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Conserved domains on  [gi|517799491|ref|WP_018969699|]
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ATP-dependent Clp protease ATP-binding subunit ClpX [Rubritalea marina]

Protein Classification

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

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

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

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
ClpX COG1219
ATP-dependent protease Clp, ATPase subunit ClpX [Posttranslational modification, protein ...
 1-423 0e+00

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


:

Pssm-ID: 440832 [Multi-domain]  Cd Length: 409  Bit Score: 792.33  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517799491   1 MARSKNLTL-CSFCGKSHSEVKKLIAGPGVYICNECIDVCSSILQKEIKElgelsstdgtlGTDLQSDDSLLTPAEICAR 79
Cdd:COG1219    1 MAGDSKKELkCSFCGKSQDEVRKLIAGPGVYICDECVELCNEIIEEELKE-----------EEAEEELKKLPKPKEIKAF 69

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517799491  80 LDEYIIGQEHAKKTLSVAVYNHYQRLRQSNHSHDpeldGVEIEKSNILMLGPTGSGKTLLARTLARVLDVPFSIVDATTL 159
Cdd:COG1219   70 LDEYVIGQERAKKVLSVAVYNHYKRLNSGSKDDD----DVELEKSNILLIGPTGSGKTLLAQTLARILDVPFAIADATTL 145

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517799491 160 TEAGYVGEDVENIILRLLQAADGDIERAERGIIYVDEIDKIGRKTENVSITRDVSGEGVQQALLKILEGTVCNVPPQGGR 239
Cdd:COG1219  146 TEAGYVGEDVENILLKLLQAADYDVEKAERGIIYIDEIDKIARKSENPSITRDVSGEGVQQALLKILEGTVANVPPQGGR 225

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517799491 240 KHPQQEYIQVNTEKILFIVGGAFVGMEDLVRDRLGKRSLGFQVSQEDSLQTEDRELLTKVQPEDLLHFGLIPEFIGRLPV 319
Cdd:COG1219  226 KHPQQEFIQIDTTNILFICGGAFDGLEKIIERRLGKKSIGFGAEVKSKKEKDEGELLKQVEPEDLIKFGLIPEFIGRLPV 305

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517799491 320 FSSLRKLNEEELVRILTEPKNAMVKQYQKLLGMNDVKLKITKDGLTALAEEAVRRGTGARALRSIVENLMLDVMYDVPSR 399
Cdd:COG1219  306 IATLEELDEEALVRILTEPKNALVKQYQKLFEMDGVELEFTDEALEAIAKKAIERKTGARGLRSILEEILLDVMYELPSR 385

                        410       420
                 ....*....|....*....|....
gi 517799491 400 TDIESVTINRPVVEGEKPPMLKKK 423
Cdd:COG1219  386 KDVKKVVITKEVVEGKAKPILVYK 409
 
Name Accession Description Interval E-value
ClpX COG1219
ATP-dependent protease Clp, ATPase subunit ClpX [Posttranslational modification, protein ...
 1-423 0e+00

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


Pssm-ID: 440832 [Multi-domain]  Cd Length: 409  Bit Score: 792.33  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517799491   1 MARSKNLTL-CSFCGKSHSEVKKLIAGPGVYICNECIDVCSSILQKEIKElgelsstdgtlGTDLQSDDSLLTPAEICAR 79
Cdd:COG1219    1 MAGDSKKELkCSFCGKSQDEVRKLIAGPGVYICDECVELCNEIIEEELKE-----------EEAEEELKKLPKPKEIKAF 69

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517799491  80 LDEYIIGQEHAKKTLSVAVYNHYQRLRQSNHSHDpeldGVEIEKSNILMLGPTGSGKTLLARTLARVLDVPFSIVDATTL 159
Cdd:COG1219   70 LDEYVIGQERAKKVLSVAVYNHYKRLNSGSKDDD----DVELEKSNILLIGPTGSGKTLLAQTLARILDVPFAIADATTL 145

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517799491 160 TEAGYVGEDVENIILRLLQAADGDIERAERGIIYVDEIDKIGRKTENVSITRDVSGEGVQQALLKILEGTVCNVPPQGGR 239
Cdd:COG1219  146 TEAGYVGEDVENILLKLLQAADYDVEKAERGIIYIDEIDKIARKSENPSITRDVSGEGVQQALLKILEGTVANVPPQGGR 225

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517799491 240 KHPQQEYIQVNTEKILFIVGGAFVGMEDLVRDRLGKRSLGFQVSQEDSLQTEDRELLTKVQPEDLLHFGLIPEFIGRLPV 319
Cdd:COG1219  226 KHPQQEFIQIDTTNILFICGGAFDGLEKIIERRLGKKSIGFGAEVKSKKEKDEGELLKQVEPEDLIKFGLIPEFIGRLPV 305

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517799491 320 FSSLRKLNEEELVRILTEPKNAMVKQYQKLLGMNDVKLKITKDGLTALAEEAVRRGTGARALRSIVENLMLDVMYDVPSR 399
Cdd:COG1219  306 IATLEELDEEALVRILTEPKNALVKQYQKLFEMDGVELEFTDEALEAIAKKAIERKTGARGLRSILEEILLDVMYELPSR 385

                        410       420
                 ....*....|....*....|....
gi 517799491 400 TDIESVTINRPVVEGEKPPMLKKK 423
Cdd:COG1219  386 KDVKKVVITKEVVEGKAKPILVYK 409
clpX PRK05342
ATP-dependent Clp protease ATP-binding subunit ClpX;
1-420 0e+00

ATP-dependent Clp protease ATP-binding subunit ClpX;


Pssm-ID: 235422 [Multi-domain]  Cd Length: 412  Bit Score: 751.99  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517799491   1 MARSKNLTLCSFCGKSHSEVKKLIAGPGVYICNECIDVCSSILQKEIKELGELSStdgtlgtdlqsddSLLTPAEICARL 80
Cdd:PRK05342   3 GGDSKKLLYCSFCGKSQHEVRKLIAGPGVYICDECIELCNEIIREELKEEAVELK-------------ELPTPKEIKAHL 69

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517799491  81 DEYIIGQEHAKKTLSVAVYNHYQRLRQSNHshdpELDGVEIEKSNILMLGPTGSGKTLLARTLARVLDVPFSIVDATTLT 160
Cdd:PRK05342  70 DQYVIGQERAKKVLSVAVYNHYKRLRHGDK----KDDDVELQKSNILLIGPTGSGKTLLAQTLARILDVPFAIADATTLT 145

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517799491 161 EAGYVGEDVENIILRLLQAADGDIERAERGIIYVDEIDKIGRKTENVSITRDVSGEGVQQALLKILEGTVCNVPPQGGRK 240
Cdd:PRK05342 146 EAGYVGEDVENILLKLLQAADYDVEKAQRGIVYIDEIDKIARKSENPSITRDVSGEGVQQALLKILEGTVASVPPQGGRK 225

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517799491 241 HPQQEYIQVNTEKILFIVGGAFVGMEDLVRDRLGKRSLGF--QVSQEDSLQTEDrELLTKVQPEDLLHFGLIPEFIGRLP 318
Cdd:PRK05342 226 HPQQEFIQVDTTNILFICGGAFDGLEKIIKQRLGKKGIGFgaEVKSKKEKRTEG-ELLKQVEPEDLIKFGLIPEFIGRLP 304

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517799491 319 VFSSLRKLNEEELVRILTEPKNAMVKQYQKLLGMNDVKLKITKDGLTALAEEAVRRGTGARALRSIVENLMLDVMYDVPS 398
Cdd:PRK05342 305 VVATLEELDEEALVRILTEPKNALVKQYQKLFEMDGVELEFTDEALEAIAKKAIERKTGARGLRSILEEILLDVMFELPS 384

                        410       420
                 ....*....|....*....|..
gi 517799491 399 RTDIESVTINRPVVEGEKPPML 420
Cdd:PRK05342 385 REDVEKVVITKEVVEGKAKPLL 406
clpX TIGR00382
endopeptidase Clp ATP-binding regulatory subunit (clpX); A member of the ATP-dependent ...
 1-420 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: 583.65  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517799491    1 MARSKNLTLCSFCGKSHSEVKKLIAGPGVYICNECIDVCSSILQKEIKELGELSSTDgtlgTDLQSDDsLLTPAEICARL 80
Cdd:TIGR00382   1 MTKKNETLYCSFCGKSQDEVRKLIAGPGVYICDECIELCHDILEEELGTRKESKEYE----EEFELSY-LPTPKEIKAHL 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517799491   81 DEYIIGQEHAKKTLSVAVYNHYQRLRQSNHSHDPelDGVEIEKSNILMLGPTGSGKTLLARTLARVLDVPFSIVDATTLT 160
Cdd:TIGR00382  76 DEYVIGQEQAKKVLSVAVYNHYKRLNFEKNKKSD--NGVELSKSNILLIGPTGSGKTLLAQTLARILNVPFAIADATTLT 153

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517799491  161 EAGYVGEDVENIILRLLQAADGDIERAERGIIYVDEIDKIGRKTENVSITRDVSGEGVQQALLKILEGTVCNVPPQGGRK 240
Cdd:TIGR00382 154 EAGYVGEDVENILLKLLQAADYDVEKAQKGIIYIDEIDKISRKSENPSITRDVSGEGVQQALLKIIEGTVANVPPQGGRK 233

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517799491  241 HPQQEYIQVNTEKILFIVGGAFVGMEDLVRDRLGKRSLGFqVSQEDSLQTEDRELLTKVQPEDLLHFGLIPEFIGRLPVF 320
Cdd:TIGR00382 234 HPYQEFIQIDTSNILFICGGAFVGLEKIIKKRTGKSSIGF-GAEVKKKSKEKADLLRQVEPEDLVKFGLIPEFIGRLPVI 312

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517799491  321 SSLRKLNEEELVRILTEPKNAMVKQYQKLLGMNDVKLKITKDGLTALAEEAVRRGTGARALRSIVENLMLDVMYDVPSRT 400
Cdd:TIGR00382 313 ATLEKLDEEALIAILTKPKNALVKQYQALFKMDNVELDFEEEALKAIAKKALERKTGARGLRSIVEGLLLDVMFDLPSLE 392

                         410       420
                  ....*....|....*....|
gi 517799491  401 DIESVTINRPVVEGEKPPML 420
Cdd:TIGR00382 393 DLEKVVITKETVLKQSEPLL 412
RecA-like_ClpX cd19497
ATP-dependent Clp protease ATP-binding subunit ClpX; ClpX is a component of the ATP-dependent ...
 71-323 1.04e-162

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: 457.83  E-value: 1.04e-162
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517799491  71 LTPAEICARLDEYIIGQEHAKKTLSVAVYNHYQRLRQSNHSHDpelDGVEIEKSNILMLGPTGSGKTLLARTLARVLDVP 150
Cdd:cd19497    1 PTPKEIKEHLDKYVIGQERAKKVLSVAVYNHYKRIRNNLKQKD---DDVELEKSNILLIGPTGSGKTLLAQTLAKILDVP 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517799491 151 FSIVDATTLTEAGYVGEDVENIILRLLQAADGDIERAERGIIYVDEIDKIGRKTENVSITRDVSGEGVQQALLKILEGTV 230
Cdd:cd19497   78 FAIADATTLTEAGYVGEDVENILLKLLQAADYDVERAQRGIVYIDEIDKIARKSENPSITRDVSGEGVQQALLKILEGTV 157

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517799491 231 CNVPPQGGRKHPQQEYIQVNTEKILFIVGGAFVGMEDLVRDRLGKRSLGF--QVSQEDSLQTEDrELLTKVQPEDLLHFG 308
Cdd:cd19497  158 ANVPPQGGRKHPQQEFIQVDTTNILFICGGAFVGLEKIIARRLGKKSLGFgaETSSEKDEKERD-ELLSKVEPEDLIKFG 236

                        250
                 ....*....|....*
gi 517799491 309 LIPEFIGRLPVFSSL 323
Cdd:cd19497  237 LIPEFVGRLPVIVTL 251
AAA_2 pfam07724
AAA domain (Cdc48 subfamily); This Pfam entry includes some of the AAA proteins not detected ...
 122-319 3.72e-39

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: 138.48  E-value: 3.72e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517799491  122 EKSNILMLGPTGSGKTLLARTLARVLDV---PFSIVDATTLTEagyvgedvENIILRLLQAADGDIERAERG-------- 190
Cdd:pfam07724   2 PIGSFLFLGPTGVGKTELAKALAELLFGderALIRIDMSEYME--------EHSVSRLIGAPPGYVGYEEGGqlteavrr 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517799491  191 ----IIYVDEIDKIGRktenvsitrdvsgeGVQQALLKILEGTVcnVPPQGGRkhpqqeyiQVNTEKILFIVGGAFvGME 266
Cdd:pfam07724  74 kpysIVLIDEIEKAHP--------------GVQNDLLQILEGGT--LTDKQGR--------TVDFKNTLFIMTGNF-GSE 128

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 517799491  267 DLvrdrlgkrslgfqvSQEDSLQTEDRELLTKVQPEDLLHFGLIPEFIGRLPV 319
Cdd:pfam07724 129 KI--------------SDASRLGDSPDYELLKEEVMDLLKKGFIPEFLGRLPI 167
zf-C4_ClpX smart00994
ClpX C4-type zinc finger; The ClpX heat shock protein of Escherichia coli is a member of the ...
 10-46 1.42e-19

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


Pssm-ID: 198062 [Multi-domain]  Cd Length: 39  Bit Score: 81.46  E-value: 1.42e-19
                           10        20        30
                   ....*....|....*....|....*....|....*..
gi 517799491    10 CSFCGKSHSEVKKLIAGPGVYICNECIDVCSSILQKE 46
Cdd:smart00994   3 CSFCGKSESEVRKLIAGPGVYICDECVELCYEILEEE 39
 
Name Accession Description Interval E-value
ClpX COG1219
ATP-dependent protease Clp, ATPase subunit ClpX [Posttranslational modification, protein ...
 1-423 0e+00

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


Pssm-ID: 440832 [Multi-domain]  Cd Length: 409  Bit Score: 792.33  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517799491   1 MARSKNLTL-CSFCGKSHSEVKKLIAGPGVYICNECIDVCSSILQKEIKElgelsstdgtlGTDLQSDDSLLTPAEICAR 79
Cdd:COG1219    1 MAGDSKKELkCSFCGKSQDEVRKLIAGPGVYICDECVELCNEIIEEELKE-----------EEAEEELKKLPKPKEIKAF 69

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517799491  80 LDEYIIGQEHAKKTLSVAVYNHYQRLRQSNHSHDpeldGVEIEKSNILMLGPTGSGKTLLARTLARVLDVPFSIVDATTL 159
Cdd:COG1219   70 LDEYVIGQERAKKVLSVAVYNHYKRLNSGSKDDD----DVELEKSNILLIGPTGSGKTLLAQTLARILDVPFAIADATTL 145

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517799491 160 TEAGYVGEDVENIILRLLQAADGDIERAERGIIYVDEIDKIGRKTENVSITRDVSGEGVQQALLKILEGTVCNVPPQGGR 239
Cdd:COG1219  146 TEAGYVGEDVENILLKLLQAADYDVEKAERGIIYIDEIDKIARKSENPSITRDVSGEGVQQALLKILEGTVANVPPQGGR 225

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517799491 240 KHPQQEYIQVNTEKILFIVGGAFVGMEDLVRDRLGKRSLGFQVSQEDSLQTEDRELLTKVQPEDLLHFGLIPEFIGRLPV 319
Cdd:COG1219  226 KHPQQEFIQIDTTNILFICGGAFDGLEKIIERRLGKKSIGFGAEVKSKKEKDEGELLKQVEPEDLIKFGLIPEFIGRLPV 305

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517799491 320 FSSLRKLNEEELVRILTEPKNAMVKQYQKLLGMNDVKLKITKDGLTALAEEAVRRGTGARALRSIVENLMLDVMYDVPSR 399
Cdd:COG1219  306 IATLEELDEEALVRILTEPKNALVKQYQKLFEMDGVELEFTDEALEAIAKKAIERKTGARGLRSILEEILLDVMYELPSR 385

                        410       420
                 ....*....|....*....|....
gi 517799491 400 TDIESVTINRPVVEGEKPPMLKKK 423
Cdd:COG1219  386 KDVKKVVITKEVVEGKAKPILVYK 409
clpX PRK05342
ATP-dependent Clp protease ATP-binding subunit ClpX;
1-420 0e+00

ATP-dependent Clp protease ATP-binding subunit ClpX;


Pssm-ID: 235422 [Multi-domain]  Cd Length: 412  Bit Score: 751.99  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517799491   1 MARSKNLTLCSFCGKSHSEVKKLIAGPGVYICNECIDVCSSILQKEIKELGELSStdgtlgtdlqsddSLLTPAEICARL 80
Cdd:PRK05342   3 GGDSKKLLYCSFCGKSQHEVRKLIAGPGVYICDECIELCNEIIREELKEEAVELK-------------ELPTPKEIKAHL 69

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517799491  81 DEYIIGQEHAKKTLSVAVYNHYQRLRQSNHshdpELDGVEIEKSNILMLGPTGSGKTLLARTLARVLDVPFSIVDATTLT 160
Cdd:PRK05342  70 DQYVIGQERAKKVLSVAVYNHYKRLRHGDK----KDDDVELQKSNILLIGPTGSGKTLLAQTLARILDVPFAIADATTLT 145

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517799491 161 EAGYVGEDVENIILRLLQAADGDIERAERGIIYVDEIDKIGRKTENVSITRDVSGEGVQQALLKILEGTVCNVPPQGGRK 240
Cdd:PRK05342 146 EAGYVGEDVENILLKLLQAADYDVEKAQRGIVYIDEIDKIARKSENPSITRDVSGEGVQQALLKILEGTVASVPPQGGRK 225

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517799491 241 HPQQEYIQVNTEKILFIVGGAFVGMEDLVRDRLGKRSLGF--QVSQEDSLQTEDrELLTKVQPEDLLHFGLIPEFIGRLP 318
Cdd:PRK05342 226 HPQQEFIQVDTTNILFICGGAFDGLEKIIKQRLGKKGIGFgaEVKSKKEKRTEG-ELLKQVEPEDLIKFGLIPEFIGRLP 304

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517799491 319 VFSSLRKLNEEELVRILTEPKNAMVKQYQKLLGMNDVKLKITKDGLTALAEEAVRRGTGARALRSIVENLMLDVMYDVPS 398
Cdd:PRK05342 305 VVATLEELDEEALVRILTEPKNALVKQYQKLFEMDGVELEFTDEALEAIAKKAIERKTGARGLRSILEEILLDVMFELPS 384

                        410       420
                 ....*....|....*....|..
gi 517799491 399 RTDIESVTINRPVVEGEKPPML 420
Cdd:PRK05342 385 REDVEKVVITKEVVEGKAKPLL 406
clpX TIGR00382
endopeptidase Clp ATP-binding regulatory subunit (clpX); A member of the ATP-dependent ...
 1-420 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: 583.65  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517799491    1 MARSKNLTLCSFCGKSHSEVKKLIAGPGVYICNECIDVCSSILQKEIKELGELSSTDgtlgTDLQSDDsLLTPAEICARL 80
Cdd:TIGR00382   1 MTKKNETLYCSFCGKSQDEVRKLIAGPGVYICDECIELCHDILEEELGTRKESKEYE----EEFELSY-LPTPKEIKAHL 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517799491   81 DEYIIGQEHAKKTLSVAVYNHYQRLRQSNHSHDPelDGVEIEKSNILMLGPTGSGKTLLARTLARVLDVPFSIVDATTLT 160
Cdd:TIGR00382  76 DEYVIGQEQAKKVLSVAVYNHYKRLNFEKNKKSD--NGVELSKSNILLIGPTGSGKTLLAQTLARILNVPFAIADATTLT 153

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517799491  161 EAGYVGEDVENIILRLLQAADGDIERAERGIIYVDEIDKIGRKTENVSITRDVSGEGVQQALLKILEGTVCNVPPQGGRK 240
Cdd:TIGR00382 154 EAGYVGEDVENILLKLLQAADYDVEKAQKGIIYIDEIDKISRKSENPSITRDVSGEGVQQALLKIIEGTVANVPPQGGRK 233

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517799491  241 HPQQEYIQVNTEKILFIVGGAFVGMEDLVRDRLGKRSLGFqVSQEDSLQTEDRELLTKVQPEDLLHFGLIPEFIGRLPVF 320
Cdd:TIGR00382 234 HPYQEFIQIDTSNILFICGGAFVGLEKIIKKRTGKSSIGF-GAEVKKKSKEKADLLRQVEPEDLVKFGLIPEFIGRLPVI 312

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517799491  321 SSLRKLNEEELVRILTEPKNAMVKQYQKLLGMNDVKLKITKDGLTALAEEAVRRGTGARALRSIVENLMLDVMYDVPSRT 400
Cdd:TIGR00382 313 ATLEKLDEEALIAILTKPKNALVKQYQALFKMDNVELDFEEEALKAIAKKALERKTGARGLRSIVEGLLLDVMFDLPSLE 392

                         410       420
                  ....*....|....*....|
gi 517799491  401 DIESVTINRPVVEGEKPPML 420
Cdd:TIGR00382 393 DLEKVVITKETVLKQSEPLL 412
RecA-like_ClpX cd19497
ATP-dependent Clp protease ATP-binding subunit ClpX; ClpX is a component of the ATP-dependent ...
 71-323 1.04e-162

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: 457.83  E-value: 1.04e-162
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517799491  71 LTPAEICARLDEYIIGQEHAKKTLSVAVYNHYQRLRQSNHSHDpelDGVEIEKSNILMLGPTGSGKTLLARTLARVLDVP 150
Cdd:cd19497    1 PTPKEIKEHLDKYVIGQERAKKVLSVAVYNHYKRIRNNLKQKD---DDVELEKSNILLIGPTGSGKTLLAQTLAKILDVP 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517799491 151 FSIVDATTLTEAGYVGEDVENIILRLLQAADGDIERAERGIIYVDEIDKIGRKTENVSITRDVSGEGVQQALLKILEGTV 230
Cdd:cd19497   78 FAIADATTLTEAGYVGEDVENILLKLLQAADYDVERAQRGIVYIDEIDKIARKSENPSITRDVSGEGVQQALLKILEGTV 157

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517799491 231 CNVPPQGGRKHPQQEYIQVNTEKILFIVGGAFVGMEDLVRDRLGKRSLGF--QVSQEDSLQTEDrELLTKVQPEDLLHFG 308
Cdd:cd19497  158 ANVPPQGGRKHPQQEFIQVDTTNILFICGGAFVGLEKIIARRLGKKSLGFgaETSSEKDEKERD-ELLSKVEPEDLIKFG 236

                        250
                 ....*....|....*
gi 517799491 309 LIPEFIGRLPVFSSL 323
Cdd:cd19497  237 LIPEFVGRLPVIVTL 251
hslU PRK05201
ATP-dependent protease ATPase subunit HslU;
71-413 5.50e-63

ATP-dependent protease ATPase subunit HslU;


Pssm-ID: 235364 [Multi-domain]  Cd Length: 443  Bit Score: 209.55  E-value: 5.50e-63
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517799491  71 LTPAEICARLDEYIIGQEHAKKTLSVAVYNHYQRLRQsnhshDPEL-DgvEIEKSNILMLGPTGSGKTLLARTLARVLDV 149
Cdd:PRK05201   4 LTPREIVSELDKYIIGQDDAKRAVAIALRNRWRRMQL-----PEELrD--EVTPKNILMIGPTGVGKTEIARRLAKLANA 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517799491 150 PFSIVDATTLTEAGYVGEDVENII--L--------------------------RLLQA---------------------- 179
Cdd:PRK05201  77 PFIKVEATKFTEVGYVGRDVESIIrdLveiavkmvreekrekvrekaeeaaeeRILDAllppaknnwgeeeekeeisatr 156

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517799491 180 -------ADGD--------------------------------------------------------------------- 183
Cdd:PRK05201 157 qkfrkklREGElddkeieievaeaapmmeimgppgmeemtiqlqdmfgnlgpkkkkkrklkvkearkilieeeaaklidm 236

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517799491 184 -------IERAE-RGIIYVDEIDKIGRKTENVSitRDVSGEGVQQALLKILEGTVCNVppqggrkhpqqEYIQVNTEKIL 255
Cdd:PRK05201 237 eeikqeaIERVEqNGIVFIDEIDKIAARGGSSG--PDVSREGVQRDLLPLVEGSTVST-----------KYGMVKTDHIL 303

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517799491 256 FIVGGAfvgmedlvrdrlgkrslgFQVSqedslqtedrelltkvQPEDllhfgLIPEFIGRLPVFSSLRKLNEEELVRIL 335
Cdd:PRK05201 304 FIASGA------------------FHVS----------------KPSD-----LIPELQGRFPIRVELDALTEEDFVRIL 344

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517799491 336 TEPKNAMVKQYQKLLGMNDVKLKITKDGLTALAEEA--VRRGT---GARALRSIVENLMLDVMYDVPSRTDiESVTINRP 410
Cdd:PRK05201 345 TEPKASLIKQYQALLATEGVTLEFTDDAIRRIAEIAyqVNEKTeniGARRLHTVMEKLLEDISFEAPDMSG-ETVTIDAA 423


                 ...
gi 517799491 411 VVE 413
Cdd:PRK05201 424 YVD 426
HslU COG1220
ATP-dependent protease HslVU (ClpYQ), ATPase subunit HslU [Posttranslational modification, ...
 71-413 6.63e-58

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


Pssm-ID: 440833 [Multi-domain]  Cd Length: 454  Bit Score: 196.42  E-value: 6.63e-58
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517799491  71 LTPAEICARLDEYIIGQEHAKKTLSVAVYNHYQRLRQsnhshDPELDGvEIEKSNILMLGPTGSGKTLLARTLARVLDVP 150
Cdd:COG1220    4 LTPREIVAELDKYIIGQDEAKRAVAIALRNRWRRQQL-----PEELRD-EITPKNILMIGPTGVGKTEIARRLAKLANAP 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517799491 151 FSIVDATTLTEAGYVGEDVENII--L--------------------------RLLQA----------------------- 179
Cdd:COG1220   78 FIKVEATKFTEVGYVGRDVESMIrdLveiavkmvreekmekvrekaeeaaeeRILDLllpppkkkagsnnpfeeeeeeee 157

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517799491 180 ----------------ADGD------------------------------------------------------------ 183
Cdd:COG1220  158 eeeeisrtrekfrkklREGElddreieieveessspgveimgppgmeemgmnlqdmfgnlmpkkkkkrkvkvkearkilt 237

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517799491 184 -----------------IERAE-RGIIYVDEIDKIGRKTENVSItrDVSGEGVQQALLKILEGTVCNVppqggrkhpqqE 245
Cdd:COG1220  238 qeeaaklidmdevkqeaIERAEqNGIIFIDEIDKIASRGGGSGP--DVSREGVQRDLLPIVEGSTVNT-----------K 304

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517799491 246 YIQVNTEKILFIVGGAfvgmedlvrdrlgkrslgFQVSqedslqtedrelltkvQPEDllhfgLIPEFIGRLPVFSSLRK 325
Cdd:COG1220  305 YGMVKTDHILFIAAGA------------------FHVS----------------KPSD-----LIPELQGRFPIRVELDS 345

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517799491 326 LNEEELVRILTEPKNAMVKQYQKLLGMNDVKLKITKDGLTALAEEA--VRRGT---GARALRSIVENLMLDVMYDVPSRT 400
Cdd:COG1220  346 LTEEDFVRILTEPKNALTKQYQALLATEGVELEFTDDAIREIAEIAfeVNERTeniGARRLHTVMEKLLEDISFEAPDLS 425

                        490
                 ....*....|...
gi 517799491 401 DiESVTINRPVVE 413
Cdd:COG1220  426 G-KTVVIDAAYVD 437
hslU TIGR00390
ATP-dependent protease HslVU, ATPase subunit; This model represents the ATPase subunit of ...
 71-413 1.00e-49

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: 174.62  E-value: 1.00e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517799491   71 LTPAEICARLDEYIIGQEHAKKTLSVAVYNHYQRLRQSNHSHDpeldgvEIEKSNILMLGPTGSGKTLLARTLARVLDVP 150
Cdd:TIGR00390   1 MTPREIVAELDKYIIGQDNAKKSVAIALRNRYRRSQLNEELKD------EVTPKNILMIGPTGVGKTEIARRLAKLANAP 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517799491  151 FSIVDATTLTEAGYVGEDVENIILRLLQAA-------------------------------------------------- 180
Cdd:TIGR00390  75 FIKVEATKFTEVGYVGRDVESMVRDLTDAAvklvkeeaiekvrdraeelaeerivdvllppaknqwgqteqqqepesare 154

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517799491  181 ------------DGDIE--------------------------------------------------------------- 185
Cdd:TIGR00390 155 afrkklregeldDKEIEidvsakmpsgieimappgmeemtmqlqslfqnlggqkkkkrklkikdakkaliaeeaaklvdp 234

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517799491  186 ---------RAER-GIIYVDEIDKIGRKTENVSitRDVSGEGVQQALLKILEGTVCNVppqggrkhpqqEYIQVNTEKIL 255
Cdd:TIGR00390 235 eeikqeaidAVEQsGIIFIDEIDKIAKKGESSG--ADVSREGVQRDLLPIVEGSTVNT-----------KYGMVKTDHIL 301

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517799491  256 FIVGGAFvgmedlvrdrlgkrslgfQVSQedslqtedrelltkvqPEDLlhfglIPEFIGRLPVFSSLRKLNEEELVRIL 335
Cdd:TIGR00390 302 FIAAGAF------------------QLAK----------------PSDL-----IPELQGRFPIRVELQALTTDDFERIL 342

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517799491  336 TEPKNAMVKQYQKLLGMNDVKLKITKDGLTALAEEAVR-----RGTGARALRSIVENLMLDVMYDVPSRTdIESVTINRP 410
Cdd:TIGR00390 343 TEPKNSLIKQYKALMKTEGVNIEFSDEAIKRIAELAYNvnektENIGARRLHTVLERLLEDISFEAPDLS-GQNITIDAD 421


                  ...
gi 517799491  411 VVE 413
Cdd:TIGR00390 422 YVS 424
RecA-like_HslU cd19498
ATP-dependent protease ATPase subunit HslU; HslU is a component of the ATP-dependent protease ...
 72-262 5.21e-49

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: 164.86  E-value: 5.21e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517799491  72 TPAEICARLDEYIIGQEHAKKTLSVAVYNHYQRLRQSNHSHDpeldgvEIEKSNILMLGPTGSGKTLLARTLARVLDVPF 151
Cdd:cd19498    1 TPREIVSELDKYIIGQDEAKRAVAIALRNRWRRMQLPEELRD------EVTPKNILMIGPTGVGKTEIARRLAKLAGAPF 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517799491 152 SIVDATTLTEAGYVGEDVENIILRLLQaadgdieraerGIIYVDEIDKIGRKTENVSitRDVSGEGVQQALLKILEGTVC 231
Cdd:cd19498   75 IKVEATKFTEVGYVGRDVESIIRDLVE-----------GIVFIDEIDKIAKRGGSSG--PDVSREGVQRDLLPIVEGSTV 141

                        170       180       190
                 ....*....|....*....|....*....|.
gi 517799491 232 NVppqggrkhpqqEYIQVNTEKILFIVGGAF 262
Cdd:cd19498  142 ST-----------KYGPVKTDHILFIAAGAF 161
AAA_2 pfam07724
AAA domain (Cdc48 subfamily); This Pfam entry includes some of the AAA proteins not detected ...
 122-319 3.72e-39

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: 138.48  E-value: 3.72e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517799491  122 EKSNILMLGPTGSGKTLLARTLARVLDV---PFSIVDATTLTEagyvgedvENIILRLLQAADGDIERAERG-------- 190
Cdd:pfam07724   2 PIGSFLFLGPTGVGKTELAKALAELLFGderALIRIDMSEYME--------EHSVSRLIGAPPGYVGYEEGGqlteavrr 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517799491  191 ----IIYVDEIDKIGRktenvsitrdvsgeGVQQALLKILEGTVcnVPPQGGRkhpqqeyiQVNTEKILFIVGGAFvGME 266
Cdd:pfam07724  74 kpysIVLIDEIEKAHP--------------GVQNDLLQILEGGT--LTDKQGR--------TVDFKNTLFIMTGNF-GSE 128

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 517799491  267 DLvrdrlgkrslgfqvSQEDSLQTEDRELLTKVQPEDLLHFGLIPEFIGRLPV 319
Cdd:pfam07724 129 KI--------------SDASRLGDSPDYELLKEEVMDLLKKGFIPEFLGRLPI 167
zf-C4_ClpX smart00994
ClpX C4-type zinc finger; The ClpX heat shock protein of Escherichia coli is a member of the ...
 10-46 1.42e-19

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


Pssm-ID: 198062 [Multi-domain]  Cd Length: 39  Bit Score: 81.46  E-value: 1.42e-19
                           10        20        30
                   ....*....|....*....|....*....|....*..
gi 517799491    10 CSFCGKSHSEVKKLIAGPGVYICNECIDVCSSILQKE 46
Cdd:smart00994   3 CSFCGKSESEVRKLIAGPGVYICDECVELCYEILEEE 39
zf-C4_ClpX pfam06689
ClpX C4-type zinc finger; The ClpX heat shock protein of Escherichia coli is a member of the ...
 10-44 2.50e-18

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: 77.96  E-value: 2.50e-18
                          10        20        30
                  ....*....|....*....|....*....|....*.
gi 517799491   10 CSFCGKSHSEVKKLIAGP-GVYICNECIDVCSSILQ 44
Cdd:pfam06689   3 CSFCGKSEDEVKKLIAGPnGVYICDECVELCYEILE 38
ClpB_D2-small smart01086
C-terminal, D2-small domain, of ClpB protein; This is the C-terminal domain of ClpB protein, ...
 326-417 7.36e-18

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: 78.25  E-value: 7.36e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517799491   326 LNEEELVRILTEPKNAMVKQYQkllgMNDVKLKITKDGLTALAEEAVRRGTGARALRSIVENLMLDVMYDVPSRTDIESV 405
Cdd:smart01086   1 LDKEDLVRIVDLPLNALQKRLA----EKGITLEFTDEALDWLAEKGYDPKYGARPLRRIIQRELEDPLAELILSGELKDG 76

                           90
                   ....*....|..
gi 517799491   406 TINRPVVEGEKP 417
Cdd:smart01086  77 DTVVVDVDDGEL 88
RecA-like_protease cd19481
proteases similar to RecA; RecA-like NTPases. This family includes the NTP binding domain of ...
 110-228 1.51e-17

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: 79.25  E-value: 1.51e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517799491 110 HSHDPELDGVEIEKSNILMLGPTGSGKTLLARTLARVLDVPFSIVDATTLTEAgYVGEDVENiILRLLQAAdgdiERAER 189
Cdd:cd19481   13 RRGSRLRRYGLGLPKGILLYGPPGTGKTLLAKALAGELGLPLIVVKLSSLLSK-YVGESEKN-LRKIFERA----RRLAP 86

                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 517799491 190 GIIYVDEIDKIGRKTENVSITRDVSgeGVQQALLKILEG 228
Cdd:cd19481   87 CILFIDEIDAIGRKRDSSGESGELR--RVLNQLLTELDG 123
AAA cd00009
The AAA+ (ATPases Associated with a wide variety of cellular Activities) superfamily ...
 85-206 1.74e-14

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


Pssm-ID: 99707 [Multi-domain]  Cd Length: 151  Bit Score: 70.64  E-value: 1.74e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517799491  85 IGQEHAKKTLSVAVYNHYqrlrqsnhshdpeldgveieKSNILMLGPTGSGKTLLARTLARVL---DVPFSIVDATTLTE 161
Cdd:cd00009    1 VGQEEAIEALREALELPP--------------------PKNLLLYGPPGTGKTTLARAIANELfrpGAPFLYLNASDLLE 60

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 517799491 162 AGYVGEDVENIILRLLQAAdgdIERAERGIIYVDEIDKIGRKTEN 206
Cdd:cd00009   61 GLVVAELFGHFLVRLLFEL---AEKAKPGVLFIDEIDSLSRGAQN 102
AAA pfam00004
ATPase family associated with various cellular activities (AAA); AAA family proteins often ...
 126-228 4.68e-13

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: 65.69  E-value: 4.68e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517799491  126 ILMLGPTGSGKTLLARTLARVLDVPFSIVDATTLTEaGYVGEDVENIILRLLQAadgdiERAERGIIYVDEIDKIGRKte 205
Cdd:pfam00004   1 LLLYGPPGTGKTTLAKAVAKELGAPFIEISGSELVS-KYVGESEKRLRELFEAA-----KKLAPCVIFIDEIDALAGS-- 72

                          90       100
                  ....*....|....*....|...
gi 517799491  206 nVSITRDVSGEGVQQALLKILEG 228
Cdd:pfam00004  73 -RGSGGDSESRRVVNQLLTELDG 94
SpoVK COG0464
AAA+-type ATPase, SpoVK/Ycf46/Vps4 family [Cell wall/membrane/envelope biogenesis, Cell cycle ...
 84-228 9.65e-13

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: 69.17  E-value: 9.65e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517799491  84 IIGQEHAKKTL--SVAVYNHYQRLRQsNHSHDPELdgveieksNILMLGPTGSGKTLLARTLARVLDVPFSIVDATTLTe 161
Cdd:COG0464  159 LGGLEEVKEELreLVALPLKRPELRE-EYGLPPPR--------GLLLYGPPGTGKTLLARALAGELGLPLIEVDLSDLV- 228

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 517799491 162 AGYVGEDVENiILRLLQAAdgdiERAERGIIYVDEIDKIGRKTENVsitRDVSGEGVQQALLKILEG 228
Cdd:COG0464  229 SKYVGETEKN-LREVFDKA----RGLAPCVLFIDEADALAGKRGEV---GDGVGRRVVNTLLTEMEE 287
RecA-like_CDC48_NLV2_r1-like cd19503
first of two ATPase domains of CDC48 and NLV2, and similar ATPase domains; CDC48 in yeast and ...
 126-228 3.62e-10

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: 58.46  E-value: 3.62e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517799491 126 ILMLGPTGSGKTLLARTLARVLDVPFSIVDATTLTeAGYVGEDVENiiLRLLQAadgDIERAERGIIYVDEIDKIGRKTE 205
Cdd:cd19503   37 VLLHGPPGTGKTLLARAVANEAGANFLSISGPSIV-SKYLGESEKN--LREIFE---EARSHAPSIIFIDEIDALAPKRE 110

                         90       100
                 ....*....|....*....|...
gi 517799491 206 NVSitRDVSGEGVQQaLLKILEG 228
Cdd:cd19503  111 EDQ--REVERRVVAQ-LLTLMDG 130
ClpB_D2-small pfam10431
C-terminal, D2-small domain, of ClpB protein; This is the C-terminal domain of ClpB protein, ...
 326-404 1.02e-09

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: 54.72  E-value: 1.02e-09
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 517799491  326 LNEEELVRILTEpknAMVKQYQKLLGmNDVKLKITKDGLTALAEEAVRRGTGARALRSIVENLMLDVMYDVPSRTDIES 404
Cdd:pfam10431   1 LSKEELRKIVDL---QLKELQKRLAE-RGITLELTDAAKDWLAEKGYDPEYGARPLRRAIQREIEDPLAEEILSGELKE 75
RPT1 COG1222
ATP-dependent 26S proteasome regulatory subunit [Posttranslational modification, protein ...
 118-203 3.20e-09

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


Pssm-ID: 440835 [Multi-domain]  Cd Length: 326  Bit Score: 58.09  E-value: 3.20e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517799491 118 GVEIEKSnILMLGPTGSGKTLLARTLARVLDVPFSIVDATTLTEAgYVGEDvENIILRLLQAAdgdiERAERGIIYVDEI 197
Cdd:COG1222  108 GIEPPKG-VLLYGPPGTGKTLLAKAVAGELGAPFIRVRGSELVSK-YIGEG-ARNVREVFELA----REKAPSIIFIDEI 180


                 ....*.
gi 517799491 198 DKIGRK 203
Cdd:COG1222  181 DAIAAR 186
RecA-like_NVL_r1-like cd19518
first of two ATPase domains of NVL (nuclear VCP-like protein) and similar ATPase domains; NVL ...
 126-222 1.35e-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: 53.95  E-value: 1.35e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517799491 126 ILMLGPTGSGKTLLARTLARVLDVPFSIVDATTLTeAGYVGEDVENiILRLLQAAdgdiERAERGIIYVDEIDKIGRKTE 205
Cdd:cd19518   37 VLLHGPPGCGKTMLANAIAGELKVPFLKISATEIV-SGVSGESEEK-IRELFDQA----ISNAPCIVFIDEIDAITPKRE 110

                         90
                 ....*....|....*..
gi 517799491 206 NVSitRDVSGEGVQQAL 222
Cdd:cd19518  111 SAQ--REMERRIVSQLL 125
RecA-like_VPS4-like cd19509
ATPase domain of VPS4, ATAD1, K, KTNA1, Spastin, FIGL-1 and similar ATPase domains; This ...
 84-220 1.85e-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: 53.51  E-value: 1.85e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517799491  84 IIGQEHAKKTLSVAVYnhYQRLRQSNHSHDPELdgveieKSNILMLGPTGSGKTLLARTLARVLDVPFSIVDATTLTeAG 163
Cdd:cd19509    1 IAGLDDAKEALKEAVI--LPSLRPDLFPGLRGP------PRGILLYGPPGTGKTLLARAVASESGSTFFSISASSLV-SK 71

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 517799491 164 YVGEDvENIILRLLQAADgdiERAErGIIYVDEIDKIG--RKTENVSITRDVSGEGVQQ 220
Cdd:cd19509   72 WVGES-EKIVRALFALAR---ELQP-SIIFIDEIDSLLseRGSGEHEASRRVKTEFLVQ 125
hflB PRK10733
ATP-dependent zinc metalloprotease FtsH;
126-203 1.85e-07

ATP-dependent zinc metalloprotease FtsH;


Pssm-ID: 182683 [Multi-domain]  Cd Length: 644  Bit Score: 53.50  E-value: 1.85e-07
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 517799491 126 ILMLGPTGSGKTLLARTLARVLDVPFSIVDATTLTEAgYVGEDVENIILRLLQAadgdiERAERGIIYVDEIDKIGRK 203
Cdd:PRK10733 188 VLMVGPPGTGKTLLAKAIAGEAKVPFFTISGSDFVEM-FVGVGASRVRDMFEQA-----KKAAPCIIFIDEIDAVGRQ 259
RecA-like_FtsH cd19501
ATP-dependent zinc metalloprotease FtsH; FtsH ATPase is a processive, ATP-dependent zinc ...
 118-203 3.61e-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: 3.61e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517799491 118 GVEIEKSnILMLGPTGSGKTLLARTLARVLDVPFSIVDATTLTEAgYVGEDVENIilRLL--QAadgdiERAERGIIYVD 195
Cdd:cd19501   33 GAKIPKG-VLLVGPPGTGKTLLAKAVAGEAGVPFFSISGSDFVEM-FVGVGASRV--RDLfeQA-----KKNAPCIVFID 103


                 ....*...
gi 517799491 196 EIDKIGRK 203
Cdd:cd19501  104 EIDAVGRK 111
AAA smart00382
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ...
 123-209 6.97e-07

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: 48.52  E-value: 6.97e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517799491   123 KSNILMLGPTGSGKTLLARTLARVLDVP---FSIVDATTLTEAGYVGEDVENIILRLL-----QAADGDIERAER---GI 191
Cdd:smart00382   2 GEVILIVGPPGSGKTTLARALARELGPPgggVIYIDGEDILEEVLDQLLLIIVGGKKAsgsgeLRLRLALALARKlkpDV 81

                           90
                   ....*....|....*...
gi 517799491   192 IYVDEIDKIGRKTENVSI 209
Cdd:smart00382  82 LILDEITSLLDAEQEALL 99
RecA-like_spastin cd19524
ATPase domain of spastin; Spastin is an ATP-dependent microtubule-severing protein involved in ...
 84-200 1.06e-06

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: 48.31  E-value: 1.06e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517799491  84 IIGQEHAKKTLSVAVYNHYQRlrqsnhshdPEL-DGVEIEKSNILMLGPTGSGKTLLARTLARVLDVPFSIVDATTLTeA 162
Cdd:cd19524    2 IAGQDLAKQALQEMVILPSLR---------PELfTGLRAPARGLLLFGPPGNGKTMLAKAVAAESNATFFNISAASLT-S 71

                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 517799491 163 GYVGEDvENIILRLLQAAdgdiERAERGIIYVDEIDKI 200
Cdd:cd19524   72 KYVGEG-EKLVRALFAVA----RELQPSIIFIDEVDSL 104
PRK13342 PRK13342
recombination factor protein RarA; Reviewed
 79-197 1.11e-06

recombination factor protein RarA; Reviewed


Pssm-ID: 237355 [Multi-domain]  Cd Length: 413  Bit Score: 50.47  E-value: 1.11e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517799491  79 RLDEYIiGQEH---AKKTLSVAVynhyqrlrQSNHSHdpeldgveiekSNILMlGPTGSGKTLLARTLARVLDVPFSIVD 155
Cdd:PRK13342  10 TLDEVV-GQEHllgPGKPLRRMI--------EAGRLS-----------SMILW-GPPGTGKTTLARIIAGATDAPFEALS 68

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 517799491 156 ATTlteAGyVgEDVENIIlrllQAADGDIERAERGIIYVDEI 197
Cdd:PRK13342  69 AVT---SG-V-KDLREVI----EEARQRRSAGRRTILFIDEI 101
RecA-like_CDC48_r1-like cd19519
first of two ATPase domains of CDC48 and similar ATPase domains; CDC48 in yeast and p97 or VCP ...
 126-228 1.17e-06

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: 48.20  E-value: 1.17e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517799491 126 ILMLGPTGSGKTLLARTLARVLDVPFSIVDATTLTeAGYVGEDVENiilrlLQAADGDIERAERGIIYVDEIDKIGRKTE 205
Cdd:cd19519   37 ILLYGPPGTGKTLIARAVANETGAFFFLINGPEIM-SKLAGESESN-----LRKAFEEAEKNAPAIIFIDEIDAIAPKRE 110

                         90       100
                 ....*....|....*....|...
gi 517799491 206 NVsiTRDVSGEGVQQaLLKILEG 228
Cdd:cd19519  111 KT--HGEVERRIVSQ-LLTLMDG 130
AAA_5 pfam07728
AAA domain (dynein-related subfamily); This Pfam entry includes some of the AAA proteins not ...
 125-207 1.20e-06

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: 47.67  E-value: 1.20e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517799491  125 NILMLGPTGSGKTLLARTLARVLD-VPFSIVDATTLTEAgyvgEDVE---NIILRLLQAADGDIERAER--GIIYVDEID 198
Cdd:pfam07728   1 GVLLVGPPGTGKTELAERLAAALSnRPVFYVQLTRDTTE----EDLFgrrNIDPGGASWVDGPLVRAARegEIAVLDEIN 76


                  ....*....
gi 517799491  199 KIGRKTENV 207
Cdd:pfam07728  77 RANPDVLNS 85
RecA-like_PAN_like cd19502
proteasome activating nucleotidase PAN and related proteasome subunits; This subfamily ...
 114-226 1.49e-06

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: 48.10  E-value: 1.49e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517799491 114 PEL-DGVEIEK-SNILMLGPTGSGKTLLARTLARVLDVPFSIVDATTLTEAgYVGEDVEnIILRLLQAAdgdiERAERGI 191
Cdd:cd19502   26 PELfEELGIEPpKGVLLYGPPGTGKTLLAKAVANHTDATFIRVVGSELVQK-YIGEGAR-LVRELFEMA----REKAPSI 99

                         90       100       110
                 ....*....|....*....|....*....|....*
gi 517799491 192 IYVDEIDKIGRKTENVSITRDvsgEGVQQALLKIL 226
Cdd:cd19502  100 IFIDEIDAIGAKRFDSGTGGD---REVQRTMLELL 131
RecA-like_ClpB_Hsp104-like cd19499
Chaperone protein ClpB/Hsp104 subfamily; Bacterial Caseinolytic peptidase B (ClpB) and ...
 79-199 2.32e-06

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


Pssm-ID: 410907 [Multi-domain]  Cd Length: 178  Bit Score: 47.56  E-value: 2.32e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517799491  79 RLDEYIIGQEHAKKTLSVAVYnhyqrlRQSNHSHDPEL-DGVeieksnILMLGPTGSGKTLLARTLARVL---DVPFSIV 154
Cdd:cd19499    8 RLHERVVGQDEAVKAVSDAIR------RARAGLSDPNRpIGS------FLFLGPTGVGKTELAKALAELLfgdEDNLIRI 75

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 517799491 155 D---------ATTLTEA--GYVGEDVENIILrllqaadGDIERAERGIIYVDEIDK 199
Cdd:cd19499   76 DmseymekhsVSRLIGAppGYVGYTEGGQLT-------EAVRRKPYSVVLLDEIEK 124
MoxR COG0714
MoxR-like ATPase [General function prediction only]; MoxR-like ATPase is part of the Pathway ...
 72-206 2.45e-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: 49.01  E-value: 2.45e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517799491  72 TPAEICARLDEYIIGQEHAKKTLSVAVYnhyqrlrqsnhshdpeLDGveieksNILMLGPTGSGKTLLARTLARVLDVPF 151
Cdd:COG0714    2 TEARLRAEIGKVYVGQEELIELVLIALL----------------AGG------HLLLEGVPGVGKTTLAKALARALGLPF 59

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 517799491 152 SIVDAT-TLTEAGYVGEDVeniilrlLQAADGDiERAERG-----IIYVDEIDKIGRKTEN 206
Cdd:COG0714   60 IRIQFTpDLLPSDILGTYI-------YDQQTGE-FEFRPGplfanVLLADEINRAPPKTQS 112
CDC48 TIGR01243
AAA family ATPase, CDC48 subfamily; This subfamily of the AAA family ATPases includes two ...
 118-228 3.09e-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: 49.52  E-value: 3.09e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517799491  118 GVEIEKSnILMLGPTGSGKTLLARTLARVLDVPFSIVDATTLTeAGYVGEDVENiilrlLQAADGDIERAERGIIYVDEI 197
Cdd:TIGR01243 208 GIEPPKG-VLLYGPPGTGKTLLAKAVANEAGAYFISINGPEIM-SKYYGESEER-----LREIFKEAEENAPSIIFIDEI 280

                          90       100       110
                  ....*....|....*....|....*....|.
gi 517799491  198 DKIGRKTENVsiTRDVSGEGVQQaLLKILEG 228
Cdd:TIGR01243 281 DAIAPKREEV--TGEVEKRVVAQ-LLTLMDG 308
RecA-like_NSF-SEC18_r1-like cd19504
first of two ATPase domains of NSF and SEC18, and similar ATPase domains; ...
 126-225 4.14e-06

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: 47.10  E-value: 4.14e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517799491 126 ILMLGPTGSGKTLLARTLARVLDV--PfSIVDATTLTEAgYVGEDVENIilRLLqAADGDIERAERG------IIYVDEI 197
Cdd:cd19504   38 ILLYGPPGTGKTLMARQIGKMLNAreP-KIVNGPEILNK-YVGESEANI--RKL-FADAEEEQRRLGansglhIIIFDEI 112

                         90       100
                 ....*....|....*....|....*...
gi 517799491 198 DKIGRKTENVSITRDVSGEGVQQALLKI 225
Cdd:cd19504  113 DAICKQRGSMAGSTGVHDTVVNQLLSKI 140
ClpA COG0542
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ...
 278-391 4.86e-06

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


Pssm-ID: 440308 [Multi-domain]  Cd Length: 836  Bit Score: 48.92  E-value: 4.86e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517799491 278 LGFQVSQEDSLQTEDRE-LLTKVQPEDLLHFGliPEFIGRLP---VFsslRKLNEEELVRILtepkNAMVKQYQKLLGMN 353
Cdd:COG0542  701 IGSELILDLAEDEPDYEeMKEAVMEELKKHFR--PEFLNRIDeiiVF---HPLSKEELRKIV----DLQLKRLRKRLAER 771

                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 517799491 354 DVKLKITKDGLTALAEEAVRRGTGARALRSIVENLMLD 391
Cdd:COG0542  772 GITLELTDAAKDFLAEKGYDPEYGARPLKRAIQRELED 809
RecA-like_Figl-1 cd19525
ATPase domain of Fidgetin-Like 1 (FIGL-1); FIGL-1 may participate in DNA repair in the nucleus; ...
 82-200 1.11e-05

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


Pssm-ID: 410933 [Multi-domain]  Cd Length: 186  Bit Score: 45.75  E-value: 1.11e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517799491  82 EYIIGQEHAKKTLSVAVYNHYQRlrqsnhshdPEL-DGVEIEKSNILMLGPTGSGKTLLARTLARVLDVPFSIVDATTLT 160
Cdd:cd19525   22 ADIAGLEFAKKTIKEIVVWPMLR---------PDIfTGLRGPPKGILLFGPPGTGKTLIGKCIASQSGATFFSISASSLT 92

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 517799491 161 eAGYVGEDvENIILRLLQAAdgdieRAER-GIIYVDEIDKI 200
Cdd:cd19525   93 -SKWVGEG-EKMVRALFSVA-----RCKQpAVIFIDEIDSL 126
RecA-like_KTNA1 cd19522
Katanin p60 ATPase-containing subunit A1; Katanin p60 ATPase-containing subunit A1 (KTNA1) is ...
 126-200 1.72e-05

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: 44.98  E-value: 1.72e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 517799491 126 ILMLGPTGSGKTLLARTLARVLDVPFSIVDATTLTeAGYVGEDVEniILRLLqaadGDIERA-ERGIIYVDEIDKI 200
Cdd:cd19522   36 VLMVGPPGTGKTLLAKAVATECGTTFFNVSSSTLT-SKYRGESEK--LVRLL----FEMARFyAPTTIFIDEIDSI 104
clpC CHL00095
Clp protease ATP binding subunit
 277-391 1.94e-05

Clp protease ATP binding subunit


Pssm-ID: 214361 [Multi-domain]  Cd Length: 821  Bit Score: 46.97  E-value: 1.94e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517799491 277 SLGFQVSQEDSLQTEDRELLTKVQpEDLLHFgLIPEFIGRLPVFSSLRKLNEEELVRILtepkNAMVKQYQKLLGMNDVK 356
Cdd:CHL00095 672 GLGFELSENQLSEKQYKRLSNLVN-EELKQF-FRPEFLNRLDEIIVFRQLTKNDVWEIA----EIMLKNLFKRLNEQGIQ 745

                         90       100       110
                 ....*....|....*....|....*....|....*
gi 517799491 357 LKITKDGLTALAEEAVRRGTGARALRSIVENLMLD 391
Cdd:CHL00095 746 LEVTERIKTLLIEEGYNPLYGARPLRRAIMRLLED 780
Mg_chelatase pfam01078
Magnesium chelatase, subunit ChlI; Magnesium-chelatase is a three-component enzyme that ...
 84-147 2.07e-05

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


Pssm-ID: 426032 [Multi-domain]  Cd Length: 207  Bit Score: 45.22  E-value: 2.07e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 517799491   84 IIGQEHAKKTLSVAVY-NHyqrlrqsnhshdpeldgveieksNILMLGPTGSGKTLLARTLARVL 147
Cdd:pfam01078   5 VKGQEQAKRALEIAAAgGH-----------------------NLLMIGPPGSGKTMLAKRLPGIL 46
YifB COG0606
Predicted Mg-chelatase, contains ChlI-like and ATPase domains, YifB family [Posttranslational ...
 84-147 4.85e-05

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: 45.42  E-value: 4.85e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 517799491  84 IIGQEHAKKTLSVAVY-NHyqrlrqsnhshdpeldgveieksNILMLGPTGSGKTLLARTLARVL 147
Cdd:COG0606  194 VKGQEQAKRALEIAAAgGH-----------------------NLLMIGPPGSGKTMLARRLPGIL 235
RecA-like_PEX6_r2 cd19527
second of two ATPase domains of Peroxisomal biogenesis factor 6 (PEX6); PEX6(also known as ...
 114-225 6.93e-05

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


Pssm-ID: 410935 [Multi-domain]  Cd Length: 160  Bit Score: 42.89  E-value: 6.93e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517799491 114 PEL--DGVEiEKSNILMLGPTGSGKTLLARTLARVLDVPFSIVDATTLTEAgYVGEDVENiILRLLQAAdgdiERAERGI 191
Cdd:cd19527   16 PELfsSGLR-KRSGILLYGPPGTGKTLLAKAIATECSLNFLSVKGPELINM-YIGESEAN-VREVFQKA----RDAKPCV 88

                         90       100       110
                 ....*....|....*....|....*....|....
gi 517799491 192 IYVDEIDKIGRKTENVSITRDVSGEGVQQALLKI 225
Cdd:cd19527   89 IFFDELDSLAPSRGNSGDSGGVMDRVVSQLLAEL 122
DnaX COG2812
DNA polymerase III, gamma/tau subunits [Replication, recombination and repair];
84-147 1.13e-04

DNA polymerase III, gamma/tau subunits [Replication, recombination and repair];


Pssm-ID: 442061 [Multi-domain]  Cd Length: 340  Bit Score: 44.03  E-value: 1.13e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 517799491  84 IIGQEHAKKTLSVAVYNhyQRLrqsNHShdpeldgveieksnILMLGPTGSGKTLLARTLARVL 147
Cdd:COG2812   12 VVGQEHVVRTLKNALAS--GRL---AHA--------------YLFTGPRGVGKTTLARILAKAL 56
RecA-like_CDC48_r2-like cd19511
second of two ATPase domains of CDC48/p97, PEX1 and -6, VAT and NVL, and similar ATPase ...
 126-208 1.22e-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: 42.27  E-value: 1.22e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517799491 126 ILMLGPTGSGKTLLARTLARVLDVPFSIVDATTLTEAgYVGEDvENIILRLLQAAdgdiERAERGIIYVDEIDKI-GRKT 204
Cdd:cd19511   30 VLLYGPPGCGKTLLAKALASEAGLNFISVKGPELFSK-YVGES-ERAVREIFQKA----RQAAPCIIFFDEIDSLaPRRG 103


                 ....
gi 517799491 205 ENVS 208
Cdd:cd19511  104 QSDS 107
AcoR COG3284
Transcriptional regulator DhaR of acetoin/glycerol metabolism [Transcription];
124-198 2.36e-04

Transcriptional regulator DhaR of acetoin/glycerol metabolism [Transcription];


Pssm-ID: 442514 [Multi-domain]  Cd Length: 625  Bit Score: 43.35  E-value: 2.36e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517799491 124 SNILMLGPTGSGKTLLARTLARVL---DVPFSIVDATTLTEA-------GYV-----GEDVEniilrllqAADGDIERAE 188
Cdd:COG3284  345 IPVLILGETGTGKELFARAIHAASpraDGPFVAVNCAAIPEElieselfGYEpgaftGARRK--------GRPGKIEQAD 416

                         90
                 ....*....|
gi 517799491 189 RGIIYVDEID 198
Cdd:COG3284  417 GGTLFLDEIG 426
RecA-like_ATAD1 cd19520
ATPase domain of ATPase family AAA domain-containing protein 1 and similar ATPase domains; ...
 126-198 4.69e-04

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


Pssm-ID: 410928 [Multi-domain]  Cd Length: 166  Bit Score: 40.87  E-value: 4.69e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 517799491 126 ILMLGPTGSGKTLLARTLARVLDVPFSIVDATTLTEAGYvGEDVeniilRLLQAADGDIERAERGIIYVDEID 198
Cdd:cd19520   38 VLLYGPPGCGKTMLAKATAKEAGARFINLQVSSLTDKWY-GESQ-----KLVAAVFSLASKLQPSIIFIDEID 104
RecA-like_ATAD3-like cd19512
ATPase domains of ATPase AAA-domain protein 3A (ATAD3A), -3B, and -3C, and similar ATPase ...
 125-212 7.29e-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: 39.82  E-value: 7.29e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517799491 125 NILMLGPTGSGKTLLARTLARVLDVPFSIVdatTLTEAGYVGEDVENIILRLLQAADgdieRAERG-IIYVDEIDKIGRK 203
Cdd:cd19512   24 NILFYGPPGTGKTLFAKKLALHSGMDYAIM---TGGDVAPMGREGVTAIHKVFDWAN----TSRRGlLLFVDEADAFLRK 96


                 ....*....
gi 517799491 204 TENVSITRD 212
Cdd:cd19512   97 RSTEKISED 105
RecA-like_VPS4 cd19521
ATPase domain of vacuolar protein sorting-associated protein 4; Vacuolar protein ...
 124-208 1.15e-03

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


Pssm-ID: 410929 [Multi-domain]  Cd Length: 170  Bit Score: 39.46  E-value: 1.15e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517799491 124 SNILMLGPTGSGKTLLARTLARVLDVPFSIVDATTLTeAGYVGEDvENIILRLLQAAdgdiERAERGIIYVDEIDKI-GR 202
Cdd:cd19521   41 SGILLYGPPGTGKSYLAKAVATEANSTFFSVSSSDLV-SKWMGES-EKLVKQLFAMA----RENKPSIIFIDEVDSLcGT 114


                 ....*.
gi 517799491 203 KTENVS 208
Cdd:cd19521  115 RGEGES 120
RecA-like_VCP_r2 cd19529
second of two ATPase domains of Valosin-containing protein-like ATPase (VAT) and similar ...
 126-200 1.38e-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: 1.38e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 517799491 126 ILMLGPTGSGKTLLARTLARVLDVPFSIVDATTLTeAGYVGEDvENIILRLLQAAdgdiERAERGIIYVDEIDKI 200
Cdd:cd19529   30 ILLYGPPGTGKTLLAKAVATESNANFISVKGPELL-SKWVGES-EKAIREIFRKA----RQVAPCVIFFDEIDSI 98
RecA-like_Ycf46-like cd19507
ATPase domain of Ycf46 and similar ATPase domains; Ycf46 may play a role in the regulation of ...
 126-199 1.49e-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: 39.27  E-value: 1.49e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 517799491 126 ILMLGPTGSGKTLLARTLARVLDVPFSIVDATTLTeAGYVGEDVENiILRLLQAAdgdiERAERGIIYVDEIDK 199
Cdd:cd19507   34 LLLVGIQGTGKSLTAKAIAGVWQLPLLRLDMGRLF-GGLVGESESR-LRQMIQTA----EAIAPCVLWIDEIEK 101
CDC6 COG1474
Cdc6-related protein, AAA superfamily ATPase [Replication, recombination and repair];
124-206 2.94e-03

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


Pssm-ID: 441083 [Multi-domain]  Cd Length: 389  Bit Score: 39.83  E-value: 2.94e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517799491 124 SNILMLGPTGSGKTLLARTLARVL-------DVPFSIV-----DATTLTEA-----------------GYVGEDVENIIL 174
Cdd:COG1474   52 SNVLIYGPTGTGKTAVAKYVLEELeeeaeerGVDVRVVyvncrQASTRYRVlsrileelgsgedipstGLSTDELFDRLY 131

                         90       100       110
                 ....*....|....*....|....*....|..
gi 517799491 175 RLLQAADGDIeraergIIYVDEIDKIGRKTEN 206
Cdd:COG1474  132 EALDERDGVL------VVVLDEIDYLVDDEGD 157
RecA-like_fidgetin cd19523
ATPase domain of fidgetin; Fidgetin (FIGN) is a ATP-dependent microtubule severing protein. ...
 126-237 3.13e-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: 38.33  E-value: 3.13e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517799491 126 ILMLGPTGSGKTLLARTLARVLDVPFSIVDATTLTeAGYVGEDVeniilRLLQAADGDIERAERGIIYVDEIDKI--GRK 203
Cdd:cd19523   36 ILLFGPRGTGKTLLGRCLASQLGATFLRLRGSTLV-AKWAGEGE-----KILQASFLAARCRQPSVLFISDLDALlsSQD 109

                         90       100       110
                 ....*....|....*....|....*....|....
gi 517799491 204 TENVSITRdvsgegVQQALLKILEGtVCNVPPQG 237
Cdd:cd19523  110 DEASPVGR------LQVELLAQLDG-VLGSGEDG 136
ClpA COG0542
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ...
 79-147 4.67e-03

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


Pssm-ID: 440308 [Multi-domain]  Cd Length: 836  Bit Score: 39.29  E-value: 4.67e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 517799491  79 RLDEYIIGQEHAKKTLSVAVynhyqrlRQSnhshdpeldgveieKSNI----------LMLGPTGSGKTLLARTLARVL 147
Cdd:COG0542  546 ELHERVIGQDEAVEAVADAI-------RRS--------------RAGLkdpnrpigsfLFLGPTGVGKTELAKALAEFL 603
RecA-like_PEX1_r2 cd19526
second of two ATPase domains of Peroxisomal biogenesis factor 1 (PEX1); PEX1(also known as ...
 123-203 4.95e-03

second of two ATPase domains of Peroxisomal biogenesis factor 1 (PEX1); PEX1(also known as Peroxin-1)/PEX6 is a protein unfoldase; PEX1 and PEX6 form a heterohexameric Type-2 AAA-ATPase complex and are essential for peroxisome biogenesis as they are required for the import of folded proteins into the peroxisomal matrix. PEX-1 is required for stability of PEX5. This subfamily belongs to the RecA-like NTPase family which includes the NTP binding domain of F1 and V1 H(+)ATPases, DnaB and related helicases as well as bacterial RecA and related eukaryotic and archaeal recombinases. The RecA-like NTPase family also includes bacterial conjugation proteins and related DNA transfer proteins involved in type II and type IV secretion.


Pssm-ID: 410934 [Multi-domain]  Cd Length: 158  Bit Score: 37.41  E-value: 4.95e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517799491 123 KSNILMLGPTGSGKTLLARTLARVLDVPFSIVDATTLTeAGYVGEDVENIilRLLqaadgdIERAERG---IIYVDEIDK 199
Cdd:cd19526   27 RSGILLYGPPGCGKTLLASAIASECGLNFISVKGPELL-NKYIGASEQNV--RDL------FSRAQSAkpcILFFDEFDS 97


                 ....
gi 517799491 200 IGRK 203
Cdd:cd19526   98 IAPK 101
SK cd00464
Shikimate kinase (SK) is the fifth enzyme in the shikimate pathway, a seven-step biosynthetic ...
 125-188 6.24e-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: 37.15  E-value: 6.24e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 517799491 125 NILMLGPTGSGKTLLARTLARVLDVPFsiVDATTLTEAgYVGEDVENIILRLLQAADGDIERAE 188
Cdd:cd00464    1 NIVLIGMMGAGKTTVGRLLAKALGLPF--VDLDELIEQ-RAGMSIPEIFAEEGEEGFRELEREV 61
PRK03992 PRK03992
proteasome-activating nucleotidase; Provisional
 114-226 7.21e-03

proteasome-activating nucleotidase; Provisional


Pssm-ID: 179699 [Multi-domain]  Cd Length: 389  Bit Score: 38.27  E-value: 7.21e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517799491 114 PEL-DGVEIEK-SNILMLGPTGSGKTLLARTLArvldvpfSIVDATTLTEAG------YVGEDVEniILR-LLQAADgdi 184
Cdd:PRK03992 154 PELfEEVGIEPpKGVLLYGPPGTGKTLLAKAVA-------HETNATFIRVVGselvqkFIGEGAR--LVReLFELAR--- 221

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 517799491 185 ERAErGIIYVDEIDKIG-RKTEnvSITrdvSGEG-VQQALLKIL 226
Cdd:PRK03992 222 EKAP-SIIFIDEIDAIAaKRTD--SGT---SGDReVQRTLMQLL 259
PRK14953 PRK14953
DNA polymerase III subunits gamma and tau; Provisional
 84-148 8.04e-03

DNA polymerase III subunits gamma and tau; Provisional


Pssm-ID: 237867 [Multi-domain]  Cd Length: 486  Bit Score: 38.27  E-value: 8.04e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 517799491  84 IIGQEHAKKTLSVAVynhyqRLRQSNHSHdpeldgveieksniLMLGPTGSGKTLLARTLARVLD 148
Cdd:PRK14953  18 VIGQEIVVRILKNAV-----KLQRVSHAY--------------IFAGPRGTGKTTIARILAKVLN 63
 
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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