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Conserved domains on  [gi|1434243542|gb|RDC11444|]
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ATP-dependent Clp protease ATP-binding subunit ClpX [Eggerthella lenta]

Protein Classification

ATP-dependent Clp protease ATP-binding subunit ClpX( domain architecture ID 11440654)

ATP-dependent Clp protease ATP-binding subunit ClpX is an ATP-dependent specificity component of the Clp protease that uses cycles of ATP-binding and hydrolysis to unfold proteins and translocate them to the ClpP protease

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
ClpX COG1219
ATP-dependent protease Clp, ATPase subunit ClpX [Posttranslational modification, protein ...
18-453 0e+00

ATP-dependent protease Clp, ATPase subunit ClpX [Posttranslational modification, protein turnover, chaperones];


:

Pssm-ID: 440832 [Multi-domain]  Cd Length: 409  Bit Score: 749.95  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434243542  18 CAFCGKQPHQVAAMISGPnGIYICDECISVCADAMmrdlglsvpghdeaamaegfshAEEGRharvgdgvvtasvaDPAP 97
Cdd:COG1219    11 CSFCGKSQDEVRKLIAGP-GVYICDECVELCNEII----------------------EEELK--------------EEEA 53
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434243542  98 EDVLADLPTPHELYAELSEHVVGQEQAKRALSVAVYNHYKRISLGADAVDgDVELAKSNIMLLGPTGSGKTLLAQTLART 177
Cdd:COG1219    54 EEELKKLPKPKEIKAFLDEYVIGQERAKKVLSVAVYNHYKRLNSGSKDDD-DVELEKSNILLIGPTGSGKTLLAQTLARI 132
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434243542 178 LRVPFAIADATTLTEAGYVGEDVENILLKLMTAADFDIPRAEIGIIYIDEIDKVARKAENLSITRDVSGEGVQQALLKIV 257
Cdd:COG1219   133 LDVPFAIADATTLTEAGYVGEDVENILLKLLQAADYDVEKAERGIIYIDEIDKIARKSENPSITRDVSGEGVQQALLKIL 212
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434243542 258 EGTEASVPPQGGRKHPQQELIHIDTTNILFILGGAFVGLADIIADRVGKKGLGFNAELPESKKHAEAELLARVLPEDLNK 337
Cdd:COG1219   213 EGTVANVPPQGGRKHPQQEFIQIDTTNILFICGGAFDGLEKIIERRLGKKSIGFGAEVKSKKEKDEGELLKQVEPEDLIK 292
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434243542 338 YGMIPEFVGRIPVVTSLNELSEEDLVRILTEPKNALVKQYTKMFEFEDSVLTFEPEALKAIAHEAVEHGTGARGLRSICE 417
Cdd:COG1219   293 FGLIPEFIGRLPVIATLEELDEEALVRILTEPKNALVKQYQKLFEMDGVELEFTDEALEAIAKKAIERKTGARGLRSILE 372
                         410       420       430
                  ....*....|....*....|....*....|....*.
gi 1434243542 418 RVLQDVMYDLPEQKGPSTVTIRATDITGETKPDIEP 453
Cdd:COG1219   373 EILLDVMYELPSRKDVKKVVITKEVVEGKAKPILVY 408
 
Name Accession Description Interval E-value
ClpX COG1219
ATP-dependent protease Clp, ATPase subunit ClpX [Posttranslational modification, protein ...
18-453 0e+00

ATP-dependent protease Clp, ATPase subunit ClpX [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 440832 [Multi-domain]  Cd Length: 409  Bit Score: 749.95  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434243542  18 CAFCGKQPHQVAAMISGPnGIYICDECISVCADAMmrdlglsvpghdeaamaegfshAEEGRharvgdgvvtasvaDPAP 97
Cdd:COG1219    11 CSFCGKSQDEVRKLIAGP-GVYICDECVELCNEII----------------------EEELK--------------EEEA 53
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434243542  98 EDVLADLPTPHELYAELSEHVVGQEQAKRALSVAVYNHYKRISLGADAVDgDVELAKSNIMLLGPTGSGKTLLAQTLART 177
Cdd:COG1219    54 EEELKKLPKPKEIKAFLDEYVIGQERAKKVLSVAVYNHYKRLNSGSKDDD-DVELEKSNILLIGPTGSGKTLLAQTLARI 132
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434243542 178 LRVPFAIADATTLTEAGYVGEDVENILLKLMTAADFDIPRAEIGIIYIDEIDKVARKAENLSITRDVSGEGVQQALLKIV 257
Cdd:COG1219   133 LDVPFAIADATTLTEAGYVGEDVENILLKLLQAADYDVEKAERGIIYIDEIDKIARKSENPSITRDVSGEGVQQALLKIL 212
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434243542 258 EGTEASVPPQGGRKHPQQELIHIDTTNILFILGGAFVGLADIIADRVGKKGLGFNAELPESKKHAEAELLARVLPEDLNK 337
Cdd:COG1219   213 EGTVANVPPQGGRKHPQQEFIQIDTTNILFICGGAFDGLEKIIERRLGKKSIGFGAEVKSKKEKDEGELLKQVEPEDLIK 292
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434243542 338 YGMIPEFVGRIPVVTSLNELSEEDLVRILTEPKNALVKQYTKMFEFEDSVLTFEPEALKAIAHEAVEHGTGARGLRSICE 417
Cdd:COG1219   293 FGLIPEFIGRLPVIATLEELDEEALVRILTEPKNALVKQYQKLFEMDGVELEFTDEALEAIAKKAIERKTGARGLRSILE 372
                         410       420       430
                  ....*....|....*....|....*....|....*.
gi 1434243542 418 RVLQDVMYDLPEQKGPSTVTIRATDITGETKPDIEP 453
Cdd:COG1219   373 EILLDVMYELPSRKDVKKVVITKEVVEGKAKPILVY 408
clpX PRK05342
ATP-dependent Clp protease ATP-binding subunit ClpX;
18-457 0e+00

ATP-dependent Clp protease ATP-binding subunit ClpX;


Pssm-ID: 235422 [Multi-domain]  Cd Length: 412  Bit Score: 700.37  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434243542  18 CAFCGKQPHQVAAMISGPnGIYICDECISVCADAMmrdlglsvpghdeaamaegfshAEEGRHARVGdgvvtasvadpap 97
Cdd:PRK05342   12 CSFCGKSQHEVRKLIAGP-GVYICDECIELCNEII----------------------REELKEEAVE------------- 55
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434243542  98 edvLADLPTPHELYAELSEHVVGQEQAKRALSVAVYNHYKRISLGADAVDgDVELAKSNIMLLGPTGSGKTLLAQTLART 177
Cdd:PRK05342   56 ---LKELPTPKEIKAHLDQYVIGQERAKKVLSVAVYNHYKRLRHGDKKDD-DVELQKSNILLIGPTGSGKTLLAQTLARI 131
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434243542 178 LRVPFAIADATTLTEAGYVGEDVENILLKLMTAADFDIPRAEIGIIYIDEIDKVARKAENLSITRDVSGEGVQQALLKIV 257
Cdd:PRK05342  132 LDVPFAIADATTLTEAGYVGEDVENILLKLLQAADYDVEKAQRGIVYIDEIDKIARKSENPSITRDVSGEGVQQALLKIL 211
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434243542 258 EGTEASVPPQGGRKHPQQELIHIDTTNILFILGGAFVGLADIIADRVGKKGLGFNAEL-PESKKHAEAELLARVLPEDLN 336
Cdd:PRK05342  212 EGTVASVPPQGGRKHPQQEFIQVDTTNILFICGGAFDGLEKIIKQRLGKKGIGFGAEVkSKKEKRTEGELLKQVEPEDLI 291
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434243542 337 KYGMIPEFVGRIPVVTSLNELSEEDLVRILTEPKNALVKQYTKMFEFEDSVLTFEPEALKAIAHEAVEHGTGARGLRSIC 416
Cdd:PRK05342  292 KFGLIPEFIGRLPVVATLEELDEEALVRILTEPKNALVKQYQKLFEMDGVELEFTDEALEAIAKKAIERKTGARGLRSIL 371
                         410       420       430       440
                  ....*....|....*....|....*....|....*....|.
gi 1434243542 417 ERVLQDVMYDLPEQKGPSTVTIRATDITGETKPDIEPTDGA 457
Cdd:PRK05342  372 EEILLDVMFELPSREDVEKVVITKEVVEGKAKPLLIYREKS 412
clpX TIGR00382
endopeptidase Clp ATP-binding regulatory subunit (clpX); A member of the ATP-dependent ...
13-452 0e+00

endopeptidase Clp ATP-binding regulatory subunit (clpX); A member of the ATP-dependent proteases, ClpX has ATP-dependent chaperone activity and is required for specific ATP-dependent proteolytic activities expressed by ClpPX. The gene is also found to be involved in stress tolerance in Bacillus subtilis and is essential for the efficient acquisition of genes specifying type IA and IB restriction. [Protein fate, Protein folding and stabilization, Protein fate, Degradation of proteins, peptides, and glycopeptides]


Pssm-ID: 273047 [Multi-domain]  Cd Length: 413  Bit Score: 557.07  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434243542  13 DADIACAFCGKQPHQVAAMISGPnGIYICDECISVCADAMMRDLGlsvpghdeaamaegfshaeegrharvgdgvVTASV 92
Cdd:TIGR00382   5 NETLYCSFCGKSQDEVRKLIAGP-GVYICDECIELCHDILEEELG------------------------------TRKES 53
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434243542  93 ADPAPEDVLADLPTPHELYAELSEHVVGQEQAKRALSVAVYNHYKRISLGA-DAVDGDVELAKSNIMLLGPTGSGKTLLA 171
Cdd:TIGR00382  54 KEYEEEFELSYLPTPKEIKAHLDEYVIGQEQAKKVLSVAVYNHYKRLNFEKnKKSDNGVELSKSNILLIGPTGSGKTLLA 133
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434243542 172 QTLARTLRVPFAIADATTLTEAGYVGEDVENILLKLMTAADFDIPRAEIGIIYIDEIDKVARKAENLSITRDVSGEGVQQ 251
Cdd:TIGR00382 134 QTLARILNVPFAIADATTLTEAGYVGEDVENILLKLLQAADYDVEKAQKGIIYIDEIDKISRKSENPSITRDVSGEGVQQ 213
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434243542 252 ALLKIVEGTEASVPPQGGRKHPQQELIHIDTTNILFILGGAFVGLADIIADRVGKKGLGFNAELpESKKHAEAELLARVL 331
Cdd:TIGR00382 214 ALLKIIEGTVANVPPQGGRKHPYQEFIQIDTSNILFICGGAFVGLEKIIKKRTGKSSIGFGAEV-KKKSKEKADLLRQVE 292
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434243542 332 PEDLNKYGMIPEFVGRIPVVTSLNELSEEDLVRILTEPKNALVKQYTKMFEFEDSVLTFEPEALKAIAHEAVEHGTGARG 411
Cdd:TIGR00382 293 PEDLVKFGLIPEFIGRLPVIATLEKLDEEALIAILTKPKNALVKQYQALFKMDNVELDFEEEALKAIAKKALERKTGARG 372
                         410       420       430       440
                  ....*....|....*....|....*....|....*....|.
gi 1434243542 412 LRSICERVLQDVMYDLPEQKGPSTVTIRATDITGETKPDIE 452
Cdd:TIGR00382 373 LRSIVEGLLLDVMFDLPSLEDLEKVVITKETVLKQSEPLLI 413
RecA-like_ClpX cd19497
ATP-dependent Clp protease ATP-binding subunit ClpX; ClpX is a component of the ATP-dependent ...
105-354 2.86e-161

ATP-dependent Clp protease ATP-binding subunit ClpX; ClpX is a component of the ATP-dependent protease ClpXP. In ClpXP, ClpX ATPase serves to specifically recognize, unfold, and translocate protein substrates into the chamber of ClpP protease for degradation. This RecA-like_ClpX 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: 410905 [Multi-domain]  Cd Length: 251  Bit Score: 455.91  E-value: 2.86e-161
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434243542 105 PTPHELYAELSEHVVGQEQAKRALSVAVYNHYKRISLGADAVDGDVELAKSNIMLLGPTGSGKTLLAQTLARTLRVPFAI 184
Cdd:cd19497     1 PTPKEIKEHLDKYVIGQERAKKVLSVAVYNHYKRIRNNLKQKDDDVELEKSNILLIGPTGSGKTLLAQTLAKILDVPFAI 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434243542 185 ADATTLTEAGYVGEDVENILLKLMTAADFDIPRAEIGIIYIDEIDKVARKAENLSITRDVSGEGVQQALLKIVEGTEASV 264
Cdd:cd19497    81 ADATTLTEAGYVGEDVENILLKLLQAADYDVERAQRGIVYIDEIDKIARKSENPSITRDVSGEGVQQALLKILEGTVANV 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434243542 265 PPQGGRKHPQQELIHIDTTNILFILGGAFVGLADIIADRVGKKGLGFNAELPESKKHAEA-ELLARVLPEDLNKYGMIPE 343
Cdd:cd19497   161 PPQGGRKHPQQEFIQVDTTNILFICGGAFVGLEKIIARRLGKKSLGFGAETSSEKDEKERdELLSKVEPEDLIKFGLIPE 240
                         250
                  ....*....|.
gi 1434243542 344 FVGRIPVVTSL 354
Cdd:cd19497   241 FVGRLPVIVTL 251
AAA_2 pfam07724
AAA domain (Cdc48 subfamily); This Pfam entry includes some of the AAA proteins not detected ...
154-351 2.27e-37

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: 134.63  E-value: 2.27e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434243542 154 KSNIMLLGPTGSGKTLLAQTLARTLRV---PFAIADATTLTEagyvgedvENILLKLMTAADFDIPRAEIG--------- 221
Cdd:pfam07724   3 IGSFLFLGPTGVGKTELAKALAELLFGderALIRIDMSEYME--------EHSVSRLIGAPPGYVGYEEGGqlteavrrk 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434243542 222 ---IIYIDEIDKVARkaenlsitrdvsgeGVQQALLKIVEGTEASvpPQGGRKhpqqelihIDTTNILFILGGAFVGLAD 298
Cdd:pfam07724  75 pysIVLIDEIEKAHP--------------GVQNDLLQILEGGTLT--DKQGRT--------VDFKNTLFIMTGNFGSEKI 130
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1434243542 299 IIADRVGKKglgfnaelpeskkhaEAELLARVLPEDLNKYGMIPEFVGRIPVV 351
Cdd:pfam07724 131 SDASRLGDS---------------PDYELLKEEVMDLLKKGFIPEFLGRLPII 168
ClpB_D2-small smart01086
C-terminal, D2-small domain, of ClpB protein; This is the C-terminal domain of ClpB protein, ...
357-442 2.05e-19

C-terminal, D2-small domain, of ClpB protein; This is the C-terminal domain of ClpB protein, referred to as the D2-small domain, and is a mixed alpha-beta structure. Compared with the D1-small domain (included in AAA) it lacks the long coiled-coil insertion, and instead of helix C4 contains a beta-strand (e3) that is part of a three stranded beta-pleated sheet. In Thermophilus the whole protein forms a hexamer with the D1-small and D2-small domains located on the outside of the hexamer, with the long coiled-coil being exposed on the surface. The D2-small domain is essential for oligomerisation, forming a tight interface with the D2-large domain of a neighbouring subunit and thereby providing enough binding energy to stabilise the functional assembly. The domain is associated with two Clp_N at the N-terminus as well as AAA and AAA_2.


Pssm-ID: 198154 [Multi-domain]  Cd Length: 90  Bit Score: 82.49  E-value: 2.05e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434243542  357 LSEEDLVRILTEPKNALVKQYtkmfEFEDSVLTFEPEALKAIAHEAVEHGTGARGLRSICERVLQDVMYDLP---EQKGP 433
Cdd:smart01086   1 LDKEDLVRIVDLPLNALQKRL----AEKGITLEFTDEALDWLAEKGYDPKYGARPLRRIIQRELEDPLAELIlsgELKDG 76

                   ....*....
gi 1434243542  434 STVTIRATD 442
Cdd:smart01086  77 DTVVVDVDD 85
 
Name Accession Description Interval E-value
ClpX COG1219
ATP-dependent protease Clp, ATPase subunit ClpX [Posttranslational modification, protein ...
18-453 0e+00

ATP-dependent protease Clp, ATPase subunit ClpX [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 440832 [Multi-domain]  Cd Length: 409  Bit Score: 749.95  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434243542  18 CAFCGKQPHQVAAMISGPnGIYICDECISVCADAMmrdlglsvpghdeaamaegfshAEEGRharvgdgvvtasvaDPAP 97
Cdd:COG1219    11 CSFCGKSQDEVRKLIAGP-GVYICDECVELCNEII----------------------EEELK--------------EEEA 53
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434243542  98 EDVLADLPTPHELYAELSEHVVGQEQAKRALSVAVYNHYKRISLGADAVDgDVELAKSNIMLLGPTGSGKTLLAQTLART 177
Cdd:COG1219    54 EEELKKLPKPKEIKAFLDEYVIGQERAKKVLSVAVYNHYKRLNSGSKDDD-DVELEKSNILLIGPTGSGKTLLAQTLARI 132
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434243542 178 LRVPFAIADATTLTEAGYVGEDVENILLKLMTAADFDIPRAEIGIIYIDEIDKVARKAENLSITRDVSGEGVQQALLKIV 257
Cdd:COG1219   133 LDVPFAIADATTLTEAGYVGEDVENILLKLLQAADYDVEKAERGIIYIDEIDKIARKSENPSITRDVSGEGVQQALLKIL 212
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434243542 258 EGTEASVPPQGGRKHPQQELIHIDTTNILFILGGAFVGLADIIADRVGKKGLGFNAELPESKKHAEAELLARVLPEDLNK 337
Cdd:COG1219   213 EGTVANVPPQGGRKHPQQEFIQIDTTNILFICGGAFDGLEKIIERRLGKKSIGFGAEVKSKKEKDEGELLKQVEPEDLIK 292
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434243542 338 YGMIPEFVGRIPVVTSLNELSEEDLVRILTEPKNALVKQYTKMFEFEDSVLTFEPEALKAIAHEAVEHGTGARGLRSICE 417
Cdd:COG1219   293 FGLIPEFIGRLPVIATLEELDEEALVRILTEPKNALVKQYQKLFEMDGVELEFTDEALEAIAKKAIERKTGARGLRSILE 372
                         410       420       430
                  ....*....|....*....|....*....|....*.
gi 1434243542 418 RVLQDVMYDLPEQKGPSTVTIRATDITGETKPDIEP 453
Cdd:COG1219   373 EILLDVMYELPSRKDVKKVVITKEVVEGKAKPILVY 408
clpX PRK05342
ATP-dependent Clp protease ATP-binding subunit ClpX;
18-457 0e+00

ATP-dependent Clp protease ATP-binding subunit ClpX;


Pssm-ID: 235422 [Multi-domain]  Cd Length: 412  Bit Score: 700.37  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434243542  18 CAFCGKQPHQVAAMISGPnGIYICDECISVCADAMmrdlglsvpghdeaamaegfshAEEGRHARVGdgvvtasvadpap 97
Cdd:PRK05342   12 CSFCGKSQHEVRKLIAGP-GVYICDECIELCNEII----------------------REELKEEAVE------------- 55
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434243542  98 edvLADLPTPHELYAELSEHVVGQEQAKRALSVAVYNHYKRISLGADAVDgDVELAKSNIMLLGPTGSGKTLLAQTLART 177
Cdd:PRK05342   56 ---LKELPTPKEIKAHLDQYVIGQERAKKVLSVAVYNHYKRLRHGDKKDD-DVELQKSNILLIGPTGSGKTLLAQTLARI 131
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434243542 178 LRVPFAIADATTLTEAGYVGEDVENILLKLMTAADFDIPRAEIGIIYIDEIDKVARKAENLSITRDVSGEGVQQALLKIV 257
Cdd:PRK05342  132 LDVPFAIADATTLTEAGYVGEDVENILLKLLQAADYDVEKAQRGIVYIDEIDKIARKSENPSITRDVSGEGVQQALLKIL 211
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434243542 258 EGTEASVPPQGGRKHPQQELIHIDTTNILFILGGAFVGLADIIADRVGKKGLGFNAEL-PESKKHAEAELLARVLPEDLN 336
Cdd:PRK05342  212 EGTVASVPPQGGRKHPQQEFIQVDTTNILFICGGAFDGLEKIIKQRLGKKGIGFGAEVkSKKEKRTEGELLKQVEPEDLI 291
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434243542 337 KYGMIPEFVGRIPVVTSLNELSEEDLVRILTEPKNALVKQYTKMFEFEDSVLTFEPEALKAIAHEAVEHGTGARGLRSIC 416
Cdd:PRK05342  292 KFGLIPEFIGRLPVVATLEELDEEALVRILTEPKNALVKQYQKLFEMDGVELEFTDEALEAIAKKAIERKTGARGLRSIL 371
                         410       420       430       440
                  ....*....|....*....|....*....|....*....|.
gi 1434243542 417 ERVLQDVMYDLPEQKGPSTVTIRATDITGETKPDIEPTDGA 457
Cdd:PRK05342  372 EEILLDVMFELPSREDVEKVVITKEVVEGKAKPLLIYREKS 412
clpX TIGR00382
endopeptidase Clp ATP-binding regulatory subunit (clpX); A member of the ATP-dependent ...
13-452 0e+00

endopeptidase Clp ATP-binding regulatory subunit (clpX); A member of the ATP-dependent proteases, ClpX has ATP-dependent chaperone activity and is required for specific ATP-dependent proteolytic activities expressed by ClpPX. The gene is also found to be involved in stress tolerance in Bacillus subtilis and is essential for the efficient acquisition of genes specifying type IA and IB restriction. [Protein fate, Protein folding and stabilization, Protein fate, Degradation of proteins, peptides, and glycopeptides]


Pssm-ID: 273047 [Multi-domain]  Cd Length: 413  Bit Score: 557.07  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434243542  13 DADIACAFCGKQPHQVAAMISGPnGIYICDECISVCADAMMRDLGlsvpghdeaamaegfshaeegrharvgdgvVTASV 92
Cdd:TIGR00382   5 NETLYCSFCGKSQDEVRKLIAGP-GVYICDECIELCHDILEEELG------------------------------TRKES 53
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434243542  93 ADPAPEDVLADLPTPHELYAELSEHVVGQEQAKRALSVAVYNHYKRISLGA-DAVDGDVELAKSNIMLLGPTGSGKTLLA 171
Cdd:TIGR00382  54 KEYEEEFELSYLPTPKEIKAHLDEYVIGQEQAKKVLSVAVYNHYKRLNFEKnKKSDNGVELSKSNILLIGPTGSGKTLLA 133
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434243542 172 QTLARTLRVPFAIADATTLTEAGYVGEDVENILLKLMTAADFDIPRAEIGIIYIDEIDKVARKAENLSITRDVSGEGVQQ 251
Cdd:TIGR00382 134 QTLARILNVPFAIADATTLTEAGYVGEDVENILLKLLQAADYDVEKAQKGIIYIDEIDKISRKSENPSITRDVSGEGVQQ 213
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434243542 252 ALLKIVEGTEASVPPQGGRKHPQQELIHIDTTNILFILGGAFVGLADIIADRVGKKGLGFNAELpESKKHAEAELLARVL 331
Cdd:TIGR00382 214 ALLKIIEGTVANVPPQGGRKHPYQEFIQIDTSNILFICGGAFVGLEKIIKKRTGKSSIGFGAEV-KKKSKEKADLLRQVE 292
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434243542 332 PEDLNKYGMIPEFVGRIPVVTSLNELSEEDLVRILTEPKNALVKQYTKMFEFEDSVLTFEPEALKAIAHEAVEHGTGARG 411
Cdd:TIGR00382 293 PEDLVKFGLIPEFIGRLPVIATLEKLDEEALIAILTKPKNALVKQYQALFKMDNVELDFEEEALKAIAKKALERKTGARG 372
                         410       420       430       440
                  ....*....|....*....|....*....|....*....|.
gi 1434243542 412 LRSICERVLQDVMYDLPEQKGPSTVTIRATDITGETKPDIE 452
Cdd:TIGR00382 373 LRSIVEGLLLDVMFDLPSLEDLEKVVITKETVLKQSEPLLI 413
RecA-like_ClpX cd19497
ATP-dependent Clp protease ATP-binding subunit ClpX; ClpX is a component of the ATP-dependent ...
105-354 2.86e-161

ATP-dependent Clp protease ATP-binding subunit ClpX; ClpX is a component of the ATP-dependent protease ClpXP. In ClpXP, ClpX ATPase serves to specifically recognize, unfold, and translocate protein substrates into the chamber of ClpP protease for degradation. This RecA-like_ClpX 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: 410905 [Multi-domain]  Cd Length: 251  Bit Score: 455.91  E-value: 2.86e-161
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434243542 105 PTPHELYAELSEHVVGQEQAKRALSVAVYNHYKRISLGADAVDGDVELAKSNIMLLGPTGSGKTLLAQTLARTLRVPFAI 184
Cdd:cd19497     1 PTPKEIKEHLDKYVIGQERAKKVLSVAVYNHYKRIRNNLKQKDDDVELEKSNILLIGPTGSGKTLLAQTLAKILDVPFAI 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434243542 185 ADATTLTEAGYVGEDVENILLKLMTAADFDIPRAEIGIIYIDEIDKVARKAENLSITRDVSGEGVQQALLKIVEGTEASV 264
Cdd:cd19497    81 ADATTLTEAGYVGEDVENILLKLLQAADYDVERAQRGIVYIDEIDKIARKSENPSITRDVSGEGVQQALLKILEGTVANV 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434243542 265 PPQGGRKHPQQELIHIDTTNILFILGGAFVGLADIIADRVGKKGLGFNAELPESKKHAEA-ELLARVLPEDLNKYGMIPE 343
Cdd:cd19497   161 PPQGGRKHPQQEFIQVDTTNILFICGGAFVGLEKIIARRLGKKSLGFGAETSSEKDEKERdELLSKVEPEDLIKFGLIPE 240
                         250
                  ....*....|.
gi 1434243542 344 FVGRIPVVTSL 354
Cdd:cd19497   241 FVGRLPVIVTL 251
hslU PRK05201
ATP-dependent protease ATPase subunit HslU;
106-438 1.07e-53

ATP-dependent protease ATPase subunit HslU;


Pssm-ID: 235364 [Multi-domain]  Cd Length: 443  Bit Score: 186.05  E-value: 1.07e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434243542 106 TPHELYAELSEHVVGQEQAKRALSVAVYNHYKRISLGADAVDgdvELAKSNIMLLGPTGSGKTLLAQTLARTLRVPFAIA 185
Cdd:PRK05201    5 TPREIVSELDKYIIGQDDAKRAVAIALRNRWRRMQLPEELRD---EVTPKNILMIGPTGVGKTEIARRLAKLANAPFIKV 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434243542 186 DATTLTEAGYVGEDVENILLKLMTAA------------------------------------------------------ 211
Cdd:PRK05201   82 EATKFTEVGYVGRDVESIIRDLVEIAvkmvreekrekvrekaeeaaeerildallppaknnwgeeeekeeisatrqkfrk 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434243542 212 --------D----------------FDIP--------------------------------------------------- 216
Cdd:PRK05201  162 klregeldDkeieievaeaapmmeiMGPPgmeemtiqlqdmfgnlgpkkkkkrklkvkearkilieeeaaklidmeeikq 241
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434243542 217 ----RAE-IGIIYIDEIDKVARKAENLSitRDVSGEGVQQALLKIVEGTEASVppqggrKHPQqelihIDTTNILFILGG 291
Cdd:PRK05201  242 eaieRVEqNGIVFIDEIDKIAARGGSSG--PDVSREGVQRDLLPLVEGSTVST------KYGM-----VKTDHILFIASG 308
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434243542 292 AFvgladiiadrvgkkglgfnaelpeskkHaeaelLARvlPEDLnkygmIPEFVGRIPVVTSLNELSEEDLVRILTEPKN 371
Cdd:PRK05201  309 AF---------------------------H-----VSK--PSDL-----IPELQGRFPIRVELDALTEEDFVRILTEPKA 349
                         410       420       430       440       450       460       470
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1434243542 372 ALVKQYTKMFEFEDSVLTFEPEALKAIAHEAVE--HGT---GARGLRSICERVLQDVMYDLPEQKGpSTVTI 438
Cdd:PRK05201  350 SLIKQYQALLATEGVTLEFTDDAIRRIAEIAYQvnEKTeniGARRLHTVMEKLLEDISFEAPDMSG-ETVTI 420
HslU COG1220
ATP-dependent protease HslVU (ClpYQ), ATPase subunit HslU [Posttranslational modification, ...
106-438 2.36e-49

ATP-dependent protease HslVU (ClpYQ), ATPase subunit HslU [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 440833 [Multi-domain]  Cd Length: 454  Bit Score: 174.85  E-value: 2.36e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434243542 106 TPHELYAELSEHVVGQEQAKRALSVAVYNHYKRISLGADAVDgdvELAKSNIMLLGPTGSGKTLLAQTLARTLRVPFAIA 185
Cdd:COG1220     5 TPREIVAELDKYIIGQDEAKRAVAIALRNRWRRQQLPEELRD---EITPKNILMIGPTGVGKTEIARRLAKLANAPFIKV 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434243542 186 DATTLTEAGYVGEDVENI-------------------------------LLKL--------------------------- 207
Cdd:COG1220    82 EATKFTEVGYVGRDVESMirdlveiavkmvreekmekvrekaeeaaeerILDLllpppkkkagsnnpfeeeeeeeeeeee 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434243542 208 --------------------------------------------MT---------------------------------A 210
Cdd:COG1220   162 isrtrekfrkklregelddreieieveessspgveimgppgmeeMGmnlqdmfgnlmpkkkkkrkvkvkearkiltqeeA 241
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434243542 211 A---DFD------IPRAE-IGIIYIDEIDKVARKAENLSItrDVSGEGVQQALLKIVEGTEASVppqggrKHPQqelihI 280
Cdd:COG1220   242 AkliDMDevkqeaIERAEqNGIIFIDEIDKIASRGGGSGP--DVSREGVQRDLLPIVEGSTVNT------KYGM-----V 308
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434243542 281 DTTNILFILGGAFvgladiiadrvgkkglgfnaelpeskkHaeaelLARvlPEDLnkygmIPEFVGRIPVVTSLNELSEE 360
Cdd:COG1220   309 KTDHILFIAAGAF---------------------------H-----VSK--PSDL-----IPELQGRFPIRVELDSLTEE 349
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434243542 361 DLVRILTEPKNALVKQYTKMFEFEDSVLTFEPEALKAIAHEAVE--HGT---GARGLRSICERVLQDVMYDLPEQKGpST 435
Cdd:COG1220   350 DFVRILTEPKNALTKQYQALLATEGVELEFTDDAIREIAEIAFEvnERTeniGARRLHTVMEKLLEDISFEAPDLSG-KT 428

                  ...
gi 1434243542 436 VTI 438
Cdd:COG1220   429 VVI 431
hslU TIGR00390
ATP-dependent protease HslVU, ATPase subunit; This model represents the ATPase subunit of ...
106-440 3.74e-46

ATP-dependent protease HslVU, ATPase subunit; This model represents the ATPase subunit of HslVU, while the proteasome-related peptidase subunit is HslV. Residues 54-61 of the model contain a P-loop ATP-binding motif. Cys-287 of E. coli (position 308 in the seed alignment) is Ser in other members of the seed alignment. [Protein fate, Protein folding and stabilization]


Pssm-ID: 273052 [Multi-domain]  Cd Length: 441  Bit Score: 166.14  E-value: 3.74e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434243542 106 TPHELYAELSEHVVGQEQAKRALSVAVYNHYKRISLGADAVDgdvELAKSNIMLLGPTGSGKTLLAQTLARTLRVPFAIA 185
Cdd:TIGR00390   2 TPREIVAELDKYIIGQDNAKKSVAIALRNRYRRSQLNEELKD---EVTPKNILMIGPTGVGKTEIARRLAKLANAPFIKV 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434243542 186 DATTLTEAGYVGEDVENILLKLMTAA------------------------------------------------------ 211
Cdd:TIGR00390  79 EATKFTEVGYVGRDVESMVRDLTDAAvklvkeeaiekvrdraeelaeerivdvllppaknqwgqteqqqepesareafrk 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434243542     --------------------------------------------------------------------------------
Cdd:TIGR00390 159 klregelddkeieidvsakmpsgieimappgmeemtmqlqslfqnlggqkkkkrklkikdakkaliaeeaaklvdpeeik 238
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434243542 212 DFDIPRAE-IGIIYIDEIDKVARKAEnlSITRDVSGEGVQQALLKIVEGTEASVppqggrKHPQqelihIDTTNILFILG 290
Cdd:TIGR00390 239 QEAIDAVEqSGIIFIDEIDKIAKKGE--SSGADVSREGVQRDLLPIVEGSTVNT------KYGM-----VKTDHILFIAA 305
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434243542 291 GAFvgladiiadrvgkkglgfnaelpeskkhaeaeLLARvlPEDLnkygmIPEFVGRIPVVTSLNELSEEDLVRILTEPK 370
Cdd:TIGR00390 306 GAF--------------------------------QLAK--PSDL-----IPELQGRFPIRVELQALTTDDFERILTEPK 346
                         410       420       430       440       450       460       470
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1434243542 371 NALVKQYTKMFEFEDSVLTFEPEALKAIAHEAVE-----HGTGARGLRSICERVLQDVMYDLPEQKGpSTVTIRA 440
Cdd:TIGR00390 347 NSLIKQYKALMKTEGVNIEFSDEAIKRIAELAYNvnektENIGARRLHTVLERLLEDISFEAPDLSG-QNITIDA 420
RecA-like_HslU cd19498
ATP-dependent protease ATPase subunit HslU; HslU is a component of the ATP-dependent protease ...
106-293 7.69e-43

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: 149.84  E-value: 7.69e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434243542 106 TPHELYAELSEHVVGQEQAKRALSVAVYNHYKRISLGADAVDgdvELAKSNIMLLGPTGSGKTLLAQTLARTLRVPFAIA 185
Cdd:cd19498     1 TPREIVSELDKYIIGQDEAKRAVAIALRNRWRRMQLPEELRD---EVTPKNILMIGPTGVGKTEIARRLAKLAGAPFIKV 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434243542 186 DATTLTEAGYVGEDVENILLKLMTaadfdipraeiGIIYIDEIDKVARKAEnlSITRDVSGEGVQQALLKIVEGTEASVp 265
Cdd:cd19498    78 EATKFTEVGYVGRDVESIIRDLVE-----------GIVFIDEIDKIAKRGG--SSGPDVSREGVQRDLLPIVEGSTVST- 143
                         170       180
                  ....*....|....*....|....*...
gi 1434243542 266 pqggrKHPQqelihIDTTNILFILGGAF 293
Cdd:cd19498   144 -----KYGP-----VKTDHILFIAAGAF 161
AAA_2 pfam07724
AAA domain (Cdc48 subfamily); This Pfam entry includes some of the AAA proteins not detected ...
154-351 2.27e-37

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: 134.63  E-value: 2.27e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434243542 154 KSNIMLLGPTGSGKTLLAQTLARTLRV---PFAIADATTLTEagyvgedvENILLKLMTAADFDIPRAEIG--------- 221
Cdd:pfam07724   3 IGSFLFLGPTGVGKTELAKALAELLFGderALIRIDMSEYME--------EHSVSRLIGAPPGYVGYEEGGqlteavrrk 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434243542 222 ---IIYIDEIDKVARkaenlsitrdvsgeGVQQALLKIVEGTEASvpPQGGRKhpqqelihIDTTNILFILGGAFVGLAD 298
Cdd:pfam07724  75 pysIVLIDEIEKAHP--------------GVQNDLLQILEGGTLT--DKQGRT--------VDFKNTLFIMTGNFGSEKI 130
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1434243542 299 IIADRVGKKglgfnaelpeskkhaEAELLARVLPEDLNKYGMIPEFVGRIPVV 351
Cdd:pfam07724 131 SDASRLGDS---------------PDYELLKEEVMDLLKKGFIPEFLGRLPII 168
ClpB_D2-small smart01086
C-terminal, D2-small domain, of ClpB protein; This is the C-terminal domain of ClpB protein, ...
357-442 2.05e-19

C-terminal, D2-small domain, of ClpB protein; This is the C-terminal domain of ClpB protein, referred to as the D2-small domain, and is a mixed alpha-beta structure. Compared with the D1-small domain (included in AAA) it lacks the long coiled-coil insertion, and instead of helix C4 contains a beta-strand (e3) that is part of a three stranded beta-pleated sheet. In Thermophilus the whole protein forms a hexamer with the D1-small and D2-small domains located on the outside of the hexamer, with the long coiled-coil being exposed on the surface. The D2-small domain is essential for oligomerisation, forming a tight interface with the D2-large domain of a neighbouring subunit and thereby providing enough binding energy to stabilise the functional assembly. The domain is associated with two Clp_N at the N-terminus as well as AAA and AAA_2.


Pssm-ID: 198154 [Multi-domain]  Cd Length: 90  Bit Score: 82.49  E-value: 2.05e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434243542  357 LSEEDLVRILTEPKNALVKQYtkmfEFEDSVLTFEPEALKAIAHEAVEHGTGARGLRSICERVLQDVMYDLP---EQKGP 433
Cdd:smart01086   1 LDKEDLVRIVDLPLNALQKRL----AEKGITLEFTDEALDWLAEKGYDPKYGARPLRRIIQRELEDPLAELIlsgELKDG 76

                   ....*....
gi 1434243542  434 STVTIRATD 442
Cdd:smart01086  77 DTVVVDVDD 85
RecA-like_protease cd19481
proteases similar to RecA; RecA-like NTPases. This family includes the NTP binding domain of ...
124-262 4.21e-16

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


Pssm-ID: 410889 [Multi-domain]  Cd Length: 158  Bit Score: 75.40  E-value: 4.21e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434243542 124 AKRALSVAVYNHYKRislgaDAVDGDVELAKSNIMLLGPTGSGKTLLAQTLARTLRVPFAIADATTLTEAgYVGEDVENi 203
Cdd:cd19481     1 LKASLREAVEAPRRG-----SRLRRYGLGLPKGILLYGPPGTGKTLLAKALAGELGLPLIVVKLSSLLSK-YVGESEKN- 73
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1434243542 204 LLKLMTAADfdipRAEIGIIYIDEIDKVARKAENLSITRDVSgeGVQQALLKIVEGTEA 262
Cdd:cd19481    74 LRKIFERAR----RLAPCILFIDEIDAIGRKRDSSGESGELR--RVLNQLLTELDGVNS 126
AAA cd00009
The AAA+ (ATPases Associated with a wide variety of cellular Activities) superfamily ...
119-237 4.75e-14

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: 69.48  E-value: 4.75e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434243542 119 VGQEQAKRALSVAVYNHYKRislgadavdgdvelaksNIMLLGPTGSGKTLLAQTLARTL---RVPFAIADATTLTEAGY 195
Cdd:cd00009     1 VGQEEAIEALREALELPPPK-----------------NLLLYGPPGTGKTTLARAIANELfrpGAPFLYLNASDLLEGLV 63
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 1434243542 196 VGEDVENILLKLMTAAdfdIPRAEIGIIYIDEIDKVARKAEN 237
Cdd:cd00009    64 VAELFGHFLVRLLFEL---AEKAKPGVLFIDEIDSLSRGAQN 102
zf-C4_ClpX pfam06689
ClpX C4-type zinc finger; The ClpX heat shock protein of Escherichia coli is a member of the ...
16-50 1.58e-13

ClpX C4-type zinc finger; The ClpX heat shock protein of Escherichia coli is a member of the universally conserved Hsp100 family of proteins, and possesses a putative zinc finger motif of the C4 type. This presumed zinc binding domain is found at the N-terminus of the ClpX protein. ClpX is an ATPase which functions both as a substrate specificity component of the ClpXP protease and as a molecular chaperone. The molecular function of this domain is now known.


Pssm-ID: 461988 [Multi-domain]  Cd Length: 39  Bit Score: 64.48  E-value: 1.58e-13
                          10        20        30
                  ....*....|....*....|....*....|....*
gi 1434243542  16 IACAFCGKQPHQVAAMISGPNGIYICDECISVCAD 50
Cdd:pfam06689   1 LRCSFCGKSEDEVKKLIAGPNGVYICDECVELCYE 35
AAA pfam00004
ATPase family associated with various cellular activities (AAA); AAA family proteins often ...
157-300 1.19e-12

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: 64.92  E-value: 1.19e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434243542 157 IMLLGPTGSGKTLLAQTLARTLRVPFAIADATTLTEaGYVGEDVENIlLKLMTAADFDIPraeiGIIYIDEIDKVARKAE 236
Cdd:pfam00004   1 LLLYGPPGTGKTTLAKAVAKELGAPFIEISGSELVS-KYVGESEKRL-RELFEAAKKLAP----CVIFIDEIDALAGSRG 74
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1434243542 237 NlsiTRDVSGEGVQQALLKIVEGTEASVPPqggrkhpqqeLIHIDTTNILFILGGAFVGLADII 300
Cdd:pfam00004  75 S---GGDSESRRVVNQLLTELDGFTSSNSK----------VIVIAATNRPDKLDPALLGRFDRI 125
SpoVK COG0464
AAA+-type ATPase, SpoVK/Ycf46/Vps4 family [Cell wall/membrane/envelope biogenesis, Cell cycle ...
51-264 1.35e-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: 63.01  E-value: 1.35e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434243542  51 AMMRDLGLSVPGHDEAAMAEGFSHAEEGRHARVGDGVVTASVADPAPEDVLADLPTPHELYAELSEHVVGQEQAKRALSV 130
Cdd:COG0464    92 LLLGELLLLLLLLLLLLLLLLDLERALLELLRESAEALALAAPLVTYEDIGGLEEELLELREAILDDLGGLEEVKEELRE 171
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434243542 131 AV----YNHYKRISLGADAVDGdvelaksnIMLLGPTGSGKTLLAQTLARTLRVPFAIADATTLTeAGYVGEDVENILLK 206
Cdd:COG0464   172 LValplKRPELREEYGLPPPRG--------LLLYGPPGTGKTLLARALAGELGLPLIEVDLSDLV-SKYVGETEKNLREV 242
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1434243542 207 LMTAAdfdipRAEIGIIYIDEIDKVARKAENlsiTRDVSGEGVQQALLKIVEGTEASV 264
Cdd:COG0464   243 FDKAR-----GLAPCVLFIDEADALAGKRGE---VGDGVGRRVVNTLLTEMEELRSDV 292
ClpB_D2-small pfam10431
C-terminal, D2-small domain, of ClpB protein; This is the C-terminal domain of ClpB protein, ...
357-438 4.85e-10

C-terminal, D2-small domain, of ClpB protein; This is the C-terminal domain of ClpB protein, referred to as the D2-small domain, and is a mixed alpha-beta structure. Compared with the D1-small domain (included in AAA, pfam00004) it lacks the long coiled-coil insertion, and instead of helix C4 contains a beta-strand (e3) that is part of a three stranded beta-pleated sheet. In Thermophilus the whole protein forms a hexamer with the D1-small and D2-small domains located on the outside of the hexamer, with the long coiled-coil being exposed on the surface. The D2-small domain is essential for oligomerization, forming a tight interface with the D2-large domain of a neighbouring subunit and thereby providing enough binding energy to stabilize the functional assembly. The domain is associated with two Clp_N, pfam02861, at the N-terminus as well as AAA, pfam00004 and AAA_2, pfam07724.


Pssm-ID: 463090 [Multi-domain]  Cd Length: 81  Bit Score: 55.87  E-value: 4.85e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434243542 357 LSEEDLVRILTEpknALVKQYTKMFEfEDSVLTFEPEALKAIAHEAVEHGTGARGLRSICERVLQDVMYDLP---EQKGP 433
Cdd:pfam10431   1 LSKEELRKIVDL---QLKELQKRLAE-RGITLELTDAAKDWLAEKGYDPEYGARPLRRAIQREIEDPLAEEIlsgELKEG 76

                  ....*
gi 1434243542 434 STVTI 438
Cdd:pfam10431  77 DTVRV 81
zf-C4_ClpX smart00994
ClpX C4-type zinc finger; The ClpX heat shock protein of Escherichia coli is a member of the ...
18-50 1.36e-09

ClpX C4-type zinc finger; The ClpX heat shock protein of Escherichia coli is a member of the universally conserved Hsp100 family of proteins, and possesses a putative zinc finger motif of the C4 type. This presumed zinc binding domain is found at the N-terminus of the ClpX protein. ClpX is an ATPase which functions both as a substrate specificity component of the ClpXP protease and as a molecular chaperone. The molecular function of this domain is now known.


Pssm-ID: 198062 [Multi-domain]  Cd Length: 39  Bit Score: 53.34  E-value: 1.36e-09
                           10        20        30
                   ....*....|....*....|....*....|...
gi 1434243542   18 CAFCGKQPHQVAAMISGPNGiYICDECISVCAD 50
Cdd:smart00994   3 CSFCGKSESEVRKLIAGPGV-YICDECVELCYE 34
RecA-like_VPS4-like cd19509
ATPase domain of VPS4, ATAD1, K, KTNA1, Spastin, FIGL-1 and similar ATPase domains; This ...
118-229 4.80e-09

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: 55.44  E-value: 4.80e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434243542 118 VVGQEQAKRALSVAVYNHYKRislgADAVDGDVELAKSnIMLLGPTGSGKTLLAQTLARTLRVPFAIADATTLTeAGYVG 197
Cdd:cd19509     1 IAGLDDAKEALKEAVILPSLR----PDLFPGLRGPPRG-ILLYGPPGTGKTLLARAVASESGSTFFSISASSLV-SKWVG 74
                          90       100       110
                  ....*....|....*....|....*....|..
gi 1434243542 198 EDvENILLKLMTAADFDIPraeiGIIYIDEID 229
Cdd:cd19509    75 ES-EKIVRALFALARELQP----SIIFIDEID 101
RecA-like_NVL_r1-like cd19518
first of two ATPase domains of NVL (nuclear VCP-like protein) and similar ATPase domains; NVL ...
157-253 1.77e-07

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: 50.87  E-value: 1.77e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434243542 157 IMLLGPTGSGKTLLAQTLARTLRVPFAIADATTLTeAGYVGEDVENIlLKLMTAADFDIPraeiGIIYIDEIDKVARKAE 236
Cdd:cd19518    37 VLLHGPPGCGKTMLANAIAGELKVPFLKISATEIV-SGVSGESEEKI-RELFDQAISNAP----CIVFIDEIDAITPKRE 110
                          90
                  ....*....|....*..
gi 1434243542 237 NLSitRDVSGEGVQQAL 253
Cdd:cd19518   111 SAQ--REMERRIVSQLL 125
RecA-like_Figl-1 cd19525
ATPase domain of Fidgetin-Like 1 (FIGL-1); FIGL-1 may participate in DNA repair in the nucleus; ...
116-284 2.95e-07

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: 50.76  E-value: 2.95e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434243542 116 EHVVGQEQAKRALSVAVYNHYKRislgADAVDGdVELAKSNIMLLGPTGSGKTLLAQTLARTLRVPFAIADATTLTeAGY 195
Cdd:cd19525    22 ADIAGLEFAKKTIKEIVVWPMLR----PDIFTG-LRGPPKGILLFGPPGTGKTLIGKCIASQSGATFFSISASSLT-SKW 95
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434243542 196 VGEDvENILLKLMTAADFDIPraeiGIIYIDEIDKVARKaenlsitrdvSGEGVQQALLKIveGTEASVPPQGGRKHPQQ 275
Cdd:cd19525    96 VGEG-EKMVRALFSVARCKQP----AVIFIDEIDSLLSQ----------RGEGEHESSRRI--KTEFLVQLDGATTSSED 158

                  ....*....
gi 1434243542 276 ELIHIDTTN 284
Cdd:cd19525   159 RILVVGATN 167
RecA-like_CDC48_NLV2_r1-like cd19503
first of two ATPase domains of CDC48 and NLV2, and similar ATPase domains; CDC48 in yeast and ...
157-237 4.65e-07

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: 49.60  E-value: 4.65e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434243542 157 IMLLGPTGSGKTLLAQTLARTLRVPFAIADATTLTeAGYVGEDVENiLLKLMTAADFDIPraeiGIIYIDEIDKVARKAE 236
Cdd:cd19503    37 VLLHGPPGTGKTLLARAVANEAGANFLSISGPSIV-SKYLGESEKN-LREIFEEARSHAP----SIIFIDEIDALAPKRE 110

                  .
gi 1434243542 237 N 237
Cdd:cd19503   111 E 111
RecA-like_ClpB_Hsp104-like cd19499
Chaperone protein ClpB/Hsp104 subfamily; Bacterial Caseinolytic peptidase B (ClpB) and ...
110-231 7.55e-07

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: 49.10  E-value: 7.55e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434243542 110 LYAELSEHVVGQEQAKRALSVAVYNHykRISLGaDAVDGDVelaksNIMLLGPTGSGKTLLAQTLARTL--------RVP 181
Cdd:cd19499     5 LEERLHERVVGQDEAVKAVSDAIRRA--RAGLS-DPNRPIG-----SFLFLGPTGVGKTELAKALAELLfgdednliRID 76
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1434243542 182 FAIA----DATTLTEA--GYVGEDVENILLKlmtaadfDIPRAEIGIIYIDEIDKV 231
Cdd:cd19499    77 MSEYmekhSVSRLIGAppGYVGYTEGGQLTE-------AVRRKPYSVVLLDEIEKA 125
Mg_chelatase pfam01078
Magnesium chelatase, subunit ChlI; Magnesium-chelatase is a three-component enzyme that ...
118-174 4.39e-06

Magnesium chelatase, subunit ChlI; Magnesium-chelatase is a three-component enzyme that catalyzes the insertion of Mg2+ into protoporphyrin IX. This is the first unique step in the synthesis of (bacterio)chlorophyll. Due to this, it is thought that Mg-chelatase has an important role in channelling inter- mediates into the (bacterio)chlorophyll branch in response to conditions suitable for photosynthetic growth. ChlI and BchD have molecular weight between 38-42 kDa.


Pssm-ID: 426032 [Multi-domain]  Cd Length: 207  Bit Score: 47.53  E-value: 4.39e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1434243542 118 VVGQEQAKRALSVAVY-NHykrislgadavdgdvelaksNIMLLGPTGSGKTLLAQTL 174
Cdd:pfam01078   5 VKGQEQAKRALEIAAAgGH--------------------NLLMIGPPGSGKTMLAKRL 42
CDC48 TIGR01243
AAA family ATPase, CDC48 subfamily; This subfamily of the AAA family ATPases includes two ...
157-259 4.82e-06

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


Pssm-ID: 273521 [Multi-domain]  Cd Length: 733  Bit Score: 49.14  E-value: 4.82e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434243542 157 IMLLGPTGSGKTLLAQTLARTLRVPFAIADATTLTeAGYVGEDVENiLLKLMTAADFDIPraeiGIIYIDEIDKVARKAE 236
Cdd:TIGR01243 215 VLLYGPPGTGKTLLAKAVANEAGAYFISINGPEIM-SKYYGESEER-LREIFKEAEENAP----SIIFIDEIDAIAPKRE 288
                          90       100
                  ....*....|....*....|...
gi 1434243542 237 nlSITRDVSGEGVQQaLLKIVEG 259
Cdd:TIGR01243 289 --EVTGEVEKRVVAQ-LLTLMDG 308
RecA-like_FtsH cd19501
ATP-dependent zinc metalloprotease FtsH; FtsH ATPase is a processive, ATP-dependent zinc ...
118-234 5.40e-06

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


Pssm-ID: 410909 [Multi-domain]  Cd Length: 171  Bit Score: 46.46  E-value: 5.40e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434243542 118 VVGQEQAKRALSVAV---YNHYKRISLGADAVDGdvelaksnIMLLGPTGSGKTLLAQTLARTLRVPFAIADATTLTEAg 194
Cdd:cd19501     6 VAGCEEAKEELKEVVeflKNPEKFTKLGAKIPKG--------VLLVGPPGTGKTLLAKAVAGEAGVPFFSISGSDFVEM- 76
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 1434243542 195 YVGEDVENIlLKLMTAADFDIPraeiGIIYIDEIDKVARK 234
Cdd:cd19501    77 FVGVGASRV-RDLFEQAKKNAP----CIVFIDEIDAVGRK 111
AAA smart00382
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ...
154-240 6.91e-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: 45.83  E-value: 6.91e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434243542  154 KSNIMLLGPTGSGKTLLAQTLARTLRVP---FAIADATTLTEAGYVGEDVENILLKLMTAADFDIPR--------AEIGI 222
Cdd:smart00382   2 GEVILIVGPPGSGKTTLARALARELGPPgggVIYIDGEDILEEVLDQLLLIIVGGKKASGSGELRLRlalalarkLKPDV 81
                           90
                   ....*....|....*...
gi 1434243542  223 IYIDEIDKVARKAENLSI 240
Cdd:smart00382  82 LILDEITSLLDAEQEALL 99
RecA-like_KTNA1 cd19522
Katanin p60 ATPase-containing subunit A1; Katanin p60 ATPase-containing subunit A1 (KTNA1) is ...
157-271 9.52e-06

Katanin p60 ATPase-containing subunit A1; Katanin p60 ATPase-containing subunit A1 (KTNA1) is the catalytic subunit of the Katanin complex which is severs microtubules in an ATP-dependent manner, and is implicated in multiple aspects of microtubule dynamics. In addition to the p60 catalytic ATPase subunit, Katanin contains an accessory subunit (p80 or p80-like). The microtubule-severing activity of the ATPase is essential for female meiotic spindle assembly, and male gamete production; and the katanin complex severing microtubules is under tight regulation during the transition from the meiotic to mitotic stage to allow proper embryogenesis. 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: 410930 [Multi-domain]  Cd Length: 170  Bit Score: 45.75  E-value: 9.52e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434243542 157 IMLLGPTGSGKTLLAQTLARTLRVPFAIADATTLTeAGYVGEDvENILLKLMTAADFDIPRAeigiIYIDEIDKVARKae 236
Cdd:cd19522    36 VLMVGPPGTGKTLLAKAVATECGTTFFNVSSSTLT-SKYRGES-EKLVRLLFEMARFYAPTT----IFIDEIDSICSR-- 107
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 1434243542 237 nlsitRDVSGEG-----VQQALLKIVEGTEASVPPQGGRK 271
Cdd:cd19522   108 -----RGTSEEHeasrrVKSELLVQMDGVGGASENDDPSK 142
RecA-like_spastin cd19524
ATPase domain of spastin; Spastin is an ATP-dependent microtubule-severing protein involved in ...
118-231 1.12e-05

ATPase domain of spastin; Spastin is an ATP-dependent microtubule-severing protein involved in microtubule dynamics; it specifically recognizes and cuts microtubules that are polyglutamylated. This subfamily belongs to the RecA-like NTPase family which includes the NTP binding domain of F1 and V1 H(+)ATPases, DnaB and related helicases as well as bacterial RecA and related eukaryotic and archaeal recombinases. The RecA-like NTPase family also includes bacterial conjugation proteins and related DNA transfer proteins involved in type II and type IV secretion.


Pssm-ID: 410932 [Multi-domain]  Cd Length: 164  Bit Score: 45.61  E-value: 1.12e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434243542 118 VVGQEQAKRALSVAVYNHYKRislgADAVDGDVELAKSnIMLLGPTGSGKTLLAQTLARTLRVPFAIADATTLTeAGYVG 197
Cdd:cd19524     2 IAGQDLAKQALQEMVILPSLR----PELFTGLRAPARG-LLLFGPPGNGKTMLAKAVAAESNATFFNISAASLT-SKYVG 75
                          90       100       110
                  ....*....|....*....|....*....|....
gi 1434243542 198 EDvENILLKLMTAADFDIPraeiGIIYIDEIDKV 231
Cdd:cd19524    76 EG-EKLVRALFAVARELQP----SIIFIDEVDSL 104
RecA-like_CDC48_r1-like cd19519
first of two ATPase domains of CDC48 and similar ATPase domains; CDC48 in yeast and p97 or VCP ...
157-263 2.22e-05

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: 44.73  E-value: 2.22e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434243542 157 IMLLGPTGSGKTLLAQTLARTLRVPFAIADATTLTeAGYVGEDVENiLLKLMTAADFDIPraeiGIIYIDEIDKVARKAE 236
Cdd:cd19519    37 ILLYGPPGTGKTLIARAVANETGAFFFLINGPEIM-SKLAGESESN-LRKAFEEAEKNAP----AIIFIDEIDAIAPKRE 110
                          90       100
                  ....*....|....*....|....*..
gi 1434243542 237 NlsITRDVSGEGVQQaLLKIVEGTEAS 263
Cdd:cd19519   111 K--THGEVERRIVSQ-LLTLMDGLKQR 134
hflB PRK10733
ATP-dependent zinc metalloprotease FtsH;
157-262 2.74e-05

ATP-dependent zinc metalloprotease FtsH;


Pssm-ID: 182683 [Multi-domain]  Cd Length: 644  Bit Score: 46.57  E-value: 2.74e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434243542 157 IMLLGPTGSGKTLLAQTLARTLRVPFAIADATTLTEAgYVGEDVENILLKLMTAAdfdipRAEIGIIYIDEIDKVAR-KA 235
Cdd:PRK10733  188 VLMVGPPGTGKTLLAKAIAGEAKVPFFTISGSDFVEM-FVGVGASRVRDMFEQAK-----KAAPCIIFIDEIDAVGRqRG 261
                          90       100
                  ....*....|....*....|....*....
gi 1434243542 236 ENLSITRDVSGEGVQQALLKI--VEGTEA 262
Cdd:PRK10733  262 AGLGGGHDEREQTLNQMLVEMdgFEGNEG 290
MoxR COG0714
MoxR-like ATPase [General function prediction only]; MoxR-like ATPase is part of the Pathway ...
106-237 3.30e-05

MoxR-like ATPase [General function prediction only]; MoxR-like ATPase is part of the Pathway/BioSystem: Cobalamine/B12 biosynthesis


Pssm-ID: 440478 [Multi-domain]  Cd Length: 292  Bit Score: 45.54  E-value: 3.30e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434243542 106 TPHELYAELSEHVVGQEQAKRALSVAVynhykrislgadavdgdveLAKSNIMLLGPTGSGKTLLAQTLARTLRVPFAIA 185
Cdd:COG0714     2 TEARLRAEIGKVYVGQEELIELVLIAL-------------------LAGGHLLLEGVPGVGKTTLAKALARALGLPFIRI 62
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1434243542 186 DAT-TLTEAGYVGEDVENillklMTAADFDIPRAEIG--IIYIDEIDKVARKAEN 237
Cdd:COG0714    63 QFTpDLLPSDILGTYIYD-----QQTGEFEFRPGPLFanVLLADEINRAPPKTQS 112
AAA_5 pfam07728
AAA domain (dynein-related subfamily); This Pfam entry includes some of the AAA proteins not ...
156-235 5.91e-05

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: 42.66  E-value: 5.91e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434243542 156 NIMLLGPTGSGKTLLAQTLARTL--RVPFAIADATTLTEAGYVGE-DVENILLK-----LMTAAdfdiprAEIGIIYIDE 227
Cdd:pfam07728   1 GVLLVGPPGTGKTELAERLAAALsnRPVFYVQLTRDTTEEDLFGRrNIDPGGASwvdgpLVRAA------REGEIAVLDE 74

                  ....*...
gi 1434243542 228 IDKVARKA 235
Cdd:pfam07728  75 INRANPDV 82
RecA-like_NSF-SEC18_r1-like cd19504
first of two ATPase domains of NSF and SEC18, and similar ATPase domains; ...
157-262 6.57e-05

first of two ATPase domains of NSF and SEC18, and similar ATPase domains; N-ethylmaleimide-sensitive factor (NSF) and Saccharomyces cerevisiae Vesicular-fusion protein Sec18, key factors for eukaryotic trafficking, are ATPases and SNARE disassembly chaperones. NSF/Sec18 activate or prime SNAREs, the terminal catalysts of membrane fusion. Sec18/NSF associates with SNARE complexes through binding Sec17/alpha-SNAP. Sec18 has an N-terminal cap domain and two nucleotide-binding domains (D1 and D2) which form the two rings of the hexameric complex. The hydrolysis of ATP by D1 generates most of the energy necessary to disassemble inactive SNARE bundles, while the D2 ring binds ATP to stabilize the homohexamer. This subfamily includes the first (D1) ATPase domain of NSF/Sec18, and belongs to the RecA-like NTPase family which includes the NTP binding domain of F1 and V1 H(+)ATPases, DnaB and related helicases as well as bacterial RecA and related eukaryotic and archaeal recombinases. The RecA-like NTPase family also includes bacterial conjugation proteins and related DNA transfer proteins involved in type II and type IV secretion.


Pssm-ID: 410912 [Multi-domain]  Cd Length: 177  Bit Score: 43.63  E-value: 6.57e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434243542 157 IMLLGPTGSGKTLLAQTLARTL--RVPFAIADATTLTEagYVGEDVENIlLKLMTAADFDIPR----AEIGIIYIDEIDK 230
Cdd:cd19504    38 ILLYGPPGTGKTLMARQIGKMLnaREPKIVNGPEILNK--YVGESEANI-RKLFADAEEEQRRlganSGLHIIIFDEIDA 114
                          90       100       110
                  ....*....|....*....|....*....|..
gi 1434243542 231 VARKAENLSITRDVSGEGVQQALLKIvEGTEA 262
Cdd:cd19504   115 ICKQRGSMAGSTGVHDTVVNQLLSKI-DGVEQ 145
RecA-like_PEX6_r2 cd19527
second of two ATPase domains of Peroxisomal biogenesis factor 6 (PEX6); PEX6(also known as ...
154-256 8.30e-05

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


Pssm-ID: 410935 [Multi-domain]  Cd Length: 160  Bit Score: 42.89  E-value: 8.30e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434243542 154 KSNIMLLGPTGSGKTLLAQTLARTLRVPFAIADATTLTEAgYVGEDVENILLKLMTAADfdiprAEIGIIYIDEIDKVAR 233
Cdd:cd19527    26 RSGILLYGPPGTGKTLLAKAIATECSLNFLSVKGPELINM-YIGESEANVREVFQKARD-----AKPCVIFFDELDSLAP 99
                          90       100
                  ....*....|....*....|...
gi 1434243542 234 KAENLSITRDVSGEGVQQALLKI 256
Cdd:cd19527   100 SRGNSGDSGGVMDRVVSQLLAEL 122
ClpA COG0542
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ...
113-178 8.49e-05

ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 440308 [Multi-domain]  Cd Length: 836  Bit Score: 45.07  E-value: 8.49e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1434243542 113 ELSEHVVGQEQAKRALSVAVynhyKRislgadavdgdvelAKSNI----------MLLGPTGSGKTLLAQTLARTL 178
Cdd:COG0542   546 ELHERVIGQDEAVEAVADAI----RR--------------SRAGLkdpnrpigsfLFLGPTGVGKTELAKALAEFL 603
RecA-like_ATAD1 cd19520
ATPase domain of ATPase family AAA domain-containing protein 1 and similar ATPase domains; ...
153-233 1.39e-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: 42.41  E-value: 1.39e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434243542 153 AKSNIMLLGPTGSGKTLLAQTLARTLRVPFAIADATTLTEAGYvGEDvenillKLMTAADFDIP-RAEIGIIYIDEIDKV 231
Cdd:cd19520    34 PPKGVLLYGPPGCGKTMLAKATAKEAGARFINLQVSSLTDKWY-GES------QKLVAAVFSLAsKLQPSIIFIDEIDSF 106

                  ..
gi 1434243542 232 AR 233
Cdd:cd19520   107 LR 108
AAA_22 pfam13401
AAA domain;
150-253 2.25e-04

AAA domain;


Pssm-ID: 379165 [Multi-domain]  Cd Length: 129  Bit Score: 41.17  E-value: 2.25e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434243542 150 VELAKSNIMLLGPTGSGKTLLAQTLARTL---RVPFAIADATTLTEAGYVGEDVENIL-LKLMTAADFDIPRAEI----- 220
Cdd:pfam13401   1 IRFGAGILVLTGESGTGKTTLLRRLLEQLpevRDSVVFVDLPSGTSPKDLLRALLRALgLPLSGRLSKEELLAALqqlll 80
                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 1434243542 221 -----GIIYIDEIDKVARKA-ENLSITRDVSGEGVQQAL 253
Cdd:pfam13401  81 alavaVVLIIDEAQHLSLEAlEELRDLLNLSSKLLQLIL 119
PRK09862 PRK09862
ATP-dependent protease;
77-178 2.90e-04

ATP-dependent protease;


Pssm-ID: 182120 [Multi-domain]  Cd Length: 506  Bit Score: 43.04  E-value: 2.90e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434243542  77 EGRHArvgdgvvtasVADPAPEDVLADlptphELYAELSEhVVGQEQAKRALSVAvynhykrislgadAVDGdvelakSN 156
Cdd:PRK09862  168 EGKHA----------LERPKPTDAVSR-----ALQHDLSD-VIGQEQGKRGLEIT-------------AAGG------HN 212
                          90       100
                  ....*....|....*....|..
gi 1434243542 157 IMLLGPTGSGKTLLAQTLARTL 178
Cdd:PRK09862  213 LLLIGPPGTGKTMLASRINGLL 234
RecA-like_VPS4 cd19521
ATPase domain of vacuolar protein sorting-associated protein 4; Vacuolar protein ...
118-292 1.46e-03

ATPase domain of vacuolar protein sorting-associated protein 4; Vacuolar protein sorting-associated protein 4 (Vps4) is believed to be involved in intracellular protein transport out of a prevacuolar endosomal compartment. This subfamily belongs to the RecA-like NTPase family which includes the NTP binding domain of F1 and V1 H(+)ATPases, DnaB and related helicases as well as bacterial RecA and related eukaryotic and archaeal recombinases. The RecA-like NTPase family also includes bacterial conjugation proteins and related DNA transfer proteins involved in type II and type IV secretion.


Pssm-ID: 410929 [Multi-domain]  Cd Length: 170  Bit Score: 39.46  E-value: 1.46e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434243542 118 VVGQEQAKRALSVAVYNHYKRISLGADAvdgdvELAKSNIMLLGPTGSGKTLLAQTLARTLRVPFAIADATTLTeAGYVG 197
Cdd:cd19521     9 VAGLEGAKEALKEAVILPVKFPHLFTGN-----RKPWSGILLYGPPGTGKSYLAKAVATEANSTFFSVSSSDLV-SKWMG 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434243542 198 EDvENILLKLMTAADFDIPraeiGIIYIDEIDkvarkaeNLSITRdvsGEGVQQALLKIveGTEASVPPQGGRKHPQQEL 277
Cdd:cd19521    83 ES-EKLVKQLFAMARENKP----SIIFIDEVD-------SLCGTR---GEGESEASRRI--KTELLVQMNGVGNDSQGVL 145
                         170
                  ....*....|....*
gi 1434243542 278 IhIDTTNILFILGGA 292
Cdd:cd19521   146 V-LGATNIPWQLDSA 159
RecA-like_CDC48_r2-like cd19511
second of two ATPase domains of CDC48/p97, PEX1 and -6, VAT and NVL, and similar ATPase ...
157-232 1.96e-03

second of two ATPase domains of CDC48/p97, PEX1 and -6, VAT and NVL, and similar ATPase domains; This subfamily includes the second of two ATPase domains of the molecular chaperone CDC48 in yeast and p97 or VCP in metazoans, Peroxisomal biogenesis factor 1 (PEX1) and -6 (PEX6), Valosin-containing protein-like ATPase (VAT), and nuclear VCP-like protein (NVL). This subfamily belongs to the RecA-like NTPase family which includes the NTP binding domain of F1 and V1 H(+)ATPases, DnaB and related helicases as well as bacterial RecA and related eukaryotic and archaeal recombinases. The RecA-like NTPase family also includes bacterial conjugation proteins and related DNA transfer proteins involved in type II and type IV secretion.


Pssm-ID: 410919 [Multi-domain]  Cd Length: 159  Bit Score: 38.80  E-value: 1.96e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434243542 157 IMLLGPTGSGKTLLAQTLARTLRVPF-AIADATTLTEagYVGED---VENILLKLMTAAdfdiPraeiGIIYIDEIDKVA 232
Cdd:cd19511    30 VLLYGPPGCGKTLLAKALASEAGLNFiSVKGPELFSK--YVGESeraVREIFQKARQAA----P----CIIFFDEIDSLA 99
RecA-like_PEX1_r2 cd19526
second of two ATPase domains of Peroxisomal biogenesis factor 1 (PEX1); PEX1(also known as ...
154-259 3.23e-03

second of two ATPase domains of Peroxisomal biogenesis factor 1 (PEX1); PEX1(also known as Peroxin-1)/PEX6 is a protein unfoldase; PEX1 and PEX6 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. PEX-1 is required for stability of PEX5. 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: 410934 [Multi-domain]  Cd Length: 158  Bit Score: 38.18  E-value: 3.23e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1434243542 154 KSNIMLLGPTGSGKTLLAQTLARTLRVPFAIADATTLTeAGYVGEDVENILLKLMTAAdfdipRAEIGIIYIDEIDKVA- 232
Cdd:cd19526    27 RSGILLYGPPGCGKTLLASAIASECGLNFISVKGPELL-NKYIGASEQNVRDLFSRAQ-----SAKPCILFFDEFDSIAp 100
                          90       100       110
                  ....*....|....*....|....*....|
gi 1434243542 233 -RKAENLSITRDVsgegVQQALLKI--VEG 259
Cdd:cd19526   101 kRGHDSTGVTDRV----VNQLLTQLdgVEG 126
RecA-like_PAN_like cd19502
proteasome activating nucleotidase PAN and related proteasome subunits; This subfamily ...
157-234 5.73e-03

proteasome activating nucleotidase PAN and related proteasome subunits; This subfamily contains ATPase subunits of the eukaryotic 26S proteasome, and of the archaeal proteasome which carry out ATP-dependent degradation of substrates of the ubiquitin-proteasome pathway. The eukaryotic 26S proteasome consists of a proteolytic 20S core particle (CP), and a 19S regulatory particle (RP) which provides the ATP-dependence and the specificity for ubiquitinated proteins. In the archaea the RP is a homohexameric complex of proteasome-activating nucleotidase (PAN). This subfamily also includes various eukaryotic 26S subunits including, proteasome 26S subunit, ATPase 2 (PSMC2, also known as S7 and MSS1) which is a member of the 19S RP and has a chaperone like activity; and proteasome 20S subunit alpha 6 (PSMA6, also known as IOTA, p27K, and PROS27) which is a member of the 20S CP. This RecA-like_PAN subfamily belongs to the RecA-like NTPase family which includes the NTP binding domain of F1 and V1 H(+)ATPases, DnaB and related helicases as well as bacterial RecA and related eukaryotic and archaeal recombinases. The RecA-like NTPase family also includes bacterial conjugation proteins and related DNA transfer proteins involved in type II and type IV secretion.


Pssm-ID: 410910 [Multi-domain]  Cd Length: 171  Bit Score: 37.70  E-value: 5.73e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1434243542 157 IMLLGPTGSGKTLLAQTLARTLRVPFAIADATTLTEAgYVGEDVEnillklMTAADFDIPRAEI-GIIYIDEIDKVARK 234
Cdd:cd19502    40 VLLYGPPGTGKTLLAKAVANHTDATFIRVVGSELVQK-YIGEGAR------LVRELFEMAREKApSIIFIDEIDAIGAK 111
RecA-like_Ycf46-like cd19507
ATPase domain of Ycf46 and similar ATPase domains; Ycf46 may play a role in the regulation of ...
157-230 6.75e-03

ATPase domain of Ycf46 and similar ATPase domains; Ycf46 may play a role in the regulation of photosynthesis in cyanobacteria, especially in CO2 uptake and utilization. This subfamily belongs to the RecA-like NTPase family which includes the NTP binding domain of F1 and V1 H(+)ATPases, DnaB and related helicases as well as bacterial RecA and related eukaryotic and archaeal recombinases. The RecA-like NTPase family also includes bacterial conjugation proteins and related DNA transfer proteins involved in type II and type IV secretion.


Pssm-ID: 410915 [Multi-domain]  Cd Length: 161  Bit Score: 37.35  E-value: 6.75e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1434243542 157 IMLLGPTGSGKTLLAQTLARTLRVPFAIADATTLTeAGYVGEDVENiLLKLMTAADFDIPraeiGIIYIDEIDK 230
Cdd:cd19507    34 LLLVGIQGTGKSLTAKAIAGVWQLPLLRLDMGRLF-GGLVGESESR-LRQMIQTAEAIAP----CVLWIDEIEK 101
 
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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