NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|446394447|ref|WP_000472302|]
View 

MULTISPECIES: ATP-dependent Clp protease ATP-binding subunit ClpX [Staphylococcus]

Protein Classification

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

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

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

Name Accession Description Interval E-value
ClpX COG1219
ATP-dependent protease Clp, ATPase subunit ClpX [Posttranslational modification, protein ...
4-405 0e+00

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


:

Pssm-ID: 440832 [Multi-domain]  Cd Length: 409  Bit Score: 822.76  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446394447   4 FNEDEENLKCSFCGKDQDQVKKLVAGSGVYICNECIELCSEIVEEELAQNTSEAM-TELPTPKEIMDHLNEYVIGQEKAK 82
Cdd:COG1219    2 AGDSKKELKCSFCGKSQDEVRKLIAGPGVYICDECVELCNEIIEEELKEEEAEEElKKLPKPKEIKAFLDEYVIGQERAK 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446394447  83 KSLAVAVYNHYKRIQQLGPKEDDVELQKSNIALIGPTGSGKTLLAQTLAKTLNVPFAIADATSLTEAGYVGDDVENILLR 162
Cdd:COG1219   82 KVLSVAVYNHYKRLNSGSKDDDDVELEKSNILLIGPTGSGKTLLAQTLARILDVPFAIADATTLTEAGYVGEDVENILLK 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446394447 163 LIQAADFDIDKAEKGIIYVDEIDKIARKSENTSITRDVSGEGVQQALLKILEGTTASVPPQGGRKHPNQEMIQIDTTNIL 242
Cdd:COG1219  162 LLQAADYDVEKAERGIIYIDEIDKIARKSENPSITRDVSGEGVQQALLKILEGTVANVPPQGGRKHPQQEFIQIDTTNIL 241
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446394447 243 FILGGAFDGIEEVIKRRLGEKVIGFSSN--EADKYDEQALLAQIRPEDLQAYGLIPEFIGRVPIVANLETLDVTALKNIL 320
Cdd:COG1219  242 FICGGAFDGLEKIIERRLGKKSIGFGAEvkSKKEKDEGELLKQVEPEDLIKFGLIPEFIGRLPVIATLEELDEEALVRIL 321
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446394447 321 TQPKNALVKQYTKMLELDDVDLEFTEEALSAISEKAIERKTGARGLRSIIEESLIDIMFDVPSNENVTKVVITAQTINEE 400
Cdd:COG1219  322 TEPKNALVKQYQKLFEMDGVELEFTDEALEAIAKKAIERKTGARGLRSILEEILLDVMYELPSRKDVKKVVITKEVVEGK 401

                 ....*
gi 446394447 401 TEPEL 405
Cdd:COG1219  402 AKPIL 406
 
Name Accession Description Interval E-value
ClpX COG1219
ATP-dependent protease Clp, ATPase subunit ClpX [Posttranslational modification, protein ...
4-405 0e+00

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


Pssm-ID: 440832 [Multi-domain]  Cd Length: 409  Bit Score: 822.76  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446394447   4 FNEDEENLKCSFCGKDQDQVKKLVAGSGVYICNECIELCSEIVEEELAQNTSEAM-TELPTPKEIMDHLNEYVIGQEKAK 82
Cdd:COG1219    2 AGDSKKELKCSFCGKSQDEVRKLIAGPGVYICDECVELCNEIIEEELKEEEAEEElKKLPKPKEIKAFLDEYVIGQERAK 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446394447  83 KSLAVAVYNHYKRIQQLGPKEDDVELQKSNIALIGPTGSGKTLLAQTLAKTLNVPFAIADATSLTEAGYVGDDVENILLR 162
Cdd:COG1219   82 KVLSVAVYNHYKRLNSGSKDDDDVELEKSNILLIGPTGSGKTLLAQTLARILDVPFAIADATTLTEAGYVGEDVENILLK 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446394447 163 LIQAADFDIDKAEKGIIYVDEIDKIARKSENTSITRDVSGEGVQQALLKILEGTTASVPPQGGRKHPNQEMIQIDTTNIL 242
Cdd:COG1219  162 LLQAADYDVEKAERGIIYIDEIDKIARKSENPSITRDVSGEGVQQALLKILEGTVANVPPQGGRKHPQQEFIQIDTTNIL 241
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446394447 243 FILGGAFDGIEEVIKRRLGEKVIGFSSN--EADKYDEQALLAQIRPEDLQAYGLIPEFIGRVPIVANLETLDVTALKNIL 320
Cdd:COG1219  242 FICGGAFDGLEKIIERRLGKKSIGFGAEvkSKKEKDEGELLKQVEPEDLIKFGLIPEFIGRLPVIATLEELDEEALVRIL 321
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446394447 321 TQPKNALVKQYTKMLELDDVDLEFTEEALSAISEKAIERKTGARGLRSIIEESLIDIMFDVPSNENVTKVVITAQTINEE 400
Cdd:COG1219  322 TEPKNALVKQYQKLFEMDGVELEFTDEALEAIAKKAIERKTGARGLRSILEEILLDVMYELPSRKDVKKVVITKEVVEGK 401

                 ....*
gi 446394447 401 TEPEL 405
Cdd:COG1219  402 AKPIL 406
clpX PRK05342
ATP-dependent Clp protease ATP-binding subunit ClpX;
3-411 0e+00

ATP-dependent Clp protease ATP-binding subunit ClpX;


Pssm-ID: 235422 [Multi-domain]  Cd Length: 412  Bit Score: 793.21  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446394447   3 KFNEDEENLKCSFCGKDQDQVKKLVAGSGVYICNECIELCSEIVEEELAQNTSEAmTELPTPKEIMDHLNEYVIGQEKAK 82
Cdd:PRK05342   2 RGGDSKKLLYCSFCGKSQHEVRKLIAGPGVYICDECIELCNEIIREELKEEAVEL-KELPTPKEIKAHLDQYVIGQERAK 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446394447  83 KSLAVAVYNHYKRIQQLGPKEDDVELQKSNIALIGPTGSGKTLLAQTLAKTLNVPFAIADATSLTEAGYVGDDVENILLR 162
Cdd:PRK05342  81 KVLSVAVYNHYKRLRHGDKKDDDVELQKSNILLIGPTGSGKTLLAQTLARILDVPFAIADATTLTEAGYVGEDVENILLK 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446394447 163 LIQAADFDIDKAEKGIIYVDEIDKIARKSENTSITRDVSGEGVQQALLKILEGTTASVPPQGGRKHPNQEMIQIDTTNIL 242
Cdd:PRK05342 161 LLQAADYDVEKAQRGIVYIDEIDKIARKSENPSITRDVSGEGVQQALLKILEGTVASVPPQGGRKHPQQEFIQVDTTNIL 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446394447 243 FILGGAFDGIEEVIKRRLGEKVIGFSSNEADKYDEQ---ALLAQIRPEDLQAYGLIPEFIGRVPIVANLETLDVTALKNI 319
Cdd:PRK05342 241 FICGGAFDGLEKIIKQRLGKKGIGFGAEVKSKKEKRtegELLKQVEPEDLIKFGLIPEFIGRLPVVATLEELDEEALVRI 320
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446394447 320 LTQPKNALVKQYTKMLELDDVDLEFTEEALSAISEKAIERKTGARGLRSIIEESLIDIMFDVPSNENVTKVVITAQTINE 399
Cdd:PRK05342 321 LTEPKNALVKQYQKLFEMDGVELEFTDEALEAIAKKAIERKTGARGLRSILEEILLDVMFELPSREDVEKVVITKEVVEG 400
                        410
                 ....*....|..
gi 446394447 400 ETEPELYDAEGN 411
Cdd:PRK05342 401 KAKPLLIYREKS 412
clpX TIGR00382
endopeptidase Clp ATP-binding regulatory subunit (clpX); A member of the ATP-dependent ...
1-405 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: 610.62  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446394447    1 MFKFNEDeenLKCSFCGKDQDQVKKLVAGSGVYICNECIELCSEIVEEELA-QNTSEAMTE------LPTPKEIMDHLNE 73
Cdd:TIGR00382   1 MTKKNET---LYCSFCGKSQDEVRKLIAGPGVYICDECIELCHDILEEELGtRKESKEYEEefelsyLPTPKEIKAHLDE 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446394447   74 YVIGQEKAKKSLAVAVYNHYKRIQQLGPKEDD--VELQKSNIALIGPTGSGKTLLAQTLAKTLNVPFAIADATSLTEAGY 151
Cdd:TIGR00382  78 YVIGQEQAKKVLSVAVYNHYKRLNFEKNKKSDngVELSKSNILLIGPTGSGKTLLAQTLARILNVPFAIADATTLTEAGY 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446394447  152 VGDDVENILLRLIQAADFDIDKAEKGIIYVDEIDKIARKSENTSITRDVSGEGVQQALLKILEGTTASVPPQGGRKHPNQ 231
Cdd:TIGR00382 158 VGEDVENILLKLLQAADYDVEKAQKGIIYIDEIDKISRKSENPSITRDVSGEGVQQALLKIIEGTVANVPPQGGRKHPYQ 237
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446394447  232 EMIQIDTTNILFILGGAFDGIEEVIKRRLGEKVIGFSS-NEADKYDEQALLAQIRPEDLQAYGLIPEFIGRVPIVANLET 310
Cdd:TIGR00382 238 EFIQIDTSNILFICGGAFVGLEKIIKKRTGKSSIGFGAeVKKKSKEKADLLRQVEPEDLVKFGLIPEFIGRLPVIATLEK 317
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446394447  311 LDVTALKNILTQPKNALVKQYTKMLELDDVDLEFTEEALSAISEKAIERKTGARGLRSIIEESLIDIMFDVPSNENVTKV 390
Cdd:TIGR00382 318 LDEEALIAILTKPKNALVKQYQALFKMDNVELDFEEEALKAIAKKALERKTGARGLRSIVEGLLLDVMFDLPSLEDLEKV 397
                         410
                  ....*....|....*
gi 446394447  391 VITAQTINEETEPEL 405
Cdd:TIGR00382 398 VITKETVLKQSEPLL 412
RecA-like_ClpX cd19497
ATP-dependent Clp protease ATP-binding subunit ClpX; ClpX is a component of the ATP-dependent ...
62-308 1.06e-165

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: 465.15  E-value: 1.06e-165
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446394447  62 PTPKEIMDHLNEYVIGQEKAKKSLAVAVYNHYKRI-QQLGPKEDDVELQKSNIALIGPTGSGKTLLAQTLAKTLNVPFAI 140
Cdd:cd19497    1 PTPKEIKEHLDKYVIGQERAKKVLSVAVYNHYKRIrNNLKQKDDDVELEKSNILLIGPTGSGKTLLAQTLAKILDVPFAI 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446394447 141 ADATSLTEAGYVGDDVENILLRLIQAADFDIDKAEKGIIYVDEIDKIARKSENTSITRDVSGEGVQQALLKILEGTTASV 220
Cdd:cd19497   81 ADATTLTEAGYVGEDVENILLKLLQAADYDVERAQRGIVYIDEIDKIARKSENPSITRDVSGEGVQQALLKILEGTVANV 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446394447 221 PPQGGRKHPNQEMIQIDTTNILFILGGAFDGIEEVIKRRLGEKVIGF---SSNEADKYDEQALLAQIRPEDLQAYGLIPE 297
Cdd:cd19497  161 PPQGGRKHPQQEFIQVDTTNILFICGGAFVGLEKIIARRLGKKSLGFgaeTSSEKDEKERDELLSKVEPEDLIKFGLIPE 240
                        250
                 ....*....|.
gi 446394447 298 FIGRVPIVANL 308
Cdd:cd19497  241 FVGRLPVIVTL 251
AAA_2 pfam07724
AAA domain (Cdc48 subfamily); This Pfam entry includes some of the AAA proteins not detected ...
110-305 3.76e-40

AAA domain (Cdc48 subfamily); This Pfam entry includes some of the AAA proteins not detected by the pfam00004 model.


Pssm-ID: 400187 [Multi-domain]  Cd Length: 168  Bit Score: 140.79  E-value: 3.76e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446394447  110 KSNIALIGPTGSGKTLLAQTLAKTLNV---PFAIADATSLTEagyvgddvENILLRLIQAADFDIDKAEKG--------- 177
Cdd:pfam07724   3 IGSFLFLGPTGVGKTELAKALAELLFGderALIRIDMSEYME--------EHSVSRLIGAPPGYVGYEEGGqlteavrrk 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446394447  178 ---IIYVDEIDKIARksentsitrdvsgeGVQQALLKILEGTTASvppqggrkhPNQEmIQIDTTNILFILGGAFDGIEE 254
Cdd:pfam07724  75 pysIVLIDEIEKAHP--------------GVQNDLLQILEGGTLT---------DKQG-RTVDFKNTLFIMTGNFGSEKI 130
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 446394447  255 VIKRRLGEkvigfssneadkyDEQALLAQIRPEDLQAYGLIPEFIGRVPIV 305
Cdd:pfam07724 131 SDASRLGD-------------SPDYELLKEEVMDLLKKGFIPEFLGRLPII 168
zf-C4_ClpX smart00994
ClpX C4-type zinc finger; The ClpX heat shock protein of Escherichia coli is a member of the ...
11-49 5.44e-20

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


Pssm-ID: 198062 [Multi-domain]  Cd Length: 39  Bit Score: 82.23  E-value: 5.44e-20
                           10        20        30
                   ....*....|....*....|....*....|....*....
gi 446394447    11 LKCSFCGKDQDQVKKLVAGSGVYICNECIELCSEIVEEE 49
Cdd:smart00994   1 LRCSFCGKSESEVRKLIAGPGVYICDECVELCYEILEEE 39
 
Name Accession Description Interval E-value
ClpX COG1219
ATP-dependent protease Clp, ATPase subunit ClpX [Posttranslational modification, protein ...
4-405 0e+00

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


Pssm-ID: 440832 [Multi-domain]  Cd Length: 409  Bit Score: 822.76  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446394447   4 FNEDEENLKCSFCGKDQDQVKKLVAGSGVYICNECIELCSEIVEEELAQNTSEAM-TELPTPKEIMDHLNEYVIGQEKAK 82
Cdd:COG1219    2 AGDSKKELKCSFCGKSQDEVRKLIAGPGVYICDECVELCNEIIEEELKEEEAEEElKKLPKPKEIKAFLDEYVIGQERAK 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446394447  83 KSLAVAVYNHYKRIQQLGPKEDDVELQKSNIALIGPTGSGKTLLAQTLAKTLNVPFAIADATSLTEAGYVGDDVENILLR 162
Cdd:COG1219   82 KVLSVAVYNHYKRLNSGSKDDDDVELEKSNILLIGPTGSGKTLLAQTLARILDVPFAIADATTLTEAGYVGEDVENILLK 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446394447 163 LIQAADFDIDKAEKGIIYVDEIDKIARKSENTSITRDVSGEGVQQALLKILEGTTASVPPQGGRKHPNQEMIQIDTTNIL 242
Cdd:COG1219  162 LLQAADYDVEKAERGIIYIDEIDKIARKSENPSITRDVSGEGVQQALLKILEGTVANVPPQGGRKHPQQEFIQIDTTNIL 241
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446394447 243 FILGGAFDGIEEVIKRRLGEKVIGFSSN--EADKYDEQALLAQIRPEDLQAYGLIPEFIGRVPIVANLETLDVTALKNIL 320
Cdd:COG1219  242 FICGGAFDGLEKIIERRLGKKSIGFGAEvkSKKEKDEGELLKQVEPEDLIKFGLIPEFIGRLPVIATLEELDEEALVRIL 321
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446394447 321 TQPKNALVKQYTKMLELDDVDLEFTEEALSAISEKAIERKTGARGLRSIIEESLIDIMFDVPSNENVTKVVITAQTINEE 400
Cdd:COG1219  322 TEPKNALVKQYQKLFEMDGVELEFTDEALEAIAKKAIERKTGARGLRSILEEILLDVMYELPSRKDVKKVVITKEVVEGK 401

                 ....*
gi 446394447 401 TEPEL 405
Cdd:COG1219  402 AKPIL 406
clpX PRK05342
ATP-dependent Clp protease ATP-binding subunit ClpX;
3-411 0e+00

ATP-dependent Clp protease ATP-binding subunit ClpX;


Pssm-ID: 235422 [Multi-domain]  Cd Length: 412  Bit Score: 793.21  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446394447   3 KFNEDEENLKCSFCGKDQDQVKKLVAGSGVYICNECIELCSEIVEEELAQNTSEAmTELPTPKEIMDHLNEYVIGQEKAK 82
Cdd:PRK05342   2 RGGDSKKLLYCSFCGKSQHEVRKLIAGPGVYICDECIELCNEIIREELKEEAVEL-KELPTPKEIKAHLDQYVIGQERAK 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446394447  83 KSLAVAVYNHYKRIQQLGPKEDDVELQKSNIALIGPTGSGKTLLAQTLAKTLNVPFAIADATSLTEAGYVGDDVENILLR 162
Cdd:PRK05342  81 KVLSVAVYNHYKRLRHGDKKDDDVELQKSNILLIGPTGSGKTLLAQTLARILDVPFAIADATTLTEAGYVGEDVENILLK 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446394447 163 LIQAADFDIDKAEKGIIYVDEIDKIARKSENTSITRDVSGEGVQQALLKILEGTTASVPPQGGRKHPNQEMIQIDTTNIL 242
Cdd:PRK05342 161 LLQAADYDVEKAQRGIVYIDEIDKIARKSENPSITRDVSGEGVQQALLKILEGTVASVPPQGGRKHPQQEFIQVDTTNIL 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446394447 243 FILGGAFDGIEEVIKRRLGEKVIGFSSNEADKYDEQ---ALLAQIRPEDLQAYGLIPEFIGRVPIVANLETLDVTALKNI 319
Cdd:PRK05342 241 FICGGAFDGLEKIIKQRLGKKGIGFGAEVKSKKEKRtegELLKQVEPEDLIKFGLIPEFIGRLPVVATLEELDEEALVRI 320
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446394447 320 LTQPKNALVKQYTKMLELDDVDLEFTEEALSAISEKAIERKTGARGLRSIIEESLIDIMFDVPSNENVTKVVITAQTINE 399
Cdd:PRK05342 321 LTEPKNALVKQYQKLFEMDGVELEFTDEALEAIAKKAIERKTGARGLRSILEEILLDVMFELPSREDVEKVVITKEVVEG 400
                        410
                 ....*....|..
gi 446394447 400 ETEPELYDAEGN 411
Cdd:PRK05342 401 KAKPLLIYREKS 412
clpX TIGR00382
endopeptidase Clp ATP-binding regulatory subunit (clpX); A member of the ATP-dependent ...
1-405 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: 610.62  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446394447    1 MFKFNEDeenLKCSFCGKDQDQVKKLVAGSGVYICNECIELCSEIVEEELA-QNTSEAMTE------LPTPKEIMDHLNE 73
Cdd:TIGR00382   1 MTKKNET---LYCSFCGKSQDEVRKLIAGPGVYICDECIELCHDILEEELGtRKESKEYEEefelsyLPTPKEIKAHLDE 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446394447   74 YVIGQEKAKKSLAVAVYNHYKRIQQLGPKEDD--VELQKSNIALIGPTGSGKTLLAQTLAKTLNVPFAIADATSLTEAGY 151
Cdd:TIGR00382  78 YVIGQEQAKKVLSVAVYNHYKRLNFEKNKKSDngVELSKSNILLIGPTGSGKTLLAQTLARILNVPFAIADATTLTEAGY 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446394447  152 VGDDVENILLRLIQAADFDIDKAEKGIIYVDEIDKIARKSENTSITRDVSGEGVQQALLKILEGTTASVPPQGGRKHPNQ 231
Cdd:TIGR00382 158 VGEDVENILLKLLQAADYDVEKAQKGIIYIDEIDKISRKSENPSITRDVSGEGVQQALLKIIEGTVANVPPQGGRKHPYQ 237
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446394447  232 EMIQIDTTNILFILGGAFDGIEEVIKRRLGEKVIGFSS-NEADKYDEQALLAQIRPEDLQAYGLIPEFIGRVPIVANLET 310
Cdd:TIGR00382 238 EFIQIDTSNILFICGGAFVGLEKIIKKRTGKSSIGFGAeVKKKSKEKADLLRQVEPEDLVKFGLIPEFIGRLPVIATLEK 317
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446394447  311 LDVTALKNILTQPKNALVKQYTKMLELDDVDLEFTEEALSAISEKAIERKTGARGLRSIIEESLIDIMFDVPSNENVTKV 390
Cdd:TIGR00382 318 LDEEALIAILTKPKNALVKQYQALFKMDNVELDFEEEALKAIAKKALERKTGARGLRSIVEGLLLDVMFDLPSLEDLEKV 397
                         410
                  ....*....|....*
gi 446394447  391 VITAQTINEETEPEL 405
Cdd:TIGR00382 398 VITKETVLKQSEPLL 412
RecA-like_ClpX cd19497
ATP-dependent Clp protease ATP-binding subunit ClpX; ClpX is a component of the ATP-dependent ...
62-308 1.06e-165

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: 465.15  E-value: 1.06e-165
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446394447  62 PTPKEIMDHLNEYVIGQEKAKKSLAVAVYNHYKRI-QQLGPKEDDVELQKSNIALIGPTGSGKTLLAQTLAKTLNVPFAI 140
Cdd:cd19497    1 PTPKEIKEHLDKYVIGQERAKKVLSVAVYNHYKRIrNNLKQKDDDVELEKSNILLIGPTGSGKTLLAQTLAKILDVPFAI 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446394447 141 ADATSLTEAGYVGDDVENILLRLIQAADFDIDKAEKGIIYVDEIDKIARKSENTSITRDVSGEGVQQALLKILEGTTASV 220
Cdd:cd19497   81 ADATTLTEAGYVGEDVENILLKLLQAADYDVERAQRGIVYIDEIDKIARKSENPSITRDVSGEGVQQALLKILEGTVANV 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446394447 221 PPQGGRKHPNQEMIQIDTTNILFILGGAFDGIEEVIKRRLGEKVIGF---SSNEADKYDEQALLAQIRPEDLQAYGLIPE 297
Cdd:cd19497  161 PPQGGRKHPQQEFIQVDTTNILFICGGAFVGLEKIIARRLGKKSLGFgaeTSSEKDEKERDELLSKVEPEDLIKFGLIPE 240
                        250
                 ....*....|.
gi 446394447 298 FIGRVPIVANL 308
Cdd:cd19497  241 FVGRLPVIVTL 251
hslU PRK05201
ATP-dependent protease ATPase subunit HslU;
58-399 2.15e-58

ATP-dependent protease ATPase subunit HslU;


Pssm-ID: 235364 [Multi-domain]  Cd Length: 443  Bit Score: 197.22  E-value: 2.15e-58
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446394447  58 MTELpTPKEIMDHLNEYVIGQEKAKKSLAVAVYNHYKRiQQLGPkeddvELQKS----NIALIGPTGSGKTLLAQTLAKT 133
Cdd:PRK05201   1 MSEL-TPREIVSELDKYIIGQDDAKRAVAIALRNRWRR-MQLPE-----ELRDEvtpkNILMIGPTGVGKTEIARRLAKL 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446394447 134 LNVPFAIADATSLTEAGYVGDDVENIL----------------------------------------------------- 160
Cdd:PRK05201  74 ANAPFIKVEATKFTEVGYVGRDVESIIrdlveiavkmvreekrekvrekaeeaaeerildallppaknnwgeeeekeeis 153
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446394447 161 ---------LR--------------------------------------------------------------------- 162
Cdd:PRK05201 154 atrqkfrkkLRegelddkeieievaeaapmmeimgppgmeemtiqlqdmfgnlgpkkkkkrklkvkearkilieeeaakl 233
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446394447 163 -----LIQAAdfdIDKAEK-GIIYVDEIDKIARKSENTSitRDVSGEGVQQALLKILEGTTASVppqggrKHPnqemiQI 236
Cdd:PRK05201 234 idmeeIKQEA---IERVEQnGIVFIDEIDKIAARGGSSG--PDVSREGVQRDLLPLVEGSTVST------KYG-----MV 297
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446394447 237 DTTNILFILGGAFdgieevikrrlgekvigfssNEAdkydeqallaqiRPEDlqaygLIPEFIGRVPIVANLETLDVTAL 316
Cdd:PRK05201 298 KTDHILFIASGAF--------------------HVS------------KPSD-----LIPELQGRFPIRVELDALTEEDF 340
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446394447 317 KNILTQPKNALVKQYTKMLELDDVDLEFTEEALSAISEKAIE--RKT---GARGLRSIIEESLIDIMFDVPSNENvTKVV 391
Cdd:PRK05201 341 VRILTEPKASLIKQYQALLATEGVTLEFTDDAIRRIAEIAYQvnEKTeniGARRLHTVMEKLLEDISFEAPDMSG-ETVT 419

                 ....*...
gi 446394447 392 ITAQTINE 399
Cdd:PRK05201 420 IDAAYVDE 427
HslU COG1220
ATP-dependent protease HslVU (ClpYQ), ATPase subunit HslU [Posttranslational modification, ...
58-399 2.65e-56

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


Pssm-ID: 440833 [Multi-domain]  Cd Length: 454  Bit Score: 191.80  E-value: 2.65e-56
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446394447  58 MTELpTPKEIMDHLNEYVIGQEKAKKSLAVAVYNHYKRiQQLGPkeddvELQK----SNIALIGPTGSGKTLLAQTLAKT 133
Cdd:COG1220    1 MSEL-TPREIVAELDKYIIGQDEAKRAVAIALRNRWRR-QQLPE-----ELRDeitpKNILMIGPTGVGKTEIARRLAKL 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446394447 134 LNVPFAIADATSLTEAGYVGDDVENI------------------------------------------------------ 159
Cdd:COG1220   74 ANAPFIKVEATKFTEVGYVGRDVESMirdlveiavkmvreekmekvrekaeeaaeerildlllpppkkkagsnnpfeeee 153
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446394447 160 ------------------LLR----------------------------------------------------------- 162
Cdd:COG1220  154 eeeeeeeeisrtrekfrkKLRegelddreieieveessspgveimgppgmeemgmnlqdmfgnlmpkkkkkrkvkvkear 233
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446394447 163 --LIQ--AA---DFD------IDKAEK-GIIYVDEIDKIARKSENTSItrDVSGEGVQQALLKILEGTTASVppqggrKH 228
Cdd:COG1220  234 kiLTQeeAAkliDMDevkqeaIERAEQnGIIFIDEIDKIASRGGGSGP--DVSREGVQRDLLPIVEGSTVNT------KY 305
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446394447 229 PnqemiQIDTTNILFILGGAFDgieevikrrlgekvigfssneadkydeqalLAqiRPEDlqaygLIPEFIGRVPIVANL 308
Cdd:COG1220  306 G-----MVKTDHILFIAAGAFH------------------------------VS--KPSD-----LIPELQGRFPIRVEL 343
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446394447 309 ETLDVTALKNILTQPKNALVKQYTKMLELDDVDLEFTEEALSAISEKAIE--RKT---GARGLRSIIEESLIDIMFDVPS 383
Cdd:COG1220  344 DSLTEEDFVRILTEPKNALTKQYQALLATEGVELEFTDDAIREIAEIAFEvnERTeniGARRLHTVMEKLLEDISFEAPD 423
                        490
                 ....*....|....*.
gi 446394447 384 NENvTKVVITAQTINE 399
Cdd:COG1220  424 LSG-KTVVIDAAYVDE 438
hslU TIGR00390
ATP-dependent protease HslVU, ATPase subunit; This model represents the ATPase subunit of ...
63-402 2.79e-47

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: 167.68  E-value: 2.79e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446394447   63 TPKEIMDHLNEYVIGQEKAKKSLAVAVYNHYKRIQQlgPKEDDVELQKSNIALIGPTGSGKTLLAQTLAKTLNVPFAIAD 142
Cdd:TIGR00390   2 TPREIVAELDKYIIGQDNAKKSVAIALRNRYRRSQL--NEELKDEVTPKNILMIGPTGVGKTEIARRLAKLANAPFIKVE 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446394447  143 ATSLTEAGYVGDDVENILLRLIQAA------------------------------------------------------- 167
Cdd:TIGR00390  80 ATKFTEVGYVGRDVESMVRDLTDAAvklvkeeaiekvrdraeelaeerivdvllppaknqwgqteqqqepesareafrkk 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446394447  168 -------------------------------------------------------------------------------D 168
Cdd:TIGR00390 160 lregelddkeieidvsakmpsgieimappgmeemtmqlqslfqnlggqkkkkrklkikdakkaliaeeaaklvdpeeikQ 239
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446394447  169 FDIDKAEK-GIIYVDEIDKIARKSENTSitRDVSGEGVQQALLKILEGTTASVppqggrKHPnqemiQIDTTNILFILGG 247
Cdd:TIGR00390 240 EAIDAVEQsGIIFIDEIDKIAKKGESSG--ADVSREGVQRDLLPIVEGSTVNT------KYG-----MVKTDHILFIAAG 306
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446394447  248 AFDgieevikrrlgekvigfssneadkydeqalLAqiRPEDLqayglIPEFIGRVPIVANLETLDVTALKNILTQPKNAL 327
Cdd:TIGR00390 307 AFQ------------------------------LA--KPSDL-----IPELQGRFPIRVELQALTTDDFERILTEPKNSL 349
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446394447  328 VKQYTKMLELDDVDLEFTEEALSAISEKA--IERKT---GARGLRSIIEESLIDIMFDVPsNENVTKVVITAQTINEETE 402
Cdd:TIGR00390 350 IKQYKALMKTEGVNIEFSDEAIKRIAELAynVNEKTeniGARRLHTVLERLLEDISFEAP-DLSGQNITIDADYVSKKLG 428
RecA-like_HslU cd19498
ATP-dependent protease ATPase subunit HslU; HslU is a component of the ATP-dependent protease ...
63-249 8.14e-47

ATP-dependent protease ATPase subunit HslU; HslU is a component of the ATP-dependent protease HslVU. In HslVU, HslU ATPase serves to unfold and translocate protein substrate, and the HslV protease degrades the unfolded proteins. This RecA-like_HslU subfamily belongs to the RecA-like NTPase family which includes the NTP binding domain of F1 and V1 H(+)ATPases, DnaB and related helicases as well as bacterial RecA and related eukaryotic and archaeal recombinases. The RecA-like NTPase family also includes bacterial conjugation proteins and related DNA transfer proteins involved in type II and type IV secretion.


Pssm-ID: 410906 [Multi-domain]  Cd Length: 183  Bit Score: 159.08  E-value: 8.14e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446394447  63 TPKEIMDHLNEYVIGQEKAKKSLAVAVYNHYKRiQQLgPKEDDVELQKSNIALIGPTGSGKTLLAQTLAKTLNVPFAIAD 142
Cdd:cd19498    1 TPREIVSELDKYIIGQDEAKRAVAIALRNRWRR-MQL-PEELRDEVTPKNILMIGPTGVGKTEIARRLAKLAGAPFIKVE 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446394447 143 ATSLTEAGYVGDDVENILLRLIqaadfdidkaeKGIIYVDEIDKIARKSENTSitRDVSGEGVQQALLKILEGTTASVpp 222
Cdd:cd19498   79 ATKFTEVGYVGRDVESIIRDLV-----------EGIVFIDEIDKIAKRGGSSG--PDVSREGVQRDLLPIVEGSTVST-- 143
                        170       180
                 ....*....|....*....|....*..
gi 446394447 223 QGGrkhpnqemiQIDTTNILFILGGAF 249
Cdd:cd19498  144 KYG---------PVKTDHILFIAAGAF 161
AAA_2 pfam07724
AAA domain (Cdc48 subfamily); This Pfam entry includes some of the AAA proteins not detected ...
110-305 3.76e-40

AAA domain (Cdc48 subfamily); This Pfam entry includes some of the AAA proteins not detected by the pfam00004 model.


Pssm-ID: 400187 [Multi-domain]  Cd Length: 168  Bit Score: 140.79  E-value: 3.76e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446394447  110 KSNIALIGPTGSGKTLLAQTLAKTLNV---PFAIADATSLTEagyvgddvENILLRLIQAADFDIDKAEKG--------- 177
Cdd:pfam07724   3 IGSFLFLGPTGVGKTELAKALAELLFGderALIRIDMSEYME--------EHSVSRLIGAPPGYVGYEEGGqlteavrrk 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446394447  178 ---IIYVDEIDKIARksentsitrdvsgeGVQQALLKILEGTTASvppqggrkhPNQEmIQIDTTNILFILGGAFDGIEE 254
Cdd:pfam07724  75 pysIVLIDEIEKAHP--------------GVQNDLLQILEGGTLT---------DKQG-RTVDFKNTLFIMTGNFGSEKI 130
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 446394447  255 VIKRRLGEkvigfssneadkyDEQALLAQIRPEDLQAYGLIPEFIGRVPIV 305
Cdd:pfam07724 131 SDASRLGD-------------SPDYELLKEEVMDLLKKGFIPEFLGRLPII 168
zf-C4_ClpX smart00994
ClpX C4-type zinc finger; The ClpX heat shock protein of Escherichia coli is a member of the ...
11-49 5.44e-20

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


Pssm-ID: 198062 [Multi-domain]  Cd Length: 39  Bit Score: 82.23  E-value: 5.44e-20
                           10        20        30
                   ....*....|....*....|....*....|....*....
gi 446394447    11 LKCSFCGKDQDQVKKLVAGSGVYICNECIELCSEIVEEE 49
Cdd:smart00994   1 LRCSFCGKSESEVRKLIAGPGVYICDECVELCYEILEEE 39
zf-C4_ClpX pfam06689
ClpX C4-type zinc finger; The ClpX heat shock protein of Escherichia coli is a member of the ...
11-48 1.23e-19

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


Pssm-ID: 461988 [Multi-domain]  Cd Length: 39  Bit Score: 81.43  E-value: 1.23e-19
                          10        20        30
                  ....*....|....*....|....*....|....*....
gi 446394447   11 LKCSFCGKDQDQVKKLVAGS-GVYICNECIELCSEIVEE 48
Cdd:pfam06689   1 LRCSFCGKSEDEVKKLIAGPnGVYICDECVELCYEILEE 39
ClpB_D2-small smart01086
C-terminal, D2-small domain, of ClpB protein; This is the C-terminal domain of ClpB protein, ...
311-395 1.57e-19

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


Pssm-ID: 198154 [Multi-domain]  Cd Length: 90  Bit Score: 82.49  E-value: 1.57e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446394447   311 LDVTALKNILTQPKNALVKQYtkmlELDDVDLEFTEEALSAISEKAIERKTGARGLRSIIEESLIDIMFDVPSN---ENV 387
Cdd:smart01086   1 LDKEDLVRIVDLPLNALQKRL----AEKGITLEFTDEALDWLAEKGYDPKYGARPLRRIIQRELEDPLAELILSgelKDG 76

                   ....*...
gi 446394447   388 TKVVITAQ 395
Cdd:smart01086  77 DTVVVDVD 84
RecA-like_protease cd19481
proteases similar to RecA; RecA-like NTPases. This family includes the NTP binding domain of ...
81-215 3.72e-19

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: 83.87  E-value: 3.72e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446394447  81 AKKSLAVAVYNHYKRiqqlGPKEDDVELQKSNIALIGPTGSGKTLLAQTLAKTLNVPFAIADATSLTEAgYVGDDVENiL 160
Cdd:cd19481    1 LKASLREAVEAPRRG----SRLRRYGLGLPKGILLYGPPGTGKTLLAKALAGELGLPLIVVKLSSLLSK-YVGESEKN-L 74
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 446394447 161 LRLIQAAdfdiDKAEKGIIYVDEIDKIARKSENTSITRDVSgeGVQQALLKILEG 215
Cdd:cd19481   75 RKIFERA----RRLAPCILFIDEIDAIGRKRDSSGESGELR--RVLNQLLTELDG 123
AAA pfam00004
ATPase family associated with various cellular activities (AAA); AAA family proteins often ...
115-222 1.37e-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: 67.23  E-value: 1.37e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446394447  115 LIGPTGSGKTLLAQTLAKTLNVPFAIADATSLTEaGYVGDDVENILLRLIQAadfdiDKAEKGIIYVDEIDKIARKSENT 194
Cdd:pfam00004   3 LYGPPGTGKTTLAKAVAKELGAPFIEISGSELVS-KYVGESEKRLRELFEAA-----KKLAPCVIFIDEIDALAGSRGSG 76
                          90       100
                  ....*....|....*....|....*...
gi 446394447  195 SitrDVSGEGVQQALLKILEGTTASVPP 222
Cdd:pfam00004  77 G---DSESRRVVNQLLTELDGFTSSNSK 101
AAA cd00009
The AAA+ (ATPases Associated with a wide variety of cellular Activities) superfamily ...
76-194 1.31e-12

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: 65.25  E-value: 1.31e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446394447  76 IGQEKAKKSLAVAVYNHykriqqlgpkeddvelQKSNIALIGPTGSGKTLLAQTLAKTL---NVPFAIADATSLTEAGYV 152
Cdd:cd00009    1 VGQEEAIEALREALELP----------------PPKNLLLYGPPGTGKTTLARAIANELfrpGAPFLYLNASDLLEGLVV 64
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 446394447 153 GDDVENILLRLIQAAdfdIDKAEKGIIYVDEIDKIARKSENT 194
Cdd:cd00009   65 AELFGHFLVRLLFEL---AEKAKPGVLFIDEIDSLSRGAQNA 103
ClpB_D2-small pfam10431
C-terminal, D2-small domain, of ClpB protein; This is the C-terminal domain of ClpB protein, ...
311-389 1.26e-11

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: 60.11  E-value: 1.26e-11
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446394447  311 LDVTALKNILTQpknALVKQYTKMLElDDVDLEFTEEALSAISEKAIERKTGARGLRSIIEESLIDIMFDVPSNENVTK 389
Cdd:pfam10431   1 LSKEELRKIVDL---QLKELQKRLAE-RGITLELTDAAKDWLAEKGYDPEYGARPLRRAIQREIEDPLAEEILSGELKE 75
SpoVK COG0464
AAA+-type ATPase, SpoVK/Ycf46/Vps4 family [Cell wall/membrane/envelope biogenesis, Cell cycle ...
115-220 6.16e-10

AAA+-type ATPase, SpoVK/Ycf46/Vps4 family [Cell wall/membrane/envelope biogenesis, Cell cycle control, cell division, chromosome partitioning, Signal transduction mechanisms];


Pssm-ID: 440232 [Multi-domain]  Cd Length: 397  Bit Score: 60.70  E-value: 6.16e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446394447 115 LIGPTGSGKTLLAQTLAKTLNVPFAIADATSLTeAGYVGDDVENIllRLIqaadfdIDKAEK---GIIYVDEIDKIARKS 191
Cdd:COG0464  196 LYGPPGTGKTLLARALAGELGLPLIEVDLSDLV-SKYVGETEKNL--REV------FDKARGlapCVLFIDEADALAGKR 266
                         90       100
                 ....*....|....*....|....*....
gi 446394447 192 ENtsiTRDVSGEGVQQALLKILEGTTASV 220
Cdd:COG0464  267 GE---VGDGVGRRVVNTLLTEMEELRSDV 292
RecA-like_CDC48_NLV2_r1-like cd19503
first of two ATPase domains of CDC48 and NLV2, and similar ATPase domains; CDC48 in yeast and ...
115-215 1.14e-08

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: 54.22  E-value: 1.14e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446394447 115 LIGPTGSGKTLLAQTLAKTLNVPFAIADATSLTeAGYVGDDVENilLRLIQAadfDIDKAEKGIIYVDEIDKIARKSENT 194
Cdd:cd19503   39 LHGPPGTGKTLLARAVANEAGANFLSISGPSIV-SKYLGESEKN--LREIFE---EARSHAPSIIFIDEIDALAPKREED 112
                         90       100
                 ....*....|....*....|.
gi 446394447 195 SitRDVSGEGVQQaLLKILEG 215
Cdd:cd19503  113 Q--REVERRVVAQ-LLTLMDG 130
RecA-like_NVL_r1-like cd19518
first of two ATPase domains of NVL (nuclear VCP-like protein) and similar ATPase domains; NVL ...
113-209 1.85e-07

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


Pssm-ID: 410926 [Multi-domain]  Cd Length: 169  Bit Score: 50.48  E-value: 1.85e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446394447 113 IALIGPTGSGKTLLAQTLAKTLNVPFAIADATSLTeAGYVGDDVENIllRLIqaadFDIDKAEK-GIIYVDEIDKIARKS 191
Cdd:cd19518   37 VLLHGPPGCGKTMLANAIAGELKVPFLKISATEIV-SGVSGESEEKI--REL----FDQAISNApCIVFIDEIDAITPKR 109
                         90
                 ....*....|....*...
gi 446394447 192 ENTSitRDVSGEGVQQAL 209
Cdd:cd19518  110 ESAQ--REMERRIVSQLL 125
hflB PRK10733
ATP-dependent zinc metalloprotease FtsH;
75-190 7.65e-07

ATP-dependent zinc metalloprotease FtsH;


Pssm-ID: 182683 [Multi-domain]  Cd Length: 644  Bit Score: 51.19  E-value: 7.65e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446394447  75 VIGQEKAKKSLA--VAVYNHYKRIQQLGPKeddvelQKSNIALIGPTGSGKTLLAQTLAKTLNVPFAIADATSLTEAgYV 152
Cdd:PRK10733 154 VAGCDEAKEEVAelVEYLREPSRFQKLGGK------IPKGVLMVGPPGTGKTLLAKAIAGEAKVPFFTISGSDFVEM-FV 226
                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 446394447 153 GDDVENILLRLIQAadfdiDKAEKGIIYVDEIDKIARK 190
Cdd:PRK10733 227 GVGASRVRDMFEQA-----KKAAPCIIFIDEIDAVGRQ 259
RecA-like_FtsH cd19501
ATP-dependent zinc metalloprotease FtsH; FtsH ATPase is a processive, ATP-dependent zinc ...
75-190 1.00e-06

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


Pssm-ID: 410909 [Multi-domain]  Cd Length: 171  Bit Score: 48.38  E-value: 1.00e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446394447  75 VIGQEKAKKSL--AVAVYNHYKRIQQLG---PKeddvelqksNIALIGPTGSGKTLLAQTLAKTLNVPFAIADATSLTEA 149
Cdd:cd19501    6 VAGCEEAKEELkeVVEFLKNPEKFTKLGakiPK---------GVLLVGPPGTGKTLLAKAVAGEAGVPFFSISGSDFVEM 76
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 446394447 150 gYVGddvenillrlIQAADF-DI-DKAEKG---IIYVDEIDKIARK 190
Cdd:cd19501   77 -FVG----------VGASRVrDLfEQAKKNapcIVFIDEIDAVGRK 111
RecA-like_VPS4-like cd19509
ATPase domain of VPS4, ATAD1, K, KTNA1, Spastin, FIGL-1 and similar ATPase domains; This ...
75-241 1.44e-06

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


Pssm-ID: 410917 [Multi-domain]  Cd Length: 163  Bit Score: 48.12  E-value: 1.44e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446394447  75 VIGQEKAKKSLAVAVYNHYKRIQ----QLGPKeddvelqkSNIALIGPTGSGKTLLAQTLAKTLNVPFAIADATSLTeAG 150
Cdd:cd19509    1 IAGLDDAKEALKEAVILPSLRPDlfpgLRGPP--------RGILLYGPPGTGKTLLARAVASESGSTFFSISASSLV-SK 71
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446394447 151 YVGDDVENIllrliqAADFDIDKAEK-GIIYVDEIDKI--ARKSENTSITRDVSGEgvqqaLLKILEGTTASvppqggrk 227
Cdd:cd19509   72 WVGESEKIV------RALFALARELQpSIIFIDEIDSLlsERGSGEHEASRRVKTE-----FLVQMDGVLNK-------- 132
                        170
                 ....*....|....
gi 446394447 228 hPNQEMIQIDTTNI 241
Cdd:cd19509  133 -PEDRVLVLGATNR 145
AAA smart00382
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ...
109-193 5.41e-06

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


Pssm-ID: 214640 [Multi-domain]  Cd Length: 148  Bit Score: 45.83  E-value: 5.41e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446394447   109 QKSNIALIGPTGSGKTLLAQTLAKTLNVP---FAIADATSLTEAGYVGDDVENILLRL-----IQAADFDIDKAEK---G 177
Cdd:smart00382   1 PGEVILIVGPPGSGKTTLARALARELGPPgggVIYIDGEDILEEVLDQLLLIIVGGKKasgsgELRLRLALALARKlkpD 80
                           90
                   ....*....|....*.
gi 446394447   178 IIYVDEIDKIARKSEN 193
Cdd:smart00382  81 VLILDEITSLLDAEQE 96
RecA-like_PEX1_r2 cd19526
second of two ATPase domains of Peroxisomal biogenesis factor 1 (PEX1); PEX1(also known as ...
109-215 6.94e-06

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: 45.88  E-value: 6.94e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446394447 109 QKSNIALIGPTGSGKTLLAQTLAKTLNVPFAIADATSLTeAGYVGDDVENILLRLIQAAdfdidKAEKGIIYVDEIDKIA 188
Cdd:cd19526   26 LRSGILLYGPPGCGKTLLASAIASECGLNFISVKGPELL-NKYIGASEQNVRDLFSRAQ-----SAKPCILFFDEFDSIA 99
                         90       100
                 ....*....|....*....|....*....
gi 446394447 189 --RKSENTSITRDVsgegVQQaLLKILEG 215
Cdd:cd19526  100 pkRGHDSTGVTDRV----VNQ-LLTQLDG 123
RecA-like_Figl-1 cd19525
ATPase domain of Fidgetin-Like 1 (FIGL-1); FIGL-1 may participate in DNA repair in the nucleus; ...
66-264 8.66e-06

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: 46.13  E-value: 8.66e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446394447  66 EIMDHLNEY----VIGQEKAKKSLAVAVYNHYKRIQQL----GPKEddvelqksNIALIGPTGSGKTLLAQTLAKTLNVP 137
Cdd:cd19525   11 EIMDHGPPInwadIAGLEFAKKTIKEIVVWPMLRPDIFtglrGPPK--------GILLFGPPGTGKTLIGKCIASQSGAT 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446394447 138 FAIADATSLTeAGYVGDDvENILLRLIQAADFDidkaEKGIIYVDEIDKIARK---SENTSITRdvsgegVQQALLKILE 214
Cdd:cd19525   83 FFSISASSLT-SKWVGEG-EKMVRALFSVARCK----QPAVIFIDEIDSLLSQrgeGEHESSRR------IKTEFLVQLD 150
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 446394447 215 GTTASvppqggrkhPNQEMIQIDTTNilfilggAFDGIEEVIKRRLGEKV 264
Cdd:cd19525  151 GATTS---------SEDRILVVGATN-------RPQEIDEAARRRLVKRL 184
RecA-like_spastin cd19524
ATPase domain of spastin; Spastin is an ATP-dependent microtubule-severing protein involved in ...
75-203 1.10e-05

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


Pssm-ID: 410932 [Multi-domain]  Cd Length: 164  Bit Score: 45.23  E-value: 1.10e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446394447  75 VIGQEKAKKSLAVAVYNHYKRIQQLgpkeDDVELQKSNIALIGPTGSGKTLLAQTLAKTLNVPFAIADATSLTeAGYVGD 154
Cdd:cd19524    2 IAGQDLAKQALQEMVILPSLRPELF----TGLRAPARGLLLFGPPGNGKTMLAKAVAAESNATFFNISAASLT-SKYVGE 76
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 446394447 155 DvENILLRLIQAAdfdiDKAEKGIIYVDEIDKI--ARKSENTSITRDVSGE 203
Cdd:cd19524   77 G-EKLVRALFAVA----RELQPSIIFIDEVDSLlsERSEGEHEASRRLKTE 122
CDC48 TIGR01243
AAA family ATPase, CDC48 subfamily; This subfamily of the AAA family ATPases includes two ...
113-215 1.22e-05

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: 47.59  E-value: 1.22e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446394447  113 IALIGPTGSGKTLLAQTLAKTLNVPFAIADATSLTeAGYVGDDVENilLRLIqaadfdIDKAEK---GIIYVDEIDKIAR 189
Cdd:TIGR01243 215 VLLYGPPGTGKTLLAKAVANEAGAYFISINGPEIM-SKYYGESEER--LREI------FKEAEEnapSIIFIDEIDAIAP 285
                          90       100
                  ....*....|....*....|....*.
gi 446394447  190 KSEntSITRDVSGEGVQQaLLKILEG 215
Cdd:TIGR01243 286 KRE--EVTGEVEKRVVAQ-LLTLMDG 308
RecA-like_KTNA1 cd19522
Katanin p60 ATPase-containing subunit A1; Katanin p60 ATPase-containing subunit A1 (KTNA1) is ...
113-264 2.51e-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: 44.59  E-value: 2.51e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446394447 113 IALIGPTGSGKTLLAQTLAKTLNVPFAIADATSLTeAGYVGDDVEniLLRLIqaadFDIDKA-EKGIIYVDEIDKIARK- 190
Cdd:cd19522   36 VLMVGPPGTGKTLLAKAVATECGTTFFNVSSSTLT-SKYRGESEK--LVRLL----FEMARFyAPTTIFIDEIDSICSRr 108
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446394447 191 --SENTSITRDVSGEgvqqaLLKILEGTTASVPPQGGRKHpnqeMIQIDTTNILFilggafdGIEEVIKRRLGEKV 264
Cdd:cd19522  109 gtSEEHEASRRVKSE-----LLVQMDGVGGASENDDPSKM----VMVLAATNFPW-------DIDEALRRRLEKRI 168
clpA PRK11034
ATP-dependent Clp protease ATP-binding subunit; Provisional
65-374 2.62e-05

ATP-dependent Clp protease ATP-binding subunit; Provisional


Pssm-ID: 236828 [Multi-domain]  Cd Length: 758  Bit Score: 46.37  E-value: 2.62e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446394447  65 KEIMDHLNEYVIGQEKAKKSLAVAVynhykRIQQLGPKEDDVELqkSNIALIGPTGSGKTLLAQTLAKTLNVPFAIADAT 144
Cdd:PRK11034 450 KNLGDRLKMLVFGQDKAIEALTEAI-----KMSRAGLGHEHKPV--GSFLFAGPTGVGKTEVTVQLSKALGIELLRFDMS 522
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446394447 145 SLTE-----------AGYVGDDVENILlrliqaADFDIdKAEKGIIYVDEIDKiarksentsitrdvSGEGVQQALLKIL 213
Cdd:PRK11034 523 EYMErhtvsrligapPGYVGFDQGGLL------TDAVI-KHPHAVLLLDEIEK--------------AHPDVFNLLLQVM 581
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446394447 214 EGTTASvpPQGGRKHPNQEMIQIDTTNIlfilggafdGIEEVIKrrlgeKVIGFSSNEaDKYDEQALLAQIrpedlqayg 293
Cdd:PRK11034 582 DNGTLT--DNNGRKADFRNVVLVMTTNA---------GVRETER-----KSIGLIHQD-NSTDAMEEIKKI--------- 635
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446394447 294 LIPEFIGRVPIVANLETLDvtalKNILTQPKNALVKQYTKMLELDDVDLEFTEEALSAISEKAIERKTGARGLRSIIEES 373
Cdd:PRK11034 636 FTPEFRNRLDNIIWFDHLS----TDVIHQVVDKFIVELQAQLDQKGVSLEVSQEARDWLAEKGYDRAMGARPMARVIQDN 711

                 .
gi 446394447 374 L 374
Cdd:PRK11034 712 L 712
RecA-like_PEX6_r2 cd19527
second of two ATPase domains of Peroxisomal biogenesis factor 6 (PEX6); PEX6(also known as ...
109-219 3.34e-05

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


Pssm-ID: 410935 [Multi-domain]  Cd Length: 160  Bit Score: 44.04  E-value: 3.34e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446394447 109 QKSNIALIGPTGSGKTLLAQTLAKTLNVPFAIADATSLTEAgYVGDDVENIlLRLIQAAdfdiDKAEKGIIYVDEIDKIA 188
Cdd:cd19527   25 KRSGILLYGPPGTGKTLLAKAIATECSLNFLSVKGPELINM-YIGESEANV-REVFQKA----RDAKPCVIFFDELDSLA 98
                         90       100       110
                 ....*....|....*....|....*....|.
gi 446394447 189 RKSENTSITRDVSGEGVQQaLLKILEGTTAS 219
Cdd:cd19527   99 PSRGNSGDSGGVMDRVVSQ-LLAELDGMSSS 128
RecA-like_CDC48_r1-like cd19519
first of two ATPase domains of CDC48 and similar ATPase domains; CDC48 in yeast and p97 or VCP ...
113-215 3.95e-05

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


Pssm-ID: 410927 [Multi-domain]  Cd Length: 166  Bit Score: 43.96  E-value: 3.95e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446394447 113 IALIGPTGSGKTLLAQTLAKTLNVPFAIADATSLTeAGYVGDDVENilLRLIqaadfdIDKAEK---GIIYVDEIDKIAR 189
Cdd:cd19519   37 ILLYGPPGTGKTLIARAVANETGAFFFLINGPEIM-SKLAGESESN--LRKA------FEEAEKnapAIIFIDEIDAIAP 107
                         90       100
                 ....*....|....*....|....*.
gi 446394447 190 KSENTsiTRDVSGEGVQQaLLKILEG 215
Cdd:cd19519  108 KREKT--HGEVERRIVSQ-LLTLMDG 130
RecA-like_ClpB_Hsp104-like cd19499
Chaperone protein ClpB/Hsp104 subfamily; Bacterial Caseinolytic peptidase B (ClpB) and ...
65-135 5.28e-05

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: 43.71  E-value: 5.28e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446394447  65 KEIMDHLNEYVIGQEKAKKSLAVAVynhykRIQQLGpkEDDVELQKSNIALIGPTGSGKTLLAQTLAKTLN 135
Cdd:cd19499    3 LNLEERLHERVVGQDEAVKAVSDAI-----RRARAG--LSDPNRPIGSFLFLGPTGVGKTELAKALAELLF 66
AAA_5 pfam07728
AAA domain (dynein-related subfamily); This Pfam entry includes some of the AAA proteins not ...
112-242 6.01e-05

AAA domain (dynein-related subfamily); This Pfam entry includes some of the AAA proteins not detected by the pfam00004 model.


Pssm-ID: 400191 [Multi-domain]  Cd Length: 135  Bit Score: 42.66  E-value: 6.01e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446394447  112 NIALIGPTGSGKTLLAQTLAKTLN--VPFAIADATSLTEagyvgDDVE---NILLRLIQAADFDIDKA--EKGIIYVDEI 184
Cdd:pfam07728   1 GVLLVGPPGTGKTELAERLAAALSnrPVFYVQLTRDTTE-----EDLFgrrNIDPGGASWVDGPLVRAarEGEIAVLDEI 75
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 446394447  185 DKIARKsentsitrdvsgegVQQALLKILEGTTASVPPQGGR-KHPNQEMIQIDTTNIL 242
Cdd:pfam07728  76 NRANPD--------------VLNSLLSLLDERRLLLPDGGELvKAAPDGFRLIATMNPL 120
SK cd00464
Shikimate kinase (SK) is the fifth enzyme in the shikimate pathway, a seven-step biosynthetic ...
112-138 6.28e-05

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: 42.93  E-value: 6.28e-05
                         10        20
                 ....*....|....*....|....*..
gi 446394447 112 NIALIGPTGSGKTLLAQTLAKTLNVPF 138
Cdd:cd00464    1 NIVLIGMMGAGKTTVGRLLAKALGLPF 27
RecA-like_NSF-SEC18_r1-like cd19504
first of two ATPase domains of NSF and SEC18, and similar ATPase domains; ...
113-212 6.29e-05

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


Pssm-ID: 410912 [Multi-domain]  Cd Length: 177  Bit Score: 43.25  E-value: 6.29e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446394447 113 IALIGPTGSGKTLLAQTLAKTLNV--PFAIADATSLTEagYVGDDVENIlLRLIqaADFDIDKAEKG------IIYVDEI 184
Cdd:cd19504   38 ILLYGPPGTGKTLMARQIGKMLNArePKIVNGPEILNK--YVGESEANI-RKLF--ADAEEEQRRLGansglhIIIFDEI 112
                         90       100
                 ....*....|....*....|....*...
gi 446394447 185 DKIARKSENTSITRDVSGEGVQQALLKI 212
Cdd:cd19504  113 DAICKQRGSMAGSTGVHDTVVNQLLSKI 140
ruvB PRK00080
Holliday junction branch migration DNA helicase RuvB;
71-192 9.03e-05

Holliday junction branch migration DNA helicase RuvB;


Pssm-ID: 234619 [Multi-domain]  Cd Length: 328  Bit Score: 44.35  E-value: 9.03e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446394447  71 LNEYvIGQEKAKKSLAVAVYNHYKRIQQLGPkeddvelqksnIALIGPTGSGKTLLAQTLAKTLNVPFAIADATSLTEAG 150
Cdd:PRK00080  24 LDEF-IGQEKVKENLKIFIEAAKKRGEALDH-----------VLLYGPPGLGKTTLANIIANEMGVNIRITSGPALEKPG 91
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 446394447 151 yvgdDVENILLRLiqaadfdidkaEKG-IIYVDEIDKIARKSE 192
Cdd:PRK00080  92 ----DLAAILTNL-----------EEGdVLFIDEIHRLSPVVE 119
aroK PRK00131
shikimate kinase; Reviewed
108-138 1.05e-04

shikimate kinase; Reviewed


Pssm-ID: 234654 [Multi-domain]  Cd Length: 175  Bit Score: 42.48  E-value: 1.05e-04
                         10        20        30
                 ....*....|....*....|....*....|.
gi 446394447 108 LQKSNIALIGPTGSGKTLLAQTLAKTLNVPF 138
Cdd:PRK00131   2 LKGPNIVLIGFMGAGKSTIGRLLAKRLGYDF 32
RecA-like_PAN_like cd19502
proteasome activating nucleotidase PAN and related proteasome subunits; This subfamily ...
115-213 1.06e-04

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


Pssm-ID: 410910 [Multi-domain]  Cd Length: 171  Bit Score: 42.71  E-value: 1.06e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446394447 115 LIGPTGSGKTLLAQTLAKTLNVPFAIADATSLTEAgYVGDDVenillRLIQAAdFDIDKAEK-GIIYVDEIDKIA--RKS 191
Cdd:cd19502   42 LYGPPGTGKTLLAKAVANHTDATFIRVVGSELVQK-YIGEGA-----RLVREL-FEMAREKApSIIFIDEIDAIGakRFD 114
                         90       100
                 ....*....|....*....|..
gi 446394447 192 ENTSITRDvsgegVQQALLKIL 213
Cdd:cd19502  115 SGTGGDRE-----VQRTMLELL 131
RecA-like_CDC48_r2-like cd19511
second of two ATPase domains of CDC48/p97, PEX1 and -6, VAT and NVL, and similar ATPase ...
113-195 1.26e-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: 1.26e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446394447 113 IALIGPTGSGKTLLAQTLAKTLNVPF-AIADATSLTEagYVGDDvENILLRLIQAAdfdiDKAEKGIIYVDEIDKIA-RK 190
Cdd:cd19511   30 VLLYGPPGCGKTLLAKALASEAGLNFiSVKGPELFSK--YVGES-ERAVREIFQKA----RQAAPCIIFFDEIDSLApRR 102

                 ....*
gi 446394447 191 SENTS 195
Cdd:cd19511  103 GQSDS 107
RecA-like_ATAD1 cd19520
ATPase domain of ATPase family AAA domain-containing protein 1 and similar ATPase domains; ...
113-194 2.02e-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: 41.64  E-value: 2.02e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446394447 113 IALIGPTGSGKTLLAQTLAKTLNVPFAIADATSLTEAGYvGDDVEnillrlIQAADFDI-DKAEKGIIYVDEIDKIARKS 191
Cdd:cd19520   38 VLLYGPPGCGKTMLAKATAKEAGARFINLQVSSLTDKWY-GESQK------LVAAVFSLaSKLQPSIIFIDEIDSFLRQR 110

                 ...
gi 446394447 192 ENT 194
Cdd:cd19520  111 SST 113
AAA_22 pfam13401
AAA domain;
106-209 2.50e-04

AAA domain;


Pssm-ID: 379165 [Multi-domain]  Cd Length: 129  Bit Score: 40.79  E-value: 2.50e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446394447  106 VELQKSNIALIGPTGSGKTLLAQTLAKTL---NVPFAIADATSLTEAGYV--------------GDDVENILLRLIQAAD 168
Cdd:pfam13401   1 IRFGAGILVLTGESGTGKTTLLRRLLEQLpevRDSVVFVDLPSGTSPKDLlrallralglplsgRLSKEELLAALQQLLL 80
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 446394447  169 fdiDKAEKGIIYVDEIDKIARKSENT-SITRDVSGEGVQQAL 209
Cdd:pfam13401  81 ---ALAVAVVLIIDEAQHLSLEALEElRDLLNLSSKLLQLIL 119
NadR3 COG3172
Nicotinamide riboside kinase [Coenzyme transport and metabolism]; Nicotinamide riboside kinase ...
113-179 2.65e-04

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


Pssm-ID: 442405 [Multi-domain]  Cd Length: 178  Bit Score: 41.34  E-value: 2.65e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446394447 113 IALIGPTGSGKTLLAQTLAKTLNVPFAiadatslTEAG----------YVGDDVENILLRLIQAADFDIDKAEKGII 179
Cdd:COG3172   11 IVLLGAESTGKTTLARALAAHYNTPWV-------PEYGreyleekgraLTYDDLLAIARGQLALEDAAAKRANKLLF 80
FlhF COG1419
Flagellar biosynthesis GTPase FlhF [Cell motility];
65-132 3.22e-04

Flagellar biosynthesis GTPase FlhF [Cell motility];


Pssm-ID: 441029 [Multi-domain]  Cd Length: 361  Bit Score: 42.55  E-value: 3.22e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446394447  65 KEIMDHLNEyVIGQEKAKKSLAVAVynhykrIQQLGPKEDDVELQKSNIALIGPTGSGKTLlaqTLAK 132
Cdd:COG1419  126 RELLEKLPE-DLSAEEAWRALLEAL------ARRLPVAEDPLLDEGGVIALVGPTGVGKTT---TIAK 183
Mg_chelatase pfam01078
Magnesium chelatase, subunit ChlI; Magnesium-chelatase is a three-component enzyme that ...
75-130 4.61e-04

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: 41.37  E-value: 4.61e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 446394447   75 VIGQEKAKKSLAVAVY-NHykriqqlgpkeddvelqksNIALIGPTGSGKTLLAQTL 130
Cdd:pfam01078   5 VKGQEQAKRALEIAAAgGH-------------------NLLMIGPPGSGKTMLAKRL 42
YifB COG0606
Predicted Mg-chelatase, contains ChlI-like and ATPase domains, YifB family [Posttranslational ...
75-130 7.49e-04

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: 41.56  E-value: 7.49e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 446394447  75 VIGQEKAKKSLAVAVY-NHykriqqlgpkeddvelqksNIALIGPTGSGKTLLAQTL 130
Cdd:COG0606  194 VKGQEQAKRALEIAAAgGH-------------------NLLMIGPPGSGKTMLARRL 231
PRK13342 PRK13342
recombination factor protein RarA; Reviewed
117-184 7.54e-04

recombination factor protein RarA; Reviewed


Pssm-ID: 237355 [Multi-domain]  Cd Length: 413  Bit Score: 41.61  E-value: 7.54e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446394447 117 GPTGSGKTLLAQTLAKTLNVPFAIADATSlteAGyVGDdveniLLRLIQAADFDIDKAEKGIIYVDEI 184
Cdd:PRK13342  43 GPPGTGKTTLARIIAGATDAPFEALSAVT---SG-VKD-----LREVIEEARQRRSAGRRTILFIDEI 101
AroK COG0703
Shikimate kinase [Amino acid transport and metabolism]; Shikimate kinase is part of the ...
113-138 8.17e-04

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


Pssm-ID: 440467 [Multi-domain]  Cd Length: 165  Bit Score: 39.73  E-value: 8.17e-04
                         10        20
                 ....*....|....*....|....*.
gi 446394447 113 IALIGPTGSGKTLLAQTLAKTLNVPF 138
Cdd:COG0703    1 IVLIGMMGAGKSTVGRLLAKRLGLPF 26
PRK09862 PRK09862
ATP-dependent protease;
26-134 9.48e-04

ATP-dependent protease;


Pssm-ID: 182120 [Multi-domain]  Cd Length: 506  Bit Score: 41.50  E-value: 9.48e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446394447  26 LVAGSGVYICNECIELCSEIV-EEELAQNTSEAMTELPTPKEIMDhlneyVIGQEKAKKSLAV-AVYNHykriqqlgpke 103
Cdd:PRK09862 148 LINGEGCLIADHLQAVCAFLEgKHALERPKPTDAVSRALQHDLSD-----VIGQEQGKRGLEItAAGGH----------- 211
                         90       100       110
                 ....*....|....*....|....*....|.
gi 446394447 104 ddvelqksNIALIGPTGSGKTLLAQTLAKTL 134
Cdd:PRK09862 212 --------NLLLIGPPGTGKTMLASRINGLL 234
FlhF TIGR03499
flagellar biosynthetic protein FlhF; [Cellular processes, Chemotaxis and motility]
46-132 1.00e-03

flagellar biosynthetic protein FlhF; [Cellular processes, Chemotaxis and motility]


Pssm-ID: 274609 [Multi-domain]  Cd Length: 282  Bit Score: 40.78  E-value: 1.00e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446394447   46 VEEELAQNTSEAMTELPTPKEIMDHLNEYVIGQEKAKkslavavynhykriqqlgPKEDDVELQKSNIALIGPTGSGKTl 125
Cdd:TIGR03499 148 VSEELARELLEKLPEDADAEDAWRWLREALEGMLPVK------------------PEEDPILEQGGVIALVGPTGVGKT- 208

                  ....*..
gi 446394447  126 laQTLAK 132
Cdd:TIGR03499 209 --TTLAK 213
RecA-like_Lon cd19500
lon protease homolog 2 peroxisomal; Lon protease (also known as Lon peptidase) is an ...
113-244 1.31e-03

lon protease homolog 2 peroxisomal; Lon protease (also known as Lon peptidase) is an evolutionarily conserved ATP-dependent serine protease, present in bacteria and eukaryotic mitochondria and peroxisomes, which mediates the selective degradation of mutant and abnormal proteins as well as certain short-lived regulatory proteins. Lon protease is both an ATP-dependent peptidase and a protein-activated ATPase. This RecA-like Lon domain subfamily belongs to the RecA-like NTPase family which includes the NTP binding domain of F1 and V1 H(+)ATPases, DnaB and related helicases as well as bacterial RecA and related eukaryotic and archaeal recombinases. The RecA-like NTPase family also includes bacterial conjugation proteins and related DNA transfer proteins involved in type II and type IV secretion.


Pssm-ID: 410908 [Multi-domain]  Cd Length: 182  Bit Score: 39.46  E-value: 1.31e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446394447 113 IALIGPTGSGKTLLAQTLAKTLNVPFAiadATSLteaGYVGDDVE----------NILLRLIQAadfdIDKAEKG--IIY 180
Cdd:cd19500   40 LCLVGPPGVGKTSLGKSIARALGRKFV---RISL---GGVRDEAEirghrrtyvgAMPGRIIQA----LKKAGTNnpVFL 109
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446394447 181 VDEIDKiarksentsITRDVSGEGvQQALLKILEgttasvPPQGGRKHPNQEMIQIDTTNILFI 244
Cdd:cd19500  110 LDEIDK---------IGSSFRGDP-ASALLEVLD------PEQNSTFSDHYLDVPFDLSKVLFI 157
RecA-like_ATAD3-like cd19512
ATPase domains of ATPase AAA-domain protein 3A (ATAD3A), -3B, and -3C, and similar ATPase ...
112-199 1.79e-03

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


Pssm-ID: 410920 [Multi-domain]  Cd Length: 150  Bit Score: 38.66  E-value: 1.79e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446394447 112 NIALIGPTGSGKTLLAQTLAKTLNVPFAIadatslteagYVGDDVENILLRLIQAAD--FD-IDKAEKG-IIYVDEIDKI 187
Cdd:cd19512   24 NILFYGPPGTGKTLFAKKLALHSGMDYAI----------MTGGDVAPMGREGVTAIHkvFDwANTSRRGlLLFVDEADAF 93
                         90
                 ....*....|..
gi 446394447 188 ARKSENTSITRD 199
Cdd:cd19512   94 LRKRSTEKISED 105
ClpA COG0542
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ...
272-376 1.85e-03

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


Pssm-ID: 440308 [Multi-domain]  Cd Length: 836  Bit Score: 40.45  E-value: 1.85e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446394447 272 ADKYDEQALLAQIRPEdLQAYgLIPEFIGRVPIVANLETLDVTALKNILtqpkNALVKQYTKMLELDDVDLEFTEEALSA 351
Cdd:COG0542  711 EDEPDYEEMKEAVMEE-LKKH-FRPEFLNRIDEIIVFHPLSKEELRKIV----DLQLKRLRKRLAERGITLELTDAAKDF 784
                         90       100
                 ....*....|....*....|....*
gi 446394447 352 ISEKAIERKTGARGLRSIIEESLID 376
Cdd:COG0542  785 LAEKGYDPEYGARPLKRAIQRELED 809
MoxR COG0714
MoxR-like ATPase [General function prediction only]; MoxR-like ATPase is part of the Pathway ...
63-186 2.70e-03

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: 39.38  E-value: 2.70e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446394447  63 TPKEIMDHLNEYVIGQEKAKKSLAVAVYNHykriqqlGPkeddvelqksnIALIGPTGSGKTLLAQTLAKTLNVPFAIAD 142
Cdd:COG0714    2 TEARLRAEIGKVYVGQEELIELVLIALLAG-------GH-----------LLLEGVPGVGKTTLAKALARALGLPFIRIQ 63
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 446394447 143 ATS-LTEAgyvgdDV--ENILLRliQAADFDIdkaEKG-----IIYVDEIDK 186
Cdd:COG0714   64 FTPdLLPS-----DIlgTYIYDQ--QTGEFEF---RPGplfanVLLADEINR 105
RecA-like_VCP_r2 cd19529
second of two ATPase domains of Valosin-containing protein-like ATPase (VAT) and similar ...
113-215 6.33e-03

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


Pssm-ID: 410937 [Multi-domain]  Cd Length: 159  Bit Score: 37.09  E-value: 6.33e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446394447 113 IALIGPTGSGKTLLAQTLAKTLNVPFAIADATSLTeAGYVGDD---VENILLRLIQAAdfdidkaeKGIIYVDEIDKIAR 189
Cdd:cd19529   30 ILLYGPPGTGKTLLAKAVATESNANFISVKGPELL-SKWVGESekaIREIFRKARQVA--------PCVIFFDEIDSIAP 100
                         90       100
                 ....*....|....*....|....*.
gi 446394447 190 KSENTSiTRDVSGEGVQQaLLKILEG 215
Cdd:cd19529  101 RRGTTG-DSGVTERVVNQ-LLTELDG 124
MiaA COG0324
tRNA A37 N6-isopentenylltransferase MiaA [Translation, ribosomal structure and biogenesis]; ...
113-136 6.97e-03

tRNA A37 N6-isopentenylltransferase MiaA [Translation, ribosomal structure and biogenesis]; tRNA A37 N6-isopentenylltransferase MiaA is part of the Pathway/BioSystem: tRNA modification


Pssm-ID: 440093  Cd Length: 306  Bit Score: 38.12  E-value: 6.97e-03
                         10        20
                 ....*....|....*....|....
gi 446394447 113 IALIGPTGSGKTLLAQTLAKTLNV 136
Cdd:COG0324    5 IVIVGPTASGKTALAIELAKRLGG 28
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH