DPFG 399

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 16128424   449 NVAFSD--HYLEVDYDLSDVMFVATSNSMNipaPLLDRME--------VIRLSGYTEDEKLNIAKR 504
Cdd:TIGR03922 400 LEAIDTllARMENDRDRLVVIGAGYRKDLD---KFLEVNEglrsrftrVIEFPSYSPDELVEIARR 462
AroK COG0703
Shikimate kinase [Amino acid transport and metabolism]; Shikimate kinase is part of the ...
 352-378 2.54e-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: 39.34  E-value: 2.54e-03
                        10        20
                ....*....|....*....|....*..
gi 16128424 352 LCLVGPPGVGKTSLGQSIAKATGRKYV 378
Cdd:COG0703   1 IVLIGMMGAGKSTVGRLLAKRLGLPFV 27
SK cd00464
Shikimate kinase (SK) is the fifth enzyme in the shikimate pathway, a seven-step biosynthetic ...
 354-378 2.62e-03

Shikimate kinase (SK) is the fifth enzyme in the shikimate pathway, a seven-step biosynthetic pathway which converts erythrose-4-phosphate to chorismic acid, found in bacteria, fungi and plants. Chorismic acid is a important intermediate in the synthesis of aromatic compounds, such as aromatic amino acids, p-aminobenzoic acid, folate and ubiquinone. Shikimate kinase catalyses the phosphorylation of the 3-hydroxyl group of shikimic acid using ATP.


Pssm-ID: 238260 [Multi-domain]  Cd Length: 154  Bit Score: 39.08  E-value: 2.62e-03
                        10        20
                ....*....|....*....|....*
gi 16128424 354 LVGPPGVGKTSLGQSIAKATGRKYV 378
Cdd:cd00464   4 LIGMMGAGKTTVGRLLAKALGLPFV 28
RecA-like_ClpB_Hsp104-like cd19499
Chaperone protein ClpB/Hsp104 subfamily; Bacterial Caseinolytic peptidase B (ClpB) and ...
 352-488 7.07e-03

Chaperone protein ClpB/Hsp104 subfamily; Bacterial Caseinolytic peptidase B (ClpB) and eukaryotic Heat shock protein 104 (Hsp104) are ATP-dependent molecular chaperones and essential proteins of the heat-shock response. ClpB/Hsp104 ATPases, in concert with the DnaK/Hsp70 chaperone system, disaggregate and reactivate aggregated proteins. This RecA-like_ClpB_Hsp104_like subfamily belongs to the RecA-like NTPase family which includes the NTP binding domain of F1 and V1 H(+)ATPases, DnaB and related helicases as well as bacterial RecA and related eukaryotic and archaeal recombinases. The RecA-like NTPase family also includes bacterial conjugation proteins and related DNA transfer proteins involved in type II and type IV secretion.


Pssm-ID: 410907 [Multi-domain]  Cd Length: 178  Bit Score: 38.31  E-value: 7.07e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128424 352 LCLVGPPGVGKTSLGQSIAKA---TGRKYVRMALGgvrdeAEIRGHR-RTYIGSMPG--------KLIQKMAkvgvKNP- 418
Cdd:cd19499  44 FLFLGPTGVGKTELAKALAELlfgDEDNLIRIDMS-----EYMEKHSvSRLIGAPPGyvgyteggQLTEAVR----RKPy 114

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 16128424 419 -LFLLDEIDKMSSDMRGdpasALLEVLDpeqNVAFSDHYlEVDYDLSDVMFVATSNsmNIPAPLLDRMEVI 488
Cdd:cd19499 115 sVVLLDEIEKAHPDVQN----LLLQVLD---DGRLTDSH-GRTVDFKNTIIIMTSN--HFRPEFLNRIDEI 175
AAA_PrkA pfam08298
PrkA AAA domain; This is a family of PrkA bacterial and archaeal serine kinases approximately ...
 323-372 8.52e-03

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: 116881  Cd Length: 358  Bit Score: 39.36  E-value: 8.52e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 16128424   323 DHYGLERVKDRILEYLAVQSRVNKIKGPILCLVGPPGVGKTSLGQSIAKA 372
Cdd:pfam08298  59 DFFGMEETIERIVNYFRHAAQGLEERKQILYLLGPVGGGKSSLAERLKKL 108
PRK04195 PRK04195
replication factor C large subunit; Provisional
 346-445 8.79e-03

replication factor C large subunit; Provisional


Pssm-ID: 235250 [Multi-domain]  Cd Length: 482  Bit Score: 39.52  E-value: 8.79e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128424  346 KIKGPILcLVGPPGVGKTSLGQSIAKATGRKYVRMALGGVRDEAEIR---GHRRTY--IGSMPGKLIqkmakvgvknplf 420
Cdd:PRK04195  37 KPKKALL-LYGPPGVGKTSLAHALANDYGWEVIELNASDQRTADVIErvaGEAATSgsLFGARRKLI------------- 102

                         90       100
                 ....*....|....*....|....*..
gi 16128424  421 LLDEIDKMSSdmRGDP--ASALLEVLD 445
Cdd:PRK04195 103 LLDEVDGIHG--NEDRggARAILELIK 127
 
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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