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Conserved domains on  [gi|488980973|ref|WP_002891807|]
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MULTISPECIES: ATP-dependent protease ATP-binding subunit ClpX [Klebsiella]

Protein Classification

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

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

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
ClpX COG1219
ATP-dependent protease Clp, ATPase subunit ClpX [Posttranslational modification, protein ...
1-413 0e+00

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


:

Pssm-ID: 440832 [Multi-domain]  Cd Length: 409  Bit Score: 883.23  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488980973   1 MTDKRKdgsgKLLYCSFCGKSQHEVRKLIAGPSVYICDECVDLCNDIIREEIKEVAPHRERSALPTPHEIRHHLDDYVIG 80
Cdd:COG1219    1 MAGDSK----KELKCSFCGKSQDEVRKLIAGPGVYICDECVELCNEIIEEELKEEEAEEELKKLPKPKEIKAFLDEYVIG 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488980973  81 QEQAKKVLAVAVYNHYKRLRNGDTS-NGVELGKSNILLIGPTGSGKTLLAETLARLLDVPFTMADATTLTEAGYVGEDVE 159
Cdd:COG1219   77 QERAKKVLSVAVYNHYKRLNSGSKDdDDVELEKSNILLIGPTGSGKTLLAQTLARILDVPFAIADATTLTEAGYVGEDVE 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488980973 160 NIIQKLLQKCDYDVQKAQRGIVYIDEIDKISRKSDNPSITRDVSGEGVQQALLKLIEGTVAAVPPQGGRKHPQQEFLQVD 239
Cdd:COG1219  157 NILLKLLQAADYDVEKAERGIIYIDEIDKIARKSENPSITRDVSGEGVQQALLKILEGTVANVPPQGGRKHPQQEFIQID 236
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488980973 240 TSKILFICGGAFAGLDKVISHRVETgSGIGFGATVKAKSDKaSEGELLAQVEPEDLIKFGLIPEFIGRLPVVATLNELSE 319
Cdd:COG1219  237 TTNILFICGGAFDGLEKIIERRLGK-KSIGFGAEVKSKKEK-DEGELLKQVEPEDLIKFGLIPEFIGRLPVIATLEELDE 314
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488980973 320 EALIQILKEPKNALTKQYQALFSLEGAELEFRDEALDAIAKKAMARKTGARGLRSIVEAALLDTMYDLPSMEDVEKVVID 399
Cdd:COG1219  315 EALVRILTEPKNALVKQYQKLFEMDGVELEFTDEALEAIAKKAIERKTGARGLRSILEEILLDVMYELPSRKDVKKVVIT 394
                        410
                 ....*....|....
gi 488980973 400 ESVIAGQSKPLLIY 413
Cdd:COG1219  395 KEVVEGKAKPILVY 408
 
Name Accession Description Interval E-value
ClpX COG1219
ATP-dependent protease Clp, ATPase subunit ClpX [Posttranslational modification, protein ...
1-413 0e+00

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


Pssm-ID: 440832 [Multi-domain]  Cd Length: 409  Bit Score: 883.23  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488980973   1 MTDKRKdgsgKLLYCSFCGKSQHEVRKLIAGPSVYICDECVDLCNDIIREEIKEVAPHRERSALPTPHEIRHHLDDYVIG 80
Cdd:COG1219    1 MAGDSK----KELKCSFCGKSQDEVRKLIAGPGVYICDECVELCNEIIEEELKEEEAEEELKKLPKPKEIKAFLDEYVIG 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488980973  81 QEQAKKVLAVAVYNHYKRLRNGDTS-NGVELGKSNILLIGPTGSGKTLLAETLARLLDVPFTMADATTLTEAGYVGEDVE 159
Cdd:COG1219   77 QERAKKVLSVAVYNHYKRLNSGSKDdDDVELEKSNILLIGPTGSGKTLLAQTLARILDVPFAIADATTLTEAGYVGEDVE 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488980973 160 NIIQKLLQKCDYDVQKAQRGIVYIDEIDKISRKSDNPSITRDVSGEGVQQALLKLIEGTVAAVPPQGGRKHPQQEFLQVD 239
Cdd:COG1219  157 NILLKLLQAADYDVEKAERGIIYIDEIDKIARKSENPSITRDVSGEGVQQALLKILEGTVANVPPQGGRKHPQQEFIQID 236
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488980973 240 TSKILFICGGAFAGLDKVISHRVETgSGIGFGATVKAKSDKaSEGELLAQVEPEDLIKFGLIPEFIGRLPVVATLNELSE 319
Cdd:COG1219  237 TTNILFICGGAFDGLEKIIERRLGK-KSIGFGAEVKSKKEK-DEGELLKQVEPEDLIKFGLIPEFIGRLPVIATLEELDE 314
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488980973 320 EALIQILKEPKNALTKQYQALFSLEGAELEFRDEALDAIAKKAMARKTGARGLRSIVEAALLDTMYDLPSMEDVEKVVID 399
Cdd:COG1219  315 EALVRILTEPKNALVKQYQKLFEMDGVELEFTDEALEAIAKKAIERKTGARGLRSILEEILLDVMYELPSRKDVKKVVIT 394
                        410
                 ....*....|....
gi 488980973 400 ESVIAGQSKPLLIY 413
Cdd:COG1219  395 KEVVEGKAKPILVY 408
clpX PRK05342
ATP-dependent Clp protease ATP-binding subunit ClpX;
4-417 0e+00

ATP-dependent Clp protease ATP-binding subunit ClpX;


Pssm-ID: 235422 [Multi-domain]  Cd Length: 412  Bit Score: 866.78  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488980973   4 KRKDGSGKLLYCSFCGKSQHEVRKLIAGPSVYICDECVDLCNDIIREEIKEVAPhrERSALPTPHEIRHHLDDYVIGQEQ 83
Cdd:PRK05342   1 ARGGDSKKLLYCSFCGKSQHEVRKLIAGPGVYICDECIELCNEIIREELKEEAV--ELKELPTPKEIKAHLDQYVIGQER 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488980973  84 AKKVLAVAVYNHYKRLRNG-DTSNGVELGKSNILLIGPTGSGKTLLAETLARLLDVPFTMADATTLTEAGYVGEDVENII 162
Cdd:PRK05342  79 AKKVLSVAVYNHYKRLRHGdKKDDDVELQKSNILLIGPTGSGKTLLAQTLARILDVPFAIADATTLTEAGYVGEDVENIL 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488980973 163 QKLLQKCDYDVQKAQRGIVYIDEIDKISRKSDNPSITRDVSGEGVQQALLKLIEGTVAAVPPQGGRKHPQQEFLQVDTSK 242
Cdd:PRK05342 159 LKLLQAADYDVEKAQRGIVYIDEIDKIARKSENPSITRDVSGEGVQQALLKILEGTVASVPPQGGRKHPQQEFIQVDTTN 238
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488980973 243 ILFICGGAFAGLDKVISHRVEtGSGIGFGATVKAKSDKASEGELLAQVEPEDLIKFGLIPEFIGRLPVVATLNELSEEAL 322
Cdd:PRK05342 239 ILFICGGAFDGLEKIIKQRLG-KKGIGFGAEVKSKKEKRTEGELLKQVEPEDLIKFGLIPEFIGRLPVVATLEELDEEAL 317
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488980973 323 IQILKEPKNALTKQYQALFSLEGAELEFRDEALDAIAKKAMARKTGARGLRSIVEAALLDTMYDLPSMEDVEKVVIDESV 402
Cdd:PRK05342 318 VRILTEPKNALVKQYQKLFEMDGVELEFTDEALEAIAKKAIERKTGARGLRSILEEILLDVMFELPSREDVEKVVITKEV 397
                        410
                 ....*....|....*
gi 488980973 403 IAGQSKPLLIYGKPE 417
Cdd:PRK05342 398 VEGKAKPLLIYREKS 412
clpX TIGR00382
endopeptidase Clp ATP-binding regulatory subunit (clpX); A member of the ATP-dependent ...
1-412 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: 715.39  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488980973    1 MTDKRKDgsgklLYCSFCGKSQHEVRKLIAGPSVYICDECVDLCNDIIRE------EIKEVAPHRERSALPTPHEIRHHL 74
Cdd:TIGR00382   1 MTKKNET-----LYCSFCGKSQDEVRKLIAGPGVYICDECIELCHDILEEelgtrkESKEYEEEFELSYLPTPKEIKAHL 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488980973   75 DDYVIGQEQAKKVLAVAVYNHYKRLR---NGDTSNGVELGKSNILLIGPTGSGKTLLAETLARLLDVPFTMADATTLTEA 151
Cdd:TIGR00382  76 DEYVIGQEQAKKVLSVAVYNHYKRLNfekNKKSDNGVELSKSNILLIGPTGSGKTLLAQTLARILNVPFAIADATTLTEA 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488980973  152 GYVGEDVENIIQKLLQKCDYDVQKAQRGIVYIDEIDKISRKSDNPSITRDVSGEGVQQALLKLIEGTVAAVPPQGGRKHP 231
Cdd:TIGR00382 156 GYVGEDVENILLKLLQAADYDVEKAQKGIIYIDEIDKISRKSENPSITRDVSGEGVQQALLKIIEGTVANVPPQGGRKHP 235
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488980973  232 QQEFLQVDTSKILFICGGAFAGLDKVISHRVETGSgIGFGATVKAKSDKasEGELLAQVEPEDLIKFGLIPEFIGRLPVV 311
Cdd:TIGR00382 236 YQEFIQIDTSNILFICGGAFVGLEKIIKKRTGKSS-IGFGAEVKKKSKE--KADLLRQVEPEDLVKFGLIPEFIGRLPVI 312
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488980973  312 ATLNELSEEALIQILKEPKNALTKQYQALFSLEGAELEFRDEALDAIAKKAMARKTGARGLRSIVEAALLDTMYDLPSME 391
Cdd:TIGR00382 313 ATLEKLDEEALIAILTKPKNALVKQYQALFKMDNVELDFEEEALKAIAKKALERKTGARGLRSIVEGLLLDVMFDLPSLE 392
                         410       420
                  ....*....|....*....|.
gi 488980973  392 DVEKVVIDESVIAGQSKPLLI 412
Cdd:TIGR00382 393 DLEKVVITKETVLKQSEPLLI 413
RecA-like_ClpX cd19497
ATP-dependent Clp protease ATP-binding subunit ClpX; ClpX is a component of the ATP-dependent ...
65-314 4.77e-177

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: 494.04  E-value: 4.77e-177
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488980973  65 PTPHEIRHHLDDYVIGQEQAKKVLAVAVYNHYKRLRNG--DTSNGVELGKSNILLIGPTGSGKTLLAETLARLLDVPFTM 142
Cdd:cd19497    1 PTPKEIKEHLDKYVIGQERAKKVLSVAVYNHYKRIRNNlkQKDDDVELEKSNILLIGPTGSGKTLLAQTLAKILDVPFAI 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488980973 143 ADATTLTEAGYVGEDVENIIQKLLQKCDYDVQKAQRGIVYIDEIDKISRKSDNPSITRDVSGEGVQQALLKLIEGTVAAV 222
Cdd:cd19497   81 ADATTLTEAGYVGEDVENILLKLLQAADYDVERAQRGIVYIDEIDKIARKSENPSITRDVSGEGVQQALLKILEGTVANV 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488980973 223 PPQGGRKHPQQEFLQVDTSKILFICGGAFAGLDKVISHRVETGSgIGFGATVKAKSDKASEGELLAQVEPEDLIKFGLIP 302
Cdd:cd19497  161 PPQGGRKHPQQEFIQVDTTNILFICGGAFVGLEKIIARRLGKKS-LGFGAETSSEKDEKERDELLSKVEPEDLIKFGLIP 239
                        250
                 ....*....|..
gi 488980973 303 EFIGRLPVVATL 314
Cdd:cd19497  240 EFVGRLPVIVTL 251
AAA_2 pfam07724
AAA domain (Cdc48 subfamily); This Pfam entry includes some of the AAA proteins not detected ...
112-311 4.71e-40

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: 140.79  E-value: 4.71e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488980973  112 KSNILLIGPTGSGKTLLAETLARLLDV---PFTMADATTLTEagyvgedvENIIQKLLQKCDYDVQKAQRG--------- 179
Cdd:pfam07724   3 IGSFLFLGPTGVGKTELAKALAELLFGderALIRIDMSEYME--------EHSVSRLIGAPPGYVGYEEGGqlteavrrk 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488980973  180 ---IVYIDEIDKISRksdnpsitrdvsgeGVQQALLKLIEGTVaaVPPQGGRkhpqqeflQVDTSKILFICGGAFAGLDK 256
Cdd:pfam07724  75 pysIVLIDEIEKAHP--------------GVQNDLLQILEGGT--LTDKQGR--------TVDFKNTLFIMTGNFGSEKI 130
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 488980973  257 VIshrvetgsgigfgatvkAKSDKASEGELLAQVEPEDLIKFGLIPEFIGRLPVV 311
Cdd:pfam07724 131 SD-----------------ASRLGDSPDYELLKEEVMDLLKKGFIPEFLGRLPII 168
zf-C4_ClpX smart00994
ClpX C4-type zinc finger; The ClpX heat shock protein of Escherichia coli is a member of the ...
13-51 2.06e-22

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: 89.16  E-value: 2.06e-22
                           10        20        30
                   ....*....|....*....|....*....|....*....
gi 488980973    13 LYCSFCGKSQHEVRKLIAGPSVYICDECVDLCNDIIREE 51
Cdd:smart00994   1 LRCSFCGKSESEVRKLIAGPGVYICDECVELCYEILEEE 39
 
Name Accession Description Interval E-value
ClpX COG1219
ATP-dependent protease Clp, ATPase subunit ClpX [Posttranslational modification, protein ...
1-413 0e+00

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


Pssm-ID: 440832 [Multi-domain]  Cd Length: 409  Bit Score: 883.23  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488980973   1 MTDKRKdgsgKLLYCSFCGKSQHEVRKLIAGPSVYICDECVDLCNDIIREEIKEVAPHRERSALPTPHEIRHHLDDYVIG 80
Cdd:COG1219    1 MAGDSK----KELKCSFCGKSQDEVRKLIAGPGVYICDECVELCNEIIEEELKEEEAEEELKKLPKPKEIKAFLDEYVIG 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488980973  81 QEQAKKVLAVAVYNHYKRLRNGDTS-NGVELGKSNILLIGPTGSGKTLLAETLARLLDVPFTMADATTLTEAGYVGEDVE 159
Cdd:COG1219   77 QERAKKVLSVAVYNHYKRLNSGSKDdDDVELEKSNILLIGPTGSGKTLLAQTLARILDVPFAIADATTLTEAGYVGEDVE 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488980973 160 NIIQKLLQKCDYDVQKAQRGIVYIDEIDKISRKSDNPSITRDVSGEGVQQALLKLIEGTVAAVPPQGGRKHPQQEFLQVD 239
Cdd:COG1219  157 NILLKLLQAADYDVEKAERGIIYIDEIDKIARKSENPSITRDVSGEGVQQALLKILEGTVANVPPQGGRKHPQQEFIQID 236
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488980973 240 TSKILFICGGAFAGLDKVISHRVETgSGIGFGATVKAKSDKaSEGELLAQVEPEDLIKFGLIPEFIGRLPVVATLNELSE 319
Cdd:COG1219  237 TTNILFICGGAFDGLEKIIERRLGK-KSIGFGAEVKSKKEK-DEGELLKQVEPEDLIKFGLIPEFIGRLPVIATLEELDE 314
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488980973 320 EALIQILKEPKNALTKQYQALFSLEGAELEFRDEALDAIAKKAMARKTGARGLRSIVEAALLDTMYDLPSMEDVEKVVID 399
Cdd:COG1219  315 EALVRILTEPKNALVKQYQKLFEMDGVELEFTDEALEAIAKKAIERKTGARGLRSILEEILLDVMYELPSRKDVKKVVIT 394
                        410
                 ....*....|....
gi 488980973 400 ESVIAGQSKPLLIY 413
Cdd:COG1219  395 KEVVEGKAKPILVY 408
clpX PRK05342
ATP-dependent Clp protease ATP-binding subunit ClpX;
4-417 0e+00

ATP-dependent Clp protease ATP-binding subunit ClpX;


Pssm-ID: 235422 [Multi-domain]  Cd Length: 412  Bit Score: 866.78  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488980973   4 KRKDGSGKLLYCSFCGKSQHEVRKLIAGPSVYICDECVDLCNDIIREEIKEVAPhrERSALPTPHEIRHHLDDYVIGQEQ 83
Cdd:PRK05342   1 ARGGDSKKLLYCSFCGKSQHEVRKLIAGPGVYICDECIELCNEIIREELKEEAV--ELKELPTPKEIKAHLDQYVIGQER 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488980973  84 AKKVLAVAVYNHYKRLRNG-DTSNGVELGKSNILLIGPTGSGKTLLAETLARLLDVPFTMADATTLTEAGYVGEDVENII 162
Cdd:PRK05342  79 AKKVLSVAVYNHYKRLRHGdKKDDDVELQKSNILLIGPTGSGKTLLAQTLARILDVPFAIADATTLTEAGYVGEDVENIL 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488980973 163 QKLLQKCDYDVQKAQRGIVYIDEIDKISRKSDNPSITRDVSGEGVQQALLKLIEGTVAAVPPQGGRKHPQQEFLQVDTSK 242
Cdd:PRK05342 159 LKLLQAADYDVEKAQRGIVYIDEIDKIARKSENPSITRDVSGEGVQQALLKILEGTVASVPPQGGRKHPQQEFIQVDTTN 238
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488980973 243 ILFICGGAFAGLDKVISHRVEtGSGIGFGATVKAKSDKASEGELLAQVEPEDLIKFGLIPEFIGRLPVVATLNELSEEAL 322
Cdd:PRK05342 239 ILFICGGAFDGLEKIIKQRLG-KKGIGFGAEVKSKKEKRTEGELLKQVEPEDLIKFGLIPEFIGRLPVVATLEELDEEAL 317
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488980973 323 IQILKEPKNALTKQYQALFSLEGAELEFRDEALDAIAKKAMARKTGARGLRSIVEAALLDTMYDLPSMEDVEKVVIDESV 402
Cdd:PRK05342 318 VRILTEPKNALVKQYQKLFEMDGVELEFTDEALEAIAKKAIERKTGARGLRSILEEILLDVMFELPSREDVEKVVITKEV 397
                        410
                 ....*....|....*
gi 488980973 403 IAGQSKPLLIYGKPE 417
Cdd:PRK05342 398 VEGKAKPLLIYREKS 412
clpX TIGR00382
endopeptidase Clp ATP-binding regulatory subunit (clpX); A member of the ATP-dependent ...
1-412 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: 715.39  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488980973    1 MTDKRKDgsgklLYCSFCGKSQHEVRKLIAGPSVYICDECVDLCNDIIRE------EIKEVAPHRERSALPTPHEIRHHL 74
Cdd:TIGR00382   1 MTKKNET-----LYCSFCGKSQDEVRKLIAGPGVYICDECIELCHDILEEelgtrkESKEYEEEFELSYLPTPKEIKAHL 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488980973   75 DDYVIGQEQAKKVLAVAVYNHYKRLR---NGDTSNGVELGKSNILLIGPTGSGKTLLAETLARLLDVPFTMADATTLTEA 151
Cdd:TIGR00382  76 DEYVIGQEQAKKVLSVAVYNHYKRLNfekNKKSDNGVELSKSNILLIGPTGSGKTLLAQTLARILNVPFAIADATTLTEA 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488980973  152 GYVGEDVENIIQKLLQKCDYDVQKAQRGIVYIDEIDKISRKSDNPSITRDVSGEGVQQALLKLIEGTVAAVPPQGGRKHP 231
Cdd:TIGR00382 156 GYVGEDVENILLKLLQAADYDVEKAQKGIIYIDEIDKISRKSENPSITRDVSGEGVQQALLKIIEGTVANVPPQGGRKHP 235
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488980973  232 QQEFLQVDTSKILFICGGAFAGLDKVISHRVETGSgIGFGATVKAKSDKasEGELLAQVEPEDLIKFGLIPEFIGRLPVV 311
Cdd:TIGR00382 236 YQEFIQIDTSNILFICGGAFVGLEKIIKKRTGKSS-IGFGAEVKKKSKE--KADLLRQVEPEDLVKFGLIPEFIGRLPVI 312
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488980973  312 ATLNELSEEALIQILKEPKNALTKQYQALFSLEGAELEFRDEALDAIAKKAMARKTGARGLRSIVEAALLDTMYDLPSME 391
Cdd:TIGR00382 313 ATLEKLDEEALIAILTKPKNALVKQYQALFKMDNVELDFEEEALKAIAKKALERKTGARGLRSIVEGLLLDVMFDLPSLE 392
                         410       420
                  ....*....|....*....|.
gi 488980973  392 DVEKVVIDESVIAGQSKPLLI 412
Cdd:TIGR00382 393 DLEKVVITKETVLKQSEPLLI 413
RecA-like_ClpX cd19497
ATP-dependent Clp protease ATP-binding subunit ClpX; ClpX is a component of the ATP-dependent ...
65-314 4.77e-177

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: 494.04  E-value: 4.77e-177
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488980973  65 PTPHEIRHHLDDYVIGQEQAKKVLAVAVYNHYKRLRNG--DTSNGVELGKSNILLIGPTGSGKTLLAETLARLLDVPFTM 142
Cdd:cd19497    1 PTPKEIKEHLDKYVIGQERAKKVLSVAVYNHYKRIRNNlkQKDDDVELEKSNILLIGPTGSGKTLLAQTLAKILDVPFAI 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488980973 143 ADATTLTEAGYVGEDVENIIQKLLQKCDYDVQKAQRGIVYIDEIDKISRKSDNPSITRDVSGEGVQQALLKLIEGTVAAV 222
Cdd:cd19497   81 ADATTLTEAGYVGEDVENILLKLLQAADYDVERAQRGIVYIDEIDKIARKSENPSITRDVSGEGVQQALLKILEGTVANV 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488980973 223 PPQGGRKHPQQEFLQVDTSKILFICGGAFAGLDKVISHRVETGSgIGFGATVKAKSDKASEGELLAQVEPEDLIKFGLIP 302
Cdd:cd19497  161 PPQGGRKHPQQEFIQVDTTNILFICGGAFVGLEKIIARRLGKKS-LGFGAETSSEKDEKERDELLSKVEPEDLIKFGLIP 239
                        250
                 ....*....|..
gi 488980973 303 EFIGRLPVVATL 314
Cdd:cd19497  240 EFVGRLPVIVTL 251
hslU PRK05201
ATP-dependent protease ATPase subunit HslU;
66-400 6.86e-61

ATP-dependent protease ATPase subunit HslU;


Pssm-ID: 235364 [Multi-domain]  Cd Length: 443  Bit Score: 203.77  E-value: 6.86e-61
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488980973  66 TPHEIRHHLDDYVIGQEQAKKVLAVAVYNHYKR------LRNgdtsngvELGKSNILLIGPTGSGKTLLAETLARLLDVP 139
Cdd:PRK05201   5 TPREIVSELDKYIIGQDDAKRAVAIALRNRWRRmqlpeeLRD-------EVTPKNILMIGPTGVGKTEIARRLAKLANAP 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488980973 140 FTMADATTLTEAGYVGEDVENII--------------------------------------------------------- 162
Cdd:PRK05201  78 FIKVEATKFTEVGYVGRDVESIIrdlveiavkmvreekrekvrekaeeaaeerildallppaknnwgeeeekeeisatrq 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488980973 163 ------------------------------------------QKLLQKC----------------------------DYD 172
Cdd:PRK05201 158 kfrkklregelddkeieievaeaapmmeimgppgmeemtiqlQDMFGNLgpkkkkkrklkvkearkilieeeaakliDME 237
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488980973 173 --VQKA-----QRGIVYIDEIDKISRKSDNPSitRDVSGEGVQQALLKLIEGTVAAVppqggrKHPqqeflQVDTSKILF 245
Cdd:PRK05201 238 eiKQEAierveQNGIVFIDEIDKIAARGGSSG--PDVSREGVQRDLLPLVEGSTVST------KYG-----MVKTDHILF 304
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488980973 246 ICGGAFagldkvisHrvetgsgigfgatvKAK-SDkasegellaqvepedlikfgLIPEFIGRLPVVATLNELSEEALIQ 324
Cdd:PRK05201 305 IASGAF--------H--------------VSKpSD--------------------LIPELQGRFPIRVELDALTEEDFVR 342
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488980973 325 ILKEPKNALTKQYQALFSLEGAELEFRDEALDAIAKKA--MARKT---GARGLRSIVEAALLDTMYDLPSMEDvEKVVID 399
Cdd:PRK05201 343 ILTEPKASLIKQYQALLATEGVTLEFTDDAIRRIAEIAyqVNEKTeniGARRLHTVMEKLLEDISFEAPDMSG-ETVTID 421

                 .
gi 488980973 400 E 400
Cdd:PRK05201 422 A 422
HslU COG1220
ATP-dependent protease HslVU (ClpYQ), ATPase subunit HslU [Posttranslational modification, ...
66-400 4.88e-57

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


Pssm-ID: 440833 [Multi-domain]  Cd Length: 454  Bit Score: 194.11  E-value: 4.88e-57
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488980973  66 TPHEIRHHLDDYVIGQEQAKKVLAVAVYNHYKR------LRNgdtsngvELGKSNILLIGPTGSGKTLLAETLARLLDVP 139
Cdd:COG1220    5 TPREIVAELDKYIIGQDEAKRAVAIALRNRWRRqqlpeeLRD-------EITPKNILMIGPTGVGKTEIARRLAKLANAP 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488980973 140 FTMADATTLTEAGYVGEDVENII--------------------------------------------------------- 162
Cdd:COG1220   78 FIKVEATKFTEVGYVGRDVESMIrdlveiavkmvreekmekvrekaeeaaeerildlllpppkkkagsnnpfeeeeeeee 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488980973 163 ---------QKLLQK----------------------------------------------------------------- 168
Cdd:COG1220  158 eeeeisrtrEKFRKKlregelddreieieveessspgveimgppgmeemgmnlqdmfgnlmpkkkkkrkvkvkearkilt 237
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488980973 169 -------CDYD--VQKA-----QRGIVYIDEIDKISRKSDNPSItrDVSGEGVQQALLKLIEG-TVAAvppqggrKHPQq 233
Cdd:COG1220  238 qeeaaklIDMDevKQEAieraeQNGIIFIDEIDKIASRGGGSGP--DVSREGVQRDLLPIVEGsTVNT-------KYGM- 307
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488980973 234 eflqVDTSKILFICGGAFagldkvisHRvetgsgigfgatvkAK-SDkasegellaqvepedlikfgLIPEFIGRLPVVA 312
Cdd:COG1220  308 ----VKTDHILFIAAGAF--------HV--------------SKpSD--------------------LIPELQGRFPIRV 341
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488980973 313 TLNELSEEALIQILKEPKNALTKQYQALFSLEGAELEFRDEALDAIAKKA--MARKT---GARGLRSIVEAALLDTMYDL 387
Cdd:COG1220  342 ELDSLTEEDFVRILTEPKNALTKQYQALLATEGVELEFTDDAIREIAEIAfeVNERTeniGARRLHTVMEKLLEDISFEA 421
                        490
                 ....*....|...
gi 488980973 388 PSMEDvEKVVIDE 400
Cdd:COG1220  422 PDLSG-KTVVIDA 433
hslU TIGR00390
ATP-dependent protease HslVU, ATPase subunit; This model represents the ATPase subunit of ...
66-399 6.20e-48

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


Pssm-ID: 273052 [Multi-domain]  Cd Length: 441  Bit Score: 169.61  E-value: 6.20e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488980973   66 TPHEIRHHLDDYVIGQEQAKKVLAVAVYNHYKRLRNgDTSNGVELGKSNILLIGPTGSGKTLLAETLARLLDVPFTMADA 145
Cdd:TIGR00390   2 TPREIVAELDKYIIGQDNAKKSVAIALRNRYRRSQL-NEELKDEVTPKNILMIGPTGVGKTEIARRLAKLANAPFIKVEA 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488980973  146 TTLTEAGYVGEDVENII--------------------------------------------------------------- 162
Cdd:TIGR00390  81 TKFTEVGYVGRDVESMVrdltdaavklvkeeaiekvrdraeelaeerivdvllppaknqwgqteqqqepesareafrkkl 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488980973  163 -------------------------------------QKLLQKCDYDVQKA----------------------------- 176
Cdd:TIGR00390 161 regelddkeieidvsakmpsgieimappgmeemtmqlQSLFQNLGGQKKKKrklkikdakkaliaeeaaklvdpeeikqe 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488980973  177 ------QRGIVYIDEIDKISRKSDNPSitRDVSGEGVQQALLKLIEGTVAAVppqggrKHPQqeflqVDTSKILFICGGA 250
Cdd:TIGR00390 241 aidaveQSGIIFIDEIDKIAKKGESSG--ADVSREGVQRDLLPIVEGSTVNT------KYGM-----VKTDHILFIAAGA 307
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488980973  251 FAgldkvishrvetgsgigfgatvkaksdkasegelLAQvePEDLIkfgliPEFIGRLPVVATLNELSEEALIQILKEPK 330
Cdd:TIGR00390 308 FQ----------------------------------LAK--PSDLI-----PELQGRFPIRVELQALTTDDFERILTEPK 346
                         410       420       430       440       450       460       470
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 488980973  331 NALTKQYQALFSLEGAELEFRDEALDAIAKKA--MARKT---GARGLRSIVEAALLDTMYDLPSMEdVEKVVID 399
Cdd:TIGR00390 347 NSLIKQYKALMKTEGVNIEFSDEAIKRIAELAynVNEKTeniGARRLHTVLERLLEDISFEAPDLS-GQNITID 419
RecA-like_HslU cd19498
ATP-dependent protease ATPase subunit HslU; HslU is a component of the ATP-dependent protease ...
66-251 6.90e-47

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: 159.08  E-value: 6.90e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488980973  66 TPHEIRHHLDDYVIGQEQAKKVLAVAVYNHYKRLRnGDTSNGVELGKSNILLIGPTGSGKTLLAETLARLLDVPFTMADA 145
Cdd:cd19498    1 TPREIVSELDKYIIGQDEAKRAVAIALRNRWRRMQ-LPEELRDEVTPKNILMIGPTGVGKTEIARRLAKLAGAPFIKVEA 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488980973 146 TTLTEAGYVGEDVENIIQKLLQkcdydvqkaqrGIVYIDEIDKISRKSDnpSITRDVSGEGVQQALLKLIEGTVaaVPPQ 225
Cdd:cd19498   80 TKFTEVGYVGRDVESIIRDLVE-----------GIVFIDEIDKIAKRGG--SSGPDVSREGVQRDLLPIVEGST--VSTK 144
                        170       180
                 ....*....|....*....|....*.
gi 488980973 226 GGrkhpqqeflQVDTSKILFICGGAF 251
Cdd:cd19498  145 YG---------PVKTDHILFIAAGAF 161
AAA_2 pfam07724
AAA domain (Cdc48 subfamily); This Pfam entry includes some of the AAA proteins not detected ...
112-311 4.71e-40

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: 140.79  E-value: 4.71e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488980973  112 KSNILLIGPTGSGKTLLAETLARLLDV---PFTMADATTLTEagyvgedvENIIQKLLQKCDYDVQKAQRG--------- 179
Cdd:pfam07724   3 IGSFLFLGPTGVGKTELAKALAELLFGderALIRIDMSEYME--------EHSVSRLIGAPPGYVGYEEGGqlteavrrk 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488980973  180 ---IVYIDEIDKISRksdnpsitrdvsgeGVQQALLKLIEGTVaaVPPQGGRkhpqqeflQVDTSKILFICGGAFAGLDK 256
Cdd:pfam07724  75 pysIVLIDEIEKAHP--------------GVQNDLLQILEGGT--LTDKQGR--------TVDFKNTLFIMTGNFGSEKI 130
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 488980973  257 VIshrvetgsgigfgatvkAKSDKASEGELLAQVEPEDLIKFGLIPEFIGRLPVV 311
Cdd:pfam07724 131 SD-----------------ASRLGDSPDYELLKEEVMDLLKKGFIPEFLGRLPII 168
RecA-like_protease cd19481
proteases similar to RecA; RecA-like NTPases. This family includes the NTP binding domain of ...
84-217 8.36e-23

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: 93.89  E-value: 8.36e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488980973  84 AKKVLAVAVYNHYKRLRNgdtSNGVELGKSNILLIGPTGSGKTLLAETLARLLDVPFTMADATTLTEA--GYVGEDVENI 161
Cdd:cd19481    1 LKASLREAVEAPRRGSRL---RRYGLGLPKGILLYGPPGTGKTLLAKALAGELGLPLIVVKLSSLLSKyvGESEKNLRKI 77
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 488980973 162 IQKLLQKcdydvqkaQRGIVYIDEIDKISRKSDNPSITRDVSgeGVQQALLKLIEG 217
Cdd:cd19481   78 FERARRL--------APCILFIDEIDAIGRKRDSSGESGELR--RVLNQLLTELDG 123
zf-C4_ClpX smart00994
ClpX C4-type zinc finger; The ClpX heat shock protein of Escherichia coli is a member of the ...
13-51 2.06e-22

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: 89.16  E-value: 2.06e-22
                           10        20        30
                   ....*....|....*....|....*....|....*....
gi 488980973    13 LYCSFCGKSQHEVRKLIAGPSVYICDECVDLCNDIIREE 51
Cdd:smart00994   1 LRCSFCGKSESEVRKLIAGPGVYICDECVELCYEILEEE 39
ClpB_D2-small smart01086
C-terminal, D2-small domain, of ClpB protein; This is the C-terminal domain of ClpB protein, ...
317-400 2.17e-22

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: 90.58  E-value: 2.17e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488980973   317 LSEEALIQILKEPKNALTKQYQAlfslEGAELEFRDEALDAIAKKAMARKTGARGLRSIVEAALLDTMYDLPS---MEDV 393
Cdd:smart01086   1 LDKEDLVRIVDLPLNALQKRLAE----KGITLEFTDEALDWLAEKGYDPKYGARPLRRIIQRELEDPLAELILsgeLKDG 76

                   ....*..
gi 488980973   394 EKVVIDE 400
Cdd:smart01086  77 DTVVVDV 83
zf-C4_ClpX pfam06689
ClpX C4-type zinc finger; The ClpX heat shock protein of Escherichia coli is a member of the ...
13-50 6.01e-21

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: 85.28  E-value: 6.01e-21
                          10        20        30
                  ....*....|....*....|....*....|....*....
gi 488980973   13 LYCSFCGKSQHEVRKLIAGPS-VYICDECVDLCNDIIRE 50
Cdd:pfam06689   1 LRCSFCGKSEDEVKKLIAGPNgVYICDECVELCYEILEE 39
AAA pfam00004
ATPase family associated with various cellular activities (AAA); AAA family proteins often ...
115-247 1.68e-15

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: 72.63  E-value: 1.68e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488980973  115 ILLIGPTGSGKTLLAETLARLLDVPFTMADATTLTEaGYVGEDVENIIQKLLQkcdydVQKAQRGIVYIDEIDKISRKSD 194
Cdd:pfam00004   1 LLLYGPPGTGKTTLAKAVAKELGAPFIEISGSELVS-KYVGESEKRLRELFEA-----AKKLAPCVIFIDEIDALAGSRG 74
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 488980973  195 NPSitrDVSGEGVQQALLKLIEGtvaavppqggrkhpqqefLQVDTSKILFIC 247
Cdd:pfam00004  75 SGG---DSESRRVVNQLLTELDG------------------FTSSNSKVIVIA 106
AAA cd00009
The AAA+ (ATPases Associated with a wide variety of cellular Activities) superfamily ...
79-195 1.85e-15

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


Pssm-ID: 99707 [Multi-domain]  Cd Length: 151  Bit Score: 73.33  E-value: 1.85e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488980973  79 IGQEQAKKVLAVAVYNHYKRlrngdtsngvelgksNILLIGPTGSGKTLLAETLARLL---DVPFTMADATTLTEAGYVG 155
Cdd:cd00009    1 VGQEEAIEALREALELPPPK---------------NLLLYGPPGTGKTTLARAIANELfrpGAPFLYLNASDLLEGLVVA 65
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 488980973 156 EDVENIIQKLLQKcdyDVQKAQRGIVYIDEIDKISRKSDN 195
Cdd:cd00009   66 ELFGHFLVRLLFE---LAEKAKPGVLFIDEIDSLSRGAQN 102
SpoVK COG0464
AAA+-type ATPase, SpoVK/Ycf46/Vps4 family [Cell wall/membrane/envelope biogenesis, Cell cycle ...
46-217 7.04e-14

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: 72.64  E-value: 7.04e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488980973  46 DIIREEIKEVAPHRERSALPTPHEIRHHLDDYVIGQEQAKKVL--AVAVYNHYKRLRNgdtSNGVELGKSnILLIGPTGS 123
Cdd:COG0464  127 EALALAAPLVTYEDIGGLEEELLELREAILDDLGGLEEVKEELreLVALPLKRPELRE---EYGLPPPRG-LLLYGPPGT 202
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488980973 124 GKTLLAETLARLLDVPFTMADATTLTeAGYVGEDVENiIQKLLQKcdydVQKAQRGIVYIDEIDKISRKSDNpsiTRDVS 203
Cdd:COG0464  203 GKTLLARALAGELGLPLIEVDLSDLV-SKYVGETEKN-LREVFDK----ARGLAPCVLFIDEADALAGKRGE---VGDGV 273
                        170
                 ....*....|....
gi 488980973 204 GEGVQQALLKLIEG 217
Cdd:COG0464  274 GRRVVNTLLTEMEE 287
ClpB_D2-small pfam10431
C-terminal, D2-small domain, of ClpB protein; This is the C-terminal domain of ClpB protein, ...
317-395 7.53e-13

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: 63.58  E-value: 7.53e-13
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 488980973  317 LSEEALIQILKEpknALTKQYQALFSlEGAELEFRDEALDAIAKKAMARKTGARGLRSIVEAALLDTMYDLPSMEDVEK 395
Cdd:pfam10431   1 LSKEELRKIVDL---QLKELQKRLAE-RGITLELTDAAKDWLAEKGYDPEYGARPLRRAIQREIEDPLAEEILSGELKE 75
RecA-like_CDC48_NLV2_r1-like cd19503
first of two ATPase domains of CDC48 and NLV2, and similar ATPase domains; CDC48 in yeast and ...
115-217 8.12e-11

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: 60.38  E-value: 8.12e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488980973 115 ILLIGPTGSGKTLLAETLARLLDVPFTMADATTLTeAGYVGEDVENiiqklLQKCDYDVQKAQRGIVYIDEIDKI--SRK 192
Cdd:cd19503   37 VLLHGPPGTGKTLLARAVANEAGANFLSISGPSIV-SKYLGESEKN-----LREIFEEARSHAPSIIFIDEIDALapKRE 110
                         90       100
                 ....*....|....*....|....*
gi 488980973 193 SDNPSITRDVsgegVQQaLLKLIEG 217
Cdd:cd19503  111 EDQREVERRV----VAQ-LLTLMDG 130
RecA-like_VPS4-like cd19509
ATPase domain of VPS4, ATAD1, K, KTNA1, Spastin, FIGL-1 and similar ATPase domains; This ...
78-221 2.98e-08

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: 52.74  E-value: 2.98e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488980973  78 VIGQEQAKKVLAVAVYnhYKRLRNGDTSNGVELGKSnILLIGPTGSGKTLLAETLARLLDVPFTMADATTLTeAGYVGED 157
Cdd:cd19509    1 IAGLDDAKEALKEAVI--LPSLRPDLFPGLRGPPRG-ILLYGPPGTGKTLLARAVASESGSTFFSISASSLV-SKWVGES 76
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 488980973 158 vENIIQKLlqkcdYDV-QKAQRGIVYIDEIDKI--SRKSDNPSITRDVSGEgvqqaLLKLIEGTVAA 221
Cdd:cd19509   77 -EKIVRAL-----FALaRELQPSIIFIDEIDSLlsERGSGEHEASRRVKTE-----FLVQMDGVLNK 132
RecA-like_NVL_r1-like cd19518
first of two ATPase domains of NVL (nuclear VCP-like protein) and similar ATPase domains; NVL ...
115-211 5.60e-08

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: 52.02  E-value: 5.60e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488980973 115 ILLIGPTGSGKTLLAETLARLLDVPFTMADATTLTeAGYVGEDVENiIQKLlqkcdYDVQKAQR-GIVYIDEIDKISRKS 193
Cdd:cd19518   37 VLLHGPPGCGKTMLANAIAGELKVPFLKISATEIV-SGVSGESEEK-IREL-----FDQAISNApCIVFIDEIDAITPKR 109
                         90
                 ....*....|....*...
gi 488980973 194 DNPSitRDVSGEGVQQAL 211
Cdd:cd19518  110 ESAQ--REMERRIVSQLL 125
RPT1 COG1222
ATP-dependent 26S proteasome regulatory subunit [Posttranslational modification, protein ...
45-217 1.22e-07

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


Pssm-ID: 440835 [Multi-domain]  Cd Length: 326  Bit Score: 53.09  E-value: 1.22e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488980973  45 NDIIREEIKEVAPHRERSALPTPhEIRhhLDDyVIGQEQAKKVLAVAVYNHYKR---LRngdtSNGVELGKSnILLIGPT 121
Cdd:COG1222   51 NDANLTQKRLGTPRGTAVPAESP-DVT--FDD-IGGLDEQIEEIREAVELPLKNpelFR----KYGIEPPKG-VLLYGPP 121
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488980973 122 GSGKTLLAETLARLLDVPFTMADATTLTEAgYVGEDvENIIQKLLQKcdydVQKAQRGIVYIDEIDKISRKSDNpSITrd 201
Cdd:COG1222  122 GTGKTLLAKAVAGELGAPFIRVRGSELVSK-YIGEG-ARNVREVFEL----AREKAPSIIFIDEIDAIAARRTD-DGT-- 192
                        170
                 ....*....|....*...
gi 488980973 202 vSGEG--VQQALLKLIEG 217
Cdd:COG1222  193 -SGEVqrTVNQLLAELDG 209
YifB COG0606
Predicted Mg-chelatase, contains ChlI-like and ATPase domains, YifB family [Posttranslational ...
52-136 2.78e-07

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: 52.35  E-value: 2.78e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488980973  52 IKEVAPH-RERSALP-----TPHEIRHHLDDY--VIGQEQAKKVLAVAVynhykrlrngdtsngveLGKSNILLIGPTGS 123
Cdd:COG0606  160 LLEVVAFlRGEQPLPpaepdAPPAEPPYEPDLadVKGQEQAKRALEIAA-----------------AGGHNLLMIGPPGS 222
                         90
                 ....*....|...
gi 488980973 124 GKTLLAETLARLL 136
Cdd:COG0606  223 GKTMLARRLPGIL 235
RecA-like_FtsH cd19501
ATP-dependent zinc metalloprotease FtsH; FtsH ATPase is a processive, ATP-dependent zinc ...
78-192 3.90e-07

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: 49.92  E-value: 3.90e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488980973  78 VIGQEQAKKVLAVAVynhyKRLRNGD--TSNGVELGKSnILLIGPTGSGKTLLAETLARLLDVPFTMADATTLTEAgYVG 155
Cdd:cd19501    6 VAGCEEAKEELKEVV----EFLKNPEkfTKLGAKIPKG-VLLVGPPGTGKTLLAKAVAGEAGVPFFSISGSDFVEM-FVG 79
                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 488980973 156 EDVENiIQKLLQKcdydVQKAQRGIVYIDEIDKISRK 192
Cdd:cd19501   80 VGASR-VRDLFEQ----AKKNAPCIVFIDEIDAVGRK 111
AAA_5 pfam07728
AAA domain (dynein-related subfamily); This Pfam entry includes some of the AAA proteins not ...
114-191 6.55e-07

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: 48.44  E-value: 6.55e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488980973  114 NILLIGPTGSGKTLLAETLARLLD--VPFTMADATTLTEAGYVGE-DVENIIQKLLQKCdyDVQKAQRG-IVYIDEIDKI 189
Cdd:pfam07728   1 GVLLVGPPGTGKTELAERLAAALSnrPVFYVQLTRDTTEEDLFGRrNIDPGGASWVDGP--LVRAAREGeIAVLDEINRA 78

                  ..
gi 488980973  190 SR 191
Cdd:pfam07728  79 NP 80
Mg_chelatase pfam01078
Magnesium chelatase, subunit ChlI; Magnesium-chelatase is a three-component enzyme that ...
78-145 6.89e-07

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: 49.46  E-value: 6.89e-07
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 488980973   78 VIGQEQAKKVLAVAVynhykrlrngdtsngveLGKSNILLIGPTGSGKTLLAETLARLLDvPFTMADA 145
Cdd:pfam01078   5 VKGQEQAKRALEIAA-----------------AGGHNLLMIGPPGSGKTMLAKRLPGILP-PLTEAEA 54
RecA-like_spastin cd19524
ATPase domain of spastin; Spastin is an ATP-dependent microtubule-severing protein involved in ...
78-205 7.07e-07

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: 49.08  E-value: 7.07e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488980973  78 VIGQEQAKKVLAVAVYNHYKRlrnGDTSNGVELGKSNILLIGPTGSGKTLLAETLARLLDVPFTMADATTLTeAGYVGED 157
Cdd:cd19524    2 IAGQDLAKQALQEMVILPSLR---PELFTGLRAPARGLLLFGPPGNGKTMLAKAVAAESNATFFNISAASLT-SKYVGEG 77
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 488980973 158 vENIIQKLLQKcdydVQKAQRGIVYIDEIDKI--SRKSDNPSITRDVSGE 205
Cdd:cd19524   78 -EKLVRALFAV----ARELQPSIIFIDEVDSLlsERSEGEHEASRRLKTE 122
RecA-like_ClpB_Hsp104-like cd19499
Chaperone protein ClpB/Hsp104 subfamily; Bacterial Caseinolytic peptidase B (ClpB) and ...
73-188 7.10e-07

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


Pssm-ID: 410907 [Multi-domain]  Cd Length: 178  Bit Score: 49.10  E-value: 7.10e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488980973  73 HLDDYVIGQEQAKKVLAVAVYNHYKRLRNGDTSNGVelgksnILLIGPTGSGKTLLAETLARLL---DVPFTMAD----- 144
Cdd:cd19499    8 RLHERVVGQDEAVKAVSDAIRRARAGLSDPNRPIGS------FLFLGPTGVGKTELAKALAELLfgdEDNLIRIDmseym 81
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 488980973 145 ----ATTLTEA--GYVGEDVeniIQKLLQKcdydVQKAQRGIVYIDEIDK 188
Cdd:cd19499   82 ekhsVSRLIGAppGYVGYTE---GGQLTEA----VRRKPYSVVLLDEIEK 124
RecA-like_Figl-1 cd19525
ATPase domain of Fidgetin-Like 1 (FIGL-1); FIGL-1 may participate in DNA repair in the nucleus; ...
78-194 9.35e-07

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


Pssm-ID: 410933 [Multi-domain]  Cd Length: 186  Bit Score: 48.83  E-value: 9.35e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488980973  78 VIGQEQAKKVLAVAVYNHYKRlrnGDTSNGVELGKSNILLIGPTGSGKTLLAETLARLLDVPFTMADATTLTeAGYVGED 157
Cdd:cd19525   24 IAGLEFAKKTIKEIVVWPMLR---PDIFTGLRGPPKGILLFGPPGTGKTLIGKCIASQSGATFFSISASSLT-SKWVGEG 99
                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 488980973 158 vENIIQKLlqkcdYDVQKAQR-GIVYIDEIDK-ISRKSD 194
Cdd:cd19525  100 -EKMVRAL-----FSVARCKQpAVIFIDEIDSlLSQRGE 132
AAA smart00382
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ...
112-192 2.36e-06

ATPases associated with a variety of cellular activities; AAA - ATPases associated with a variety of cellular activities. This profile/alignment only detects a fraction of this vast family. The poorly conserved N-terminal helix is missing from the alignment.


Pssm-ID: 214640 [Multi-domain]  Cd Length: 148  Bit Score: 46.98  E-value: 2.36e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488980973   112 KSNILLIGPTGSGKTLLAETLARLLDVP---FTMADATTLTEAGYVGEDVENIIQKLLQKCDYD--------VQKAQRGI 180
Cdd:smart00382   2 GEVILIVGPPGSGKTTLARALARELGPPgggVIYIDGEDILEEVLDQLLLIIVGGKKASGSGELrlrlalalARKLKPDV 81
                           90
                   ....*....|..
gi 488980973   181 VYIDEIDKISRK 192
Cdd:smart00382  82 LILDEITSLLDA 93
MoxR COG0714
MoxR-like ATPase [General function prediction only]; MoxR-like ATPase is part of the Pathway ...
66-212 3.03e-06

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


Pssm-ID: 440478 [Multi-domain]  Cd Length: 292  Bit Score: 48.63  E-value: 3.03e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488980973  66 TPHEIRHHLDDYVIGQEQAKKVLAVAVYnhykrlrngdtSNGvelgksNILLIGPTGSGKTLLAETLARLLDVPF----- 140
Cdd:COG0714    2 TEARLRAEIGKVYVGQEELIELVLIALL-----------AGG------HLLLEGVPGVGKTTLAKALARALGLPFiriqf 64
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488980973 141 ---TM-ADATtlteaG---YVGEDVENIIQK--LLQkcdydvqkaqrGIVYIDEIDKISRKsdnpsitrdvsgegVQQAL 211
Cdd:COG0714   65 tpdLLpSDIL-----GtyiYDQQTGEFEFRPgpLFA-----------NVLLADEINRAPPK--------------TQSAL 114

                 .
gi 488980973 212 L 212
Cdd:COG0714  115 L 115
CDC48 TIGR01243
AAA family ATPase, CDC48 subfamily; This subfamily of the AAA family ATPases includes two ...
107-217 3.95e-06

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


Pssm-ID: 273521 [Multi-domain]  Cd Length: 733  Bit Score: 49.14  E-value: 3.95e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488980973  107 GVELGKSnILLIGPTGSGKTLLAETLARLLDVPFTMADATTLTeAGYVGEDVENiiqklLQKCDYDVQKAQRGIVYIDEI 186
Cdd:TIGR01243 208 GIEPPKG-VLLYGPPGTGKTLLAKAVANEAGAYFISINGPEIM-SKYYGESEER-----LREIFKEAEENAPSIIFIDEI 280
                          90       100       110
                  ....*....|....*....|....*....|.
gi 488980973  187 DKISRKSDnpSITRDVSGEGVQQaLLKLIEG 217
Cdd:TIGR01243 281 DAIAPKRE--EVTGEVEKRVVAQ-LLTLMDG 308
RecA-like_KTNA1 cd19522
Katanin p60 ATPase-containing subunit A1; Katanin p60 ATPase-containing subunit A1 (KTNA1) is ...
78-229 4.68e-06

Katanin p60 ATPase-containing subunit A1; Katanin p60 ATPase-containing subunit A1 (KTNA1) is the catalytic subunit of the Katanin complex which is severs microtubules in an ATP-dependent manner, and is implicated in multiple aspects of microtubule dynamics. In addition to the p60 catalytic ATPase subunit, Katanin contains an accessory subunit (p80 or p80-like). The microtubule-severing activity of the ATPase is essential for female meiotic spindle assembly, and male gamete production; and the katanin complex severing microtubules is under tight regulation during the transition from the meiotic to mitotic stage to allow proper embryogenesis. This subfamily belongs to the RecA-like NTPase family which includes the NTP binding domain of F1 and V1 H(+)ATPases, DnaB and related helicases as well as bacterial RecA and related eukaryotic and archaeal recombinases. The RecA-like NTPase family also includes bacterial conjugation proteins and related DNA transfer proteins involved in type II and type IV secretion.


Pssm-ID: 410930 [Multi-domain]  Cd Length: 170  Bit Score: 46.52  E-value: 4.68e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488980973  78 VIGQEQAKKVLAVAVYnhyKRLRNGDTSNGVELGKSNILLIGPTGSGKTLLAETLARLLDVPFTMADATTLTeAGYVGED 157
Cdd:cd19522    2 IADLEEAKKLLEEAVV---LPMWMPEFFKGIRRPWKGVLMVGPPGTGKTLLAKAVATECGTTFFNVSSSTLT-SKYRGES 77
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 488980973 158 veniiQKLLqKCDYDVQKAQR-GIVYIDEIDKI-SRK--SDNPSITRDVSGEgvqqaLLKLIEGTVAAVPPQGGRK 229
Cdd:cd19522   78 -----EKLV-RLLFEMARFYApTTIFIDEIDSIcSRRgtSEEHEASRRVKSE-----LLVQMDGVGGASENDDPSK 142
hflB PRK10733
ATP-dependent zinc metalloprotease FtsH;
115-192 6.24e-06

ATP-dependent zinc metalloprotease FtsH;


Pssm-ID: 182683 [Multi-domain]  Cd Length: 644  Bit Score: 48.49  E-value: 6.24e-06
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 488980973 115 ILLIGPTGSGKTLLAETLARLLDVPFTMADATTLTEAgYVGEDVENIIQKLLQkcdydVQKAQRGIVYIDEIDKISRK 192
Cdd:PRK10733 188 VLMVGPPGTGKTLLAKAIAGEAKVPFFTISGSDFVEM-FVGVGASRVRDMFEQ-----AKKAAPCIIFIDEIDAVGRQ 259
PRK09862 PRK09862
ATP-dependent protease;
47-136 6.88e-06

ATP-dependent protease;


Pssm-ID: 182120 [Multi-domain]  Cd Length: 506  Bit Score: 48.05  E-value: 6.88e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488980973  47 IIREEIKEVAPHRE-RSALPTPHEIR-------HHLDDyVIGQEQAKKVLAVAVynhykrlrngdtsngveLGKSNILLI 118
Cdd:PRK09862 155 LIADHLQAVCAFLEgKHALERPKPTDavsralqHDLSD-VIGQEQGKRGLEITA-----------------AGGHNLLLI 216
                         90
                 ....*....|....*...
gi 488980973 119 GPTGSGKTLLAETLARLL 136
Cdd:PRK09862 217 GPPGTGKTMLASRINGLL 234
RecA-like_ATAD1 cd19520
ATPase domain of ATPase family AAA domain-containing protein 1 and similar ATPase domains; ...
115-191 7.32e-06

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: 45.88  E-value: 7.32e-06
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 488980973 115 ILLIGPTGSGKTLLAETLARLLDVPFTMADATTLTEAGYvGEDveniiQKLLQKCDYDVQKAQRGIVYIDEIDKISR 191
Cdd:cd19520   38 VLLYGPPGCGKTMLAKATAKEAGARFINLQVSSLTDKWY-GES-----QKLVAAVFSLASKLQPSIIFIDEIDSFLR 108
ftsH CHL00176
cell division protein; Validated
78-192 7.70e-06

cell division protein; Validated


Pssm-ID: 214386 [Multi-domain]  Cd Length: 638  Bit Score: 48.12  E-value: 7.70e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488980973  78 VIGQEQAKKVLAVAVYnhykRLRNGD--TSNGVELGKSnILLIGPTGSGKTLLAETLARLLDVPFtmadattLTEAGyvG 155
Cdd:CHL00176 185 IAGIEEAKEEFEEVVS----FLKKPErfTAVGAKIPKG-VLLVGPPGTGKTLLAKAIAGEAEVPF-------FSISG--S 250
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 488980973 156 EDVENIIQKLLQKCDYDVQKAQRG---IVYIDEIDKISRK 192
Cdd:CHL00176 251 EFVEMFVGVGAARVRDLFKKAKENspcIVFIDEIDAVGRQ 290
ClpA COG0542
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ...
266-382 8.26e-06

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


Pssm-ID: 440308 [Multi-domain]  Cd Length: 836  Bit Score: 48.15  E-value: 8.26e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488980973 266 SGIGFGATVKAKSDKASEGELLAQVEPEDLIKFGliPEFIGRLPVVATLNELSEEALIQI----LKEPKNALTKQyqalf 341
Cdd:COG0542  699 SNIGSELILDLAEDEPDYEEMKEAVMEELKKHFR--PEFLNRIDEIIVFHPLSKEELRKIvdlqLKRLRKRLAER----- 771
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 488980973 342 sleGAELEFRDEALDAIAKKAMARKTGARGLRSIVEAALLD 382
Cdd:COG0542  772 ---GITLELTDAAKDFLAEKGYDPEYGARPLKRAIQRELED 809
PRK13342 PRK13342
recombination factor protein RarA; Reviewed
74-219 1.95e-05

recombination factor protein RarA; Reviewed


Pssm-ID: 237355 [Multi-domain]  Cd Length: 413  Bit Score: 46.62  E-value: 1.95e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488980973  74 LDDyVIGQEQ---AKKVLAVAVYNHykRLrngdtsngvelgkSNILLIGPTGSGKTLLAETLARLLDVPFTMADATTlte 150
Cdd:PRK13342  11 LDE-VVGQEHllgPGKPLRRMIEAG--RL-------------SSMILWGPPGTGKTTLARIIAGATDAPFEALSAVT--- 71
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488980973 151 AGyVgEDVENIIQKLLQKCDYDvqkaQRGIVYIDEIDKISRKSdnpsitrdvsgegvQQALLKLIE-GTV 219
Cdd:PRK13342  72 SG-V-KDLREVIEEARQRRSAG----RRTILFIDEIHRFNKAQ--------------QDALLPHVEdGTI 121
RecA-like_CDC48_r1-like cd19519
first of two ATPase domains of CDC48 and similar ATPase domains; CDC48 in yeast and p97 or VCP ...
115-217 2.35e-05

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


Pssm-ID: 410927 [Multi-domain]  Cd Length: 166  Bit Score: 44.35  E-value: 2.35e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488980973 115 ILLIGPTGSGKTLLAETLARLLDVPFTMADATTLTeAGYVGEDVENiiqklLQKCDYDVQKAQRGIVYIDEIDKISRKSD 194
Cdd:cd19519   37 ILLYGPPGTGKTLIARAVANETGAFFFLINGPEIM-SKLAGESESN-----LRKAFEEAEKNAPAIIFIDEIDAIAPKRE 110
                         90       100
                 ....*....|....*....|...
gi 488980973 195 NpsITRDVSGEGVQQaLLKLIEG 217
Cdd:cd19519  111 K--THGEVERRIVSQ-LLTLMDG 130
RecA-like_PEX6_r2 cd19527
second of two ATPase domains of Peroxisomal biogenesis factor 6 (PEX6); PEX6(also known as ...
112-214 3.16e-05

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


Pssm-ID: 410935 [Multi-domain]  Cd Length: 160  Bit Score: 44.04  E-value: 3.16e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488980973 112 KSNILLIGPTGSGKTLLAETLARLLDVPFTMADATTLTEAgYVGEDVENiIQKLLQKcdydVQKAQRGIVYIDEIDKISR 191
Cdd:cd19527   26 RSGILLYGPPGTGKTLLAKAIATECSLNFLSVKGPELINM-YIGESEAN-VREVFQK----ARDAKPCVIFFDELDSLAP 99
                         90       100
                 ....*....|....*....|...
gi 488980973 192 KSDNPSITRDVSGEGVQQALLKL 214
Cdd:cd19527  100 SRGNSGDSGGVMDRVVSQLLAEL 122
AAA_22 pfam13401
AAA domain;
108-195 5.12e-05

AAA domain;


Pssm-ID: 379165 [Multi-domain]  Cd Length: 129  Bit Score: 42.71  E-value: 5.12e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488980973  108 VELGKSNILLIGPTGSGKTLLAETLARLLD------VPFTMADATTLTE-----AGYVGEDVENIIQK---LLQKCDYDV 173
Cdd:pfam13401   1 IRFGAGILVLTGESGTGKTTLLRRLLEQLPevrdsvVFVDLPSGTSPKDllralLRALGLPLSGRLSKeelLAALQQLLL 80
                          90       100
                  ....*....|....*....|..
gi 488980973  174 QKAQRGIVYIDEIDKISRKSDN 195
Cdd:pfam13401  81 ALAVAVVLIIDEAQHLSLEALE 102
clpA PRK11034
ATP-dependent Clp protease ATP-binding subunit; Provisional
60-380 5.32e-05

ATP-dependent Clp protease ATP-binding subunit; Provisional


Pssm-ID: 236828 [Multi-domain]  Cd Length: 758  Bit Score: 45.60  E-value: 5.32e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488980973  60 ERSALPTPHEIRHHLDD----YVIGQEQAKKVLAVAVynhyKRLRNGdtsngveLGKSN-----ILLIGPTGSGKTLLAE 130
Cdd:PRK11034 438 EKSVSQSDRDTLKNLGDrlkmLVFGQDKAIEALTEAI----KMSRAG-------LGHEHkpvgsFLFAGPTGVGKTEVTV 506
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488980973 131 TLARLLDVPFTMADATTLTE-----------AGYVGEDVENIIQKLlqkcdydVQKAQRGIVYIDEIDKIsrksdNPSIT 199
Cdd:PRK11034 507 QLSKALGIELLRFDMSEYMErhtvsrligapPGYVGFDQGGLLTDA-------VIKHPHAVLLLDEIEKA-----HPDVF 574
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488980973 200 rdvsgegvqQALLKLIE-GTVAavpPQGGRKhpqqeflqVDTSKILFIcggafagldkvishrVETGSGIgfgatvkAKS 278
Cdd:PRK11034 575 ---------NLLLQVMDnGTLT---DNNGRK--------ADFRNVVLV---------------MTTNAGV-------RET 612
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488980973 279 DKASEGeLLAQVEPEDL---IKFGLIPEFIGRLPVVATLNELSEEALIQILkepkNALTKQYQALFSLEGAELEFRDEAL 355
Cdd:PRK11034 613 ERKSIG-LIHQDNSTDAmeeIKKIFTPEFRNRLDNIIWFDHLSTDVIHQVV----DKFIVELQAQLDQKGVSLEVSQEAR 687
                        330       340
                 ....*....|....*....|....*
gi 488980973 356 DAIAKKAMARKTGARGLRSIVEAAL 380
Cdd:PRK11034 688 DWLAEKGYDRAMGARPMARVIQDNL 712
RecA-like_PAN_like cd19502
proteasome activating nucleotidase PAN and related proteasome subunits; This subfamily ...
115-215 9.83e-05

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


Pssm-ID: 410910 [Multi-domain]  Cd Length: 171  Bit Score: 42.71  E-value: 9.83e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488980973 115 ILLIGPTGSGKTLLAETLARLLDVPFTMADATTLTEAgYVGEDVEnIIQKLLQKcdydVQKAQRGIVYIDEIDKI--SRK 192
Cdd:cd19502   40 VLLYGPPGTGKTLLAKAVANHTDATFIRVVGSELVQK-YIGEGAR-LVRELFEM----AREKAPSIIFIDEIDAIgaKRF 113
                         90       100
                 ....*....|....*....|...
gi 488980973 193 SDNPSITRDvsgegVQQALLKLI 215
Cdd:cd19502  114 DSGTGGDRE-----VQRTMLELL 131
RecA-like_Lon cd19500
lon protease homolog 2 peroxisomal; Lon protease (also known as Lon peptidase) is an ...
115-247 1.01e-04

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: 42.93  E-value: 1.01e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488980973 115 ILLIGPTGSGKTLLAETLARLLDVPFT------MADattltEA-------GYVGEDVENIIQKlLQKCdydvqKAQRGIV 181
Cdd:cd19500   40 LCLVGPPGVGKTSLGKSIARALGRKFVrislggVRD-----EAeirghrrTYVGAMPGRIIQA-LKKA-----GTNNPVF 108
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 488980973 182 YIDEIDKISRKSD-NPSitrdvsgegvqQALLKLIEgtvaavPPQGGRKHPQQEFLQVDTSKILFIC 247
Cdd:cd19500  109 LLDEIDKIGSSFRgDPA-----------SALLEVLD------PEQNSTFSDHYLDVPFDLSKVLFIA 158
RecA-like_PEX1_r2 cd19526
second of two ATPase domains of Peroxisomal biogenesis factor 1 (PEX1); PEX1(also known as ...
112-214 1.56e-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: 42.03  E-value: 1.56e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488980973 112 KSNILLIGPTGSGKTLLAETLARLLDVPFTMADATTLTeAGYVGEDVENiIQKLLQKcdydVQKAQRGIVYIDEIDKIS- 190
Cdd:cd19526   27 RSGILLYGPPGCGKTLLASAIASECGLNFISVKGPELL-NKYIGASEQN-VRDLFSR----AQSAKPCILFFDEFDSIAp 100
                         90       100
                 ....*....|....*....|....*
gi 488980973 191 -RKSDNPSITRDVsgegVQQALLKL 214
Cdd:cd19526  101 kRGHDSTGVTDRV----VNQLLTQL 121
clpC CHL00095
Clp protease ATP binding subunit
112-186 2.87e-04

Clp protease ATP binding subunit


Pssm-ID: 214361 [Multi-domain]  Cd Length: 821  Bit Score: 43.12  E-value: 2.87e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488980973 112 KSNILLIGPTGSGKTLLAETLARLL---DVPFTMAD--------ATTLTEAGYVGEdVENIIQKLLQkcdyDVQKAQRGI 180
Cdd:CHL00095 200 KNNPILIGEPGVGKTAIAEGLAQRIvnrDVPDILEDklvitldiGLLLAGTKYRGE-FEERLKRIFD----EIQENNNII 274

                 ....*.
gi 488980973 181 VYIDEI 186
Cdd:CHL00095 275 LVIDEV 280
RecA-like_CDC48_r2-like cd19511
second of two ATPase domains of CDC48/p97, PEX1 and -6, VAT and NVL, and similar ATPase ...
115-197 4.21e-04

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: 40.73  E-value: 4.21e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488980973 115 ILLIGPTGSGKTLLAETLARLLDVPFTMADATTLTEAgYVGEDvENIIQKLLQKcdydVQKAQRGIVYIDEIDKI-SRKS 193
Cdd:cd19511   30 VLLYGPPGCGKTLLAKALASEAGLNFISVKGPELFSK-YVGES-ERAVREIFQK----ARQAAPCIIFFDEIDSLaPRRG 103

                 ....
gi 488980973 194 DNPS 197
Cdd:cd19511  104 QSDS 107
RecA-like_ATAD3-like cd19512
ATPase domains of ATPase AAA-domain protein 3A (ATAD3A), -3B, and -3C, and similar ATPase ...
114-201 4.71e-04

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: 40.20  E-value: 4.71e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488980973 114 NILLIGPTGSGKTLLAETLARLLDVPFTMadaTTLTEAGYVGEDVENIIQKLLqkcDYdVQKAQRG-IVYIDEIDKISRK 192
Cdd:cd19512   24 NILFYGPPGTGKTLFAKKLALHSGMDYAI---MTGGDVAPMGREGVTAIHKVF---DW-ANTSRRGlLLFVDEADAFLRK 96

                 ....*....
gi 488980973 193 SDNPSITRD 201
Cdd:cd19512   97 RSTEKISED 105
RecA-like_NSF-SEC18_r1-like cd19504
first of two ATPase domains of NSF and SEC18, and similar ATPase domains; ...
115-217 5.67e-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: 40.55  E-value: 5.67e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488980973 115 ILLIGPTGSGKTLLAETLARLLDV--PFTMADATTLTEagYVGEDVENiIQKLLQkcDYDVQKAQRG------IVYIDEI 186
Cdd:cd19504   38 ILLYGPPGTGKTLMARQIGKMLNArePKIVNGPEILNK--YVGESEAN-IRKLFA--DAEEEQRRLGansglhIIIFDEI 112
                         90       100       110
                 ....*....|....*....|....*....|...
gi 488980973 187 DKISRKSDNpsiTRDVSGEG--VQQALLKLIEG 217
Cdd:cd19504  113 DAICKQRGS---MAGSTGVHdtVVNQLLSKIDG 142
clpA PRK11034
ATP-dependent Clp protease ATP-binding subunit; Provisional
112-189 9.52e-04

ATP-dependent Clp protease ATP-binding subunit; Provisional


Pssm-ID: 236828 [Multi-domain]  Cd Length: 758  Bit Score: 41.36  E-value: 9.52e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488980973 112 KSNILLIGPTGSGKTLLAETLA-RLL--DVPFTMADATT--------LTEAGYVGeDVENIIQKLLQKcdydVQKAQRGI 180
Cdd:PRK11034 207 KNNPLLVGESGVGKTAIAEGLAwRIVqgDVPEVMADCTIysldigslLAGTKYRG-DFEKRFKALLKQ----LEQDTNSI 281

                 ....*....
gi 488980973 181 VYIDEIDKI 189
Cdd:PRK11034 282 LFIDEIHTI 290
ruvB PRK00080
Holliday junction branch migration DNA helicase RuvB;
74-191 1.00e-03

Holliday junction branch migration DNA helicase RuvB;


Pssm-ID: 234619 [Multi-domain]  Cd Length: 328  Bit Score: 40.88  E-value: 1.00e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488980973  74 LDDYvIGQEQAKKVLAVAVYNHYKRlrngdtsngvelGKS--NILLIGPTGSGKTLLAETLARLLDVPFTMADATTLTEA 151
Cdd:PRK00080  24 LDEF-IGQEKVKENLKIFIEAAKKR------------GEAldHVLLYGPPGLGKTTLANIIANEMGVNIRITSGPALEKP 90
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 488980973 152 GyvgeDVENIIQkLLQKCDydvqkaqrgIVYIDEIDKISR 191
Cdd:PRK00080  91 G----DLAAILT-NLEEGD---------VLFIDEIHRLSP 116
aroK PRK00131
shikimate kinase; Reviewed
110-140 1.32e-03

shikimate kinase; Reviewed


Pssm-ID: 234654 [Multi-domain]  Cd Length: 175  Bit Score: 39.40  E-value: 1.32e-03
                         10        20        30
                 ....*....|....*....|....*....|.
gi 488980973 110 LGKSNILLIGPTGSGKTLLAETLARLLDVPF 140
Cdd:PRK00131   2 LKGPNIVLIGFMGAGKSTIGRLLAKRLGYDF 32
TIP49 COG1224
DNA helicase TIP49, TBP-interacting protein [Transcription];
51-145 1.47e-03

DNA helicase TIP49, TBP-interacting protein [Transcription];


Pssm-ID: 440837 [Multi-domain]  Cd Length: 452  Bit Score: 40.72  E-value: 1.47e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488980973  51 EIKEVAPHRERSALPTPHEIRH-HLD---------DYVIGQEQAKKVLAVAVynhyKRLRNGdtsngvELGKSNILLIGP 120
Cdd:COG1224    3 EIREIEKVKEFERISAHSHIRGlGLDengkakfvaDGLVGQVEAREAAGIVV----KMIKEG------KMAGKGILIVGP 72
                         90       100
                 ....*....|....*....|....*..
gi 488980973 121 TGSGKTLLAETLARLL--DVPFTMADA 145
Cdd:COG1224   73 PGTGKTALAVAIARELgeDTPFVAISG 99
RecA-like_VCP_r2 cd19529
second of two ATPase domains of Valosin-containing protein-like ATPase (VAT) and similar ...
115-214 1.59e-03

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


Pssm-ID: 410937 [Multi-domain]  Cd Length: 159  Bit Score: 39.02  E-value: 1.59e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488980973 115 ILLIGPTGSGKTLLAETLARLLDVPFTMADATTLTeAGYVGEDvENIIQKLLQKcdydVQKAQRGIVYIDEIDKIS--RK 192
Cdd:cd19529   30 ILLYGPPGTGKTLLAKAVATESNANFISVKGPELL-SKWVGES-EKAIREIFRK----ARQVAPCVIFFDEIDSIAprRG 103
                         90       100
                 ....*....|....*....|..
gi 488980973 193 SDNPSitrDVSGEGVQQALLKL 214
Cdd:cd19529  104 TTGDS---GVTERVVNQLLTEL 122
RecA-like_VPS4 cd19521
ATPase domain of vacuolar protein sorting-associated protein 4; Vacuolar protein ...
113-197 1.97e-03

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


Pssm-ID: 410929 [Multi-domain]  Cd Length: 170  Bit Score: 39.07  E-value: 1.97e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488980973 113 SNILLIGPTGSGKTLLAETLARLLDVPFTMADATTLTeAGYVGEDvENIIQKLLQKcdydVQKAQRGIVYIDEIDKI-SR 191
Cdd:cd19521   41 SGILLYGPPGTGKSYLAKAVATEANSTFFSVSSSDLV-SKWMGES-EKLVKQLFAM----ARENKPSIIFIDEVDSLcGT 114

                 ....*.
gi 488980973 192 KSDNPS 197
Cdd:cd19521  115 RGEGES 120
CDC48 TIGR01243
AAA family ATPase, CDC48 subfamily; This subfamily of the AAA family ATPases includes two ...
115-192 2.59e-03

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: 40.28  E-value: 2.59e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 488980973  115 ILLIGPTGSGKTLLAETLARLLDVPFTMADATTLTeAGYVGEDvENIIQKLLQKcdydVQKAQRGIVYIDEIDKISRK 192
Cdd:TIGR01243 490 VLLFGPPGTGKTLLAKAVATESGANFIAVRGPEIL-SKWVGES-EKAIREIFRK----ARQAAPAIIFFDEIDAIAPA 561
RecA-like_Ycf46-like cd19507
ATPase domain of Ycf46 and similar ATPase domains; Ycf46 may play a role in the regulation of ...
115-188 2.64e-03

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


Pssm-ID: 410915 [Multi-domain]  Cd Length: 161  Bit Score: 38.50  E-value: 2.64e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 488980973 115 ILLIGPTGSGKTLLAETLARLLDVPFTMADATTLTeAGYVGEDVENIIQKL-----LQKCdydvqkaqrgIVYIDEIDK 188
Cdd:cd19507   34 LLLVGIQGTGKSLTAKAIAGVWQLPLLRLDMGRLF-GGLVGESESRLRQMIqtaeaIAPC----------VLWIDEIEK 101
SK cd00464
Shikimate kinase (SK) is the fifth enzyme in the shikimate pathway, a seven-step biosynthetic ...
114-144 3.14e-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: 37.92  E-value: 3.14e-03
                         10        20        30
                 ....*....|....*....|....*....|.
gi 488980973 114 NILLIGPTGSGKTLLAETLARLLDVPFTMAD 144
Cdd:cd00464    1 NIVLIGMMGAGKTTVGRLLAKALGLPFVDLD 31
RecA-like_fidgetin cd19523
ATPase domain of fidgetin; Fidgetin (FIGN) is a ATP-dependent microtubule severing protein. ...
78-187 3.45e-03

ATPase domain of fidgetin; Fidgetin (FIGN) is a ATP-dependent 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: 410931 [Multi-domain]  Cd Length: 163  Bit Score: 37.94  E-value: 3.45e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488980973  78 VIGQEQAKKVLAVAVYnhYKRLRNGDTSNGVELGKSnILLIGPTGSGKTLLAETLARLLDVPFTMADATTLTeAGYVGED 157
Cdd:cd19523    2 IAGLGALKAAIKEEVL--WPLLRPDAFSGLLRLPRS-ILLFGPRGTGKTLLGRCLASQLGATFLRLRGSTLV-AKWAGEG 77
                         90       100       110
                 ....*....|....*....|....*....|..
gi 488980973 158 vENIIQK--LLQKCdydvqkAQRGIVYIDEID 187
Cdd:cd19523   78 -EKILQAsfLAARC------RQPSVLFISDLD 102
clpC CHL00095
Clp protease ATP binding subunit
69-387 5.29e-03

Clp protease ATP binding subunit


Pssm-ID: 214361 [Multi-domain]  Cd Length: 821  Bit Score: 39.27  E-value: 5.29e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488980973  69 EIRHHLDDYVIGQEQAkkvlAVAVYNHYKRLRNGdtsngveLGKSN-----ILLIGPTGSGKTLLAETLARL-------- 135
Cdd:CHL00095 502 HMEETLHKRIIGQDEA----VVAVSKAIRRARVG-------LKNPNrpiasFLFSGPTGVGKTELTKALASYffgsedam 570
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488980973 136 --LDVPFTMADATTL----TEAGYVGEDVENIIQKLLQKCDYDVqkaqrgiVYIDEIDKISRKSDNpsitrdvsgegvqq 209
Cdd:CHL00095 571 irLDMSEYMEKHTVSkligSPPGYVGYNEGGQLTEAVRKKPYTV-------VLFDEIEKAHPDIFN-------------- 629
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488980973 210 ALLKLIE-GTVAavpPQGGRKHPQQEFLQVDTSKIlficgGAfagldKVIShrvETGSGIGFGATVKAKSDKASEgELLA 288
Cdd:CHL00095 630 LLLQILDdGRLT---DSKGRTIDFKNTLIIMTSNL-----GS-----KVIE---TNSGGLGFELSENQLSEKQYK-RLSN 692
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488980973 289 QVEpEDLIKFgLIPEFIGRLPVVATLNELSEEALIQILkepkNALTKQYQALFSLEGAELEFRDEALDAIAKKAMARKTG 368
Cdd:CHL00095 693 LVN-EELKQF-FRPEFLNRLDEIIVFRQLTKNDVWEIA----EIMLKNLFKRLNEQGIQLEVTERIKTLLIEEGYNPLYG 766
                        330
                 ....*....|....*....
gi 488980973 369 ARGLRSIVEAALLDTMYDL 387
Cdd:CHL00095 767 ARPLRRAIMRLLEDPLAEE 785
CDC6 COG1474
Cdc6-related protein, AAA superfamily ATPase [Replication, recombination and repair];
113-195 7.18e-03

Cdc6-related protein, AAA superfamily ATPase [Replication, recombination and repair];


Pssm-ID: 441083 [Multi-domain]  Cd Length: 389  Bit Score: 38.29  E-value: 7.18e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488980973 113 SNILLIGPTGSGKTLLA-------ETLARLLDVPFTMA-----DATTLTEA-----------------GYVGEDVENIIQ 163
Cdd:COG1474   52 SNVLIYGPTGTGKTAVAkyvleelEEEAEERGVDVRVVyvncrQASTRYRVlsrileelgsgedipstGLSTDELFDRLY 131
                         90       100       110
                 ....*....|....*....|....*....|..
gi 488980973 164 KLLQKCDYDVqkaqrgIVYIDEIDKISRKSDN 195
Cdd:COG1474  132 EALDERDGVL------VVVLDEIDYLVDDEGD 157
AroK COG0703
Shikimate kinase [Amino acid transport and metabolism]; Shikimate kinase is part of the ...
115-140 9.61e-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: 36.65  E-value: 9.61e-03
                         10        20
                 ....*....|....*....|....*.
gi 488980973 115 ILLIGPTGSGKTLLAETLARLLDVPF 140
Cdd:COG0703    1 IVLIGMMGAGKSTVGRLLAKRLGLPF 26
 
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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