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Conserved domains on  [gi|446841159|ref|WP_000918415|]
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MULTISPECIES: ATP-dependent Clp protease ATP-binding subunit ClpX [Streptococcus]

Protein Classification

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

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

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
ClpX COG1219
ATP-dependent protease Clp, ATPase subunit ClpX [Posttranslational modification, protein ...
1-405 0e+00

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


:

Pssm-ID: 440832 [Multi-domain]  Cd Length: 409  Bit Score: 815.82  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446841159   1 MAGNrnNDMNVYCSFCGKSQDEVKKIIAGNGVFICNECVALSQEIIKEELAEEVLA-DLAEVPKPKELLEILNQYVVGQD 79
Cdd:COG1219    1 MAGD--SKKELKCSFCGKSQDEVRKLIAGPGVYICDECVELCNEIIEEELKEEEAEeELKKLPKPKEIKAFLDEYVIGQE 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446841159  80 RAKRALAVAVYNHYKRVSYTESSDDDVDLQKSNILMIGPTGSGKTFLAQTLAKSLNVPFAIADATSLTEAGYVGEDVENI 159
Cdd:COG1219   79 RAKKVLSVAVYNHYKRLNSGSKDDDDVELEKSNILLIGPTGSGKTLLAQTLARILDVPFAIADATTLTEAGYVGEDVENI 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446841159 160 LLKLIQAADYNVERAERGIIYVDEIDKIAKKGENVSITRDVSGEGVQQALLKIIEGTVASVPPQGGRKHPNQEMIQINTK 239
Cdd:COG1219  159 LLKLLQAADYDVEKAERGIIYIDEIDKIARKSENPSITRDVSGEGVQQALLKILEGTVANVPPQGGRKHPQQEFIQIDTT 238
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446841159 240 NILFIVGGAFDGIEDLVKQRLGEKVIGFGQT--SRKIDDNASYMQEIISEDIQKFGLIPEFIGRLPVVAALELLTAEDLV 317
Cdd:COG1219  239 NILFICGGAFDGLEKIIERRLGKKSIGFGAEvkSKKEKDEGELLKQVEPEDLIKFGLIPEFIGRLPVIATLEELDEEALV 318
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446841159 318 RILTEPRNALVKQYQTLLSYDGVELEFDQDALLAIADKAIERKTGARGLRSIIEETMLDIMFEIPSQEDVTKVRITKAAV 397
Cdd:COG1219  319 RILTEPKNALVKQYQKLFEMDGVELEFTDEALEAIAKKAIERKTGARGLRSILEEILLDVMYELPSRKDVKKVVITKEVV 398

                 ....*...
gi 446841159 398 EGTDKPVL 405
Cdd:COG1219  399 EGKAKPIL 406
 
Name Accession Description Interval E-value
ClpX COG1219
ATP-dependent protease Clp, ATPase subunit ClpX [Posttranslational modification, protein ...
1-405 0e+00

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


Pssm-ID: 440832 [Multi-domain]  Cd Length: 409  Bit Score: 815.82  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446841159   1 MAGNrnNDMNVYCSFCGKSQDEVKKIIAGNGVFICNECVALSQEIIKEELAEEVLA-DLAEVPKPKELLEILNQYVVGQD 79
Cdd:COG1219    1 MAGD--SKKELKCSFCGKSQDEVRKLIAGPGVYICDECVELCNEIIEEELKEEEAEeELKKLPKPKEIKAFLDEYVIGQE 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446841159  80 RAKRALAVAVYNHYKRVSYTESSDDDVDLQKSNILMIGPTGSGKTFLAQTLAKSLNVPFAIADATSLTEAGYVGEDVENI 159
Cdd:COG1219   79 RAKKVLSVAVYNHYKRLNSGSKDDDDVELEKSNILLIGPTGSGKTLLAQTLARILDVPFAIADATTLTEAGYVGEDVENI 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446841159 160 LLKLIQAADYNVERAERGIIYVDEIDKIAKKGENVSITRDVSGEGVQQALLKIIEGTVASVPPQGGRKHPNQEMIQINTK 239
Cdd:COG1219  159 LLKLLQAADYDVEKAERGIIYIDEIDKIARKSENPSITRDVSGEGVQQALLKILEGTVANVPPQGGRKHPQQEFIQIDTT 238
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446841159 240 NILFIVGGAFDGIEDLVKQRLGEKVIGFGQT--SRKIDDNASYMQEIISEDIQKFGLIPEFIGRLPVVAALELLTAEDLV 317
Cdd:COG1219  239 NILFICGGAFDGLEKIIERRLGKKSIGFGAEvkSKKEKDEGELLKQVEPEDLIKFGLIPEFIGRLPVIATLEELDEEALV 318
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446841159 318 RILTEPRNALVKQYQTLLSYDGVELEFDQDALLAIADKAIERKTGARGLRSIIEETMLDIMFEIPSQEDVTKVRITKAAV 397
Cdd:COG1219  319 RILTEPKNALVKQYQKLFEMDGVELEFTDEALEAIAKKAIERKTGARGLRSILEEILLDVMYELPSRKDVKKVVITKEVV 398

                 ....*...
gi 446841159 398 EGTDKPVL 405
Cdd:COG1219  399 EGKAKPIL 406
clpX PRK05342
ATP-dependent Clp protease ATP-binding subunit ClpX;
2-408 0e+00

ATP-dependent Clp protease ATP-binding subunit ClpX;


Pssm-ID: 235422 [Multi-domain]  Cd Length: 412  Bit Score: 793.98  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446841159   2 AGNRNNDMNVYCSFCGKSQDEVKKIIAGNGVFICNECVALSQEIIKEELAEEvLADLAEVPKPKELLEILNQYVVGQDRA 81
Cdd:PRK05342   1 ARGGDSKKLLYCSFCGKSQHEVRKLIAGPGVYICDECIELCNEIIREELKEE-AVELKELPTPKEIKAHLDQYVIGQERA 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446841159  82 KRALAVAVYNHYKRVSYTESSDDDVDLQKSNILMIGPTGSGKTFLAQTLAKSLNVPFAIADATSLTEAGYVGEDVENILL 161
Cdd:PRK05342  80 KKVLSVAVYNHYKRLRHGDKKDDDVELQKSNILLIGPTGSGKTLLAQTLARILDVPFAIADATTLTEAGYVGEDVENILL 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446841159 162 KLIQAADYNVERAERGIIYVDEIDKIAKKGENVSITRDVSGEGVQQALLKIIEGTVASVPPQGGRKHPNQEMIQINTKNI 241
Cdd:PRK05342 160 KLLQAADYDVEKAQRGIVYIDEIDKIARKSENPSITRDVSGEGVQQALLKILEGTVASVPPQGGRKHPQQEFIQVDTTNI 239
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446841159 242 LFIVGGAFDGIEDLVKQRLGEKVIGFGQTSRKIDDN---ASYMQEIISEDIQKFGLIPEFIGRLPVVAALELLTAEDLVR 318
Cdd:PRK05342 240 LFICGGAFDGLEKIIKQRLGKKGIGFGAEVKSKKEKrteGELLKQVEPEDLIKFGLIPEFIGRLPVVATLEELDEEALVR 319
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446841159 319 ILTEPRNALVKQYQTLLSYDGVELEFDQDALLAIADKAIERKTGARGLRSIIEETMLDIMFEIPSQEDVTKVRITKAAVE 398
Cdd:PRK05342 320 ILTEPKNALVKQYQKLFEMDGVELEFTDEALEAIAKKAIERKTGARGLRSILEEILLDVMFELPSREDVEKVVITKEVVE 399
                        410
                 ....*....|
gi 446841159 399 GTDKPVLETA 408
Cdd:PRK05342 400 GKAKPLLIYR 409
clpX TIGR00382
endopeptidase Clp ATP-binding regulatory subunit (clpX); A member of the ATP-dependent ...
12-406 0e+00

endopeptidase Clp ATP-binding regulatory subunit (clpX); A member of the ATP-dependent proteases, ClpX has ATP-dependent chaperone activity and is required for specific ATP-dependent proteolytic activities expressed by ClpPX. The gene is also found to be involved in stress tolerance in Bacillus subtilis and is essential for the efficient acquisition of genes specifying type IA and IB restriction. [Protein fate, Protein folding and stabilization, Protein fate, Degradation of proteins, peptides, and glycopeptides]


Pssm-ID: 273047 [Multi-domain]  Cd Length: 413  Bit Score: 597.13  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446841159   12 YCSFCGKSQDEVKKIIAGNGVFICNECVALSQEIIKEEL-------AEEVLADLAEVPKPKELLEILNQYVVGQDRAKRA 84
Cdd:TIGR00382   9 YCSFCGKSQDEVRKLIAGPGVYICDECIELCHDILEEELgtrkeskEYEEEFELSYLPTPKEIKAHLDEYVIGQEQAKKV 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446841159   85 LAVAVYNHYKRVSYT--ESSDDDVDLQKSNILMIGPTGSGKTFLAQTLAKSLNVPFAIADATSLTEAGYVGEDVENILLK 162
Cdd:TIGR00382  89 LSVAVYNHYKRLNFEknKKSDNGVELSKSNILLIGPTGSGKTLLAQTLARILNVPFAIADATTLTEAGYVGEDVENILLK 168
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446841159  163 LIQAADYNVERAERGIIYVDEIDKIAKKGENVSITRDVSGEGVQQALLKIIEGTVASVPPQGGRKHPNQEMIQINTKNIL 242
Cdd:TIGR00382 169 LLQAADYDVEKAQKGIIYIDEIDKISRKSENPSITRDVSGEGVQQALLKIIEGTVANVPPQGGRKHPYQEFIQIDTSNIL 248
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446841159  243 FIVGGAFDGIEDLVKQRLGEKVIGFGQTSR-KIDDNASYMQEIISEDIQKFGLIPEFIGRLPVVAALELLTAEDLVRILT 321
Cdd:TIGR00382 249 FICGGAFVGLEKIIKKRTGKSSIGFGAEVKkKSKEKADLLRQVEPEDLVKFGLIPEFIGRLPVIATLEKLDEEALIAILT 328
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446841159  322 EPRNALVKQYQTLLSYDGVELEFDQDALLAIADKAIERKTGARGLRSIIEETMLDIMFEIPSQEDVTKVRITKAAVEGTD 401
Cdd:TIGR00382 329 KPKNALVKQYQALFKMDNVELDFEEEALKAIAKKALERKTGARGLRSIVEGLLLDVMFDLPSLEDLEKVVITKETVLKQS 408

                  ....*
gi 446841159  402 KPVLE 406
Cdd:TIGR00382 409 EPLLI 413
RecA-like_ClpX cd19497
ATP-dependent Clp protease ATP-binding subunit ClpX; ClpX is a component of the ATP-dependent ...
62-308 1.17e-159

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: 449.36  E-value: 1.17e-159
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446841159  62 PKPKELLEILNQYVVGQDRAKRALAVAVYNHYKRVSYTES-SDDDVDLQKSNILMIGPTGSGKTFLAQTLAKSLNVPFAI 140
Cdd:cd19497    1 PTPKEIKEHLDKYVIGQERAKKVLSVAVYNHYKRIRNNLKqKDDDVELEKSNILLIGPTGSGKTLLAQTLAKILDVPFAI 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446841159 141 ADATSLTEAGYVGEDVENILLKLIQAADYNVERAERGIIYVDEIDKIAKKGENVSITRDVSGEGVQQALLKIIEGTVASV 220
Cdd:cd19497   81 ADATTLTEAGYVGEDVENILLKLLQAADYDVERAQRGIVYIDEIDKIARKSENPSITRDVSGEGVQQALLKILEGTVANV 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446841159 221 PPQGGRKHPNQEMIQINTKNILFIVGGAFDGIEDLVKQRLGEKVIGFGQTSRKIDDNAS---YMQEIISEDIQKFGLIPE 297
Cdd:cd19497  161 PPQGGRKHPQQEFIQVDTTNILFICGGAFVGLEKIIARRLGKKSLGFGAETSSEKDEKErdeLLSKVEPEDLIKFGLIPE 240
                        250
                 ....*....|.
gi 446841159 298 FIGRLPVVAAL 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 3.90e-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: 140.41  E-value: 3.90e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446841159  110 KSNILMIGPTGSGKTFLAQTLAKSLNV---PFAIADATSLTEagyvgedvENILLKLIQAADYNVERAERG--------- 177
Cdd:pfam07724   3 IGSFLFLGPTGVGKTELAKALAELLFGderALIRIDMSEYME--------EHSVSRLIGAPPGYVGYEEGGqlteavrrk 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446841159  178 ---IIYVDEIDKIAKkgenvsitrdvsgeGVQQALLKIIEGTVASvppqggrkhPNQEmIQINTKNILFIVGGAFDGIED 254
Cdd:pfam07724  75 pysIVLIDEIEKAHP--------------GVQNDLLQILEGGTLT---------DKQG-RTVDFKNTLFIMTGNFGSEKI 130
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 446841159  255 LVKQRLGekvigfgqtsrkiDDNASYMQEIISEDIQKFGLIPEFIGRLPVV 305
Cdd:pfam07724 131 SDASRLG-------------DSPDYELLKEEVMDLLKKGFIPEFLGRLPII 168
ClpB_D2-small smart01086
C-terminal, D2-small domain, of ClpB protein; This is the C-terminal domain of ClpB protein, ...
311-400 3.35e-23

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: 92.51  E-value: 3.35e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446841159   311 LTAEDLVRILTEPRNALVKQYQTllsyDGVELEFDQDALLAIADKAIERKTGARGLRSIIEETMLDIMFEIPSQ---EDV 387
Cdd:smart01086   1 LDKEDLVRIVDLPLNALQKRLAE----KGITLEFTDEALDWLAEKGYDPKYGARPLRRIIQRELEDPLAELILSgelKDG 76
                           90
                   ....*....|...
gi 446841159   388 TKVRITKAAVEGT 400
Cdd:smart01086  77 DTVVVDVDDGELV 89
IS21_help_AAA NF038214
IS21-like element helper ATPase IstB; This protein family model resembles PF01695, but was ...
109-131 6.03e-03

IS21-like element helper ATPase IstB; This protein family model resembles PF01695, but was built to hit full-length AAA+ ATPases of IS21 family IS (insertion sequence) elements.


Pssm-ID: 439516  Cd Length: 232  Bit Score: 37.84  E-value: 6.03e-03
                         10        20
                 ....*....|....*....|...
gi 446841159 109 QKSNILMIGPTGSGKTFLAQTLA 131
Cdd:NF038214  89 RAENVLLLGPPGTGKTHLAIALG 111
 
Name Accession Description Interval E-value
ClpX COG1219
ATP-dependent protease Clp, ATPase subunit ClpX [Posttranslational modification, protein ...
1-405 0e+00

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


Pssm-ID: 440832 [Multi-domain]  Cd Length: 409  Bit Score: 815.82  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446841159   1 MAGNrnNDMNVYCSFCGKSQDEVKKIIAGNGVFICNECVALSQEIIKEELAEEVLA-DLAEVPKPKELLEILNQYVVGQD 79
Cdd:COG1219    1 MAGD--SKKELKCSFCGKSQDEVRKLIAGPGVYICDECVELCNEIIEEELKEEEAEeELKKLPKPKEIKAFLDEYVIGQE 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446841159  80 RAKRALAVAVYNHYKRVSYTESSDDDVDLQKSNILMIGPTGSGKTFLAQTLAKSLNVPFAIADATSLTEAGYVGEDVENI 159
Cdd:COG1219   79 RAKKVLSVAVYNHYKRLNSGSKDDDDVELEKSNILLIGPTGSGKTLLAQTLARILDVPFAIADATTLTEAGYVGEDVENI 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446841159 160 LLKLIQAADYNVERAERGIIYVDEIDKIAKKGENVSITRDVSGEGVQQALLKIIEGTVASVPPQGGRKHPNQEMIQINTK 239
Cdd:COG1219  159 LLKLLQAADYDVEKAERGIIYIDEIDKIARKSENPSITRDVSGEGVQQALLKILEGTVANVPPQGGRKHPQQEFIQIDTT 238
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446841159 240 NILFIVGGAFDGIEDLVKQRLGEKVIGFGQT--SRKIDDNASYMQEIISEDIQKFGLIPEFIGRLPVVAALELLTAEDLV 317
Cdd:COG1219  239 NILFICGGAFDGLEKIIERRLGKKSIGFGAEvkSKKEKDEGELLKQVEPEDLIKFGLIPEFIGRLPVIATLEELDEEALV 318
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446841159 318 RILTEPRNALVKQYQTLLSYDGVELEFDQDALLAIADKAIERKTGARGLRSIIEETMLDIMFEIPSQEDVTKVRITKAAV 397
Cdd:COG1219  319 RILTEPKNALVKQYQKLFEMDGVELEFTDEALEAIAKKAIERKTGARGLRSILEEILLDVMYELPSRKDVKKVVITKEVV 398

                 ....*...
gi 446841159 398 EGTDKPVL 405
Cdd:COG1219  399 EGKAKPIL 406
clpX PRK05342
ATP-dependent Clp protease ATP-binding subunit ClpX;
2-408 0e+00

ATP-dependent Clp protease ATP-binding subunit ClpX;


Pssm-ID: 235422 [Multi-domain]  Cd Length: 412  Bit Score: 793.98  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446841159   2 AGNRNNDMNVYCSFCGKSQDEVKKIIAGNGVFICNECVALSQEIIKEELAEEvLADLAEVPKPKELLEILNQYVVGQDRA 81
Cdd:PRK05342   1 ARGGDSKKLLYCSFCGKSQHEVRKLIAGPGVYICDECIELCNEIIREELKEE-AVELKELPTPKEIKAHLDQYVIGQERA 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446841159  82 KRALAVAVYNHYKRVSYTESSDDDVDLQKSNILMIGPTGSGKTFLAQTLAKSLNVPFAIADATSLTEAGYVGEDVENILL 161
Cdd:PRK05342  80 KKVLSVAVYNHYKRLRHGDKKDDDVELQKSNILLIGPTGSGKTLLAQTLARILDVPFAIADATTLTEAGYVGEDVENILL 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446841159 162 KLIQAADYNVERAERGIIYVDEIDKIAKKGENVSITRDVSGEGVQQALLKIIEGTVASVPPQGGRKHPNQEMIQINTKNI 241
Cdd:PRK05342 160 KLLQAADYDVEKAQRGIVYIDEIDKIARKSENPSITRDVSGEGVQQALLKILEGTVASVPPQGGRKHPQQEFIQVDTTNI 239
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446841159 242 LFIVGGAFDGIEDLVKQRLGEKVIGFGQTSRKIDDN---ASYMQEIISEDIQKFGLIPEFIGRLPVVAALELLTAEDLVR 318
Cdd:PRK05342 240 LFICGGAFDGLEKIIKQRLGKKGIGFGAEVKSKKEKrteGELLKQVEPEDLIKFGLIPEFIGRLPVVATLEELDEEALVR 319
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446841159 319 ILTEPRNALVKQYQTLLSYDGVELEFDQDALLAIADKAIERKTGARGLRSIIEETMLDIMFEIPSQEDVTKVRITKAAVE 398
Cdd:PRK05342 320 ILTEPKNALVKQYQKLFEMDGVELEFTDEALEAIAKKAIERKTGARGLRSILEEILLDVMFELPSREDVEKVVITKEVVE 399
                        410
                 ....*....|
gi 446841159 399 GTDKPVLETA 408
Cdd:PRK05342 400 GKAKPLLIYR 409
clpX TIGR00382
endopeptidase Clp ATP-binding regulatory subunit (clpX); A member of the ATP-dependent ...
12-406 0e+00

endopeptidase Clp ATP-binding regulatory subunit (clpX); A member of the ATP-dependent proteases, ClpX has ATP-dependent chaperone activity and is required for specific ATP-dependent proteolytic activities expressed by ClpPX. The gene is also found to be involved in stress tolerance in Bacillus subtilis and is essential for the efficient acquisition of genes specifying type IA and IB restriction. [Protein fate, Protein folding and stabilization, Protein fate, Degradation of proteins, peptides, and glycopeptides]


Pssm-ID: 273047 [Multi-domain]  Cd Length: 413  Bit Score: 597.13  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446841159   12 YCSFCGKSQDEVKKIIAGNGVFICNECVALSQEIIKEEL-------AEEVLADLAEVPKPKELLEILNQYVVGQDRAKRA 84
Cdd:TIGR00382   9 YCSFCGKSQDEVRKLIAGPGVYICDECIELCHDILEEELgtrkeskEYEEEFELSYLPTPKEIKAHLDEYVIGQEQAKKV 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446841159   85 LAVAVYNHYKRVSYT--ESSDDDVDLQKSNILMIGPTGSGKTFLAQTLAKSLNVPFAIADATSLTEAGYVGEDVENILLK 162
Cdd:TIGR00382  89 LSVAVYNHYKRLNFEknKKSDNGVELSKSNILLIGPTGSGKTLLAQTLARILNVPFAIADATTLTEAGYVGEDVENILLK 168
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446841159  163 LIQAADYNVERAERGIIYVDEIDKIAKKGENVSITRDVSGEGVQQALLKIIEGTVASVPPQGGRKHPNQEMIQINTKNIL 242
Cdd:TIGR00382 169 LLQAADYDVEKAQKGIIYIDEIDKISRKSENPSITRDVSGEGVQQALLKIIEGTVANVPPQGGRKHPYQEFIQIDTSNIL 248
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446841159  243 FIVGGAFDGIEDLVKQRLGEKVIGFGQTSR-KIDDNASYMQEIISEDIQKFGLIPEFIGRLPVVAALELLTAEDLVRILT 321
Cdd:TIGR00382 249 FICGGAFVGLEKIIKKRTGKSSIGFGAEVKkKSKEKADLLRQVEPEDLVKFGLIPEFIGRLPVIATLEKLDEEALIAILT 328
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446841159  322 EPRNALVKQYQTLLSYDGVELEFDQDALLAIADKAIERKTGARGLRSIIEETMLDIMFEIPSQEDVTKVRITKAAVEGTD 401
Cdd:TIGR00382 329 KPKNALVKQYQALFKMDNVELDFEEEALKAIAKKALERKTGARGLRSIVEGLLLDVMFDLPSLEDLEKVVITKETVLKQS 408

                  ....*
gi 446841159  402 KPVLE 406
Cdd:TIGR00382 409 EPLLI 413
RecA-like_ClpX cd19497
ATP-dependent Clp protease ATP-binding subunit ClpX; ClpX is a component of the ATP-dependent ...
62-308 1.17e-159

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: 449.36  E-value: 1.17e-159
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446841159  62 PKPKELLEILNQYVVGQDRAKRALAVAVYNHYKRVSYTES-SDDDVDLQKSNILMIGPTGSGKTFLAQTLAKSLNVPFAI 140
Cdd:cd19497    1 PTPKEIKEHLDKYVIGQERAKKVLSVAVYNHYKRIRNNLKqKDDDVELEKSNILLIGPTGSGKTLLAQTLAKILDVPFAI 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446841159 141 ADATSLTEAGYVGEDVENILLKLIQAADYNVERAERGIIYVDEIDKIAKKGENVSITRDVSGEGVQQALLKIIEGTVASV 220
Cdd:cd19497   81 ADATTLTEAGYVGEDVENILLKLLQAADYDVERAQRGIVYIDEIDKIARKSENPSITRDVSGEGVQQALLKILEGTVANV 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446841159 221 PPQGGRKHPNQEMIQINTKNILFIVGGAFDGIEDLVKQRLGEKVIGFGQTSRKIDDNAS---YMQEIISEDIQKFGLIPE 297
Cdd:cd19497  161 PPQGGRKHPQQEFIQVDTTNILFICGGAFVGLEKIIARRLGKKSLGFGAETSSEKDEKErdeLLSKVEPEDLIKFGLIPE 240
                        250
                 ....*....|.
gi 446841159 298 FIGRLPVVAAL 308
Cdd:cd19497  241 FVGRLPVIVTL 251
hslU PRK05201
ATP-dependent protease ATPase subunit HslU;
64-398 8.05e-62

ATP-dependent protease ATPase subunit HslU;


Pssm-ID: 235364 [Multi-domain]  Cd Length: 443  Bit Score: 205.70  E-value: 8.05e-62
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446841159  64 PKELLEILNQYVVGQDRAKRALAVAVYNHYKRVSYTESSDDDVdLQKsNILMIGPTGSGKTFLAQTLAKSLNVPFAIADA 143
Cdd:PRK05201   6 PREIVSELDKYIIGQDDAKRAVAIALRNRWRRMQLPEELRDEV-TPK-NILMIGPTGVGKTEIARRLAKLANAPFIKVEA 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446841159 144 TSLTEAGYVGEDVENI-----------------------------------LL--------------------------- 161
Cdd:PRK05201  84 TKFTEVGYVGRDVESIirdlveiavkmvreekrekvrekaeeaaeerildaLLppaknnwgeeeekeeisatrqkfrkkl 163
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446841159 162 --------------------------------------------------------------------KLI------QAA 167
Cdd:PRK05201 164 regelddkeieievaeaapmmeimgppgmeemtiqlqdmfgnlgpkkkkkrklkvkearkilieeeaaKLIdmeeikQEA 243
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446841159 168 dynVERAE-RGIIYVDEIDKIAKKGENVSitRDVSGEGVQQALLKIIEGTVASVppqggrKHPnqemiQINTKNILFIVG 246
Cdd:PRK05201 244 ---IERVEqNGIVFIDEIDKIAARGGSSG--PDVSREGVQRDLLPLVEGSTVST------KYG-----MVKTDHILFIAS 307
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446841159 247 GAFdgiedlvkqrlgekvigfgQTSRKIDdnasymqeiisediqkfgLIPEFIGRLPVVAALELLTAEDLVRILTEPRNA 326
Cdd:PRK05201 308 GAF-------------------HVSKPSD------------------LIPELQGRFPIRVELDALTEEDFVRILTEPKAS 350
                        410       420       430       440       450       460       470
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446841159 327 LVKQYQTLLSYDGVELEFDQDALLAIADKAIE--RKT---GARGLRSIIEETMLDIMFEIPSQEDvTKVRITKAAVE 398
Cdd:PRK05201 351 LIKQYQALLATEGVTLEFTDDAIRRIAEIAYQvnEKTeniGARRLHTVMEKLLEDISFEAPDMSG-ETVTIDAAYVD 426
HslU COG1220
ATP-dependent protease HslVU (ClpYQ), ATPase subunit HslU [Posttranslational modification, ...
64-398 1.48e-57

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


Pssm-ID: 440833 [Multi-domain]  Cd Length: 454  Bit Score: 194.88  E-value: 1.48e-57
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446841159  64 PKELLEILNQYVVGQDRAKRALAVAVYNHYKRVSYTESSDDDVdLQKsNILMIGPTGSGKTFLAQTLAKSLNVPFAIADA 143
Cdd:COG1220    6 PREIVAELDKYIIGQDEAKRAVAIALRNRWRRQQLPEELRDEI-TPK-NILMIGPTGVGKTEIARRLAKLANAPFIKVEA 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446841159 144 TSLTEAGYVGEDVE-----------------------------------NILL--------------------------- 161
Cdd:COG1220   84 TKFTEVGYVGRDVEsmirdlveiavkmvreekmekvrekaeeaaeerilDLLLpppkkkagsnnpfeeeeeeeeeeeeis 163
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446841159 162 -------------------------------------------------------------------------------K 162
Cdd:COG1220  164 rtrekfrkklregelddreieieveessspgveimgppgmeemgmnlqdmfgnlmpkkkkkrkvkvkearkiltqeeaaK 243
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446841159 163 LI------QAAdynVERAE-RGIIYVDEIDKIAKKGENVSItrDVSGEGVQQALLKIIEGTVASVppqggrKHPnqemiQ 235
Cdd:COG1220  244 LIdmdevkQEA---IERAEqNGIIFIDEIDKIASRGGGSGP--DVSREGVQRDLLPIVEGSTVNT------KYG-----M 307
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446841159 236 INTKNILFIVGGAFdgiedlvkqrlgekvigfgQTSRKIDdnasymqeiisediqkfgLIPEFIGRLPVVAALELLTAED 315
Cdd:COG1220  308 VKTDHILFIAAGAF-------------------HVSKPSD------------------LIPELQGRFPIRVELDSLTEED 350
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446841159 316 LVRILTEPRNALVKQYQTLLSYDGVELEFDQDALLAIADKAIE--RKT---GARGLRSIIEETMLDIMFEIPSQEDvTKV 390
Cdd:COG1220  351 FVRILTEPKNALTKQYQALLATEGVELEFTDDAIREIAEIAFEvnERTeniGARRLHTVMEKLLEDISFEAPDLSG-KTV 429

                 ....*...
gi 446841159 391 RITKAAVE 398
Cdd:COG1220  430 VIDAAYVD 437
hslU TIGR00390
ATP-dependent protease HslVU, ATPase subunit; This model represents the ATPase subunit of ...
64-398 3.67e-49

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


Pssm-ID: 273052 [Multi-domain]  Cd Length: 441  Bit Score: 172.31  E-value: 3.67e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446841159   64 PKELLEILNQYVVGQDRAKRALAVAVYNHYKRVSYTESSDDDVdlQKSNILMIGPTGSGKTFLAQTLAKSLNVPFAIADA 143
Cdd:TIGR00390   3 PREIVAELDKYIIGQDNAKKSVAIALRNRYRRSQLNEELKDEV--TPKNILMIGPTGVGKTEIARRLAKLANAPFIKVEA 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446841159  144 TSLTEAGYVGEDVENILLKLIQAA-------------------------------------------------------- 167
Cdd:TIGR00390  81 TKFTEVGYVGRDVESMVRDLTDAAvklvkeeaiekvrdraeelaeerivdvllppaknqwgqteqqqepesareafrkkl 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446841159  168 ------DYNVE--------------------------------------------------------------------- 172
Cdd:TIGR00390 161 regeldDKEIEidvsakmpsgieimappgmeemtmqlqslfqnlggqkkkkrklkikdakkaliaeeaaklvdpeeikqe 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446841159  173 ---RAER-GIIYVDEIDKIAKKGEnvSITRDVSGEGVQQALLKIIEGTVASVppqggrKHPnqemiQINTKNILFIVGGA 248
Cdd:TIGR00390 241 aidAVEQsGIIFIDEIDKIAKKGE--SSGADVSREGVQRDLLPIVEGSTVNT------KYG-----MVKTDHILFIAAGA 307
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446841159  249 FdgiedlvkqrlgekvigfgQTSRKIDdnasymqeiisediqkfgLIPEFIGRLPVVAALELLTAEDLVRILTEPRNALV 328
Cdd:TIGR00390 308 F-------------------QLAKPSD------------------LIPELQGRFPIRVELQALTTDDFERILTEPKNSLI 350
                         410       420       430       440       450       460       470
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446841159  329 KQYQTLLSYDGVELEFDQDALLAIADKA--IERKT---GARGLRSIIEETMLDIMFEIPsqeDVT--KVRITKAAVE 398
Cdd:TIGR00390 351 KQYKALMKTEGVNIEFSDEAIKRIAELAynVNEKTeniGARRLHTVLERLLEDISFEAP---DLSgqNITIDADYVS 424
RecA-like_HslU cd19498
ATP-dependent protease ATPase subunit HslU; HslU is a component of the ATP-dependent protease ...
63-249 3.09e-45

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: 154.46  E-value: 3.09e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446841159  63 KPKELLEILNQYVVGQDRAKRALAVAVYNHYKRVSYTESSDDDVdlQKSNILMIGPTGSGKTFLAQTLAKSLNVPFAIAD 142
Cdd:cd19498    1 TPREIVSELDKYIIGQDEAKRAVAIALRNRWRRMQLPEELRDEV--TPKNILMIGPTGVGKTEIARRLAKLAGAPFIKVE 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446841159 143 ATSLTEAGYVGEDVENILLKLIQaadynveraerGIIYVDEIDKIAKKGENVSitRDVSGEGVQQALLKIIEGTVASVpp 222
Cdd:cd19498   79 ATKFTEVGYVGRDVESIIRDLVE-----------GIVFIDEIDKIAKRGGSSG--PDVSREGVQRDLLPIVEGSTVST-- 143
                        170       180
                 ....*....|....*....|....*..
gi 446841159 223 QGGrkhpnqemiQINTKNILFIVGGAF 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 3.90e-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: 140.41  E-value: 3.90e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446841159  110 KSNILMIGPTGSGKTFLAQTLAKSLNV---PFAIADATSLTEagyvgedvENILLKLIQAADYNVERAERG--------- 177
Cdd:pfam07724   3 IGSFLFLGPTGVGKTELAKALAELLFGderALIRIDMSEYME--------EHSVSRLIGAPPGYVGYEEGGqlteavrrk 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446841159  178 ---IIYVDEIDKIAKkgenvsitrdvsgeGVQQALLKIIEGTVASvppqggrkhPNQEmIQINTKNILFIVGGAFDGIED 254
Cdd:pfam07724  75 pysIVLIDEIEKAHP--------------GVQNDLLQILEGGTLT---------DKQG-RTVDFKNTLFIMTGNFGSEKI 130
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 446841159  255 LVKQRLGekvigfgqtsrkiDDNASYMQEIISEDIQKFGLIPEFIGRLPVV 305
Cdd:pfam07724 131 SDASRLG-------------DSPDYELLKEEVMDLLKKGFIPEFLGRLPII 168
ClpB_D2-small smart01086
C-terminal, D2-small domain, of ClpB protein; This is the C-terminal domain of ClpB protein, ...
311-400 3.35e-23

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: 92.51  E-value: 3.35e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446841159   311 LTAEDLVRILTEPRNALVKQYQTllsyDGVELEFDQDALLAIADKAIERKTGARGLRSIIEETMLDIMFEIPSQ---EDV 387
Cdd:smart01086   1 LDKEDLVRIVDLPLNALQKRLAE----KGITLEFTDEALDWLAEKGYDPKYGARPLRRIIQRELEDPLAELILSgelKDG 76
                           90
                   ....*....|...
gi 446841159   388 TKVRITKAAVEGT 400
Cdd:smart01086  77 DTVVVDVDDGELV 89
zf-C4_ClpX smart00994
ClpX C4-type zinc finger; The ClpX heat shock protein of Escherichia coli is a member of the ...
12-49 9.75e-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: 81.46  E-value: 9.75e-20
                           10        20        30
                   ....*....|....*....|....*....|....*...
gi 446841159    12 YCSFCGKSQDEVKKIIAGNGVFICNECVALSQEIIKEE 49
Cdd:smart00994   2 RCSFCGKSESEVRKLIAGPGVYICDECVELCYEILEEE 39
RecA-like_protease cd19481
proteases similar to RecA; RecA-like NTPases. This family includes the NTP binding domain of ...
81-215 2.28e-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: 84.26  E-value: 2.28e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446841159  81 AKRALAVAVYNHYKRvsytESSDDDVDLQKSNILMIGPTGSGKTFLAQTLAKSLNVPFAIADATSLTEAgYVGEDVENiL 160
Cdd:cd19481    1 LKASLREAVEAPRRG----SRLRRYGLGLPKGILLYGPPGTGKTLLAKALAGELGLPLIVVKLSSLLSK-YVGESEKN-L 74
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 446841159 161 LKLIQAAdynvERAERGIIYVDEIDKIAKKGENVSITRDVSgeGVQQALLKIIEG 215
Cdd:cd19481   75 RKIFERA----RRLAPCILFIDEIDAIGRKRDSSGESGELR--RVLNQLLTELDG 123
zf-C4_ClpX pfam06689
ClpX C4-type zinc finger; The ClpX heat shock protein of Escherichia coli is a member of the ...
11-48 2.85e-19

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


Pssm-ID: 461988 [Multi-domain]  Cd Length: 39  Bit Score: 80.27  E-value: 2.85e-19
                          10        20        30
                  ....*....|....*....|....*....|....*....
gi 446841159   11 VYCSFCGKSQDEVKKIIAG-NGVFICNECVALSQEIIKE 48
Cdd:pfam06689   1 LRCSFCGKSEDEVKKLIAGpNGVYICDECVELCYEILEE 39
ClpB_D2-small pfam10431
C-terminal, D2-small domain, of ClpB protein; This is the C-terminal domain of ClpB protein, ...
311-389 1.27e-14

C-terminal, D2-small domain, of ClpB protein; This is the C-terminal domain of ClpB protein, referred to as the D2-small domain, and is a mixed alpha-beta structure. Compared with the D1-small domain (included in AAA, pfam00004) it lacks the long coiled-coil insertion, and instead of helix C4 contains a beta-strand (e3) that is part of a three stranded beta-pleated sheet. In Thermophilus the whole protein forms a hexamer with the D1-small and D2-small domains located on the outside of the hexamer, with the long coiled-coil being exposed on the surface. The D2-small domain is essential for oligomerization, forming a tight interface with the D2-large domain of a neighbouring subunit and thereby providing enough binding energy to stabilize the functional assembly. The domain is associated with two Clp_N, pfam02861, at the N-terminus as well as AAA, pfam00004 and AAA_2, pfam07724.


Pssm-ID: 463090 [Multi-domain]  Cd Length: 81  Bit Score: 68.59  E-value: 1.27e-14
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446841159  311 LTAEDLVRILTEprnALVKQYQTLLSyDGVELEFDQDALLAIADKAIERKTGARGLRSIIEETMLDIMFEIPSQEDVTK 389
Cdd:pfam10431   1 LSKEELRKIVDL---QLKELQKRLAE-RGITLELTDAAKDWLAEKGYDPEYGARPLRRAIQREIEDPLAEEILSGELKE 75
AAA cd00009
The AAA+ (ATPases Associated with a wide variety of cellular Activities) superfamily ...
76-214 3.14e-14

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


Pssm-ID: 99707 [Multi-domain]  Cd Length: 151  Bit Score: 69.87  E-value: 3.14e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446841159  76 VGQDRAKRALAVAVYNHykrvsytessdddvdlQKSNILMIGPTGSGKTFLAQTLAKSL---NVPFAIADATSLTEAGYV 152
Cdd:cd00009    1 VGQEEAIEALREALELP----------------PPKNLLLYGPPGTGKTTLARAIANELfrpGAPFLYLNASDLLEGLVV 64
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446841159 153 GEDVENILLKLIQAAdynVERAERGIIYVDEIDKIakkgenvsitrdvsGEGVQQALLKIIE 214
Cdd:cd00009   65 AELFGHFLVRLLFEL---AEKAKPGVLFIDEIDSL--------------SRGAQNALLRVLE 109
AAA pfam00004
ATPase family associated with various cellular activities (AAA); AAA family proteins often ...
113-215 2.97e-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: 66.08  E-value: 2.97e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446841159  113 ILMIGPTGSGKTFLAQTLAKSLNVPFAIADATSLTEaGYVGEDVENIlLKLIQAAdynvERAERGIIYVDEIDKIAKKGE 192
Cdd:pfam00004   1 LLLYGPPGTGKTTLAKAVAKELGAPFIEISGSELVS-KYVGESEKRL-RELFEAA----KKLAPCVIFIDEIDALAGSRG 74
                          90       100
                  ....*....|....*....|...
gi 446841159  193 NvsiTRDVSGEGVQQALLKIIEG 215
Cdd:pfam00004  75 S---GGDSESRRVVNQLLTELDG 94
SpoVK COG0464
AAA+-type ATPase, SpoVK/Ycf46/Vps4 family [Cell wall/membrane/envelope biogenesis, Cell cycle ...
75-215 1.77e-11

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: 65.32  E-value: 1.77e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446841159  75 VVGQDRAKRALAVAVynhyKRVSYTESSDDDVDLQKSN-ILMIGPTGSGKTFLAQTLAKSLNVPFAIADATSLTeAGYVG 153
Cdd:COG0464  159 LGGLEEVKEELRELV----ALPLKRPELREEYGLPPPRgLLLYGPPGTGKTLLARALAGELGLPLIEVDLSDLV-SKYVG 233
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446841159 154 EDVENIlLKLIQAAdynvERAERGIIYVDEIDKIAKKGENVsitRDVSGEGVQQALLKIIEG 215
Cdd:COG0464  234 ETEKNL-REVFDKA----RGLAPCVLFIDEADALAGKRGEV---GDGVGRRVVNTLLTEMEE 287
RecA-like_CDC48_NLV2_r1-like cd19503
first of two ATPase domains of CDC48 and NLV2, and similar ATPase domains; CDC48 in yeast and ...
113-195 8.84e-09

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


Pssm-ID: 410911 [Multi-domain]  Cd Length: 165  Bit Score: 54.22  E-value: 8.84e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446841159 113 ILMIGPTGSGKTFLAQTLAKSLNVPFAIADATSLTeAGYVGEDVENiLLKLIQAAdynvERAERGIIYVDEIDKIAKKGE 192
Cdd:cd19503   37 VLLHGPPGTGKTLLARAVANEAGANFLSISGPSIV-SKYLGESEKN-LREIFEEA----RSHAPSIIFIDEIDALAPKRE 110

                 ...
gi 446841159 193 NVS 195
Cdd:cd19503  111 EDQ 113
RecA-like_NVL_r1-like cd19518
first of two ATPase domains of NVL (nuclear VCP-like protein) and similar ATPase domains; NVL ...
113-209 1.18e-08

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


Pssm-ID: 410926 [Multi-domain]  Cd Length: 169  Bit Score: 53.95  E-value: 1.18e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446841159 113 ILMIGPTGSGKTFLAQTLAKSLNVPFAIADATSLTeAGYVGEDVENILLKLIQAADYnveraERGIIYVDEIDKIAKKGE 192
Cdd:cd19518   37 VLLHGPPGCGKTMLANAIAGELKVPFLKISATEIV-SGVSGESEEKIRELFDQAISN-----APCIVFIDEIDAITPKRE 110
                         90
                 ....*....|....*..
gi 446841159 193 NVSitRDVSGEGVQQAL 209
Cdd:cd19518  111 SAQ--REMERRIVSQLL 125
clpA PRK11034
ATP-dependent Clp protease ATP-binding subunit; Provisional
52-374 2.76e-07

ATP-dependent Clp protease ATP-binding subunit; Provisional


Pssm-ID: 236828 [Multi-domain]  Cd Length: 758  Bit Score: 52.92  E-value: 2.76e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446841159  52 EEVLADLAEVPKP----------KELLEILNQYVVGQDRAKRALAVAVynhykRVSYTESSDDDVDLqkSNILMIGPTGS 121
Cdd:PRK11034 427 ESVVARIARIPEKsvsqsdrdtlKNLGDRLKMLVFGQDKAIEALTEAI-----KMSRAGLGHEHKPV--GSFLFAGPTGV 499
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446841159 122 GKTFLAQTLAKSLNVPFAIADATSLTE-----------AGYVGEDVENILLKliqaadyNVERAERGIIYVDEIDKiakk 190
Cdd:PRK11034 500 GKTEVTVQLSKALGIELLRFDMSEYMErhtvsrligapPGYVGFDQGGLLTD-------AVIKHPHAVLLLDEIEK---- 568
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446841159 191 genvsitrdvSGEGVQQALLKIIE-GTVASvppQGGRKHPNQEMIQINTKNIlfivggafdGIEDLVKqrlgeKVIGFGQ 269
Cdd:PRK11034 569 ----------AHPDVFNLLLQVMDnGTLTD---NNGRKADFRNVVLVMTTNA---------GVRETER-----KSIGLIH 621
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446841159 270 TsrkiDDNASYMQEIisediqKFGLIPEFIGRLPVVAALELLTAEdlvrILTEPRNALVKQYQTLLSYDGVELEFDQDAL 349
Cdd:PRK11034 622 Q----DNSTDAMEEI------KKIFTPEFRNRLDNIIWFDHLSTD----VIHQVVDKFIVELQAQLDQKGVSLEVSQEAR 687
                        330       340
                 ....*....|....*....|....*
gi 446841159 350 LAIADKAIERKTGARGLRSIIEETM 374
Cdd:PRK11034 688 DWLAEKGYDRAMGARPMARVIQDNL 712
CDC48 TIGR01243
AAA family ATPase, CDC48 subfamily; This subfamily of the AAA family ATPases includes two ...
113-215 5.22e-07

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: 51.83  E-value: 5.22e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446841159  113 ILMIGPTGSGKTFLAQTLAKSLNVPFAIADATSLTeAGYVGEDVENiLLKLIQAADYNVEraerGIIYVDEIDKIAKKGE 192
Cdd:TIGR01243 215 VLLYGPPGTGKTLLAKAVANEAGAYFISINGPEIM-SKYYGESEER-LREIFKEAEENAP----SIIFIDEIDAIAPKRE 288
                          90       100
                  ....*....|....*....|...
gi 446841159  193 NVsiTRDVSGEGVQQaLLKIIEG 215
Cdd:TIGR01243 289 EV--TGEVEKRVVAQ-LLTLMDG 308
YifB COG0606
Predicted Mg-chelatase, contains ChlI-like and ATPase domains, YifB family [Posttranslational ...
75-130 5.54e-07

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


Pssm-ID: 440371 [Multi-domain]  Cd Length: 502  Bit Score: 51.58  E-value: 5.54e-07
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 446841159  75 VVGQDRAKRALAVAVY-NHykrvsytessdddvdlqksNILMIGPTGSGKTFLAQTL 130
Cdd:COG0606  194 VKGQEQAKRALEIAAAgGH-------------------NLLMIGPPGSGKTMLARRL 231
Mg_chelatase pfam01078
Magnesium chelatase, subunit ChlI; Magnesium-chelatase is a three-component enzyme that ...
75-130 7.65e-07

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


Pssm-ID: 426032 [Multi-domain]  Cd Length: 207  Bit Score: 49.46  E-value: 7.65e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 446841159   75 VVGQDRAKRALAVAVY-NHykrvsytessdddvdlqksNILMIGPTGSGKTFLAQTL 130
Cdd:pfam01078   5 VKGQEQAKRALEIAAAgGH-------------------NLLMIGPPGSGKTMLAKRL 42
RecA-like_VPS4-like cd19509
ATPase domain of VPS4, ATAD1, K, KTNA1, Spastin, FIGL-1 and similar ATPase domains; This ...
75-185 1.40e-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: 47.73  E-value: 1.40e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446841159  75 VVGQDRAKRALAVAVYNHYKRvsyTESSDDDVDLQKSnILMIGPTGSGKTFLAQTLAKSLNVPFAIADATSLTeAGYVGE 154
Cdd:cd19509    1 IAGLDDAKEALKEAVILPSLR---PDLFPGLRGPPRG-ILLYGPPGTGKTLLARAVASESGSTFFSISASSLV-SKWVGE 75
                         90       100       110
                 ....*....|....*....|....*....|..
gi 446841159 155 DVENIllkliqAADYNVERAER-GIIYVDEID 185
Cdd:cd19509   76 SEKIV------RALFALARELQpSIIFIDEID 101
clpC CHL00095
Clp protease ATP binding subunit
69-371 2.75e-06

Clp protease ATP binding subunit


Pssm-ID: 214361 [Multi-domain]  Cd Length: 821  Bit Score: 49.67  E-value: 2.75e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446841159  69 EILNQYVVGQDRAKRALAVAVynhyKRVSytessdddVDLQKSN-----ILMIGPTGSGKTFLAQTLAKSLnvpFAIADA 143
Cdd:CHL00095 505 ETLHKRIIGQDEAVVAVSKAI----RRAR--------VGLKNPNrpiasFLFSGPTGVGKTELTKALASYF---FGSEDA 569
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446841159 144 T---SLTE--------------AGYVGEDVENILLKLIQAADYNVeraergiIYVDEIDKIAKKGENVsitrdvsgegvq 206
Cdd:CHL00095 570 MirlDMSEymekhtvskligspPGYVGYNEGGQLTEAVRKKPYTV-------VLFDEIEKAHPDIFNL------------ 630
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446841159 207 qaLLKIIE-GTVASvppQGGRkhpnqemiQINTKNILFIvggafdgiedlVKQRLGEKVI-------GFGQTSRKIDD-N 277
Cdd:CHL00095 631 --LLQILDdGRLTD---SKGR--------TIDFKNTLII-----------MTSNLGSKVIetnsgglGFELSENQLSEkQ 686
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446841159 278 ASYMQEIISEDIQKFgLIPEFIGRLPVVAALELLTAEDLVRILteprNALVKQYQTLLSYDGVELEFDQDALLAIADKAI 357
Cdd:CHL00095 687 YKRLSNLVNEELKQF-FRPEFLNRLDEIIVFRQLTKNDVWEIA----EIMLKNLFKRLNEQGIQLEVTERIKTLLIEEGY 761
                        330
                 ....*....|....
gi 446841159 358 ERKTGARGLRSIIE 371
Cdd:CHL00095 762 NPLYGARPLRRAIM 775
hflB PRK10733
ATP-dependent zinc metalloprotease FtsH;
113-212 5.68e-06

ATP-dependent zinc metalloprotease FtsH;


Pssm-ID: 182683 [Multi-domain]  Cd Length: 644  Bit Score: 48.49  E-value: 5.68e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446841159 113 ILMIGPTGSGKTFLAQTLAKSLNVPFAIADATSLTEAgYVGEDVENILLKLIQAadynvERAERGIIYVDEIDKIAK-KG 191
Cdd:PRK10733 188 VLMVGPPGTGKTLLAKAIAGEAKVPFFTISGSDFVEM-FVGVGASRVRDMFEQA-----KKAAPCIIFIDEIDAVGRqRG 261
                         90       100
                 ....*....|....*....|.
gi 446841159 192 ENVSITRDVSGEGVQQALLKI 212
Cdd:PRK10733 262 AGLGGGHDEREQTLNQMLVEM 282
RecA-like_spastin cd19524
ATPase domain of spastin; Spastin is an ATP-dependent microtubule-severing protein involved in ...
75-187 7.60e-06

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


Pssm-ID: 410932 [Multi-domain]  Cd Length: 164  Bit Score: 46.00  E-value: 7.60e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446841159  75 VVGQDRAKRALAVAVYNHYKRVSYTESsdddVDLQKSNILMIGPTGSGKTFLAQTLAKSLNVPFAIADATSLTeAGYVGE 154
Cdd:cd19524    2 IAGQDLAKQALQEMVILPSLRPELFTG----LRAPARGLLLFGPPGNGKTMLAKAVAAESNATFFNISAASLT-SKYVGE 76
                         90       100       110
                 ....*....|....*....|....*....|...
gi 446841159 155 DvENILLKLIQAAdynvERAERGIIYVDEIDKI 187
Cdd:cd19524   77 G-EKLVRALFAVA----RELQPSIIFIDEVDSL 104
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 8.59e-06

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


Pssm-ID: 410927 [Multi-domain]  Cd Length: 166  Bit Score: 45.50  E-value: 8.59e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446841159 113 ILMIGPTGSGKTFLAQTLAKSLNVPFAIADATSLTeAGYVGEDVENiLLKLIQAADYNVEraerGIIYVDEIDKIAKKGE 192
Cdd:cd19519   37 ILLYGPPGTGKTLIARAVANETGAFFFLINGPEIM-SKLAGESESN-LRKAFEEAEKNAP----AIIFIDEIDAIAPKRE 110
                         90       100
                 ....*....|....*....|...
gi 446841159 193 NVsiTRDVSGEGVQQaLLKIIEG 215
Cdd:cd19519  111 KT--HGEVERRIVSQ-LLTLMDG 130
RecA-like_ClpB_Hsp104-like cd19499
Chaperone protein ClpB/Hsp104 subfamily; Bacterial Caseinolytic peptidase B (ClpB) and ...
63-186 1.18e-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: 45.63  E-value: 1.18e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446841159  63 KPKELLEILNQYVVGQDRAKRALAVAVYNHykrvsytessddDVDLQKSN-----ILMIGPTGSGKTFLAQTLAKSL--- 134
Cdd:cd19499    1 KLLNLEERLHERVVGQDEAVKAVSDAIRRA------------RAGLSDPNrpigsFLFLGPTGVGKTELAKALAELLfgd 68
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446841159 135 NVPFAIADATSLTEA-----------GYVGEDVENILLKliqaadyNVERAERGIIYVDEIDK 186
Cdd:cd19499   69 EDNLIRIDMSEYMEKhsvsrligappGYVGYTEGGQLTE-------AVRRKPYSVVLLDEIEK 124
AAA smart00382
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ...
109-196 2.01e-05

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


Pssm-ID: 214640 [Multi-domain]  Cd Length: 148  Bit Score: 44.29  E-value: 2.01e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446841159   109 QKSNILMIGPTGSGKTFLAQTLAKSLNVP---FAIADATSLTEAGYVGEDVENILL--------KLIQAADYNVERAERG 177
Cdd:smart00382   1 PGEVILIVGPPGSGKTTLARALARELGPPgggVIYIDGEDILEEVLDQLLLIIVGGkkasgsgeLRLRLALALARKLKPD 80
                           90
                   ....*....|....*....
gi 446841159   178 IIYVDEIDKIAKKGENVSI 196
Cdd:smart00382  81 VLILDEITSLLDAEQEALL 99
RecA-like_NSF-SEC18_r1-like cd19504
first of two ATPase domains of NSF and SEC18, and similar ATPase domains; ...
113-212 2.41e-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: 44.40  E-value: 2.41e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446841159 113 ILMIGPTGSGKTFLAQTLAKSLNV--PFAIADATSLTEagYVGEDVENILLKLIQA-ADYNVERAERG--IIYVDEIDKI 187
Cdd:cd19504   38 ILLYGPPGTGKTLMARQIGKMLNArePKIVNGPEILNK--YVGESEANIRKLFADAeEEQRRLGANSGlhIIIFDEIDAI 115
                         90       100
                 ....*....|....*....|....*
gi 446841159 188 AKKGENVSITRDVSGEGVQQALLKI 212
Cdd:cd19504  116 CKQRGSMAGSTGVHDTVVNQLLSKI 140
AAA_5 pfam07728
AAA domain (dynein-related subfamily); This Pfam entry includes some of the AAA proteins not ...
112-189 2.59e-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: 43.82  E-value: 2.59e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446841159  112 NILMIGPTGSGKTFLAQTLAKSLN--VPFAIADATSLTEAGYVGE-DVENILLKLIQAAdyNVERAERG-IIYVDEIDKI 187
Cdd:pfam07728   1 GVLLVGPPGTGKTELAERLAAALSnrPVFYVQLTRDTTEEDLFGRrNIDPGGASWVDGP--LVRAAREGeIAVLDEINRA 78

                  ..
gi 446841159  188 AK 189
Cdd:pfam07728  79 NP 80
PRK13342 PRK13342
recombination factor protein RarA; Reviewed
115-217 3.73e-05

recombination factor protein RarA; Reviewed


Pssm-ID: 237355 [Multi-domain]  Cd Length: 413  Bit Score: 45.46  E-value: 3.73e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446841159 115 MI--GPTGSGKTFLAQTLAKSLNVPFAIADATSlteAGyVGEdveniLLKLIQAADYNVERAERGIIYVDEIDKIAKKge 192
Cdd:PRK13342  39 MIlwGPPGTGKTTLARIIAGATDAPFEALSAVT---SG-VKD-----LREVIEEARQRRSAGRRTILFIDEIHRFNKA-- 107
                         90       100
                 ....*....|....*....|....*..
gi 446841159 193 nvsitrdvsgegvQQ-ALLKIIE-GTV 217
Cdd:PRK13342 108 -------------QQdALLPHVEdGTI 121
RecA-like_KTNA1 cd19522
Katanin p60 ATPase-containing subunit A1; Katanin p60 ATPase-containing subunit A1 (KTNA1) is ...
113-190 4.60e-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: 43.82  E-value: 4.60e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446841159 113 ILMIGPTGSGKTFLAQTLAKSLNVPFAIADATSLTeAGYVGEDvENILLKLIQAADYNVERAergiIYVDEIDKIAKK 190
Cdd:cd19522   36 VLMVGPPGTGKTLLAKAVATECGTTFFNVSSSTLT-SKYRGES-EKLVRLLFEMARFYAPTT----IFIDEIDSICSR 107
ClpA COG0542
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ...
296-376 4.94e-05

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


Pssm-ID: 440308 [Multi-domain]  Cd Length: 836  Bit Score: 45.46  E-value: 4.94e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446841159 296 PEFIGRLPVVAALELLTAEDLVRILteprNALVKQYQTLLSYDGVELEFDQDALLAIADKAIERKTGARGLRSIIEETML 375
Cdd:COG0542  733 PEFLNRIDEIIVFHPLSKEELRKIV----DLQLKRLRKRLAERGITLELTDAAKDFLAEKGYDPEYGARPLKRAIQRELE 808

                 .
gi 446841159 376 D 376
Cdd:COG0542  809 D 809
RecA-like_FtsH cd19501
ATP-dependent zinc metalloprotease FtsH; FtsH ATPase is a processive, ATP-dependent zinc ...
113-190 5.20e-05

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


Pssm-ID: 410909 [Multi-domain]  Cd Length: 171  Bit Score: 43.38  E-value: 5.20e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446841159 113 ILMIGPTGSGKTFLAQTLAKSLNVPFAIADATSLTEAgYVGEDVENIlLKLIQAAdynvERAERGIIYVDEIDKIAKK 190
Cdd:cd19501   40 VLLVGPPGTGKTLLAKAVAGEAGVPFFSISGSDFVEM-FVGVGASRV-RDLFEQA----KKNAPCIVFIDEIDAVGRK 111
RecA-like_PEX1_r2 cd19526
second of two ATPase domains of Peroxisomal biogenesis factor 1 (PEX1); PEX1(also known as ...
109-190 7.63e-05

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


Pssm-ID: 410934 [Multi-domain]  Cd Length: 158  Bit Score: 42.80  E-value: 7.63e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446841159 109 QKSNILMIGPTGSGKTFLAQTLAKSLNVPFAIADATSLTeAGYVGEDVENILLKLIQAAdynveRAERGIIYVDEIDKIA 188
Cdd:cd19526   26 LRSGILLYGPPGCGKTLLASAIASECGLNFISVKGPELL-NKYIGASEQNVRDLFSRAQ-----SAKPCILFFDEFDSIA 99

                 ..
gi 446841159 189 KK 190
Cdd:cd19526  100 PK 101
RecA-like_PEX6_r2 cd19527
second of two ATPase domains of Peroxisomal biogenesis factor 6 (PEX6); PEX6(also known as ...
109-212 1.04e-04

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


Pssm-ID: 410935 [Multi-domain]  Cd Length: 160  Bit Score: 42.50  E-value: 1.04e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446841159 109 QKSNILMIGPTGSGKTFLAQTLAKSLNVPFAIADATSLTEAgYVGEDVENILLKLIQAADynverAERGIIYVDEIDKIA 188
Cdd:cd19527   25 KRSGILLYGPPGTGKTLLAKAIATECSLNFLSVKGPELINM-YIGESEANVREVFQKARD-----AKPCVIFFDELDSLA 98
                         90       100
                 ....*....|....*....|....
gi 446841159 189 KKGENVSITRDVSGEGVQQALLKI 212
Cdd:cd19527   99 PSRGNSGDSGGVMDRVVSQLLAEL 122
RecA-like_CDC48_r2-like cd19511
second of two ATPase domains of CDC48/p97, PEX1 and -6, VAT and NVL, and similar ATPase ...
113-190 1.05e-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: 1.05e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446841159 113 ILMIGPTGSGKTFLAQTLAKSLNVPF-AIADATSLTEagYVGED---VENILLKLIQAADynveraerGIIYVDEIDKIA 188
Cdd:cd19511   30 VLLYGPPGCGKTLLAKALASEAGLNFiSVKGPELFSK--YVGESeraVREIFQKARQAAP--------CIIFFDEIDSLA 99

                 ..
gi 446841159 189 KK 190
Cdd:cd19511  100 PR 101
RecA-like_Figl-1 cd19525
ATPase domain of Fidgetin-Like 1 (FIGL-1); FIGL-1 may participate in DNA repair in the nucleus; ...
113-192 1.30e-04

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


Pssm-ID: 410933 [Multi-domain]  Cd Length: 186  Bit Score: 42.67  E-value: 1.30e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446841159 113 ILMIGPTGSGKTFLAQTLAKSLNVPFAIADATSLTeAGYVGEDVenillKLIQAAdYNVERAER-GIIYVDEIDK-IAKK 190
Cdd:cd19525   58 ILLFGPPGTGKTLIGKCIASQSGATFFSISASSLT-SKWVGEGE-----KMVRAL-FSVARCKQpAVIFIDEIDSlLSQR 130

                 ..
gi 446841159 191 GE 192
Cdd:cd19525  131 GE 132
RecA-like_ATAD1 cd19520
ATPase domain of ATPase family AAA domain-containing protein 1 and similar ATPase domains; ...
113-185 1.82e-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: 1.82e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446841159 113 ILMIGPTGSGKTFLAQTLAKSLNVPFAIADATSLTEAGYvGEDVenillKLIQAADYNVERAERGIIYVDEID 185
Cdd:cd19520   38 VLLYGPPGCGKTMLAKATAKEAGARFINLQVSSLTDKWY-GESQ-----KLVAAVFSLASKLQPSIIFIDEID 104
RecA-like_CDC48_r2-like cd19528
second of two ATPase domains of CDC48 and similar ATPase domains; CDC48 in yeast and p97 or ...
113-246 2.86e-04

second of two ATPase domains of CDC48 and similar ATPase domains; CDC48 in yeast and p97 or VCP in 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 second 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_r2-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: 410936 [Multi-domain]  Cd Length: 161  Bit Score: 41.34  E-value: 2.86e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446841159 113 ILMIGPTGSGKTFLAQTLAKSLNVPFAIADATSLTEAgYVGE---DVENILLKLIQAADYnveraergIIYVDEIDKIAK 189
Cdd:cd19528   30 VLFYGPPGCGKTLLAKAIANECQANFISVKGPELLTM-WFGEseaNVRDIFDKARAAAPC--------VLFFDELDSIAK 100
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 446841159 190 -KGENVSITRDVSGEGVQQALlkiiegtvasvppqggrkhpnQEMIQINTKNILFIVG 246
Cdd:cd19528  101 aRGGNIGDAGGAADRVINQIL---------------------TEMDGMNTKKNVFIIG 137
DnaX COG2812
DNA polymerase III, gamma/tau subunits [Replication, recombination and repair];
75-135 4.81e-04

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


Pssm-ID: 442061 [Multi-domain]  Cd Length: 340  Bit Score: 41.72  E-value: 4.81e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446841159  75 VVGQDRAKRALAVAVYNHykRVS--YtessdddvdlqksniLMIGPTGSGKTFLAQTLAKSLN 135
Cdd:COG2812   12 VVGQEHVVRTLKNALASG--RLAhaY---------------LFTGPRGVGKTTLARILAKALN 57
PRK09862 PRK09862
ATP-dependent protease;
18-130 5.56e-04

ATP-dependent protease;


Pssm-ID: 182120 [Multi-domain]  Cd Length: 506  Bit Score: 41.89  E-value: 5.56e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446841159  18 KSQDEVKkIIAGNGVFICNE----CVALSQeiiKEELAEEVLADLAEVPKPKELLEIlnqyvVGQDRAKRALAV-AVYNH 92
Cdd:PRK09862 141 DNEDEVG-LINGEGCLIADHlqavCAFLEG---KHALERPKPTDAVSRALQHDLSDV-----IGQEQGKRGLEItAAGGH 211
                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 446841159  93 ykrvsytessdddvdlqksNILMIGPTGSGKTFLAQTL 130
Cdd:PRK09862 212 -------------------NLLLIGPPGTGKTMLASRI 230
RecA-like_VPS4 cd19521
ATPase domain of vacuolar protein sorting-associated protein 4; Vacuolar protein ...
111-195 6.86e-04

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


Pssm-ID: 410929 [Multi-domain]  Cd Length: 170  Bit Score: 40.23  E-value: 6.86e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446841159 111 SNILMIGPTGSGKTFLAQTLAKSLNVPFAIADATSLTeAGYVGEDvENILLKLIQAADYNveraERGIIYVDEIDKI-AK 189
Cdd:cd19521   41 SGILLYGPPGTGKSYLAKAVATEANSTFFSVSSSDLV-SKWMGES-EKLVKQLFAMAREN----KPSIIFIDEVDSLcGT 114

                 ....*.
gi 446841159 190 KGENVS 195
Cdd:cd19521  115 RGEGES 120
RecA-like_VCP_r2 cd19529
second of two ATPase domains of Valosin-containing protein-like ATPase (VAT) and similar ...
113-190 8.27e-04

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


Pssm-ID: 410937 [Multi-domain]  Cd Length: 159  Bit Score: 39.79  E-value: 8.27e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446841159 113 ILMIGPTGSGKTFLAQTLAKSLNVPFAIADATSLTeAGYVGED---VENILLKLIQAADynveraerGIIYVDEIDKIAK 189
Cdd:cd19529   30 ILLYGPPGTGKTLLAKAVATESNANFISVKGPELL-SKWVGESekaIREIFRKARQVAP--------CVIFFDEIDSIAP 100

                 .
gi 446841159 190 K 190
Cdd:cd19529  101 R 101
AAA_22 pfam13401
AAA domain;
106-209 9.11e-04

AAA domain;


Pssm-ID: 379165 [Multi-domain]  Cd Length: 129  Bit Score: 39.25  E-value: 9.11e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446841159  106 VDLQKSNILMIGPTGSGKTFLAQTLAKSL---NVPFAIADATSLTEAGYVGEDVENI-------------LLKLIQaaDY 169
Cdd:pfam13401   1 IRFGAGILVLTGESGTGKTTLLRRLLEQLpevRDSVVFVDLPSGTSPKDLLRALLRAlglplsgrlskeeLLAALQ--QL 78
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 446841159  170 NVERAERGIIYVDEIDKIAKKG-ENVSITRDVSGEGVQQAL 209
Cdd:pfam13401  79 LLALAVAVVLIIDEAQHLSLEAlEELRDLLNLSSKLLQLIL 119
RecA-like_PAN_like cd19502
proteasome activating nucleotidase PAN and related proteasome subunits; This subfamily ...
113-213 9.29e-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: 39.63  E-value: 9.29e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446841159 113 ILMIGPTGSGKTFLAQTLAKSLNVPFAIADATSLTEAgYVGEDVEnILLKLIQAAdynvERAERGIIYVDEIDKIAKKGE 192
Cdd:cd19502   40 VLLYGPPGTGKTLLAKAVANHTDATFIRVVGSELVQK-YIGEGAR-LVRELFEMA----REKAPSIIFIDEIDAIGAKRF 113
                         90       100
                 ....*....|....*....|.
gi 446841159 193 NVSITRDvsgEGVQQALLKII 213
Cdd:cd19502  114 DSGTGGD---REVQRTMLELL 131
aroK PRK00131
shikimate kinase; Reviewed
108-138 9.97e-04

shikimate kinase; Reviewed


Pssm-ID: 234654 [Multi-domain]  Cd Length: 175  Bit Score: 39.79  E-value: 9.97e-04
                         10        20        30
                 ....*....|....*....|....*....|.
gi 446841159 108 LQKSNILMIGPTGSGKTFLAQTLAKSLNVPF 138
Cdd:PRK00131   2 LKGPNIVLIGFMGAGKSTIGRLLAKRLGYDF 32
GntK cd02021
Gluconate kinase (GntK) catalyzes the phosphoryl transfer from ATP to gluconate. The resulting ...
113-143 1.52e-03

Gluconate kinase (GntK) catalyzes the phosphoryl transfer from ATP to gluconate. The resulting product gluconate-6-phoshate is an important precursor of gluconate metabolism. GntK acts as a dimmer composed of two identical subunits.


Pssm-ID: 238979 [Multi-domain]  Cd Length: 150  Bit Score: 38.77  E-value: 1.52e-03
                         10        20        30
                 ....*....|....*....|....*....|.
gi 446841159 113 ILMIGPTGSGKTFLAQTLAKSLNVPFAIADA 143
Cdd:cd02021    2 IVVMGVSGSGKSTVGKALAERLGAPFIDGDD 32
ruvB PRK00080
Holliday junction branch migration DNA helicase RuvB;
71-189 1.60e-03

Holliday junction branch migration DNA helicase RuvB;


Pssm-ID: 234619 [Multi-domain]  Cd Length: 328  Bit Score: 40.11  E-value: 1.60e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446841159  71 LNQYVvGQDRAKRALAVAVYNHYKRvsyTESSDddvdlqksNILMIGPTGSGKTFLAQTLAKSLNVPFAIADATSLTEAG 150
Cdd:PRK00080  24 LDEFI-GQEKVKENLKIFIEAAKKR---GEALD--------HVLLYGPPGLGKTTLANIIANEMGVNIRITSGPALEKPG 91
                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 446841159 151 yvgeDVENILlkliqaadYNVEraERGIIYVDEIDKIAK 189
Cdd:PRK00080  92 ----DLAAIL--------TNLE--EGDVLFIDEIHRLSP 116
MoxR COG0714
MoxR-like ATPase [General function prediction only]; MoxR-like ATPase is part of the Pathway ...
66-186 1.75e-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: 40.15  E-value: 1.75e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446841159  66 ELLEILNQYVVGQDRAKRALAVAVynhykrvsytessdddvdLQKSNILMIGPTGSGKTFLAQTLAKSLNVPFAIADATS 145
Cdd:COG0714    5 RLRAEIGKVYVGQEELIELVLIAL------------------LAGGHLLLEGVPGVGKTTLAKALARALGLPFIRIQFTP 66
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 446841159 146 -LTEAGYVGEDVenillkliqaadYNVERAE---------RGIIYVDEIDK 186
Cdd:COG0714   67 dLLPSDILGTYI------------YDQQTGEfefrpgplfANVLLADEINR 105
DnaC COG1484
DNA replication protein DnaC [Replication, recombination and repair];
109-131 2.94e-03

DNA replication protein DnaC [Replication, recombination and repair];


Pssm-ID: 441093 [Multi-domain]  Cd Length: 242  Bit Score: 38.99  E-value: 2.94e-03
                         10        20
                 ....*....|....*....|...
gi 446841159 109 QKSNILMIGPTGSGKTFLAQTLA 131
Cdd:COG1484   98 RGENLILLGPPGTGKTHLAIALG 120
SK cd00464
Shikimate kinase (SK) is the fifth enzyme in the shikimate pathway, a seven-step biosynthetic ...
112-138 2.96e-03

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


Pssm-ID: 238260 [Multi-domain]  Cd Length: 154  Bit Score: 37.92  E-value: 2.96e-03
                         10        20
                 ....*....|....*....|....*..
gi 446841159 112 NILMIGPTGSGKTFLAQTLAKSLNVPF 138
Cdd:cd00464    1 NIVLIGMMGAGKTTVGRLLAKALGLPF 27
RecA-like_Ycf46-like cd19507
ATPase domain of Ycf46 and similar ATPase domains; Ycf46 may play a role in the regulation of ...
113-186 3.64e-03

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


Pssm-ID: 410915 [Multi-domain]  Cd Length: 161  Bit Score: 37.73  E-value: 3.64e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446841159 113 ILMIGPTGSGKTFLAQTLAKSLNVPFAIADATSLTeAGYVGEDVENiLLKLIQAAdynvERAERGIIYVDEIDK 186
Cdd:cd19507   34 LLLVGIQGTGKSLTAKAIAGVWQLPLLRLDMGRLF-GGLVGESESR-LRQMIQTA----EAIAPCVLWIDEIEK 101
AroK COG0703
Shikimate kinase [Amino acid transport and metabolism]; Shikimate kinase is part of the ...
113-138 5.52e-03

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


Pssm-ID: 440467 [Multi-domain]  Cd Length: 165  Bit Score: 37.42  E-value: 5.52e-03
                         10        20
                 ....*....|....*....|....*.
gi 446841159 113 ILMIGPTGSGKTFLAQTLAKSLNVPF 138
Cdd:COG0703    1 IVLIGMMGAGKSTVGRLLAKRLGLPF 26
IS21_help_AAA NF038214
IS21-like element helper ATPase IstB; This protein family model resembles PF01695, but was ...
109-131 6.03e-03

IS21-like element helper ATPase IstB; This protein family model resembles PF01695, but was built to hit full-length AAA+ ATPases of IS21 family IS (insertion sequence) elements.


Pssm-ID: 439516  Cd Length: 232  Bit Score: 37.84  E-value: 6.03e-03
                         10        20
                 ....*....|....*....|...
gi 446841159 109 QKSNILMIGPTGSGKTFLAQTLA 131
Cdd:NF038214  89 RAENVLLLGPPGTGKTHLAIALG 111
VirB4 COG3451
Type IV secretory pathway, VirB4 component [Intracellular trafficking, secretion, and ...
106-131 9.13e-03

Type IV secretory pathway, VirB4 component [Intracellular trafficking, secretion, and vesicular transport];


Pssm-ID: 442674 [Multi-domain]  Cd Length: 546  Bit Score: 38.00  E-value: 9.13e-03
                         10        20
                 ....*....|....*....|....*.
gi 446841159 106 VDLQKSNILMIGPTGSGKTFLAQTLA 131
Cdd:COG3451  200 DGLDNGNTLILGPSGSGKSFLLKLLL 225
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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