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Conserved domains on  [gi|616269681|gb|KAA86057|]
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ATP-dependent protease ATPase subunit HslU [Staphylococcus aureus VET0103R]

Protein Classification

ATP-dependent protease ATPase subunit HslU( domain architecture ID 18510702)

ATP-dependent protease ATPase subunit HslU is the ATPase component of a proteasome-like degradation complex and has chaperone activity

CATH:  1.10.8.10|3.40.50.300|1.10.8.60
Gene Ontology:  GO:0006508|GO:0004176|GO:0005524|GO:0016887|GO:0036402
SCOP:  4000283

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
HslU COG1220
ATP-dependent protease HslVU (ClpYQ), ATPase subunit HslU [Posttranslational modification, ...
 8-467 0e+00

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


:

Pssm-ID: 440833 [Multi-domain]  Cd Length: 454  Bit Score: 774.99  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616269681   8 LTPKEIVSKLNEYIVGQNDAKRKVAIALRNRYRRSLLDEESKQEISPKNILMIGPTGVGKTEIARRMAKVVGAPFIKVEA 87
Cdd:COG1220    4 LTPREIVAELDKYIIGQDEAKRAVAIALRNRWRRQQLPEELRDEITPKNILMIGPTGVGKTEIARRLAKLANAPFIKVEA 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616269681  88 TKFTEVGYVGRDVESMVRDLVDVSVRLVKAQKKSLVQDEATAKANEKLVKLLVPSMKKKASQTNNPleslfggaipnfgq 167
Cdd:COG1220   84 TKFTEVGYVGRDVESMIRDLVEIAVKMVREEKMEKVREKAEEAAEERILDLLLPPPKKKAGSNNPF-------------- 149

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616269681 168 NNEDEEEPPTEEIKTKRSEIKRQLEEGKLEKEKVRIKVEQDPGA-LGMLGTNQ----NQQMQEMMNQLMPKKKVEREVAV 242
Cdd:COG1220  150 EEEEEEEEEEEEISRTREKFRKKLREGELDDREIEIEVEESSSPgVEIMGPPGmeemGMNLQDMFGNLMPKKKKKRKVKV 229

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616269681 243 ETARKILADSYADELIDQESANQEALELAEQMGIIFIDEIDKVATNNHNSGQDVSRQGVQRDILPILEGSVIQTKYGTVN 322
Cdd:COG1220  230 KEARKILTQEEAAKLIDMDEVKQEAIERAEQNGIIFIDEIDKIASRGGGSGPDVSREGVQRDLLPIVEGSTVNTKYGMVK 309

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616269681 323 TEHMLFIGAGAFHVSKPSDLIPELQGRFPIRVELDSLSVEDFVRILTEPKLSLIKQYEALLQTEEVTVNFTDEAITRLAE 402
Cdd:COG1220  310 TDHILFIAAGAFHVSKPSDLIPELQGRFPIRVELDSLTEEDFVRILTEPKNALTKQYQALLATEGVELEFTDDAIREIAE 389

                        410       420       430       440       450       460
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 616269681 403 IAYQVNQDTDNIGARRLHTILEKMLEDLSFEAPSMPNAVVDITPQYVDDKLKSISTNKDLSAFIL 467
Cdd:COG1220  390 IAFEVNERTENIGARRLHTVMEKLLEDISFEAPDLSGKTVVIDAAYVDEKLGDIVKDEDLSRYIL 454
 
Name Accession Description Interval E-value
HslU COG1220
ATP-dependent protease HslVU (ClpYQ), ATPase subunit HslU [Posttranslational modification, ...
 8-467 0e+00

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


Pssm-ID: 440833 [Multi-domain]  Cd Length: 454  Bit Score: 774.99  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616269681   8 LTPKEIVSKLNEYIVGQNDAKRKVAIALRNRYRRSLLDEESKQEISPKNILMIGPTGVGKTEIARRMAKVVGAPFIKVEA 87
Cdd:COG1220    4 LTPREIVAELDKYIIGQDEAKRAVAIALRNRWRRQQLPEELRDEITPKNILMIGPTGVGKTEIARRLAKLANAPFIKVEA 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616269681  88 TKFTEVGYVGRDVESMVRDLVDVSVRLVKAQKKSLVQDEATAKANEKLVKLLVPSMKKKASQTNNPleslfggaipnfgq 167
Cdd:COG1220   84 TKFTEVGYVGRDVESMIRDLVEIAVKMVREEKMEKVREKAEEAAEERILDLLLPPPKKKAGSNNPF-------------- 149

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616269681 168 NNEDEEEPPTEEIKTKRSEIKRQLEEGKLEKEKVRIKVEQDPGA-LGMLGTNQ----NQQMQEMMNQLMPKKKVEREVAV 242
Cdd:COG1220  150 EEEEEEEEEEEEISRTREKFRKKLREGELDDREIEIEVEESSSPgVEIMGPPGmeemGMNLQDMFGNLMPKKKKKRKVKV 229

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616269681 243 ETARKILADSYADELIDQESANQEALELAEQMGIIFIDEIDKVATNNHNSGQDVSRQGVQRDILPILEGSVIQTKYGTVN 322
Cdd:COG1220  230 KEARKILTQEEAAKLIDMDEVKQEAIERAEQNGIIFIDEIDKIASRGGGSGPDVSREGVQRDLLPIVEGSTVNTKYGMVK 309

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616269681 323 TEHMLFIGAGAFHVSKPSDLIPELQGRFPIRVELDSLSVEDFVRILTEPKLSLIKQYEALLQTEEVTVNFTDEAITRLAE 402
Cdd:COG1220  310 TDHILFIAAGAFHVSKPSDLIPELQGRFPIRVELDSLTEEDFVRILTEPKNALTKQYQALLATEGVELEFTDDAIREIAE 389

                        410       420       430       440       450       460
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 616269681 403 IAYQVNQDTDNIGARRLHTILEKMLEDLSFEAPSMPNAVVDITPQYVDDKLKSISTNKDLSAFIL 467
Cdd:COG1220  390 IAFEVNERTENIGARRLHTVMEKLLEDISFEAPDLSGKTVVIDAAYVDEKLGDIVKDEDLSRYIL 454
hslU PRK05201
ATP-dependent protease ATPase subunit HslU;
8-467 0e+00

ATP-dependent protease ATPase subunit HslU;


Pssm-ID: 235364 [Multi-domain]  Cd Length: 443  Bit Score: 766.16  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616269681   8 LTPKEIVSKLNEYIVGQNDAKRKVAIALRNRYRRSLLDEESKQEISPKNILMIGPTGVGKTEIARRMAKVVGAPFIKVEA 87
Cdd:PRK05201   4 LTPREIVSELDKYIIGQDDAKRAVAIALRNRWRRMQLPEELRDEVTPKNILMIGPTGVGKTEIARRLAKLANAPFIKVEA 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616269681  88 TKFTEVGYVGRDVESMVRDLVDVSVRLVKAQKKSLVQDEATAKANEKLVKLLVPSMKKKASQTNNPLEslfggaipnfgq 167
Cdd:PRK05201  84 TKFTEVGYVGRDVESIIRDLVEIAVKMVREEKREKVREKAEEAAEERILDALLPPAKNNWGEEEEKEE------------ 151

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616269681 168 nnedeeeppteeIKTKRSEIKRQLEEGKLEKEKVRIKVEQDPGALGMLGT----NQNQQMQEMMNQLMPKKKVEREVAVE 243
Cdd:PRK05201 152 ------------ISATRQKFRKKLREGELDDKEIEIEVAEAAPMMEIMGPpgmeEMTIQLQDMFGNLGPKKKKKRKLKVK 219

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616269681 244 TARKILADSYADELIDQESANQEALELAEQMGIIFIDEIDKVATNNHNSGQDVSRQGVQRDILPILEGSVIQTKYGTVNT 323
Cdd:PRK05201 220 EARKILIEEEAAKLIDMEEIKQEAIERVEQNGIVFIDEIDKIAARGGSSGPDVSREGVQRDLLPLVEGSTVSTKYGMVKT 299

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616269681 324 EHMLFIGAGAFHVSKPSDLIPELQGRFPIRVELDSLSVEDFVRILTEPKLSLIKQYEALLQTEEVTVNFTDEAITRLAEI 403
Cdd:PRK05201 300 DHILFIASGAFHVSKPSDLIPELQGRFPIRVELDALTEEDFVRILTEPKASLIKQYQALLATEGVTLEFTDDAIRRIAEI 379

                        410       420       430       440       450       460
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 616269681 404 AYQVNQDTDNIGARRLHTILEKMLEDLSFEAPSMPNAVVDITPQYVDDKLKSISTNKDLSAFIL 467
Cdd:PRK05201 380 AYQVNEKTENIGARRLHTVMEKLLEDISFEAPDMSGETVTIDAAYVDEKLGDLVKDEDLSRYIL 443
hslU TIGR00390
ATP-dependent protease HslVU, ATPase subunit; This model represents the ATPase subunit of ...
 8-467 0e+00

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: 544.41  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616269681    8 LTPKEIVSKLNEYIVGQNDAKRKVAIALRNRYRRSLLDEESKQEISPKNILMIGPTGVGKTEIARRMAKVVGAPFIKVEA 87
Cdd:TIGR00390   1 MTPREIVAELDKYIIGQDNAKKSVAIALRNRYRRSQLNEELKDEVTPKNILMIGPTGVGKTEIARRLAKLANAPFIKVEA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616269681   88 TKFTEVGYVGRDVESMVRDLVDVSVRLVKAQKKSLVQDEATAKANEKLVKLLVPSMKKKASQTNNPLESlfggaipnfgq 167
Cdd:TIGR00390  81 TKFTEVGYVGRDVESMVRDLTDAAVKLVKEEAIEKVRDRAEELAEERIVDVLLPPAKNQWGQTEQQQEP----------- 149

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616269681  168 nnedeeeppteeiKTKRSEIKRQLEEGKLEKEKVRIKV-EQDPGALGML-GTNQNQ---QMQEMMNQLMPKKKVEREVAV 242
Cdd:TIGR00390 150 -------------ESAREAFRKKLREGELDDKEIEIDVsAKMPSGIEIMaPPGMEEmtmQLQSLFQNLGGQKKKKRKLKI 216

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616269681  243 ETARKILADSYADELIDQESANQEALELAEQMGIIFIDEIDKVATNNHNSGQDVSRQGVQRDILPILEGSVIQTKYGTVN 322
Cdd:TIGR00390 217 KDAKKALIAEEAAKLVDPEEIKQEAIDAVEQSGIIFIDEIDKIAKKGESSGADVSREGVQRDLLPIVEGSTVNTKYGMVK 296

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616269681  323 TEHMLFIGAGAFHVSKPSDLIPELQGRFPIRVELDSLSVEDFVRILTEPKLSLIKQYEALLQTEEVTVNFTDEAITRLAE 402
Cdd:TIGR00390 297 TDHILFIAAGAFQLAKPSDLIPELQGRFPIRVELQALTTDDFERILTEPKNSLIKQYKALMKTEGVNIEFSDEAIKRIAE 376

                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 616269681  403 IAYQVNQDTDNIGARRLHTILEKMLEDLSFEAPSMPNAVVDITPQYVDDKLKSISTNKDLSAFIL 467
Cdd:TIGR00390 377 LAYNVNEKTENIGARRLHTVLERLLEDISFEAPDLSGQNITIDADYVSKKLGALVADEDLSRFIL 441
RecA-like_HslU cd19498
ATP-dependent protease ATPase subunit HslU; HslU is a component of the ATP-dependent protease ...
 9-356 4.33e-95

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: 284.66  E-value: 4.33e-95
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616269681   9 TPKEIVSKLNEYIVGQNDAKRKVAIALRNRYRRSLLDEESKQEISPKNILMIGPTGVGKTEIARRMAKVVGAPFIKVEAT 88
Cdd:cd19498    1 TPREIVSELDKYIIGQDEAKRAVAIALRNRWRRMQLPEELRDEVTPKNILMIGPTGVGKTEIARRLAKLAGAPFIKVEAT 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616269681  89 KFTEVGYVGRDVESMVRDLVDvsvrlvkaqkkslvqdeatakaneklvkllvpsmkkkasqtnnpleslfggaipnfgqn 168
Cdd:cd19498   81 KFTEVGYVGRDVESIIRDLVE----------------------------------------------------------- 101

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616269681 169 nedeeeppteeiktkrseikrqleegklekekvrikveqdpgalgmlgtnqnqqmqemmnqlmpkkkverevavetarki 248
Cdd:cd19498      --------------------------------------------------------------------------------

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616269681 249 ladsyadelidqesanqealelaeqmGIIFIDEIDKVATNNHNSGQDVSRQGVQRDILPILEGSVIQTKYGTVNTEHMLF 328
Cdd:cd19498  102 --------------------------GIVFIDEIDKIAKRGGSSGPDVSREGVQRDLLPIVEGSTVSTKYGPVKTDHILF 155

                        330       340
                 ....*....|....*....|....*...
gi 616269681 329 IGAGAFHVSKPSDLIPELQGRFPIRVEL 356
Cdd:cd19498  156 IAAGAFHVAKPSDLIPELQGRFPIRVEL 183
AAA_2 pfam07724
AAA domain (Cdc48 subfamily); This Pfam entry includes some of the AAA proteins not detected ...
 237-353 1.78e-21

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: 91.10  E-value: 1.78e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616269681  237 EREVAVETARKILADSYADELIDqesaNQEALELAEQMG------------IIFIDEIDKVATnnhnsgqdvsrqGVQRD 304
Cdd:pfam07724  31 ERALIRIDMSEYMEEHSVSRLIG----APPGYVGYEEGGqlteavrrkpysIVLIDEIEKAHP------------GVQND 94

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 616269681  305 ILPILEGSVIQTKYG-TVNTEHMLFIGAGAFHVSKPSD------------------------LIPELQGRFPIR 353
Cdd:pfam07724  95 LLQILEGGTLTDKQGrTVDFKNTLFIMTGNFGSEKISDasrlgdspdyellkeevmdllkkgFIPEFLGRLPII 168
ClpB_D2-small smart01086
C-terminal, D2-small domain, of ClpB protein; This is the C-terminal domain of ClpB protein, ...
 359-436 1.20e-14

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: 69.01  E-value: 1.20e-14
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 616269681   359 LSVEDFVRILTEPKLSLIKQYEallqTEEVTVNFTDEAITRLAEIAYQVNqdtdnIGARRLHTILEKMLEDLSFEAPS 436
Cdd:smart01086   1 LDKEDLVRIVDLPLNALQKRLA----EKGITLEFTDEALDWLAEKGYDPK-----YGARPLRRIIQRELEDPLAELIL 69
 
Name Accession Description Interval E-value
HslU COG1220
ATP-dependent protease HslVU (ClpYQ), ATPase subunit HslU [Posttranslational modification, ...
 8-467 0e+00

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


Pssm-ID: 440833 [Multi-domain]  Cd Length: 454  Bit Score: 774.99  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616269681   8 LTPKEIVSKLNEYIVGQNDAKRKVAIALRNRYRRSLLDEESKQEISPKNILMIGPTGVGKTEIARRMAKVVGAPFIKVEA 87
Cdd:COG1220    4 LTPREIVAELDKYIIGQDEAKRAVAIALRNRWRRQQLPEELRDEITPKNILMIGPTGVGKTEIARRLAKLANAPFIKVEA 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616269681  88 TKFTEVGYVGRDVESMVRDLVDVSVRLVKAQKKSLVQDEATAKANEKLVKLLVPSMKKKASQTNNPleslfggaipnfgq 167
Cdd:COG1220   84 TKFTEVGYVGRDVESMIRDLVEIAVKMVREEKMEKVREKAEEAAEERILDLLLPPPKKKAGSNNPF-------------- 149

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616269681 168 NNEDEEEPPTEEIKTKRSEIKRQLEEGKLEKEKVRIKVEQDPGA-LGMLGTNQ----NQQMQEMMNQLMPKKKVEREVAV 242
Cdd:COG1220  150 EEEEEEEEEEEEISRTREKFRKKLREGELDDREIEIEVEESSSPgVEIMGPPGmeemGMNLQDMFGNLMPKKKKKRKVKV 229

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616269681 243 ETARKILADSYADELIDQESANQEALELAEQMGIIFIDEIDKVATNNHNSGQDVSRQGVQRDILPILEGSVIQTKYGTVN 322
Cdd:COG1220  230 KEARKILTQEEAAKLIDMDEVKQEAIERAEQNGIIFIDEIDKIASRGGGSGPDVSREGVQRDLLPIVEGSTVNTKYGMVK 309

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616269681 323 TEHMLFIGAGAFHVSKPSDLIPELQGRFPIRVELDSLSVEDFVRILTEPKLSLIKQYEALLQTEEVTVNFTDEAITRLAE 402
Cdd:COG1220  310 TDHILFIAAGAFHVSKPSDLIPELQGRFPIRVELDSLTEEDFVRILTEPKNALTKQYQALLATEGVELEFTDDAIREIAE 389

                        410       420       430       440       450       460
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 616269681 403 IAYQVNQDTDNIGARRLHTILEKMLEDLSFEAPSMPNAVVDITPQYVDDKLKSISTNKDLSAFIL 467
Cdd:COG1220  390 IAFEVNERTENIGARRLHTVMEKLLEDISFEAPDLSGKTVVIDAAYVDEKLGDIVKDEDLSRYIL 454
hslU PRK05201
ATP-dependent protease ATPase subunit HslU;
8-467 0e+00

ATP-dependent protease ATPase subunit HslU;


Pssm-ID: 235364 [Multi-domain]  Cd Length: 443  Bit Score: 766.16  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616269681   8 LTPKEIVSKLNEYIVGQNDAKRKVAIALRNRYRRSLLDEESKQEISPKNILMIGPTGVGKTEIARRMAKVVGAPFIKVEA 87
Cdd:PRK05201   4 LTPREIVSELDKYIIGQDDAKRAVAIALRNRWRRMQLPEELRDEVTPKNILMIGPTGVGKTEIARRLAKLANAPFIKVEA 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616269681  88 TKFTEVGYVGRDVESMVRDLVDVSVRLVKAQKKSLVQDEATAKANEKLVKLLVPSMKKKASQTNNPLEslfggaipnfgq 167
Cdd:PRK05201  84 TKFTEVGYVGRDVESIIRDLVEIAVKMVREEKREKVREKAEEAAEERILDALLPPAKNNWGEEEEKEE------------ 151

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616269681 168 nnedeeeppteeIKTKRSEIKRQLEEGKLEKEKVRIKVEQDPGALGMLGT----NQNQQMQEMMNQLMPKKKVEREVAVE 243
Cdd:PRK05201 152 ------------ISATRQKFRKKLREGELDDKEIEIEVAEAAPMMEIMGPpgmeEMTIQLQDMFGNLGPKKKKKRKLKVK 219

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616269681 244 TARKILADSYADELIDQESANQEALELAEQMGIIFIDEIDKVATNNHNSGQDVSRQGVQRDILPILEGSVIQTKYGTVNT 323
Cdd:PRK05201 220 EARKILIEEEAAKLIDMEEIKQEAIERVEQNGIVFIDEIDKIAARGGSSGPDVSREGVQRDLLPLVEGSTVSTKYGMVKT 299

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616269681 324 EHMLFIGAGAFHVSKPSDLIPELQGRFPIRVELDSLSVEDFVRILTEPKLSLIKQYEALLQTEEVTVNFTDEAITRLAEI 403
Cdd:PRK05201 300 DHILFIASGAFHVSKPSDLIPELQGRFPIRVELDALTEEDFVRILTEPKASLIKQYQALLATEGVTLEFTDDAIRRIAEI 379

                        410       420       430       440       450       460
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 616269681 404 AYQVNQDTDNIGARRLHTILEKMLEDLSFEAPSMPNAVVDITPQYVDDKLKSISTNKDLSAFIL 467
Cdd:PRK05201 380 AYQVNEKTENIGARRLHTVMEKLLEDISFEAPDMSGETVTIDAAYVDEKLGDLVKDEDLSRYIL 443
hslU TIGR00390
ATP-dependent protease HslVU, ATPase subunit; This model represents the ATPase subunit of ...
 8-467 0e+00

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: 544.41  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616269681    8 LTPKEIVSKLNEYIVGQNDAKRKVAIALRNRYRRSLLDEESKQEISPKNILMIGPTGVGKTEIARRMAKVVGAPFIKVEA 87
Cdd:TIGR00390   1 MTPREIVAELDKYIIGQDNAKKSVAIALRNRYRRSQLNEELKDEVTPKNILMIGPTGVGKTEIARRLAKLANAPFIKVEA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616269681   88 TKFTEVGYVGRDVESMVRDLVDVSVRLVKAQKKSLVQDEATAKANEKLVKLLVPSMKKKASQTNNPLESlfggaipnfgq 167
Cdd:TIGR00390  81 TKFTEVGYVGRDVESMVRDLTDAAVKLVKEEAIEKVRDRAEELAEERIVDVLLPPAKNQWGQTEQQQEP----------- 149

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616269681  168 nnedeeeppteeiKTKRSEIKRQLEEGKLEKEKVRIKV-EQDPGALGML-GTNQNQ---QMQEMMNQLMPKKKVEREVAV 242
Cdd:TIGR00390 150 -------------ESAREAFRKKLREGELDDKEIEIDVsAKMPSGIEIMaPPGMEEmtmQLQSLFQNLGGQKKKKRKLKI 216

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616269681  243 ETARKILADSYADELIDQESANQEALELAEQMGIIFIDEIDKVATNNHNSGQDVSRQGVQRDILPILEGSVIQTKYGTVN 322
Cdd:TIGR00390 217 KDAKKALIAEEAAKLVDPEEIKQEAIDAVEQSGIIFIDEIDKIAKKGESSGADVSREGVQRDLLPIVEGSTVNTKYGMVK 296

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616269681  323 TEHMLFIGAGAFHVSKPSDLIPELQGRFPIRVELDSLSVEDFVRILTEPKLSLIKQYEALLQTEEVTVNFTDEAITRLAE 402
Cdd:TIGR00390 297 TDHILFIAAGAFQLAKPSDLIPELQGRFPIRVELQALTTDDFERILTEPKNSLIKQYKALMKTEGVNIEFSDEAIKRIAE 376

                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 616269681  403 IAYQVNQDTDNIGARRLHTILEKMLEDLSFEAPSMPNAVVDITPQYVDDKLKSISTNKDLSAFIL 467
Cdd:TIGR00390 377 LAYNVNEKTENIGARRLHTVLERLLEDISFEAPDLSGQNITIDADYVSKKLGALVADEDLSRFIL 441
RecA-like_HslU cd19498
ATP-dependent protease ATPase subunit HslU; HslU is a component of the ATP-dependent protease ...
 9-356 4.33e-95

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: 284.66  E-value: 4.33e-95
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616269681   9 TPKEIVSKLNEYIVGQNDAKRKVAIALRNRYRRSLLDEESKQEISPKNILMIGPTGVGKTEIARRMAKVVGAPFIKVEAT 88
Cdd:cd19498    1 TPREIVSELDKYIIGQDEAKRAVAIALRNRWRRMQLPEELRDEVTPKNILMIGPTGVGKTEIARRLAKLAGAPFIKVEAT 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616269681  89 KFTEVGYVGRDVESMVRDLVDvsvrlvkaqkkslvqdeatakaneklvkllvpsmkkkasqtnnpleslfggaipnfgqn 168
Cdd:cd19498   81 KFTEVGYVGRDVESIIRDLVE----------------------------------------------------------- 101

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616269681 169 nedeeeppteeiktkrseikrqleegklekekvrikveqdpgalgmlgtnqnqqmqemmnqlmpkkkverevavetarki 248
Cdd:cd19498      --------------------------------------------------------------------------------

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616269681 249 ladsyadelidqesanqealelaeqmGIIFIDEIDKVATNNHNSGQDVSRQGVQRDILPILEGSVIQTKYGTVNTEHMLF 328
Cdd:cd19498  102 --------------------------GIVFIDEIDKIAKRGGSSGPDVSREGVQRDLLPIVEGSTVSTKYGPVKTDHILF 155

                        330       340
                 ....*....|....*....|....*...
gi 616269681 329 IGAGAFHVSKPSDLIPELQGRFPIRVEL 356
Cdd:cd19498  156 IAAGAFHVAKPSDLIPELQGRFPIRVEL 183
ClpX COG1219
ATP-dependent protease Clp, ATPase subunit ClpX [Posttranslational modification, protein ...
 8-456 1.11e-62

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


Pssm-ID: 440832 [Multi-domain]  Cd Length: 409  Bit Score: 208.75  E-value: 1.11e-62
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616269681   8 LTPKEIVSKLNEYIVGQNDAKRKVAIALRNRYRR--SLLDEESKQEISPKNILMIGPTGVGKTEIARRMAKVVGAPFIKV 85
Cdd:COG1219   61 PKPKEIKAFLDEYVIGQERAKKVLSVAVYNHYKRlnSGSKDDDDVELEKSNILLIGPTGSGKTLLAQTLARILDVPFAIA 140

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616269681  86 EATKFTEVGYVGRDVESMvrdlvdvsvrlvkaqkkslvqdeatakanekLVKLLvpsmkkkasqtnnpleslfggaipnf 165
Cdd:COG1219  141 DATTLTEAGYVGEDVENI-------------------------------LLKLL-------------------------- 163

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616269681 166 gQNnedeeeppteeiktkrseikrqleegklekekvrikveqdpgalgmlgtnqnqqmqemmnqlmpkkkverevaveta 245
Cdd:COG1219  164 -QA----------------------------------------------------------------------------- 165

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616269681 246 rkilADsYadeliDQESAnqealelaeQMGIIFIDEIDKVA--TNNHNSGQDVSRQGVQRDILPILEGSVI--------- 314
Cdd:COG1219  166 ----AD-Y-----DVEKA---------ERGIIYIDEIDKIArkSENPSITRDVSGEGVQQALLKILEGTVAnvppqggrk 226

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616269681 315 --QTKYGTVNTEHMLFIGAGAF-----HVSK-----------------------------PSDL-----IPELQGRFPIR 353
Cdd:COG1219  227 hpQQEFIQIDTTNILFICGGAFdglekIIERrlgkksigfgaevkskkekdegellkqvePEDLikfglIPEFIGRLPVI 306

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616269681 354 VELDSLSVEDFVRILTEPKLSLIKQYEALLQTEEVTVNFTDEAITRLAEIAYQvnqdtDNIGARRLHTILEKMLEDLSFE 433
Cdd:COG1219  307 ATLEELDEEALVRILTEPKNALVKQYQKLFEMDGVELEFTDEALEAIAKKAIE-----RKTGARGLRSILEEILLDVMYE 381

                        490       500
                 ....*....|....*....|....
gi 616269681 434 APSMPNAV-VDITPQYVDDKLKSI 456
Cdd:COG1219  382 LPSRKDVKkVVITKEVVEGKAKPI 405
clpX PRK05342
ATP-dependent Clp protease ATP-binding subunit ClpX;
8-456 3.20e-61

ATP-dependent Clp protease ATP-binding subunit ClpX;


Pssm-ID: 235422 [Multi-domain]  Cd Length: 412  Bit Score: 205.01  E-value: 3.20e-61
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616269681   8 LTPKEIVSKLNEYIVGQNDAKRKVAIALRNRYRR--SLLDEESKQEISPKNILMIGPTGVGKTEIARRMAKVVGAPFIKV 85
Cdd:PRK05342  60 PTPKEIKAHLDQYVIGQERAKKVLSVAVYNHYKRlrHGDKKDDDVELQKSNILLIGPTGSGKTLLAQTLARILDVPFAIA 139

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616269681  86 EATKFTEVGYVGRDVESMvrdlvdvsvrlvkaqkkslvqdeatakanekLVKLLvpsmkkkasqtnnpleslfggaipnf 165
Cdd:PRK05342 140 DATTLTEAGYVGEDVENI-------------------------------LLKLL-------------------------- 162

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616269681 166 gQNnedeeeppteeiktkrseikrqleegklekekvrikveqdpgalgmlgtnqnqqmqemmnqlmpkkkverevaveta 245
Cdd:PRK05342 163 -QA----------------------------------------------------------------------------- 164

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616269681 246 rkilADsYadeliDQESAnqealelaeQMGIIFIDEIDKVATNNHNSG--QDVSRQGVQRDILPILEGSVI--------- 314
Cdd:PRK05342 165 ----AD-Y-----DVEKA---------QRGIVYIDEIDKIARKSENPSitRDVSGEGVQQALLKILEGTVAsvppqggrk 225

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616269681 315 --QTKYGTVNTEHMLFIGAGAF------------------------------------HVsKPSDL-----IPELQGRFP 351
Cdd:PRK05342 226 hpQQEFIQVDTTNILFICGGAFdglekiikqrlgkkgigfgaevkskkekrtegellkQV-EPEDLikfglIPEFIGRLP 304

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616269681 352 IRVELDSLSVEDFVRILTEPKLSLIKQYEALLQTEEVTVNFTDEAITRLAEIAYQvnqdtDNIGARRLHTILEKMLEDLS 431
Cdd:PRK05342 305 VVATLEELDEEALVRILTEPKNALVKQYQKLFEMDGVELEFTDEALEAIAKKAIE-----RKTGARGLRSILEEILLDVM 379

                        490       500
                 ....*....|....*....|....*.
gi 616269681 432 FEAPSMPNAV-VDITPQYVDDKLKSI 456
Cdd:PRK05342 380 FELPSREDVEkVVITKEVVEGKAKPL 405
clpX TIGR00382
endopeptidase Clp ATP-binding regulatory subunit (clpX); A member of the ATP-dependent ...
 9-454 5.65e-42

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: 153.77  E-value: 5.65e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616269681    9 TPKEIVSKLNEYIVGQNDAKRKVAIALRNRYRRSLLDEESKQ----EISPKNILMIGPTGVGKTEIARRMAKVVGAPFIK 84
Cdd:TIGR00382  67 TPKEIKAHLDEYVIGQEQAKKVLSVAVYNHYKRLNFEKNKKSdngvELSKSNILLIGPTGSGKTLLAQTLARILNVPFAI 146

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616269681   85 VEATKFTEVGYVGRDVESMvrdlvdvsvrlvkaqkkslvqdeatakanekLVKLLvpsmkkkasqtnnpleslfggaipn 164
Cdd:TIGR00382 147 ADATTLTEAGYVGEDVENI-------------------------------LLKLL------------------------- 170

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616269681  165 fgqnnedeeeppteeiktkrseikrQLEEGKLEKekvrikveqdpgalgmlgtnqnqqmqemmnqlmpkkkverevavet 244
Cdd:TIGR00382 171 -------------------------QAADYDVEK---------------------------------------------- 179

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616269681  245 arkiladsyadelidqesanqealelaEQMGIIFIDEIDKVATNNHNSG--QDVSRQGVQRDILPILEGSVI-------- 314
Cdd:TIGR00382 180 ---------------------------AQKGIIYIDEIDKISRKSENPSitRDVSGEGVQQALLKIIEGTVAnvppqggr 232

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616269681  315 ---QTKYGTVNTEHMLFIGAGAF---------------------------------HVSKPSD-----LIPELQGRFPIR 353
Cdd:TIGR00382 233 khpYQEFIQIDTSNILFICGGAFvglekiikkrtgkssigfgaevkkkskekadllRQVEPEDlvkfgLIPEFIGRLPVI 312

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616269681  354 VELDSLSVEDFVRILTEPKLSLIKQYEALLQTEEVTVNFTDEAITRLAEIAYQvnqdtDNIGARRLHTILEKMLEDLSFE 433
Cdd:TIGR00382 313 ATLEKLDEEALIAILTKPKNALVKQYQALFKMDNVELDFEEEALKAIAKKALE-----RKTGARGLRSIVEGLLLDVMFD 387

                         490       500
                  ....*....|....*....|..
gi 616269681  434 APSMPNAV-VDITPQYVDDKLK 454
Cdd:TIGR00382 388 LPSLEDLEkVVITKETVLKQSE 409
RecA-like_ClpX cd19497
ATP-dependent Clp protease ATP-binding subunit ClpX; ClpX is a component of the ATP-dependent ...
 8-356 1.72e-29

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: 115.78  E-value: 1.72e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616269681   8 LTPKEIVSKLNEYIVGQNDAKRKVAIALRNRYRRsLLDEESKQ----EISPKNILMIGPTGVGKTEIARRMAKVVGAPFI 83
Cdd:cd19497    1 PTPKEIKEHLDKYVIGQERAKKVLSVAVYNHYKR-IRNNLKQKdddvELEKSNILLIGPTGSGKTLLAQTLAKILDVPFA 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616269681  84 KVEATKFTEVGYVGRDVESMvrdlvdvsvrlvkaqkkslvqdeatakanekLVKLLvpsmkkkasqtnnpleslfggaip 163
Cdd:cd19497   80 IADATTLTEAGYVGEDVENI-------------------------------LLKLL------------------------ 104

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616269681 164 nfgQNnedeeeppteeiktkrseikrqleegklekekvrikveqdpgalgmlgtnqnqqmqemmnqlmpkkkverevave 243
Cdd:cd19497  105 ---QA--------------------------------------------------------------------------- 106

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616269681 244 tarkilADsyadelIDQESAnqealelaeQMGIIFIDEIDKVATNNHNSGQ--DVSRQGVQRDILPILEGSVI------- 314
Cdd:cd19497  107 ------AD------YDVERA---------QRGIVYIDEIDKIARKSENPSItrDVSGEGVQQALLKILEGTVAnvppqgg 165

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616269681 315 ----QTKYGTVNTEHMLFIGAGAF-----HVSK------------------------------PSDL-----IPELQGRF 350
Cdd:cd19497  166 rkhpQQEFIQVDTTNILFICGGAFvglekIIARrlgkkslgfgaetssekdekerdellskvePEDLikfglIPEFVGRL 245


                 ....*.
gi 616269681 351 PIRVEL 356
Cdd:cd19497  246 PVIVTL 251
AAA_2 pfam07724
AAA domain (Cdc48 subfamily); This Pfam entry includes some of the AAA proteins not detected ...
 237-353 1.78e-21

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: 91.10  E-value: 1.78e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616269681  237 EREVAVETARKILADSYADELIDqesaNQEALELAEQMG------------IIFIDEIDKVATnnhnsgqdvsrqGVQRD 304
Cdd:pfam07724  31 ERALIRIDMSEYMEEHSVSRLIG----APPGYVGYEEGGqlteavrrkpysIVLIDEIEKAHP------------GVQND 94

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 616269681  305 ILPILEGSVIQTKYG-TVNTEHMLFIGAGAFHVSKPSD------------------------LIPELQGRFPIR 353
Cdd:pfam07724  95 LLQILEGGTLTDKQGrTVDFKNTLFIMTGNFGSEKISDasrlgdspdyellkeevmdllkkgFIPEFLGRLPII 168
ClpB_D2-small smart01086
C-terminal, D2-small domain, of ClpB protein; This is the C-terminal domain of ClpB protein, ...
 359-436 1.20e-14

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: 69.01  E-value: 1.20e-14
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 616269681   359 LSVEDFVRILTEPKLSLIKQYEallqTEEVTVNFTDEAITRLAEIAYQVNqdtdnIGARRLHTILEKMLEDLSFEAPS 436
Cdd:smart01086   1 LDKEDLVRIVDLPLNALQKRLA----EKGITLEFTDEALDWLAEKGYDPK-----YGARPLRRIIQRELEDPLAELIL 69
RecA-like_protease cd19481
proteases similar to RecA; RecA-like NTPases. This family includes the NTP binding domain of ...
 27-107 9.03e-11

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: 59.99  E-value: 9.03e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616269681  27 AKRKVAIALRNRYRRSllDEESKQEISPKNILMIGPTGVGKTEIARRMAKVVGAPFIKVEATKFTE--VGYVGRDVESMV 104
Cdd:cd19481    1 LKASLREAVEAPRRGS--RLRRYGLGLPKGILLYGPPGTGKTLLAKALAGELGLPLIVVKLSSLLSkyVGESEKNLRKIF 78


                 ...
gi 616269681 105 RDL 107
Cdd:cd19481   79 ERA 81
AAA cd00009
The AAA+ (ATPases Associated with a wide variety of cellular Activities) superfamily ...
 22-139 2.91e-08

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: 52.92  E-value: 2.91e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616269681  22 VGQNDAKRKVAIALRNRyrrslldeeskqeiSPKNILMIGPTGVGKTEIARRMAK---VVGAPFIKVEATKFTEVGYVGR 98
Cdd:cd00009    1 VGQEEAIEALREALELP--------------PPKNLLLYGPPGTGKTTLARAIANelfRPGAPFLYLNASDLLEGLVVAE 66

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 616269681  99 DVESMVRDLvdVSVRLVKAQKKSLVQDEA---TAKANEKLVKLL 139
Cdd:cd00009   67 LFGHFLVRL--LFELAEKAKPGVLFIDEIdslSRGAQNALLRVL 108
RecA-like_ClpB_Hsp104-like cd19499
Chaperone protein ClpB/Hsp104 subfamily; Bacterial Caseinolytic peptidase B (ClpB) and ...
 11-102 5.56e-08

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: 52.56  E-value: 5.56e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616269681  11 KEIVSKLNEYIVGQNDAKRKVAIALRnRYRRSLLDEESKqeisPKNILMIGPTGVGKTEIARRMAKVV---GAPFIKVEA 87
Cdd:cd19499    3 LNLEERLHERVVGQDEAVKAVSDAIR-RARAGLSDPNRP----IGSFLFLGPTGVGKTELAKALAELLfgdEDNLIRIDM 77

                         90
                 ....*....|....*
gi 616269681  88 TKFTEVGYVGRDVES 102
Cdd:cd19499   78 SEYMEKHSVSRLIGA 92
AAA pfam00004
ATPase family associated with various cellular activities (AAA); AAA family proteins often ...
 265-357 8.75e-08

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: 50.67  E-value: 8.75e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616269681  265 QEALELAEQMG--IIFIDEIDKVATNNHNSGQDVSRQgVQRDILPILEGsviqtkyGTVNTEHMLFIGAGafhvSKPSDL 342
Cdd:pfam00004  47 RELFEAAKKLApcVIFIDEIDALAGSRGSGGDSESRR-VVNQLLTELDG-------FTSSNSKVIVIAAT----NRPDKL 114

                          90
                  ....*....|....*
gi 616269681  343 IPELQGRFPIRVELD 357
Cdd:pfam00004 115 DPALLGRFDRIIEFP 129
RecA-like_protease cd19481
proteases similar to RecA; RecA-like NTPases. This family includes the NTP binding domain of ...
 247-356 6.08e-07

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: 49.20  E-value: 6.08e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616269681 247 KILADSYADELIDQESAN-QEALELAEQM--GIIFIDEIDKVATNNHNSGQDVSRQGVQRDILPILEgsviqtkyGTVNT 323
Cdd:cd19481   56 VVKLSSLLSKYVGESEKNlRKIFERARRLapCILFIDEIDAIGRKRDSSGESGELRRVLNQLLTELD--------GVNSR 127

                         90       100       110
                 ....*....|....*....|....*....|....*
gi 616269681 324 EHMLFIGAGAFhvskPSDLIPELQ--GRFPIRVEL 356
Cdd:cd19481  128 SKVLVIAATNR----PDLLDPALLrpGRFDEVIEF 158
RecA-like_FtsH cd19501
ATP-dependent zinc metalloprotease FtsH; FtsH ATPase is a processive, ATP-dependent zinc ...
 54-107 2.83e-06

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


Pssm-ID: 410909 [Multi-domain]  Cd Length: 171  Bit Score: 47.23  E-value: 2.83e-06
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....
gi 616269681  54 PKNILMIGPTGVGKTEIARRMAKVVGAPFIKVEATKFTEVgYVGRDVeSMVRDL 107
Cdd:cd19501   37 PKGVLLVGPPGTGKTLLAKAVAGEAGVPFFSISGSDFVEM-FVGVGA-SRVRDL 88
RPT1 COG1222
ATP-dependent 26S proteasome regulatory subunit [Posttranslational modification, protein ...
 10-109 3.20e-06

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


Pssm-ID: 440835 [Multi-domain]  Cd Length: 326  Bit Score: 48.85  E-value: 3.20e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616269681  10 PKEIVSKLNEYIVGQNDAKRKVAIALRNRYRRSLLDEESKQEIsPKNILMIGPTGVGKTEIARRMAKVVGAPFIKVEATK 89
Cdd:COG1222   69 PAESPDVTFDDIGGLDEQIEEIREAVELPLKNPELFRKYGIEP-PKGVLLYGPPGTGKTLLAKAVAGELGAPFIRVRGSE 147

                         90       100
                 ....*....|....*....|
gi 616269681  90 FTEvGYVGrDVESMVRDLVD 109
Cdd:COG1222  148 LVS-KYIG-EGARNVREVFE 165
MoxR COG0714
MoxR-like ATPase [General function prediction only]; MoxR-like ATPase is part of the Pathway ...
 9-88 3.89e-06

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


Pssm-ID: 440478 [Multi-domain]  Cd Length: 292  Bit Score: 48.63  E-value: 3.89e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616269681   9 TPKEIVSKLNEYIVGQNDAKRKVAIALRNRyrrslldeeskqeispKNILMIGPTGVGKTEIARRMAKVVGAPFIKVEAT 88
Cdd:COG0714    2 TEARLRAEIGKVYVGQEELIELVLIALLAG----------------GHLLLEGVPGVGKTTLAKALARALGLPFIRIQFT 65
SpoVK COG0464
AAA+-type ATPase, SpoVK/Ycf46/Vps4 family [Cell wall/membrane/envelope biogenesis, Cell cycle ...
 21-97 7.84e-06

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: 47.98  E-value: 7.84e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616269681  21 IVGQNDAKRkvaiALRNRYRRSLLDEESKQEIS---PKNILMIGPTGVGKTEIARRMAKVVGAPFIKVEATKFTEvGYVG 97
Cdd:COG0464  159 LGGLEEVKE----ELRELVALPLKRPELREEYGlppPRGLLLYGPPGTGKTLLARALAGELGLPLIEVDLSDLVS-KYVG 233
AAA pfam00004
ATPase family associated with various cellular activities (AAA); AAA family proteins often ...
 57-109 3.53e-05

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: 43.35  E-value: 3.53e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 616269681   57 ILMIGPTGVGKTEIARRMAKVVGAPFIKVEATKFTEvGYVGrDVESMVRDLVD 109
Cdd:pfam00004   1 LLLYGPPGTGKTTLAKAVAKELGAPFIEISGSELVS-KYVG-ESEKRLRELFE 51
RecA-like_NVL_r1-like cd19518
first of two ATPase domains of NVL (nuclear VCP-like protein) and similar ATPase domains; NVL ...
 54-114 3.91e-05

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


Pssm-ID: 410926 [Multi-domain]  Cd Length: 169  Bit Score: 43.93  E-value: 3.91e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 616269681  54 PKNILMIGPTGVGKTEIARRMAKVVGAPFIKVEATKFteVGYVGRDVESMVRDLVDVSVRL 114
Cdd:cd19518   34 PRGVLLHGPPGCGKTMLANAIAGELKVPFLKISATEI--VSGVSGESEEKIRELFDQAISN 92
RecA-like_Figl-1 cd19525
ATPase domain of Fidgetin-Like 1 (FIGL-1); FIGL-1 may participate in DNA repair in the nucleus; ...
 54-111 4.25e-05

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


Pssm-ID: 410933 [Multi-domain]  Cd Length: 186  Bit Score: 44.21  E-value: 4.25e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 616269681  54 PKNILMIGPTGVGKTEIARRMAKVVGAPFIKVEATKFTEvGYVGRDvESMVRDLVDVS 111
Cdd:cd19525   55 PKGILLFGPPGTGKTLIGKCIASQSGATFFSISASSLTS-KWVGEG-EKMVRALFSVA 110
ftsH CHL00176
cell division protein; Validated
 54-107 6.54e-05

cell division protein; Validated


Pssm-ID: 214386 [Multi-domain]  Cd Length: 638  Bit Score: 45.43  E-value: 6.54e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 616269681  54 PKNILMIGPTGVGKTEIARRMAKVVGAPFIKVEATKFTE--VGyVGrdvESMVRDL 107
Cdd:CHL00176 216 PKGVLLVGPPGTGKTLLAKAIAGEAEVPFFSISGSEFVEmfVG-VG---AARVRDL 267
RecA-like_CDC48_NLV2_r1-like cd19503
first of two ATPase domains of CDC48 and NLV2, and similar ATPase domains; CDC48 in yeast and ...
 54-107 7.38e-05

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


Pssm-ID: 410911 [Multi-domain]  Cd Length: 165  Bit Score: 43.05  E-value: 7.38e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....
gi 616269681  54 PKNILMIGPTGVGKTEIARRMAKVVGAPFIKVEATKFTEvGYVGrDVESMVRDL 107
Cdd:cd19503   34 PRGVLLHGPPGTGKTLLARAVANEAGANFLSISGPSIVS-KYLG-ESEKNLREI 85
RecA-like_PAN_like cd19502
proteasome activating nucleotidase PAN and related proteasome subunits; This subfamily ...
 54-107 9.38e-05

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: 43.09  E-value: 9.38e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....
gi 616269681  54 PKNILMIGPTGVGKTEIARRMAKVVGAPFIKVEATKFTEvGYVGrDVESMVRDL 107
Cdd:cd19502   37 PKGVLLYGPPGTGKTLLAKAVANHTDATFIRVVGSELVQ-KYIG-EGARLVREL 88
hflB PRK10733
ATP-dependent zinc metalloprotease FtsH;
54-109 1.71e-04

ATP-dependent zinc metalloprotease FtsH;


Pssm-ID: 182683 [Multi-domain]  Cd Length: 644  Bit Score: 44.25  E-value: 1.71e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 616269681  54 PKNILMIGPTGVGKTEIARRMAKVVGAPFIKVEATKFTEVgYVGRDVeSMVRDLVD 109
Cdd:PRK10733 185 PKGVLMVGPPGTGKTLLAKAIAGEAKVPFFTISGSDFVEM-FVGVGA-SRVRDMFE 238
RecA-like_VPS4-like cd19509
ATPase domain of VPS4, ATAD1, K, KTNA1, Spastin, FIGL-1 and similar ATPase domains; This ...
 54-110 1.97e-04

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: 41.95  E-value: 1.97e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 616269681  54 PKNILMIGPTGVGKTEIARRMAKVVGAPFIKVEATKFTeVGYVGrDVESMVRDLVDV 110
Cdd:cd19509   32 PRGILLYGPPGTGKTLLARAVASESGSTFFSISASSLV-SKWVG-ESEKIVRALFAL 86
AAA_5 pfam07728
AAA domain (dynein-related subfamily); This Pfam entry includes some of the AAA proteins not ...
 56-123 2.06e-04

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: 41.12  E-value: 2.06e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 616269681   56 NILMIGPTGVGKTEIARRMAK-VVGAPFIKVEATKFTE----VGyvGRDVESMVRDLVDVSvrLVKAQKKSLV 123
Cdd:pfam07728   1 GVLLVGPPGTGKTELAERLAAaLSNRPVFYVQLTRDTTeedlFG--RRNIDPGGASWVDGP--LVRAAREGEI 69
SpoVK COG0464
AAA+-type ATPase, SpoVK/Ycf46/Vps4 family [Cell wall/membrane/envelope biogenesis, Cell cycle ...
 266-368 5.46e-04

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: 42.21  E-value: 5.46e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616269681 266 EALELAEQM--GIIFIDEIDKVATNNHNSGQDVSRQGVQRdILPILEGsviqtkygtvNTEHMLFIGAGAFhvskPSDLI 343
Cdd:COG0464  241 EVFDKARGLapCVLFIDEADALAGKRGEVGDGVGRRVVNT-LLTEMEE----------LRSDVVVIAATNR----PDLLD 305

                         90       100
                 ....*....|....*....|....*
gi 616269681 344 PELQGRFPIRVELDSLSVEDFVRIL 368
Cdd:COG0464  306 PALLRRFDEIIFFPLPDAEERLEIF 330
RecA-like_KTNA1 cd19522
Katanin p60 ATPase-containing subunit A1; Katanin p60 ATPase-containing subunit A1 (KTNA1) is ...
 55-111 5.59e-04

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: 40.74  E-value: 5.59e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 616269681  55 KNILMIGPTGVGKTEIARRMAKVVGAPFIKVEATKFTEvGYVGrDVESMVRDLVDVS 111
Cdd:cd19522   34 KGVLMVGPPGTGKTLLAKAVATECGTTFFNVSSSTLTS-KYRG-ESEKLVRLLFEMA 88
clpC CHL00095
Clp protease ATP binding subunit
 16-76 5.66e-04

Clp protease ATP binding subunit


Pssm-ID: 214361 [Multi-domain]  Cd Length: 821  Bit Score: 42.35  E-value: 5.66e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 616269681  16 KLNEYIVGQNDAKRKVAIALRnRYRRSLldEESKQEISpkNILMIGPTGVGKTEIARRMAK 76
Cdd:CHL00095 506 TLHKRIIGQDEAVVAVSKAIR-RARVGL--KNPNRPIA--SFLFSGPTGVGKTELTKALAS 561
SK cd00464
Shikimate kinase (SK) is the fifth enzyme in the shikimate pathway, a seven-step biosynthetic ...
 56-83 6.92e-04

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: 40.23  E-value: 6.92e-04
                         10        20
                 ....*....|....*....|....*...
gi 616269681  56 NILMIGPTGVGKTEIARRMAKVVGAPFI 83
Cdd:cd00464    1 NIVLIGMMGAGKTTVGRLLAKALGLPFV 28
ClpA COG0542
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ...
 15-75 9.44e-04

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


Pssm-ID: 440308 [Multi-domain]  Cd Length: 836  Bit Score: 41.61  E-value: 9.44e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 616269681  15 SKLNEYIVGQNDAKRKVAIALRnRYRRSLLDEEskqeispKNI---LMIGPTGVGKTEIARRMA 75
Cdd:COG0542  545 EELHERVIGQDEAVEAVADAIR-RSRAGLKDPN-------RPIgsfLFLGPTGVGKTELAKALA 600
AAA smart00382
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ...
 53-140 9.93e-04

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: 39.66  E-value: 9.93e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616269681    53 SPKNILMIGPTGVGKTEIARRMAK---VVGAPFIKVEATKFTEVGYVGRDVESMVRDLVDVSVRlvkaqkksLVQDEATA 129
Cdd:smart00382   1 PGEVILIVGPPGSGKTTLARALARelgPPGGGVIYIDGEDILEEVLDQLLLIIVGGKKASGSGE--------LRLRLALA 72

                           90
                   ....*....|.
gi 616269681   130 KANEKLVKLLV 140
Cdd:smart00382  73 LARKLKPDVLI 83
ClpB_D2-small pfam10431
C-terminal, D2-small domain, of ClpB protein; This is the C-terminal domain of ClpB protein, ...
 359-429 1.04e-03

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: 37.77  E-value: 1.04e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 616269681  359 LSVEDFVRILTEpklsLIKQYEALLQTEEVTVNFTDEAITRLAEIAYQVnqdtdNIGARRLHTILEKMLED 429
Cdd:pfam10431   1 LSKEELRKIVDL----QLKELQKRLAERGITLELTDAAKDWLAEKGYDP-----EYGARPLRRAIQREIED 62
RecA-like_CDC48_r2-like cd19511
second of two ATPase domains of CDC48/p97, PEX1 and -6, VAT and NVL, and similar ATPase ...
 54-109 1.05e-03

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


Pssm-ID: 410919 [Multi-domain]  Cd Length: 159  Bit Score: 39.57  E-value: 1.05e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 616269681  54 PKNILMIGPTGVGKTEIARRMAKVVGAPFIkveATKFTEV--GYVGrDVESMVRDLVD 109
Cdd:cd19511   27 PKGVLLYGPPGCGKTLLAKALASEAGLNFI---SVKGPELfsKYVG-ESERAVREIFQ 80
clpA PRK11034
ATP-dependent Clp protease ATP-binding subunit; Provisional
 11-152 1.40e-03

ATP-dependent Clp protease ATP-binding subunit; Provisional


Pssm-ID: 236828 [Multi-domain]  Cd Length: 758  Bit Score: 41.36  E-value: 1.40e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616269681  11 KEIVSKLNEYIVGQNDAKRKVAIALRnrYRRSLLDEESKQEISpknILMIGPTGVGKTEIARRMAKVVGAPFIKVEATKF 90
Cdd:PRK11034 450 KNLGDRLKMLVFGQDKAIEALTEAIK--MSRAGLGHEHKPVGS---FLFAGPTGVGKTEVTVQLSKALGIELLRFDMSEY 524

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 616269681  91 TE-----------VGYVGRDVESMVRDLVdvsvrlVKAQKKSLVQDEaTAKANEKLVKLLVPSMKKKASQTNN 152
Cdd:PRK11034 525 MErhtvsrligapPGYVGFDQGGLLTDAV------IKHPHAVLLLDE-IEKAHPDVFNLLLQVMDNGTLTDNN 590
aroK PRK00131
shikimate kinase; Reviewed
 54-107 1.64e-03

shikimate kinase; Reviewed


Pssm-ID: 234654 [Multi-domain]  Cd Length: 175  Bit Score: 39.40  E-value: 1.64e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 616269681  54 PKNILMIGPTGVGKTEIARRMAKVVGAPFI----KVEATK-------FTEVGYVG-RDVES-MVRDL 107
Cdd:PRK00131   4 GPNIVLIGFMGAGKSTIGRLLAKRLGYDFIdtdhLIEARAgksipeiFEEEGEAAfRELEEeVLAEL 70
Mg_chelatase pfam01078
Magnesium chelatase, subunit ChlI; Magnesium-chelatase is a three-component enzyme that ...
 21-74 1.71e-03

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: 39.83  E-value: 1.71e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 616269681   21 IVGQNDAKRKVAIALRNRYrrslldeeskqeispkNILMIGPTGVGKTEIARRM 74
Cdd:pfam01078   5 VKGQEQAKRALEIAAAGGH----------------NLLMIGPPGSGKTMLAKRL 42
AAA cd00009
The AAA+ (ATPases Associated with a wide variety of cellular Activities) superfamily ...
 249-358 3.16e-03

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: 38.28  E-value: 3.16e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616269681 249 LADSYADELIDQESANQEALELAEQM--GIIFIDEIDKVatnnhnsgqdvsRQGVQRDILPILEgsviQTKYGTVNTEHM 326
Cdd:cd00009   58 LLEGLVVAELFGHFLVRLLFELAEKAkpGVLFIDEIDSL------------SRGAQNALLRVLE----TLNDLRIDRENV 121

                         90       100       110
                 ....*....|....*....|....*....|..
gi 616269681 327 LFIGAGAFHVskPSDLIPELQGRFPIRVELDS 358
Cdd:cd00009  122 RVIGATNRPL--LGDLDRALYDRLDIRIVIPL 151
PRK13342 PRK13342
recombination factor protein RarA; Reviewed
 59-88 3.70e-03

recombination factor protein RarA; Reviewed


Pssm-ID: 237355 [Multi-domain]  Cd Length: 413  Bit Score: 39.68  E-value: 3.70e-03
                         10        20        30
                 ....*....|....*....|....*....|..
gi 616269681  59 MI--GPTGVGKTEIARRMAKVVGAPFIKVEAT 88
Cdd:PRK13342  39 MIlwGPPGTGKTTLARIIAGATDAPFEALSAV 70
YifB COG0606
Predicted Mg-chelatase, contains ChlI-like and ATPase domains, YifB family [Posttranslational ...
 56-74 3.82e-03

Predicted Mg-chelatase, contains ChlI-like and ATPase domains, YifB family [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 440371 [Multi-domain]  Cd Length: 502  Bit Score: 39.64  E-value: 3.82e-03
                         10
                 ....*....|....*....
gi 616269681  56 NILMIGPTGVGKTEIARRM 74
Cdd:COG0606  213 NLLMIGPPGSGKTMLARRL 231
RecA-like_spastin cd19524
ATPase domain of spastin; Spastin is an ATP-dependent microtubule-severing protein involved in ...
 54-114 4.14e-03

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


Pssm-ID: 410932 [Multi-domain]  Cd Length: 164  Bit Score: 37.91  E-value: 4.14e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 616269681  54 PKNILMIGPTGVGKTEIARRMAKVVGAPFIKVEATKFTEvGYVGrDVESMVRDLVDVSVRL 114
Cdd:cd19524   33 ARGLLLFGPPGNGKTMLAKAVAAESNATFFNISAASLTS-KYVG-EGEKLVRALFAVAREL 91
COG0645 COG0645
Predicted kinase, contains AAA domain [General function prediction only];
57-83 4.80e-03

Predicted kinase, contains AAA domain [General function prediction only];


Pssm-ID: 440410 [Multi-domain]  Cd Length: 164  Bit Score: 37.97  E-value: 4.80e-03
                         10        20
                 ....*....|....*....|....*..
gi 616269681  57 ILMIGPTGVGKTEIARRMAKVVGAPFI 83
Cdd:COG0645    2 ILVCGLPGSGKSTLARALAERLGAVRL 28
Sigma54_activat pfam00158
Sigma-54 interaction domain;
53-85 6.79e-03

Sigma-54 interaction domain;


Pssm-ID: 425491 [Multi-domain]  Cd Length: 168  Bit Score: 37.38  E-value: 6.79e-03
                          10        20        30
                  ....*....|....*....|....*....|....*.
gi 616269681   53 SPKNILMIGPTGVGKTEIARRM---AKVVGAPFIKV 85
Cdd:pfam00158  21 TDAPVLITGESGTGKELFARAIhqlSPRADGPFVAV 56
HflB COG0465
ATP-dependent Zn proteases [Posttranslational modification, protein turnover, chaperones];
54-107 7.28e-03

ATP-dependent Zn proteases [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 440233 [Multi-domain]  Cd Length: 583  Bit Score: 38.86  E-value: 7.28e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 616269681  54 PKNILMIGPTGVGKTEIARRMAKVVGAPFIKVEATKFTE--VGyVGrdvESMVRDL 107
Cdd:COG0465  175 PKGVLLVGPPGTGKTLLAKAVAGEAGVPFFSISGSDFVEmfVG-VG---ASRVRDL 226
RecA-like_VCP_r2 cd19529
second of two ATPase domains of Valosin-containing protein-like ATPase (VAT) and similar ...
 54-85 7.35e-03

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


Pssm-ID: 410937 [Multi-domain]  Cd Length: 159  Bit Score: 37.09  E-value: 7.35e-03
                         10        20        30
                 ....*....|....*....|....*....|..
gi 616269681  54 PKNILMIGPTGVGKTEIARRMAKVVGAPFIKV 85
Cdd:cd19529   27 PKGILLYGPPGTGKTLLAKAVATESNANFISV 58
RecA-like_CDC48_r1-like cd19519
first of two ATPase domains of CDC48 and similar ATPase domains; CDC48 in yeast and p97 or VCP ...
 54-85 7.63e-03

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


Pssm-ID: 410927 [Multi-domain]  Cd Length: 166  Bit Score: 37.42  E-value: 7.63e-03
                         10        20        30
                 ....*....|....*....|....*....|..
gi 616269681  54 PKNILMIGPTGVGKTEIARRMAKVVGAPFIKV 85
Cdd:cd19519   34 PRGILLYGPPGTGKTLIARAVANETGAFFFLI 65
RecA-like_Lon cd19500
lon protease homolog 2 peroxisomal; Lon protease (also known as Lon peptidase) is an ...
 49-85 7.80e-03

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: 37.54  E-value: 7.80e-03
                         10        20        30
                 ....*....|....*....|....*....|....*..
gi 616269681  49 KQEISPKNILMIGPTGVGKTEIARRMAKVVGAPFIKV 85
Cdd:cd19500   32 KGSMKGPILCLVGPPGVGKTSLGKSIARALGRKFVRI 68
 
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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