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Conserved domains on  [gi|1266728268|gb|PHG04726|]
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ATP-dependent protease ATP-binding subunit ClpX [Bacillus toyonensis]

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

CATH:  1.10.8.60
Gene Ontology:  GO:0005524|GO:0004176|GO:0016887|GO:0051082|GO:0008270|GO:0046983
SCOP:  4000283

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 ...
 4-408 0e+00

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


:

Pssm-ID: 440832 [Multi-domain]  Cd Length: 409  Bit Score: 861.66  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1266728268   4 FNDEKGQLKCSFCGKTQTQVRKLVAGPGVYICDECIELCTEIVQEELAKDE-EVEFKDVPKPVEIREILDEYVIGQDNAK 82
Cdd:COG1219     2 AGDSKKELKCSFCGKSQDEVRKLIAGPGVYICDECVELCNEIIEEELKEEEaEEELKKLPKPKEIKAFLDEYVIGQERAK 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1266728268  83 KALAVAVYNHYKRINSNS-KIDDVELAKSNISLIGPTGSGKTLLAQTLARILNVPFAIADATSLTEAGYVGEDVENILLK 161
Cdd:COG1219    82 KVLSVAVYNHYKRLNSGSkDDDDVELEKSNILLIGPTGSGKTLLAQTLARILDVPFAIADATTLTEAGYVGEDVENILLK 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1266728268 162 LIQAADYDVEKAEKGIIYIDEIDKVARKSENPSITRDVSGEGVQQALLKILEGTVASVPPQGGRKHPHQEFIQIDTTNIL 241
Cdd:COG1219   162 LLQAADYDVEKAERGIIYIDEIDKIARKSENPSITRDVSGEGVQQALLKILEGTVANVPPQGGRKHPQQEFIQIDTTNIL 241

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1266728268 242 FICGGAFDGIEPIIKRRLGEKVIGFGSE-KKNADVNEKHVLSHVLPEDLLRFGLIPEFIGRLPVIANLEPLDEDALVDIL 320
Cdd:COG1219   242 FICGGAFDGLEKIIERRLGKKSIGFGAEvKSKKEKDEGELLKQVEPEDLIKFGLIPEFIGRLPVIATLEELDEEALVRIL 321

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1266728268 321 TKPKNALVKQFQKLLELDDVELEFEEGALIEIAKKAIERKTGARGLRSIIEGLMLDVMFELPSRKDIEKCILTKETVADN 400
Cdd:COG1219   322 TEPKNALVKQYQKLFEMDGVELEFTDEALEAIAKKAIERKTGARGLRSILEEILLDVMYELPSRKDVKKVVITKEVVEGK 401


                  ....*...
gi 1266728268 401 EPPKLVLQ 408
Cdd:COG1219   402 AKPILVYK 409
 
Name Accession Description Interval E-value
ClpX COG1219
ATP-dependent protease Clp, ATPase subunit ClpX [Posttranslational modification, protein ...
 4-408 0e+00

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


Pssm-ID: 440832 [Multi-domain]  Cd Length: 409  Bit Score: 861.66  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1266728268   4 FNDEKGQLKCSFCGKTQTQVRKLVAGPGVYICDECIELCTEIVQEELAKDE-EVEFKDVPKPVEIREILDEYVIGQDNAK 82
Cdd:COG1219     2 AGDSKKELKCSFCGKSQDEVRKLIAGPGVYICDECVELCNEIIEEELKEEEaEEELKKLPKPKEIKAFLDEYVIGQERAK 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1266728268  83 KALAVAVYNHYKRINSNS-KIDDVELAKSNISLIGPTGSGKTLLAQTLARILNVPFAIADATSLTEAGYVGEDVENILLK 161
Cdd:COG1219    82 KVLSVAVYNHYKRLNSGSkDDDDVELEKSNILLIGPTGSGKTLLAQTLARILDVPFAIADATTLTEAGYVGEDVENILLK 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1266728268 162 LIQAADYDVEKAEKGIIYIDEIDKVARKSENPSITRDVSGEGVQQALLKILEGTVASVPPQGGRKHPHQEFIQIDTTNIL 241
Cdd:COG1219   162 LLQAADYDVEKAERGIIYIDEIDKIARKSENPSITRDVSGEGVQQALLKILEGTVANVPPQGGRKHPQQEFIQIDTTNIL 241

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1266728268 242 FICGGAFDGIEPIIKRRLGEKVIGFGSE-KKNADVNEKHVLSHVLPEDLLRFGLIPEFIGRLPVIANLEPLDEDALVDIL 320
Cdd:COG1219   242 FICGGAFDGLEKIIERRLGKKSIGFGAEvKSKKEKDEGELLKQVEPEDLIKFGLIPEFIGRLPVIATLEELDEEALVRIL 321

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1266728268 321 TKPKNALVKQFQKLLELDDVELEFEEGALIEIAKKAIERKTGARGLRSIIEGLMLDVMFELPSRKDIEKCILTKETVADN 400
Cdd:COG1219   322 TEPKNALVKQYQKLFEMDGVELEFTDEALEAIAKKAIERKTGARGLRSILEEILLDVMYELPSRKDVKKVVITKEVVEGK 401


                  ....*...
gi 1266728268 401 EPPKLVLQ 408
Cdd:COG1219   402 AKPILVYK 409
clpX PRK05342
ATP-dependent Clp protease ATP-binding subunit ClpX;
3-411 0e+00

ATP-dependent Clp protease ATP-binding subunit ClpX;


Pssm-ID: 235422 [Multi-domain]  Cd Length: 412  Bit Score: 828.26  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1266728268   3 KFNDEKGQLKCSFCGKTQTQVRKLVAGPGVYICDECIELCTEIVQEELaKDEEVEFKDVPKPVEIREILDEYVIGQDNAK 82
Cdd:PRK05342    2 RGGDSKKLLYCSFCGKSQHEVRKLIAGPGVYICDECIELCNEIIREEL-KEEAVELKELPTPKEIKAHLDQYVIGQERAK 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1266728268  83 KALAVAVYNHYKRINSNSKI-DDVELAKSNISLIGPTGSGKTLLAQTLARILNVPFAIADATSLTEAGYVGEDVENILLK 161
Cdd:PRK05342   81 KVLSVAVYNHYKRLRHGDKKdDDVELQKSNILLIGPTGSGKTLLAQTLARILDVPFAIADATTLTEAGYVGEDVENILLK 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1266728268 162 LIQAADYDVEKAEKGIIYIDEIDKVARKSENPSITRDVSGEGVQQALLKILEGTVASVPPQGGRKHPHQEFIQIDTTNIL 241
Cdd:PRK05342  161 LLQAADYDVEKAQRGIVYIDEIDKIARKSENPSITRDVSGEGVQQALLKILEGTVASVPPQGGRKHPQQEFIQVDTTNIL 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1266728268 242 FICGGAFDGIEPIIKRRLGEKVIGFGSE--KKNADVNEKHVLSHVLPEDLLRFGLIPEFIGRLPVIANLEPLDEDALVDI 319
Cdd:PRK05342  241 FICGGAFDGLEKIIKQRLGKKGIGFGAEvkSKKEKRTEGELLKQVEPEDLIKFGLIPEFIGRLPVVATLEELDEEALVRI 320

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1266728268 320 LTKPKNALVKQFQKLLELDDVELEFEEGALIEIAKKAIERKTGARGLRSIIEGLMLDVMFELPSRKDIEKCILTKETVAD 399
Cdd:PRK05342  321 LTEPKNALVKQYQKLFEMDGVELEFTDEALEAIAKKAIERKTGARGLRSILEEILLDVMFELPSREDVEKVVITKEVVEG 400

                         410
                  ....*....|..
gi 1266728268 400 NEPPKLVLQDGT 411
Cdd:PRK05342  401 KAKPLLIYREKS 412
clpX TIGR00382
endopeptidase Clp ATP-binding regulatory subunit (clpX); A member of the ATP-dependent ...
 1-406 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: 676.49  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1266728268   1 MFKFNdekGQLKCSFCGKTQTQVRKLVAGPGVYICDECIELCTEIVQEELAKD-------EEVEFKDVPKPVEIREILDE 73
Cdd:TIGR00382   1 MTKKN---ETLYCSFCGKSQDEVRKLIAGPGVYICDECIELCHDILEEELGTRkeskeyeEEFELSYLPTPKEIKAHLDE 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1266728268  74 YVIGQDNAKKALAVAVYNHYKRIN--SNSKIDD-VELAKSNISLIGPTGSGKTLLAQTLARILNVPFAIADATSLTEAGY 150
Cdd:TIGR00382  78 YVIGQEQAKKVLSVAVYNHYKRLNfeKNKKSDNgVELSKSNILLIGPTGSGKTLLAQTLARILNVPFAIADATTLTEAGY 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1266728268 151 VGEDVENILLKLIQAADYDVEKAEKGIIYIDEIDKVARKSENPSITRDVSGEGVQQALLKILEGTVASVPPQGGRKHPHQ 230
Cdd:TIGR00382 158 VGEDVENILLKLLQAADYDVEKAQKGIIYIDEIDKISRKSENPSITRDVSGEGVQQALLKIIEGTVANVPPQGGRKHPYQ 237

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1266728268 231 EFIQIDTTNILFICGGAFDGIEPIIKRRLGEKVIGFGSEKKNADVNEKHVLSHVLPEDLLRFGLIPEFIGRLPVIANLEP 310
Cdd:TIGR00382 238 EFIQIDTSNILFICGGAFVGLEKIIKKRTGKSSIGFGAEVKKKSKEKADLLRQVEPEDLVKFGLIPEFIGRLPVIATLEK 317

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1266728268 311 LDEDALVDILTKPKNALVKQFQKLLELDDVELEFEEGALIEIAKKAIERKTGARGLRSIIEGLMLDVMFELPSRKDIEKC 390
Cdd:TIGR00382 318 LDEEALIAILTKPKNALVKQYQALFKMDNVELDFEEEALKAIAKKALERKTGARGLRSIVEGLLLDVMFDLPSLEDLEKV 397

                         410
                  ....*....|....*.
gi 1266728268 391 ILTKETVADNEPPKLV 406
Cdd:TIGR00382 398 VITKETVLKQSEPLLI 413
RecA-like_ClpX cd19497
ATP-dependent Clp protease ATP-binding subunit ClpX; ClpX is a component of the ATP-dependent ...
 62-308 1.84e-174

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: 487.11  E-value: 1.84e-174
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1266728268  62 PKPVEIREILDEYVIGQDNAKKALAVAVYNHYKRINSNSKI--DDVELAKSNISLIGPTGSGKTLLAQTLARILNVPFAI 139
Cdd:cd19497     1 PTPKEIKEHLDKYVIGQERAKKVLSVAVYNHYKRIRNNLKQkdDDVELEKSNILLIGPTGSGKTLLAQTLAKILDVPFAI 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1266728268 140 ADATSLTEAGYVGEDVENILLKLIQAADYDVEKAEKGIIYIDEIDKVARKSENPSITRDVSGEGVQQALLKILEGTVASV 219
Cdd:cd19497    81 ADATTLTEAGYVGEDVENILLKLLQAADYDVERAQRGIVYIDEIDKIARKSENPSITRDVSGEGVQQALLKILEGTVANV 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1266728268 220 PPQGGRKHPHQEFIQIDTTNILFICGGAFDGIEPIIKRRLGEKVIGFGSEKKNADVNEK--HVLSHVLPEDLLRFGLIPE 297
Cdd:cd19497   161 PPQGGRKHPQQEFIQVDTTNILFICGGAFVGLEKIIARRLGKKSLGFGAETSSEKDEKErdELLSKVEPEDLIKFGLIPE 240

                         250
                  ....*....|.
gi 1266728268 298 FIGRLPVIANL 308
Cdd:cd19497   241 FVGRLPVIVTL 251
AAA_2 pfam07724
AAA domain (Cdc48 subfamily); This Pfam entry includes some of the AAA proteins not detected ...
 109-305 1.08e-43

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: 150.04  E-value: 1.08e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1266728268 109 KSNISLIGPTGSGKTLLAQTLARILNV---PFAIADATSLTEagyvgedvENILLKLIQAADYDVEKAEKG--------- 176
Cdd:pfam07724   3 IGSFLFLGPTGVGKTELAKALAELLFGderALIRIDMSEYME--------EHSVSRLIGAPPGYVGYEEGGqlteavrrk 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1266728268 177 ---IIYIDEIDKVARksenpsitrdvsgeGVQQALLKILEGTVASvppqggrkhPHQEfIQIDTTNILFICGGAFDGIEP 253
Cdd:pfam07724  75 pysIVLIDEIEKAHP--------------GVQNDLLQILEGGTLT---------DKQG-RTVDFKNTLFIMTGNFGSEKI 130

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1266728268 254 IIKRRLGEkvigfgsekknadvNEKHVLSHVLPEDLLRFGLIPEFIGRLPVI 305
Cdd:pfam07724 131 SDASRLGD--------------SPDYELLKEEVMDLLKKGFIPEFLGRLPII 168
ClpB_D2-small smart01086
C-terminal, D2-small domain, of ClpB protein; This is the C-terminal domain of ClpB protein, ...
 311-389 2.11e-21

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: 87.88  E-value: 2.11e-21
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1266728268  311 LDEDALVDILTKPKNALVKQfqklLELDDVELEFEEGALIEIAKKAIERKTGARGLRSIIEGLMLDVMFELPSRKDIEK 389
Cdd:smart01086   1 LDKEDLVRIVDLPLNALQKR----LAEKGITLEFTDEALDWLAEKGYDPKYGARPLRRIIQRELEDPLAELILSGELKD 75
 
Name Accession Description Interval E-value
ClpX COG1219
ATP-dependent protease Clp, ATPase subunit ClpX [Posttranslational modification, protein ...
 4-408 0e+00

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


Pssm-ID: 440832 [Multi-domain]  Cd Length: 409  Bit Score: 861.66  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1266728268   4 FNDEKGQLKCSFCGKTQTQVRKLVAGPGVYICDECIELCTEIVQEELAKDE-EVEFKDVPKPVEIREILDEYVIGQDNAK 82
Cdd:COG1219     2 AGDSKKELKCSFCGKSQDEVRKLIAGPGVYICDECVELCNEIIEEELKEEEaEEELKKLPKPKEIKAFLDEYVIGQERAK 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1266728268  83 KALAVAVYNHYKRINSNS-KIDDVELAKSNISLIGPTGSGKTLLAQTLARILNVPFAIADATSLTEAGYVGEDVENILLK 161
Cdd:COG1219    82 KVLSVAVYNHYKRLNSGSkDDDDVELEKSNILLIGPTGSGKTLLAQTLARILDVPFAIADATTLTEAGYVGEDVENILLK 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1266728268 162 LIQAADYDVEKAEKGIIYIDEIDKVARKSENPSITRDVSGEGVQQALLKILEGTVASVPPQGGRKHPHQEFIQIDTTNIL 241
Cdd:COG1219   162 LLQAADYDVEKAERGIIYIDEIDKIARKSENPSITRDVSGEGVQQALLKILEGTVANVPPQGGRKHPQQEFIQIDTTNIL 241

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1266728268 242 FICGGAFDGIEPIIKRRLGEKVIGFGSE-KKNADVNEKHVLSHVLPEDLLRFGLIPEFIGRLPVIANLEPLDEDALVDIL 320
Cdd:COG1219   242 FICGGAFDGLEKIIERRLGKKSIGFGAEvKSKKEKDEGELLKQVEPEDLIKFGLIPEFIGRLPVIATLEELDEEALVRIL 321

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1266728268 321 TKPKNALVKQFQKLLELDDVELEFEEGALIEIAKKAIERKTGARGLRSIIEGLMLDVMFELPSRKDIEKCILTKETVADN 400
Cdd:COG1219   322 TEPKNALVKQYQKLFEMDGVELEFTDEALEAIAKKAIERKTGARGLRSILEEILLDVMYELPSRKDVKKVVITKEVVEGK 401


                  ....*...
gi 1266728268 401 EPPKLVLQ 408
Cdd:COG1219   402 AKPILVYK 409
clpX PRK05342
ATP-dependent Clp protease ATP-binding subunit ClpX;
3-411 0e+00

ATP-dependent Clp protease ATP-binding subunit ClpX;


Pssm-ID: 235422 [Multi-domain]  Cd Length: 412  Bit Score: 828.26  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1266728268   3 KFNDEKGQLKCSFCGKTQTQVRKLVAGPGVYICDECIELCTEIVQEELaKDEEVEFKDVPKPVEIREILDEYVIGQDNAK 82
Cdd:PRK05342    2 RGGDSKKLLYCSFCGKSQHEVRKLIAGPGVYICDECIELCNEIIREEL-KEEAVELKELPTPKEIKAHLDQYVIGQERAK 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1266728268  83 KALAVAVYNHYKRINSNSKI-DDVELAKSNISLIGPTGSGKTLLAQTLARILNVPFAIADATSLTEAGYVGEDVENILLK 161
Cdd:PRK05342   81 KVLSVAVYNHYKRLRHGDKKdDDVELQKSNILLIGPTGSGKTLLAQTLARILDVPFAIADATTLTEAGYVGEDVENILLK 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1266728268 162 LIQAADYDVEKAEKGIIYIDEIDKVARKSENPSITRDVSGEGVQQALLKILEGTVASVPPQGGRKHPHQEFIQIDTTNIL 241
Cdd:PRK05342  161 LLQAADYDVEKAQRGIVYIDEIDKIARKSENPSITRDVSGEGVQQALLKILEGTVASVPPQGGRKHPQQEFIQVDTTNIL 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1266728268 242 FICGGAFDGIEPIIKRRLGEKVIGFGSE--KKNADVNEKHVLSHVLPEDLLRFGLIPEFIGRLPVIANLEPLDEDALVDI 319
Cdd:PRK05342  241 FICGGAFDGLEKIIKQRLGKKGIGFGAEvkSKKEKRTEGELLKQVEPEDLIKFGLIPEFIGRLPVVATLEELDEEALVRI 320

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1266728268 320 LTKPKNALVKQFQKLLELDDVELEFEEGALIEIAKKAIERKTGARGLRSIIEGLMLDVMFELPSRKDIEKCILTKETVAD 399
Cdd:PRK05342  321 LTEPKNALVKQYQKLFEMDGVELEFTDEALEAIAKKAIERKTGARGLRSILEEILLDVMFELPSREDVEKVVITKEVVEG 400

                         410
                  ....*....|..
gi 1266728268 400 NEPPKLVLQDGT 411
Cdd:PRK05342  401 KAKPLLIYREKS 412
clpX TIGR00382
endopeptidase Clp ATP-binding regulatory subunit (clpX); A member of the ATP-dependent ...
 1-406 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: 676.49  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1266728268   1 MFKFNdekGQLKCSFCGKTQTQVRKLVAGPGVYICDECIELCTEIVQEELAKD-------EEVEFKDVPKPVEIREILDE 73
Cdd:TIGR00382   1 MTKKN---ETLYCSFCGKSQDEVRKLIAGPGVYICDECIELCHDILEEELGTRkeskeyeEEFELSYLPTPKEIKAHLDE 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1266728268  74 YVIGQDNAKKALAVAVYNHYKRIN--SNSKIDD-VELAKSNISLIGPTGSGKTLLAQTLARILNVPFAIADATSLTEAGY 150
Cdd:TIGR00382  78 YVIGQEQAKKVLSVAVYNHYKRLNfeKNKKSDNgVELSKSNILLIGPTGSGKTLLAQTLARILNVPFAIADATTLTEAGY 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1266728268 151 VGEDVENILLKLIQAADYDVEKAEKGIIYIDEIDKVARKSENPSITRDVSGEGVQQALLKILEGTVASVPPQGGRKHPHQ 230
Cdd:TIGR00382 158 VGEDVENILLKLLQAADYDVEKAQKGIIYIDEIDKISRKSENPSITRDVSGEGVQQALLKIIEGTVANVPPQGGRKHPYQ 237

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1266728268 231 EFIQIDTTNILFICGGAFDGIEPIIKRRLGEKVIGFGSEKKNADVNEKHVLSHVLPEDLLRFGLIPEFIGRLPVIANLEP 310
Cdd:TIGR00382 238 EFIQIDTSNILFICGGAFVGLEKIIKKRTGKSSIGFGAEVKKKSKEKADLLRQVEPEDLVKFGLIPEFIGRLPVIATLEK 317

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1266728268 311 LDEDALVDILTKPKNALVKQFQKLLELDDVELEFEEGALIEIAKKAIERKTGARGLRSIIEGLMLDVMFELPSRKDIEKC 390
Cdd:TIGR00382 318 LDEEALIAILTKPKNALVKQYQALFKMDNVELDFEEEALKAIAKKALERKTGARGLRSIVEGLLLDVMFDLPSLEDLEKV 397

                         410
                  ....*....|....*.
gi 1266728268 391 ILTKETVADNEPPKLV 406
Cdd:TIGR00382 398 VITKETVLKQSEPLLI 413
RecA-like_ClpX cd19497
ATP-dependent Clp protease ATP-binding subunit ClpX; ClpX is a component of the ATP-dependent ...
 62-308 1.84e-174

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: 487.11  E-value: 1.84e-174
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1266728268  62 PKPVEIREILDEYVIGQDNAKKALAVAVYNHYKRINSNSKI--DDVELAKSNISLIGPTGSGKTLLAQTLARILNVPFAI 139
Cdd:cd19497     1 PTPKEIKEHLDKYVIGQERAKKVLSVAVYNHYKRIRNNLKQkdDDVELEKSNILLIGPTGSGKTLLAQTLAKILDVPFAI 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1266728268 140 ADATSLTEAGYVGEDVENILLKLIQAADYDVEKAEKGIIYIDEIDKVARKSENPSITRDVSGEGVQQALLKILEGTVASV 219
Cdd:cd19497    81 ADATTLTEAGYVGEDVENILLKLLQAADYDVERAQRGIVYIDEIDKIARKSENPSITRDVSGEGVQQALLKILEGTVANV 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1266728268 220 PPQGGRKHPHQEFIQIDTTNILFICGGAFDGIEPIIKRRLGEKVIGFGSEKKNADVNEK--HVLSHVLPEDLLRFGLIPE 297
Cdd:cd19497   161 PPQGGRKHPQQEFIQVDTTNILFICGGAFVGLEKIIARRLGKKSLGFGAETSSEKDEKErdELLSKVEPEDLIKFGLIPE 240

                         250
                  ....*....|.
gi 1266728268 298 FIGRLPVIANL 308
Cdd:cd19497   241 FVGRLPVIVTL 251
hslU PRK05201
ATP-dependent protease ATPase subunit HslU;
64-399 1.28e-53

ATP-dependent protease ATPase subunit HslU;


Pssm-ID: 235364 [Multi-domain]  Cd Length: 443  Bit Score: 184.51  E-value: 1.28e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1266728268  64 PVEIREILDEYVIGQDNAKKALAVAVYNHYKRINSNSKIDDvELAKSNISLIGPTGSGKTLLAQTLARILNVPFAIADAT 143
Cdd:PRK05201    6 PREIVSELDKYIIGQDDAKRAVAIALRNRWRRMQLPEELRD-EVTPKNILMIGPTGVGKTEIARRLAKLANAPFIKVEAT 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1266728268 144 SLTEAGYVGEDVENI-----------------------------------LL---------------------------- 160
Cdd:PRK05201   85 KFTEVGYVGRDVESIirdlveiavkmvreekrekvrekaeeaaeerildaLLppaknnwgeeeekeeisatrqkfrkklr 164

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1266728268 161 -------------------------------------------------------------------KLIqaaDYD---- 169
Cdd:PRK05201  165 egelddkeieievaeaapmmeimgppgmeemtiqlqdmfgnlgpkkkkkrklkvkearkilieeeaaKLI---DMEeikq 241

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1266728268 170 --VEKAEK-GIIYIDEIDKVARKSENPSitRDVSGEGVQQALLKILEGTVASVppqggrKHPhqefiQIDTTNILFICGG 246
Cdd:PRK05201  242 eaIERVEQnGIVFIDEIDKIAARGGSSG--PDVSREGVQRDLLPLVEGSTVST------KYG-----MVKTDHILFIASG 308

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1266728268 247 AFdgiepiikrrlgekvigfgsekknadvnekHVLShvlPEDllrfgLIPEFIGRLPVIANLEPLDEDALVDILTKPKNA 326
Cdd:PRK05201  309 AF------------------------------HVSK---PSD-----LIPELQGRFPIRVELDALTEEDFVRILTEPKAS 350

                         410       420       430       440       450       460       470
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1266728268 327 LVKQFQKLLELDDVELEFEEGALIEIAKKAIE--RKT---GARGLRSIIEGLMLDVMFELPSRKDiEKCILTKETVAD 399
Cdd:PRK05201  351 LIKQYQALLATEGVTLEFTDDAIRRIAEIAYQvnEKTeniGARRLHTVMEKLLEDISFEAPDMSG-ETVTIDAAYVDE 427
HslU COG1220
ATP-dependent protease HslVU (ClpYQ), ATPase subunit HslU [Posttranslational modification, ...
 64-397 2.39e-50

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


Pssm-ID: 440833 [Multi-domain]  Cd Length: 454  Bit Score: 176.01  E-value: 2.39e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1266728268  64 PVEIREILDEYVIGQDNAKKALAVAVYNHYKRINSNSKIDDvELAKSNISLIGPTGSGKTLLAQTLARILNVPFAIADAT 143
Cdd:COG1220     6 PREIVAELDKYIIGQDEAKRAVAIALRNRWRRQQLPEELRD-EITPKNILMIGPTGVGKTEIARRLAKLANAPFIKVEAT 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1266728268 144 SLTEAGYVGEDVE-----------------------------------NILL---------------------------- 160
Cdd:COG1220    85 KFTEVGYVGRDVEsmirdlveiavkmvreekmekvrekaeeaaeerilDLLLpppkkkagsnnpfeeeeeeeeeeeeisr 164

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1266728268 161 ------------------------------------------------------------------------------KL 162
Cdd:COG1220   165 trekfrkklregelddreieieveessspgveimgppgmeemgmnlqdmfgnlmpkkkkkrkvkvkearkiltqeeaaKL 244

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1266728268 163 IqaaDYD------VEKAEK-GIIYIDEIDKVARKSENPSItrDVSGEGVQQALLKILEGTVASVppqggrKHPhqefiQI 235
Cdd:COG1220   245 I---DMDevkqeaIERAEQnGIIFIDEIDKIASRGGGSGP--DVSREGVQRDLLPIVEGSTVNT------KYG-----MV 308

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1266728268 236 DTTNILFICGGAFdgiepiikrrlgekvigfgsekknadvnekHVLShvlPEDllrfgLIPEFIGRLPVIANLEPLDEDA 315
Cdd:COG1220   309 KTDHILFIAAGAF------------------------------HVSK---PSD-----LIPELQGRFPIRVELDSLTEED 350

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1266728268 316 LVDILTKPKNALVKQFQKLLELDDVELEFEEGALIEIAKKAIE--RKT---GARGLRSIIEGLMLDVMFELPSRKDiEKC 390
Cdd:COG1220   351 FVRILTEPKNALTKQYQALLATEGVELEFTDDAIREIAEIAFEvnERTeniGARRLHTVMEKLLEDISFEAPDLSG-KTV 429


                  ....*..
gi 1266728268 391 ILTKETV 397
Cdd:COG1220   430 VIDAAYV 436
RecA-like_HslU cd19498
ATP-dependent protease ATPase subunit HslU; HslU is a component of the ATP-dependent protease ...
 63-253 7.15e-46

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: 156.39  E-value: 7.15e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1266728268  63 KPVEIREILDEYVIGQDNAKKALAVAVYNHYKRINSNSKIDDvELAKSNISLIGPTGSGKTLLAQTLARILNVPFAIADA 142
Cdd:cd19498     1 TPREIVSELDKYIIGQDEAKRAVAIALRNRWRRMQLPEELRD-EVTPKNILMIGPTGVGKTEIARRLAKLAGAPFIKVEA 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1266728268 143 TSLTEAGYVGEDVENILLKLIqaadydvekaeKGIIYIDEIDKVARKSEnpSITRDVSGEGVQQALLKILEGTVASVppq 222
Cdd:cd19498    80 TKFTEVGYVGRDVESIIRDLV-----------EGIVFIDEIDKIAKRGG--SSGPDVSREGVQRDLLPIVEGSTVST--- 143

                         170       180       190
                  ....*....|....*....|....*....|.
gi 1266728268 223 ggrkhphqEFIQIDTTNILFICGGAFDGIEP 253
Cdd:cd19498   144 --------KYGPVKTDHILFIAAGAFHVAKP 166
AAA_2 pfam07724
AAA domain (Cdc48 subfamily); This Pfam entry includes some of the AAA proteins not detected ...
 109-305 1.08e-43

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: 150.04  E-value: 1.08e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1266728268 109 KSNISLIGPTGSGKTLLAQTLARILNV---PFAIADATSLTEagyvgedvENILLKLIQAADYDVEKAEKG--------- 176
Cdd:pfam07724   3 IGSFLFLGPTGVGKTELAKALAELLFGderALIRIDMSEYME--------EHSVSRLIGAPPGYVGYEEGGqlteavrrk 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1266728268 177 ---IIYIDEIDKVARksenpsitrdvsgeGVQQALLKILEGTVASvppqggrkhPHQEfIQIDTTNILFICGGAFDGIEP 253
Cdd:pfam07724  75 pysIVLIDEIEKAHP--------------GVQNDLLQILEGGTLT---------DKQG-RTVDFKNTLFIMTGNFGSEKI 130

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1266728268 254 IIKRRLGEkvigfgsekknadvNEKHVLSHVLPEDLLRFGLIPEFIGRLPVI 305
Cdd:pfam07724 131 SDASRLGD--------------SPDYELLKEEVMDLLKKGFIPEFLGRLPII 168
ClpB_D2-small smart01086
C-terminal, D2-small domain, of ClpB protein; This is the C-terminal domain of ClpB protein, ...
 311-389 2.11e-21

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: 87.88  E-value: 2.11e-21
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1266728268  311 LDEDALVDILTKPKNALVKQfqklLELDDVELEFEEGALIEIAKKAIERKTGARGLRSIIEGLMLDVMFELPSRKDIEK 389
Cdd:smart01086   1 LDKEDLVRIVDLPLNALQKR----LAEKGITLEFTDEALDWLAEKGYDPKYGARPLRRIIQRELEDPLAELILSGELKD 75
zf-C4_ClpX smart00994
ClpX C4-type zinc finger; The ClpX heat shock protein of Escherichia coli is a member of the ...
 11-49 6.47e-20

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: 82.23  E-value: 6.47e-20
                           10        20        30
                   ....*....|....*....|....*....|....*....
gi 1266728268   11 LKCSFCGKTQTQVRKLVAGPGVYICDECIELCTEIVQEE 49
Cdd:smart00994   1 LRCSFCGKSESEVRKLIAGPGVYICDECVELCYEILEEE 39
zf-C4_ClpX pfam06689
ClpX C4-type zinc finger; The ClpX heat shock protein of Escherichia coli is a member of the ...
 11-48 3.19e-19

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: 80.27  E-value: 3.19e-19
                          10        20        30
                  ....*....|....*....|....*....|....*....
gi 1266728268  11 LKCSFCGKTQTQVRKLVAGP-GVYICDECIELCTEIVQE 48
Cdd:pfam06689   1 LRCSFCGKSEDEVKKLIAGPnGVYICDECVELCYEILEE 39
RecA-like_protease cd19481
proteases similar to RecA; RecA-like NTPases. This family includes the NTP binding domain of ...
 81-263 4.91e-18

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: 80.79  E-value: 4.91e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1266728268  81 AKKALAVAVYNHYKRINSNSKiddVELAKSNISLIGPTGSGKTLLAQTLARILNVPFAIADATSLTEAgYVGEDVENiLL 160
Cdd:cd19481     1 LKASLREAVEAPRRGSRLRRY---GLGLPKGILLYGPPGTGKTLLAKALAGELGLPLIVVKLSSLLSK-YVGESEKN-LR 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1266728268 161 KLIQAAdydvEKAEKGIIYIDEIDKVARKSENPSITRDVSgeGVQQALLKILEGTVAsvppqggrkhphqefiqidTTNI 240
Cdd:cd19481    76 KIFERA----RRLAPCILFIDEIDAIGRKRDSSGESGELR--RVLNQLLTELDGVNS-------------------RSKV 130

                         170       180
                  ....*....|....*....|....*.
gi 1266728268 241 LFICGGAF-DGIEPIIKR--RLGEKV 263
Cdd:cd19481   131 LVIAATNRpDLLDPALLRpgRFDEVI 156
AAA pfam00004
ATPase family associated with various cellular activities (AAA); AAA family proteins often ...
 114-267 1.23e-14

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: 70.31  E-value: 1.23e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1266728268 114 LIGPTGSGKTLLAQTLARILNVPFAIADATSLTEaGYVGEDVENIlLKLIQAAdydvEKAEKGIIYIDEIDKVARKSENP 193
Cdd:pfam00004   3 LYGPPGTGKTTLAKAVAKELGAPFIEISGSELVS-KYVGESEKRL-RELFEAA----KKLAPCVIFIDEIDALAGSRGSG 76

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1266728268 194 SitrDVSGEGVQQALLKILEgtvasvppqgGRKHPHQEFIQIDTTNIlficggaFDGIEPIIKRRLgEKVIGFG 267
Cdd:pfam00004  77 G---DSESRRVVNQLLTELD----------GFTSSNSKVIVIAATNR-------PDKLDPALLGRF-DRIIEFP 129
ClpB_D2-small pfam10431
C-terminal, D2-small domain, of ClpB protein; This is the C-terminal domain of ClpB protein, ...
 311-389 1.46e-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, 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: 68.59  E-value: 1.46e-14
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1266728268 311 LDEDALVDILTKpknALVKQFQKLLElDDVELEFEEGALIEIAKKAIERKTGARGLRSIIEGLMLDVMFELPSRKDIEK 389
Cdd:pfam10431   1 LSKEELRKIVDL---QLKELQKRLAE-RGITLELTDAAKDWLAEKGYDPEYGARPLRRAIQREIEDPLAEEILSGELKE 75
AAA cd00009
The AAA+ (ATPases Associated with a wide variety of cellular Activities) superfamily ...
 76-263 3.77e-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: 3.77e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1266728268  76 IGQDNAKKALAVAVYNHYKRinsnskiddvelaksNISLIGPTGSGKTLLAQTLARIL---NVPFAIADATSLTEAGYVG 152
Cdd:cd00009     1 VGQEEAIEALREALELPPPK---------------NLLLYGPPGTGKTTLARAIANELfrpGAPFLYLNASDLLEGLVVA 65

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1266728268 153 EDVENILLKLIQAAdydVEKAEKGIIYIDEIDKVARksenpsitrdvsgeGVQQALLKILEGTVASVPpqggrkhPHQEF 232
Cdd:cd00009    66 ELFGHFLVRLLFEL---AEKAKPGVLFIDEIDSLSR--------------GAQNALLRVLETLNDLRI-------DRENV 121

                         170       180       190
                  ....*....|....*....|....*....|.
gi 1266728268 233 IQIDTTNILFicggaFDGIEPIIKRRLGEKV 263
Cdd:cd00009   122 RVIGATNRPL-----LGDLDRALYDRLDIRI 147
SpoVK COG0464
AAA+-type ATPase, SpoVK/Ycf46/Vps4 family [Cell wall/membrane/envelope biogenesis, Cell cycle ...
 66-214 5.65e-12

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: 66.86  E-value: 5.65e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1266728268  66 EIREILDEYVIGQDNAKKAL--AVAVYNHYKRINSNSKIDdvelAKSNISLIGPTGSGKTLLAQTLARILNVPFAIADAT 143
Cdd:COG0464   150 ELREAILDDLGGLEEVKEELreLVALPLKRPELREEYGLP----PPRGLLLYGPPGTGKTLLARALAGELGLPLIEVDLS 225

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1266728268 144 SLTeAGYVGEDVENIlLKLIQAAdydvEKAEKGIIYIDEIDKVARKSENpsiTRDVSGEGVQQALLKILEG 214
Cdd:COG0464   226 DLV-SKYVGETEKNL-REVFDKA----RGLAPCVLFIDEADALAGKRGE---VGDGVGRRVVNTLLTEMEE 287
RecA-like_CDC48_NLV2_r1-like cd19503
first of two ATPase domains of CDC48 and NLV2, and similar ATPase domains; CDC48 in yeast and ...
 114-214 2.40e-09

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: 56.15  E-value: 2.40e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1266728268 114 LIGPTGSGKTLLAQTLARILNVPFAIADATSLTeAGYVGEDVENiLLKLIQAAdydvEKAEKGIIYIDEIDKVARKSEnp 193
Cdd:cd19503    39 LHGPPGTGKTLLARAVANEAGANFLSISGPSIV-SKYLGESEKN-LREIFEEA----RSHAPSIIFIDEIDALAPKRE-- 110

                          90       100
                  ....*....|....*....|.
gi 1266728268 194 SITRDVSGEGVQQaLLKILEG 214
Cdd:cd19503   111 EDQREVERRVVAQ-LLTLMDG 130
RecA-like_NVL_r1-like cd19518
first of two ATPase domains of NVL (nuclear VCP-like protein) and similar ATPase domains; NVL ...
 112-208 1.79e-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: 1.79e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1266728268 112 ISLIGPTGSGKTLLAQTLARILNVPFAIADATSLTeAGYVGEDVENILLKLIQAADYdvekaEKGIIYIDEIDKVARKSE 191
Cdd:cd19518    37 VLLHGPPGCGKTMLANAIAGELKVPFLKISATEIV-SGVSGESEEKIRELFDQAISN-----APCIVFIDEIDAITPKRE 110

                          90
                  ....*....|....*..
gi 1266728268 192 NPSitRDVSGEGVQQAL 208
Cdd:cd19518   111 SAQ--REMERRIVSQLL 125
clpC CHL00095
Clp protease ATP binding subunit
 63-376 4.09e-07

Clp protease ATP binding subunit


Pssm-ID: 214361 [Multi-domain]  Cd Length: 821  Bit Score: 52.37  E-value: 4.09e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1266728268  63 KPVEIREILDEYVIGQDNAKKALAVAVynhyKRI-----NSNSKIDDVELAksnisliGPTGSGKTLLAQTLARILnvpF 137
Cdd:CHL00095  499 KLLHMEETLHKRIIGQDEAVVAVSKAI----RRArvglkNPNRPIASFLFS-------GPTGVGKTELTKALASYF---F 564

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1266728268 138 AIADAT---SLTE--------------AGYVGEDVENILLKLIQAADYDVekaekgiIYIDEIDKvARKSenpsitrdvs 200
Cdd:CHL00095  565 GSEDAMirlDMSEymekhtvskligspPGYVGYNEGGQLTEAVRKKPYTV-------VLFDEIEK-AHPD---------- 626

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1266728268 201 gegVQQALLKILE-GTVASvppQGGRkhphqefiQIDTTNILFicggafdgiepIIKRRLGEKVI-------GFGSEKKN 272
Cdd:CHL00095  627 ---IFNLLLQILDdGRLTD---SKGR--------TIDFKNTLI-----------IMTSNLGSKVIetnsgglGFELSENQ 681

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1266728268 273 ADVNEKHVLSHVLPEDLLRFgLIPEFIGRLPVIANLEPLDEDALVDILtkpkNALVKQFQKLLELDDVELEFEEGALIEI 352
Cdd:CHL00095  682 LSEKQYKRLSNLVNEELKQF-FRPEFLNRLDEIIVFRQLTKNDVWEIA----EIMLKNLFKRLNEQGIQLEVTERIKTLL 756

                         330       340
                  ....*....|....*....|....
gi 1266728268 353 AKKAIERKTGARGLRSIIEGLMLD 376
Cdd:CHL00095  757 IEEGYNPLYGARPLRRAIMRLLED 780
RecA-like_VPS4-like cd19509
ATPase domain of VPS4, ATAD1, K, KTNA1, Spastin, FIGL-1 and similar ATPase domains; This ...
 75-218 9.11e-07

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


Pssm-ID: 410917 [Multi-domain]  Cd Length: 163  Bit Score: 48.50  E-value: 9.11e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1266728268  75 VIGQDNAKKALAVAVYNHYKRINSNSkiDDVELAKSnISLIGPTGSGKTLLAQTLARILNVPFAIADATSLTeAGYVGED 154
Cdd:cd19509     1 IAGLDDAKEALKEAVILPSLRPDLFP--GLRGPPRG-ILLYGPPGTGKTLLARAVASESGSTFFSISASSLV-SKWVGES 76

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1266728268 155 vENILLKLIQAAdydvEKAEKGIIYIDEIDKV--ARKSENPSITRDVSGEgvqqaLLKILEGTVAS 218
Cdd:cd19509    77 -EKIVRALFALA----RELQPSIIFIDEIDSLlsERGSGEHEASRRVKTE-----FLVQMDGVLNK 132
RecA-like_ClpB_Hsp104-like cd19499
Chaperone protein ClpB/Hsp104 subfamily; Bacterial Caseinolytic peptidase B (ClpB) and ...
 67-213 3.87e-06

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: 46.79  E-value: 3.87e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1266728268  67 IREILDEYVIGQDNAKKALAVAVYNHYKRINSNSKIDDVELaksnisLIGPTGSGKTLLAQTLARIL---NVPFAIADAT 143
Cdd:cd19499     5 LEERLHERVVGQDEAVKAVSDAIRRARAGLSDPNRPIGSFL------FLGPTGVGKTELAKALAELLfgdEDNLIRIDMS 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1266728268 144 SLTEAGYVGedvenillKLIQAADYDVEKAEKG------------IIYIDEIDKVARKsenpsitrdvsgegVQQALLKI 211
Cdd:cd19499    79 EYMEKHSVS--------RLIGAPPGYVGYTEGGqlteavrrkpysVVLLDEIEKAHPD--------------VQNLLLQV 136


                  ..
gi 1266728268 212 LE 213
Cdd:cd19499   137 LD 138
ClpA COG0542
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ...
 296-376 4.07e-06

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


Pssm-ID: 440308 [Multi-domain]  Cd Length: 836  Bit Score: 48.92  E-value: 4.07e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1266728268 296 PEFIGRLPVIANLEPLDEDALVDILTKpknaLVKQFQKLLELDDVELEFEEGALIEIAKKAIERKTGARGLRSIIEGLML 375
Cdd:COG0542   733 PEFLNRIDEIIVFHPLSKEELRKIVDL----QLKRLRKRLAERGITLELTDAAKDFLAEKGYDPEYGARPLKRAIQRELE 808


                  .
gi 1266728268 376 D 376
Cdd:COG0542   809 D 809
YifB COG0606
Predicted Mg-chelatase, contains ChlI-like and ATPase domains, YifB family [Posttranslational ...
 75-133 4.08e-06

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: 48.88  E-value: 4.08e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1266728268  75 VIGQDNAKKALAVAVY-NHykrinsnskiddvelaksNISLIGPTGSGKTLLAQTLARIL 133
Cdd:COG0606   194 VKGQEQAKRALEIAAAgGH------------------NLLMIGPPGSGKTMLARRLPGIL 235
hflB PRK10733
ATP-dependent zinc metalloprotease FtsH;
112-189 5.05e-06

ATP-dependent zinc metalloprotease FtsH;


Pssm-ID: 182683 [Multi-domain]  Cd Length: 644  Bit Score: 48.88  E-value: 5.05e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1266728268 112 ISLIGPTGSGKTLLAQTLARILNVPFAIADATSLTEAgYVGEDVENILLKLIQAadydvEKAEKGIIYIDEIDKVARK 189
Cdd:PRK10733  188 VLMVGPPGTGKTLLAKAIAGEAKVPFFTISGSDFVEM-FVGVGASRVRDMFEQA-----KKAAPCIIFIDEIDAVGRQ 259
CDC48 TIGR01243
AAA family ATPase, CDC48 subfamily; This subfamily of the AAA family ATPases includes two ...
 112-214 5.81e-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: 48.75  E-value: 5.81e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1266728268 112 ISLIGPTGSGKTLLAQTLARILNVPFAIADATSLTeAGYVGEDVENiLLKLIQAAdydvEKAEKGIIYIDEIDKVARKSE 191
Cdd:TIGR01243 215 VLLYGPPGTGKTLLAKAVANEAGAYFISINGPEIM-SKYYGESEER-LREIFKEA----EENAPSIIFIDEIDAIAPKRE 288

                          90       100
                  ....*....|....*....|...
gi 1266728268 192 npSITRDVSGEGVQQaLLKILEG 214
Cdd:TIGR01243 289 --EVTGEVEKRVVAQ-LLTLMDG 308
RecA-like_spastin cd19524
ATPase domain of spastin; Spastin is an ATP-dependent microtubule-severing protein involved in ...
 75-202 1.03e-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: 1.03e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1266728268  75 VIGQDNAKKALAVAVYNHYKRinsNSKIDDVELAKSNISLIGPTGSGKTLLAQTLARILNVPFAIADATSLTeAGYVGED 154
Cdd:cd19524     2 IAGQDLAKQALQEMVILPSLR---PELFTGLRAPARGLLLFGPPGNGKTMLAKAVAAESNATFFNISAASLT-SKYVGEG 77

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 1266728268 155 vENILLKLIQAAdydvEKAEKGIIYIDEIDKV--ARKSENPSITRDVSGE 202
Cdd:cd19524    78 -EKLVRALFAVA----RELQPSIIFIDEVDSLlsERSEGEHEASRRLKTE 122
RecA-like_FtsH cd19501
ATP-dependent zinc metalloprotease FtsH; FtsH ATPase is a processive, ATP-dependent zinc ...
 114-189 1.06e-05

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


Pssm-ID: 410909 [Multi-domain]  Cd Length: 171  Bit Score: 45.69  E-value: 1.06e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1266728268 114 LIGPTGSGKTLLAQTLARILNVPFAIADATSLTEAgYVGEDVENIlLKLIQAAdydvEKAEKGIIYIDEIDKVARK 189
Cdd:cd19501    42 LVGPPGTGKTLLAKAVAGEAGVPFFSISGSDFVEM-FVGVGASRV-RDLFEQA----KKNAPCIVFIDEIDAVGRK 111
AAA smart00382
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ...
 109-192 1.47e-05

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: 44.67  E-value: 1.47e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1266728268  109 KSNISLIGPTGSGKTLLAQTLARILNVP---FAIADATSLTEAGYVGEDVENILL--------KLIQAADYDVEKAEKGI 177
Cdd:smart00382   2 GEVILIVGPPGSGKTTLARALARELGPPgggVIYIDGEDILEEVLDQLLLIIVGGkkasgsgeLRLRLALALARKLKPDV 81

                           90
                   ....*....|....*
gi 1266728268  178 IYIDEIDKVARKSEN 192
Cdd:smart00382  82 LILDEITSLLDAEQE 96
Mg_chelatase pfam01078
Magnesium chelatase, subunit ChlI; Magnesium-chelatase is a three-component enzyme that ...
 75-133 1.58e-05

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: 45.60  E-value: 1.58e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1266728268  75 VIGQDNAKKALAVAVY-NHykrinsnskiddvelaksNISLIGPTGSGKTLLAQTLARIL 133
Cdd:pfam01078   5 VKGQEQAKRALEIAAAgGH------------------NLLMIGPPGSGKTMLAKRLPGIL 46
AAA_5 pfam07728
AAA domain (dynein-related subfamily); This Pfam entry includes some of the AAA proteins not ...
 114-241 1.87e-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: 44.21  E-value: 1.87e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1266728268 114 LIGPTGSGKTLLAQTLARILN--VPFAIADATSLTEAGYVGE-DVENILLKLIQAADYDVEKaEKGIIYIDEIDKVARKs 190
Cdd:pfam07728   4 LVGPPGTGKTELAERLAAALSnrPVFYVQLTRDTTEEDLFGRrNIDPGGASWVDGPLVRAAR-EGEIAVLDEINRANPD- 81

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1266728268 191 enpsitrdvsgegVQQALLKILEGTVASVPPQGGR-KHPHQEFIQIDTTNIL 241
Cdd:pfam07728  82 -------------VLNSLLSLLDERRLLLPDGGELvKAAPDGFRLIATMNPL 120
RecA-like_Lon cd19500
lon protease homolog 2 peroxisomal; Lon protease (also known as Lon peptidase) is an ...
 66-244 2.88e-05

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: 44.47  E-value: 2.88e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1266728268  66 EIREILDEYVIGQDNAKKA----LAVavynhYKRINSN-SKIddvelaksnISLIGPTGSGKTLLAQTLARILNVPFA-- 138
Cdd:cd19500     3 KARKVLDADHYGLEDVKERileyLAV-----RKLKGSMkGPI---------LCLVGPPGVGKTSLGKSIARALGRKFVri 68

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1266728268 139 ----IADatsltEA-------GYVGEDVENILLKLIQAadydveKAEKGIIYIDEIDKVARKSE-NPSitrdvsgegvqQ 206
Cdd:cd19500    69 slggVRD-----EAeirghrrTYVGAMPGRIIQALKKA------GTNNPVFLLDEIDKIGSSFRgDPA-----------S 126

                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 1266728268 207 ALLKILEgtvasvPPQGGRKHPHQEFIQIDTTNILFIC 244
Cdd:cd19500   127 ALLEVLD------PEQNSTFSDHYLDVPFDLSKVLFIA 158
ruvB PRK00080
Holliday junction branch migration DNA helicase RuvB;
45-191 3.18e-05

Holliday junction branch migration DNA helicase RuvB;


Pssm-ID: 234619 [Multi-domain]  Cd Length: 328  Bit Score: 45.51  E-value: 3.18e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1266728268  45 IVQEELAKDEEVEFKdvpkpVEIR-EILDEYvIGQDNAKKALAVAVYNHYKRinsNSKIDDVeLaksnisLIGPTGSGKT 123
Cdd:PRK00080    2 LVSPETLEEEEDEIE-----RSLRpKSLDEF-IGQEKVKENLKIFIEAAKKR---GEALDHV-L------LYGPPGLGKT 65

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1266728268 124 LLAQTLARILNVPFAIADATSLTEAGyvgeDVENILLKLiqaadydvekaEKG-IIYIDEIDKVARKSE 191
Cdd:PRK00080   66 TLANIIANEMGVNIRITSGPALEKPG----DLAAILTNL-----------EEGdVLFIDEIHRLSPVVE 119
RecA-like_CDC48_r1-like cd19519
first of two ATPase domains of CDC48 and similar ATPase domains; CDC48 in yeast and p97 or VCP ...
 112-214 4.24e-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: 43.58  E-value: 4.24e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1266728268 112 ISLIGPTGSGKTLLAQTLARILNVPFAIADATSLTeAGYVGEDVENiLLKLIQAAdydvEKAEKGIIYIDEIDKVARKSE 191
Cdd:cd19519    37 ILLYGPPGTGKTLIARAVANETGAFFFLINGPEIM-SKLAGESESN-LRKAFEEA----EKNAPAIIFIDEIDAIAPKRE 110

                          90       100
                  ....*....|....*....|...
gi 1266728268 192 NpsITRDVSGEGVQQaLLKILEG 214
Cdd:cd19519   111 K--THGEVERRIVSQ-LLTLMDG 130
RecA-like_ATAD1 cd19520
ATPase domain of ATPase family AAA domain-containing protein 1 and similar ATPase domains; ...
 108-194 7.69e-05

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


Pssm-ID: 410928 [Multi-domain]  Cd Length: 166  Bit Score: 42.80  E-value: 7.69e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1266728268 108 AKSNISLIGPTGSGKTLLAQTLARILNVPFAIADATSLTEAGYvGEDVenillKLIQAADYDVEKAEKGIIYIDEIDKVA 187
Cdd:cd19520    34 PPKGVLLYGPPGCGKTMLAKATAKEAGARFINLQVSSLTDKWY-GESQ-----KLVAAVFSLASKLQPSIIFIDEIDSFL 107


                  ....*..
gi 1266728268 188 RkSENPS 194
Cdd:cd19520   108 R-QRSST 113
clpA PRK11034
ATP-dependent Clp protease ATP-binding subunit; Provisional
 59-371 7.78e-05

ATP-dependent Clp protease ATP-binding subunit; Provisional


Pssm-ID: 236828 [Multi-domain]  Cd Length: 758  Bit Score: 44.83  E-value: 7.78e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1266728268  59 KDVPKPVEIReiLDEYVIGQDNAKKALAVAVYNHYKRINSNSKiddvelAKSNISLIGPTGSGKTLLAQTLARILNVPFA 138
Cdd:PRK11034  446 RDTLKNLGDR--LKMLVFGQDKAIEALTEAIKMSRAGLGHEHK------PVGSFLFAGPTGVGKTEVTVQLSKALGIELL 517

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1266728268 139 IADATSLTE-----------AGYVGEDVENILLKLiqaadydVEKAEKGIIYIDEIDKVarkseNPSITrdvsgegvqQA 207
Cdd:PRK11034  518 RFDMSEYMErhtvsrligapPGYVGFDQGGLLTDA-------VIKHPHAVLLLDEIEKA-----HPDVF---------NL 576

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1266728268 208 LLKILE-GTVASvppQGGRKHPHQEFIQIDTTNIlficggafdGIEPIIKrrlgeKVIGFGSEKKNADVNE--KHVLShv 284
Cdd:PRK11034  577 LLQVMDnGTLTD---NNGRKADFRNVVLVMTTNA---------GVRETER-----KSIGLIHQDNSTDAMEeiKKIFT-- 637

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1266728268 285 lpedllrfgliPEFIGRLPVIANLEPLDEDALVDILTKpknaLVKQFQKLLELDDVELEFEEGALIEIAKKAIERKTGAR 364
Cdd:PRK11034  638 -----------PEFRNRLDNIIWFDHLSTDVIHQVVDK----FIVELQAQLDQKGVSLEVSQEARDWLAEKGYDRAMGAR 702


                  ....*..
gi 1266728268 365 GLRSIIE 371
Cdd:PRK11034  703 PMARVIQ 709
RecA-like_NSF-SEC18_r1-like cd19504
first of two ATPase domains of NSF and SEC18, and similar ATPase domains; ...
 112-211 1.22e-04

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: 42.48  E-value: 1.22e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1266728268 112 ISLIGPTGSGKTLLAQTLARILNV--PFAIADATSLTEagYVGEDVENIlLKLIqaADYDVEKAEKG------IIYIDEI 183
Cdd:cd19504    38 ILLYGPPGTGKTLMARQIGKMLNArePKIVNGPEILNK--YVGESEANI-RKLF--ADAEEEQRRLGansglhIIIFDEI 112

                          90       100       110
                  ....*....|....*....|....*....|.
gi 1266728268 184 DKVARKSENpsiTRDVSGEG---VQQALLKI 211
Cdd:cd19504   113 DAICKQRGS---MAGSTGVHdtvVNQLLSKI 140
RecA-like_PEX6_r2 cd19527
second of two ATPase domains of Peroxisomal biogenesis factor 6 (PEX6); PEX6(also known as ...
 109-211 1.55e-04

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


Pssm-ID: 410935 [Multi-domain]  Cd Length: 160  Bit Score: 42.12  E-value: 1.55e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1266728268 109 KSNISLIGPTGSGKTLLAQTLARILNVPFAIADATSLTEAgYVGEDVENILLKLIQAADydvekAEKGIIYIDEIDKVAR 188
Cdd:cd19527    26 RSGILLYGPPGTGKTLLAKAIATECSLNFLSVKGPELINM-YIGESEANVREVFQKARD-----AKPCVIFFDELDSLAP 99

                          90       100
                  ....*....|....*....|...
gi 1266728268 189 KSENPSITRDVSGEGVQQALLKI 211
Cdd:cd19527   100 SRGNSGDSGGVMDRVVSQLLAEL 122
MoxR COG0714
MoxR-like ATPase [General function prediction only]; MoxR-like ATPase is part of the Pathway ...
 66-213 1.74e-04

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: 43.23  E-value: 1.74e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1266728268  66 EIREILDEYVIGQDNAKKALAVAVynhykrinsnskiddveLAKSNISLIGPTGSGKTLLAQTLARILNVPFAIADATS- 144
Cdd:COG0714     5 RLRAEIGKVYVGQEELIELVLIAL-----------------LAGGHLLLEGVPGVGKTTLAKALARALGLPFIRIQFTPd 67

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1266728268 145 LTEAGYVGEDVenillkliqaadYDVEKAE---------KGIIYIDEIDKVARKsenpsitrdvsgegVQQALLKILE 213
Cdd:COG0714    68 LLPSDILGTYI------------YDQQTGEfefrpgplfANVLLADEINRAPPK--------------TQSALLEAME 119
PRK09862 PRK09862
ATP-dependent protease;
26-133 2.86e-04

ATP-dependent protease;


Pssm-ID: 182120 [Multi-domain]  Cd Length: 506  Bit Score: 43.04  E-value: 2.86e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1266728268  26 LVAGPGVYICDECIELCTEIV-QEELAKDEEvefKDVPKPVEIREILDeyVIGQDNAKKALAV-AVYNHykrinsnskid 103
Cdd:PRK09862  148 LINGEGCLIADHLQAVCAFLEgKHALERPKP---TDAVSRALQHDLSD--VIGQEQGKRGLEItAAGGH----------- 211

                          90       100       110
                  ....*....|....*....|....*....|
gi 1266728268 104 dvelaksNISLIGPTGSGKTLLAQTLARIL 133
Cdd:PRK09862  212 -------NLLLIGPPGTGKTMLASRINGLL 234
PRK13342 PRK13342
recombination factor protein RarA; Reviewed
 71-183 3.32e-04

recombination factor protein RarA; Reviewed


Pssm-ID: 237355 [Multi-domain]  Cd Length: 413  Bit Score: 42.76  E-value: 3.32e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1266728268  71 LDEyVIGQDN---AKKALAVAVynhykrinsnskiddveLAKSNISLI--GPTGSGKTLLAQTLARILNVPFAIADATSl 145
Cdd:PRK13342   11 LDE-VVGQEHllgPGKPLRRMI-----------------EAGRLSSMIlwGPPGTGKTTLARIIAGATDAPFEALSAVT- 71

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 1266728268 146 teAGyVGEdveniLLKLIQAADYDVEKAEKGIIYIDEI 183
Cdd:PRK13342   72 --SG-VKD-----LREVIEEARQRRSAGRRTILFIDEI 101
RecA-like_PAN_like cd19502
proteasome activating nucleotidase PAN and related proteasome subunits; This subfamily ...
 114-212 4.89e-04

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: 40.78  E-value: 4.89e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1266728268 114 LIGPTGSGKTLLAQTLARILNVPFAIADATSLTEAgYVGEDVEnILLKLIQAADydvEKAeKGIIYIDEIDKVARKSENP 193
Cdd:cd19502    42 LYGPPGTGKTLLAKAVANHTDATFIRVVGSELVQK-YIGEGAR-LVRELFEMAR---EKA-PSIIFIDEIDAIGAKRFDS 115

                          90
                  ....*....|....*....
gi 1266728268 194 SITRDvsgEGVQQALLKIL 212
Cdd:cd19502   116 GTGGD---REVQRTMLELL 131
RecA-like_Figl-1 cd19525
ATPase domain of Fidgetin-Like 1 (FIGL-1); FIGL-1 may participate in DNA repair in the nucleus; ...
 62-186 5.86e-04

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


Pssm-ID: 410933 [Multi-domain]  Cd Length: 186  Bit Score: 40.74  E-value: 5.86e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1266728268  62 PKPVEI--REILD-------EYVIGQDNAKKALAVAVYNHYKRINSNSKIddvELAKSNISLIGPTGSGKTLLAQTLARI 132
Cdd:cd19525     2 PKMIELimSEIMDhgppinwADIAGLEFAKKTIKEIVVWPMLRPDIFTGL---RGPPKGILLFGPPGTGKTLIGKCIASQ 78

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1266728268 133 LNVPFAIADATSLTeAGYVGEDVenillKLIQAADYDVEKAEKGIIYIDEIDKV 186
Cdd:cd19525    79 SGATFFSISASSLT-SKWVGEGE-----KMVRALFSVARCKQPAVIFIDEIDSL 126
RecA-like_Ycf46-like cd19507
ATPase domain of Ycf46 and similar ATPase domains; Ycf46 may play a role in the regulation of ...
 114-185 8.16e-04

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: 39.66  E-value: 8.16e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1266728268 114 LIGPTGSGKTLLAQTLARILNVPFAIADATSLTeAGYVGEDVENiLLKLIQAAdydvEKAEKGIIYIDEIDK 185
Cdd:cd19507    36 LVGIQGTGKSLTAKAIAGVWQLPLLRLDMGRLF-GGLVGESESR-LRQMIQTA----EAIAPCVLWIDEIEK 101
RecA-like_PEX1_r2 cd19526
second of two ATPase domains of Peroxisomal biogenesis factor 1 (PEX1); PEX1(also known as ...
 109-189 8.76e-04

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: 39.72  E-value: 8.76e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1266728268 109 KSNISLIGPTGSGKTLLAQTLARILNVPFAIADATSLTeAGYVGEDVENILLKLIQAAdydveKAEKGIIYIDEIDKVAR 188
Cdd:cd19526    27 RSGILLYGPPGCGKTLLASAIASECGLNFISVKGPELL-NKYIGASEQNVRDLFSRAQ-----SAKPCILFFDEFDSIAP 100


                  .
gi 1266728268 189 K 189
Cdd:cd19526   101 K 101
NadR3 COG3172
Nicotinamide riboside kinase [Coenzyme transport and metabolism]; Nicotinamide riboside kinase ...
 112-178 1.46e-03

Nicotinamide riboside kinase [Coenzyme transport and metabolism]; Nicotinamide riboside kinase is part of the Pathway/BioSystem: NAD biosynthesis


Pssm-ID: 442405 [Multi-domain]  Cd Length: 178  Bit Score: 39.42  E-value: 1.46e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1266728268 112 ISLIGPTGSGKTLLAQTLARILNVPFAiadatslTEAG----------YVGEDVENILLKLIQAADYDVEKAEKGII 178
Cdd:COG3172    11 IVLLGAESTGKTTLARALAAHYNTPWV-------PEYGreyleekgraLTYDDLLAIARGQLALEDAAAKRANKLLF 80
SK cd00464
Shikimate kinase (SK) is the fifth enzyme in the shikimate pathway, a seven-step biosynthetic ...
 111-137 2.33e-03

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


Pssm-ID: 238260 [Multi-domain]  Cd Length: 154  Bit Score: 38.31  E-value: 2.33e-03
                          10        20
                  ....*....|....*....|....*..
gi 1266728268 111 NISLIGPTGSGKTLLAQTLARILNVPF 137
Cdd:cd00464     1 NIVLIGMMGAGKTTVGRLLAKALGLPF 27
AroK COG0703
Shikimate kinase [Amino acid transport and metabolism]; Shikimate kinase is part of the ...
 112-137 2.43e-03

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


Pssm-ID: 440467 [Multi-domain]  Cd Length: 165  Bit Score: 38.57  E-value: 2.43e-03
                          10        20
                  ....*....|....*....|....*.
gi 1266728268 112 ISLIGPTGSGKTLLAQTLARILNVPF 137
Cdd:COG0703     1 IVLIGMMGAGKSTVGRLLAKRLGLPF 26
aroK PRK00131
shikimate kinase; Reviewed
 107-137 3.86e-03

shikimate kinase; Reviewed


Pssm-ID: 234654 [Multi-domain]  Cd Length: 175  Bit Score: 37.86  E-value: 3.86e-03
                          10        20        30
                  ....*....|....*....|....*....|.
gi 1266728268 107 LAKSNISLIGPTGSGKTLLAQTLARILNVPF 137
Cdd:PRK00131    2 LKGPNIVLIGFMGAGKSTIGRLLAKRLGYDF 32
RecA-like_ATAD3-like cd19512
ATPase domains of ATPase AAA-domain protein 3A (ATAD3A), -3B, and -3C, and similar ATPase ...
 111-198 4.62e-03

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


Pssm-ID: 410920 [Multi-domain]  Cd Length: 150  Bit Score: 37.51  E-value: 4.62e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1266728268 111 NISLIGPTGSGKTLLAQTLARILNVPFAIADATSLTEAGYVGedveniLLKLIQAADYdVEKAEKG-IIYIDEIDKVARK 189
Cdd:cd19512    24 NILFYGPPGTGKTLFAKKLALHSGMDYAIMTGGDVAPMGREG------VTAIHKVFDW-ANTSRRGlLLFVDEADAFLRK 96


                  ....*....
gi 1266728268 190 SENPSITRD 198
Cdd:cd19512    97 RSTEKISED 105
ycf46 CHL00195
Ycf46; Provisional
 114-192 5.11e-03

Ycf46; Provisional


Pssm-ID: 177094 [Multi-domain]  Cd Length: 489  Bit Score: 38.85  E-value: 5.11e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1266728268 114 LIGPTGSGKTLLAQTLARILNVPFAIADATSLTeAGYVGEDvENILLKLIQAAdydvEKAEKGIIYIDEIDKVARKSEN 192
Cdd:CHL00195  264 LVGIQGTGKSLTAKAIANDWQLPLLRLDVGKLF-GGIVGES-ESRMRQMIRIA----EALSPCILWIDEIDKAFSNSES 336
RecA-like_CDC48_r2-like cd19511
second of two ATPase domains of CDC48/p97, PEX1 and -6, VAT and NVL, and similar ATPase ...
 112-194 5.73e-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: 37.26  E-value: 5.73e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1266728268 112 ISLIGPTGSGKTLLAQTLARILNVPF-AIADATSLTEagYVGEDvENILLKLIQAAdydvEKAEKGIIYIDEIDKVA-RK 189
Cdd:cd19511    30 VLLYGPPGCGKTLLAKALASEAGLNFiSVKGPELFSK--YVGES-ERAVREIFQKA----RQAAPCIIFFDEIDSLApRR 102


                  ....*
gi 1266728268 190 SENPS 194
Cdd:cd19511   103 GQSDS 107
AAA_22 pfam13401
AAA domain;
105-192 8.79e-03

AAA domain;


Pssm-ID: 379165 [Multi-domain]  Cd Length: 129  Bit Score: 36.17  E-value: 8.79e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1266728268 105 VELAKSNISLIGPTGSGKTLLAQTLARIL---NVPFAIADATSLTEAGYVGEDVENI-------------LLKLIQaaDY 168
Cdd:pfam13401   1 IRFGAGILVLTGESGTGKTTLLRRLLEQLpevRDSVVFVDLPSGTSPKDLLRALLRAlglplsgrlskeeLLAALQ--QL 78

                          90       100
                  ....*....|....*....|....
gi 1266728268 169 DVEKAEKGIIYIDEIDKVARKSEN 192
Cdd:pfam13401  79 LLALAVAVVLIIDEAQHLSLEALE 102
 
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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