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Conserved domains on  [gi|1780585657|emb|VYS70211|]
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unnamed protein product [Arabidopsis thaliana]

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 ...
159-527 0e+00

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


:

Pssm-ID: 440832 [Multi-domain]  Cd Length: 409  Bit Score: 627.46  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1780585657 159 PTPKEICKGLNKFVIGQERAKKVLSVAVYNHYKRIYHESSqkrsagetdstaakpaDDDMVELEKSNILLMGPTGSGKTL 238
Cdd:COG1219    61 PKPKEIKAFLDEYVIGQERAKKVLSVAVYNHYKRLNSGSK----------------DDDDVELEKSNILLIGPTGSGKTL 124
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1780585657 239 LAKTLARFVNVPFVIADATTLTQAGYVGEDVESILYKLLTVADYNVAAAQQGIVYIDEVDKITKKAESLNISRDVSGEGV 318
Cdd:COG1219   125 LAQTLARILDVPFAIADATTLTEAGYVGEDVENILLKLLQAADYDVEKAERGIIYIDEIDKIARKSENPSITRDVSGEGV 204
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1780585657 319 QQALLKMLEGTIVNVPEKGARKHPRGDNIQIDTKDILFICGGAFVDIEKTISERRHDSSIGFGAPVRANmraggvtNAAV 398
Cdd:COG1219   205 QQALLKILEGTVANVPPQGGRKHPQQEFIQIDTTNILFICGGAFDGLEKIIERRLGKKSIGFGAEVKSK-------KEKD 277
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1780585657 399 ASNLMETVESSDLIAYGLIPEFVGRFPVLVSLSALTENQLMQVLTEPKNALGKQYKKMYQMNSVKLHFTESALRLIARKA 478
Cdd:COG1219   278 EGELLKQVEPEDLIKFGLIPEFIGRLPVIATLEELDEEALVRILTEPKNALVKQYQKLFEMDGVELEFTDEALEAIAKKA 357
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*....
gi 1780585657 479 ITKNTGARGLRALLESILMDSMYEIPDEGTgsdmIEAVVVDEEAVEGEG 527
Cdd:COG1219   358 IERKTGARGLRSILEEILLDVMYELPSRKD----VKKVVITKEVVEGKA 402
 
Name Accession Description Interval E-value
ClpX COG1219
ATP-dependent protease Clp, ATPase subunit ClpX [Posttranslational modification, protein ...
159-527 0e+00

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


Pssm-ID: 440832 [Multi-domain]  Cd Length: 409  Bit Score: 627.46  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1780585657 159 PTPKEICKGLNKFVIGQERAKKVLSVAVYNHYKRIYHESSqkrsagetdstaakpaDDDMVELEKSNILLMGPTGSGKTL 238
Cdd:COG1219    61 PKPKEIKAFLDEYVIGQERAKKVLSVAVYNHYKRLNSGSK----------------DDDDVELEKSNILLIGPTGSGKTL 124
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1780585657 239 LAKTLARFVNVPFVIADATTLTQAGYVGEDVESILYKLLTVADYNVAAAQQGIVYIDEVDKITKKAESLNISRDVSGEGV 318
Cdd:COG1219   125 LAQTLARILDVPFAIADATTLTEAGYVGEDVENILLKLLQAADYDVEKAERGIIYIDEIDKIARKSENPSITRDVSGEGV 204
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1780585657 319 QQALLKMLEGTIVNVPEKGARKHPRGDNIQIDTKDILFICGGAFVDIEKTISERRHDSSIGFGAPVRANmraggvtNAAV 398
Cdd:COG1219   205 QQALLKILEGTVANVPPQGGRKHPQQEFIQIDTTNILFICGGAFDGLEKIIERRLGKKSIGFGAEVKSK-------KEKD 277
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1780585657 399 ASNLMETVESSDLIAYGLIPEFVGRFPVLVSLSALTENQLMQVLTEPKNALGKQYKKMYQMNSVKLHFTESALRLIARKA 478
Cdd:COG1219   278 EGELLKQVEPEDLIKFGLIPEFIGRLPVIATLEELDEEALVRILTEPKNALVKQYQKLFEMDGVELEFTDEALEAIAKKA 357
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*....
gi 1780585657 479 ITKNTGARGLRALLESILMDSMYEIPDEGTgsdmIEAVVVDEEAVEGEG 527
Cdd:COG1219   358 IERKTGARGLRSILEEILLDVMYELPSRKD----VKKVVITKEVVEGKA 402
clpX PRK05342
ATP-dependent Clp protease ATP-binding subunit ClpX;
156-526 0e+00

ATP-dependent Clp protease ATP-binding subunit ClpX;


Pssm-ID: 235422 [Multi-domain]  Cd Length: 412  Bit Score: 612.16  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1780585657 156 SDFPTPKEICKGLNKFVIGQERAKKVLSVAVYNHYKRIYHESSqkrsagetdstaakpaDDDMVELEKSNILLMGPTGSG 235
Cdd:PRK05342   57 KELPTPKEIKAHLDQYVIGQERAKKVLSVAVYNHYKRLRHGDK----------------KDDDVELQKSNILLIGPTGSG 120
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1780585657 236 KTLLAKTLARFVNVPFVIADATTLTQAGYVGEDVESILYKLLTVADYNVAAAQQGIVYIDEVDKITKKAESLNISRDVSG 315
Cdd:PRK05342  121 KTLLAQTLARILDVPFAIADATTLTEAGYVGEDVENILLKLLQAADYDVEKAQRGIVYIDEIDKIARKSENPSITRDVSG 200
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1780585657 316 EGVQQALLKMLEGTIVNVPEKGARKHPRGDNIQIDTKDILFICGGAFVDIEKTISERRHDSSIGFGAPVRANmraggvTN 395
Cdd:PRK05342  201 EGVQQALLKILEGTVASVPPQGGRKHPQQEFIQVDTTNILFICGGAFDGLEKIIKQRLGKKGIGFGAEVKSK------KE 274
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1780585657 396 AAVASNLMETVESSDLIAYGLIPEFVGRFPVLVSLSALTENQLMQVLTEPKNALGKQYKKMYQMNSVKLHFTESALRLIA 475
Cdd:PRK05342  275 KRTEGELLKQVEPEDLIKFGLIPEFIGRLPVVATLEELDEEALVRILTEPKNALVKQYQKLFEMDGVELEFTDEALEAIA 354
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1780585657 476 RKAITKNTGARGLRALLESILMDSMYEIPDEgtgsDMIEAVVVDEEAVEGE 526
Cdd:PRK05342  355 KKAIERKTGARGLRSILEEILLDVMFELPSR----EDVEKVVITKEVVEGK 401
clpX TIGR00382
endopeptidase Clp ATP-binding regulatory subunit (clpX); A member of the ATP-dependent ...
156-525 8.00e-168

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: 483.12  E-value: 8.00e-168
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1780585657 156 SDFPTPKEICKGLNKFVIGQERAKKVLSVAVYNHYKRIYHESSQKRsagetdstaakpadDDMVELEKSNILLMGPTGSG 235
Cdd:TIGR00382  63 SYLPTPKEIKAHLDEYVIGQEQAKKVLSVAVYNHYKRLNFEKNKKS--------------DNGVELSKSNILLIGPTGSG 128
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1780585657 236 KTLLAKTLARFVNVPFVIADATTLTQAGYVGEDVESILYKLLTVADYNVAAAQQGIVYIDEVDKITKKAESLNISRDVSG 315
Cdd:TIGR00382 129 KTLLAQTLARILNVPFAIADATTLTEAGYVGEDVENILLKLLQAADYDVEKAQKGIIYIDEIDKISRKSENPSITRDVSG 208
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1780585657 316 EGVQQALLKMLEGTIVNVPEKGARKHPRGDNIQIDTKDILFICGGAFVDIEKTISERRHDSSIGFGAPVRANMRAggvtn 395
Cdd:TIGR00382 209 EGVQQALLKIIEGTVANVPPQGGRKHPYQEFIQIDTSNILFICGGAFVGLEKIIKKRTGKSSIGFGAEVKKKSKE----- 283
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1780585657 396 aavASNLMETVESSDLIAYGLIPEFVGRFPVLVSLSALTENQLMQVLTEPKNALGKQYKKMYQMNSVKLHFTESALRLIA 475
Cdd:TIGR00382 284 ---KADLLRQVEPEDLVKFGLIPEFIGRLPVIATLEKLDEEALIAILTKPKNALVKQYQALFKMDNVELDFEEEALKAIA 360
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|
gi 1780585657 476 RKAITKNTGARGLRALLESILMDSMYEIPDEgtgsDMIEAVVVDEEAVEG 525
Cdd:TIGR00382 361 KKALERKTGARGLRSIVEGLLLDVMFDLPSL----EDLEKVVITKETVLK 406
RecA-like_ClpX cd19497
ATP-dependent Clp protease ATP-binding subunit ClpX; ClpX is a component of the ATP-dependent ...
159-430 2.10e-161

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: 460.14  E-value: 2.10e-161
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1780585657 159 PTPKEICKGLNKFVIGQERAKKVLSVAVYNHYKRIYHESSQKrsagetdstaakpadDDMVELEKSNILLMGPTGSGKTL 238
Cdd:cd19497     1 PTPKEIKEHLDKYVIGQERAKKVLSVAVYNHYKRIRNNLKQK---------------DDDVELEKSNILLIGPTGSGKTL 65
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1780585657 239 LAKTLARFVNVPFVIADATTLTQAGYVGEDVESILYKLLTVADYNVAAAQQGIVYIDEVDKITKKAESLNISRDVSGEGV 318
Cdd:cd19497    66 LAQTLAKILDVPFAIADATTLTEAGYVGEDVENILLKLLQAADYDVERAQRGIVYIDEIDKIARKSENPSITRDVSGEGV 145
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1780585657 319 QQALLKMLEGTIVNVPEKGARKHPRGDNIQIDTKDILFICGGAFVDIEKTISERRHDSSIGFGAPVRAnmraggVTNAAV 398
Cdd:cd19497   146 QQALLKILEGTVANVPPQGGRKHPQQEFIQVDTTNILFICGGAFVGLEKIIARRLGKKSLGFGAETSS------EKDEKE 219
                         250       260       270
                  ....*....|....*....|....*....|..
gi 1780585657 399 ASNLMETVESSDLIAYGLIPEFVGRFPVLVSL 430
Cdd:cd19497   220 RDELLSKVEPEDLIKFGLIPEFVGRLPVIVTL 251
AAA_2 pfam07724
AAA domain (Cdc48 subfamily); This Pfam entry includes some of the AAA proteins not detected ...
222-426 6.49e-34

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: 126.54  E-value: 6.49e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1780585657 222 EKSNILLMGPTGSGKTLLAKTLARFVNV---PFVIADATTLTQagyvgedvESILYKLLTVADYNVAAAQQG-------- 290
Cdd:pfam07724   2 PIGSFLFLGPTGVGKTELAKALAELLFGderALIRIDMSEYME--------EHSVSRLIGAPPGYVGYEEGGqlteavrr 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1780585657 291 ----IVYIDEVDKITKkaeslnisrdvsgeGVQQALLKMLEGTIVNvPEKGarkhprgdnIQIDTKDILFICGGAFVDIE 366
Cdd:pfam07724  74 kpysIVLIDEIEKAHP--------------GVQNDLLQILEGGTLT-DKQG---------RTVDFKNTLFIMTGNFGSEK 129
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1780585657 367 KTISERRHDSsigfgapvranmraggvtnaavASNLMETVESSDLIAYGLIPEFVGRFPV 426
Cdd:pfam07724 130 ISDASRLGDS----------------------PDYELLKEEVMDLLKKGFIPEFLGRLPI 167
ClpB_D2-small smart01086
C-terminal, D2-small domain, of ClpB protein; This is the C-terminal domain of ClpB protein, ...
433-526 7.05e-21

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


Pssm-ID: 198154 [Multi-domain]  Cd Length: 90  Bit Score: 87.11  E-value: 7.05e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1780585657  433 LTENQLMQVLTEPKNALGKQYKkmyqMNSVKLHFTESALRLIARKAITKNTGARGLRALLESILMDSMYEIPDEGTGSDm 512
Cdd:smart01086   1 LDKEDLVRIVDLPLNALQKRLA----EKGITLEFTDEALDWLAEKGYDPKYGARPLRRIIQRELEDPLAELILSGELKD- 75
                           90
                   ....*....|....
gi 1780585657  513 IEAVVVDEEAVEGE 526
Cdd:smart01086  76 GDTVVVDVDDGELV 89
 
Name Accession Description Interval E-value
ClpX COG1219
ATP-dependent protease Clp, ATPase subunit ClpX [Posttranslational modification, protein ...
159-527 0e+00

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


Pssm-ID: 440832 [Multi-domain]  Cd Length: 409  Bit Score: 627.46  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1780585657 159 PTPKEICKGLNKFVIGQERAKKVLSVAVYNHYKRIYHESSqkrsagetdstaakpaDDDMVELEKSNILLMGPTGSGKTL 238
Cdd:COG1219    61 PKPKEIKAFLDEYVIGQERAKKVLSVAVYNHYKRLNSGSK----------------DDDDVELEKSNILLIGPTGSGKTL 124
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1780585657 239 LAKTLARFVNVPFVIADATTLTQAGYVGEDVESILYKLLTVADYNVAAAQQGIVYIDEVDKITKKAESLNISRDVSGEGV 318
Cdd:COG1219   125 LAQTLARILDVPFAIADATTLTEAGYVGEDVENILLKLLQAADYDVEKAERGIIYIDEIDKIARKSENPSITRDVSGEGV 204
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1780585657 319 QQALLKMLEGTIVNVPEKGARKHPRGDNIQIDTKDILFICGGAFVDIEKTISERRHDSSIGFGAPVRANmraggvtNAAV 398
Cdd:COG1219   205 QQALLKILEGTVANVPPQGGRKHPQQEFIQIDTTNILFICGGAFDGLEKIIERRLGKKSIGFGAEVKSK-------KEKD 277
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1780585657 399 ASNLMETVESSDLIAYGLIPEFVGRFPVLVSLSALTENQLMQVLTEPKNALGKQYKKMYQMNSVKLHFTESALRLIARKA 478
Cdd:COG1219   278 EGELLKQVEPEDLIKFGLIPEFIGRLPVIATLEELDEEALVRILTEPKNALVKQYQKLFEMDGVELEFTDEALEAIAKKA 357
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*....
gi 1780585657 479 ITKNTGARGLRALLESILMDSMYEIPDEGTgsdmIEAVVVDEEAVEGEG 527
Cdd:COG1219   358 IERKTGARGLRSILEEILLDVMYELPSRKD----VKKVVITKEVVEGKA 402
clpX PRK05342
ATP-dependent Clp protease ATP-binding subunit ClpX;
156-526 0e+00

ATP-dependent Clp protease ATP-binding subunit ClpX;


Pssm-ID: 235422 [Multi-domain]  Cd Length: 412  Bit Score: 612.16  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1780585657 156 SDFPTPKEICKGLNKFVIGQERAKKVLSVAVYNHYKRIYHESSqkrsagetdstaakpaDDDMVELEKSNILLMGPTGSG 235
Cdd:PRK05342   57 KELPTPKEIKAHLDQYVIGQERAKKVLSVAVYNHYKRLRHGDK----------------KDDDVELQKSNILLIGPTGSG 120
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1780585657 236 KTLLAKTLARFVNVPFVIADATTLTQAGYVGEDVESILYKLLTVADYNVAAAQQGIVYIDEVDKITKKAESLNISRDVSG 315
Cdd:PRK05342  121 KTLLAQTLARILDVPFAIADATTLTEAGYVGEDVENILLKLLQAADYDVEKAQRGIVYIDEIDKIARKSENPSITRDVSG 200
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1780585657 316 EGVQQALLKMLEGTIVNVPEKGARKHPRGDNIQIDTKDILFICGGAFVDIEKTISERRHDSSIGFGAPVRANmraggvTN 395
Cdd:PRK05342  201 EGVQQALLKILEGTVASVPPQGGRKHPQQEFIQVDTTNILFICGGAFDGLEKIIKQRLGKKGIGFGAEVKSK------KE 274
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1780585657 396 AAVASNLMETVESSDLIAYGLIPEFVGRFPVLVSLSALTENQLMQVLTEPKNALGKQYKKMYQMNSVKLHFTESALRLIA 475
Cdd:PRK05342  275 KRTEGELLKQVEPEDLIKFGLIPEFIGRLPVVATLEELDEEALVRILTEPKNALVKQYQKLFEMDGVELEFTDEALEAIA 354
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1780585657 476 RKAITKNTGARGLRALLESILMDSMYEIPDEgtgsDMIEAVVVDEEAVEGE 526
Cdd:PRK05342  355 KKAIERKTGARGLRSILEEILLDVMFELPSR----EDVEKVVITKEVVEGK 401
clpX TIGR00382
endopeptidase Clp ATP-binding regulatory subunit (clpX); A member of the ATP-dependent ...
156-525 8.00e-168

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: 483.12  E-value: 8.00e-168
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1780585657 156 SDFPTPKEICKGLNKFVIGQERAKKVLSVAVYNHYKRIYHESSQKRsagetdstaakpadDDMVELEKSNILLMGPTGSG 235
Cdd:TIGR00382  63 SYLPTPKEIKAHLDEYVIGQEQAKKVLSVAVYNHYKRLNFEKNKKS--------------DNGVELSKSNILLIGPTGSG 128
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1780585657 236 KTLLAKTLARFVNVPFVIADATTLTQAGYVGEDVESILYKLLTVADYNVAAAQQGIVYIDEVDKITKKAESLNISRDVSG 315
Cdd:TIGR00382 129 KTLLAQTLARILNVPFAIADATTLTEAGYVGEDVENILLKLLQAADYDVEKAQKGIIYIDEIDKISRKSENPSITRDVSG 208
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1780585657 316 EGVQQALLKMLEGTIVNVPEKGARKHPRGDNIQIDTKDILFICGGAFVDIEKTISERRHDSSIGFGAPVRANMRAggvtn 395
Cdd:TIGR00382 209 EGVQQALLKIIEGTVANVPPQGGRKHPYQEFIQIDTSNILFICGGAFVGLEKIIKKRTGKSSIGFGAEVKKKSKE----- 283
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1780585657 396 aavASNLMETVESSDLIAYGLIPEFVGRFPVLVSLSALTENQLMQVLTEPKNALGKQYKKMYQMNSVKLHFTESALRLIA 475
Cdd:TIGR00382 284 ---KADLLRQVEPEDLVKFGLIPEFIGRLPVIATLEKLDEEALIAILTKPKNALVKQYQALFKMDNVELDFEEEALKAIA 360
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|
gi 1780585657 476 RKAITKNTGARGLRALLESILMDSMYEIPDEgtgsDMIEAVVVDEEAVEG 525
Cdd:TIGR00382 361 KKALERKTGARGLRSIVEGLLLDVMFDLPSL----EDLEKVVITKETVLK 406
RecA-like_ClpX cd19497
ATP-dependent Clp protease ATP-binding subunit ClpX; ClpX is a component of the ATP-dependent ...
159-430 2.10e-161

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: 460.14  E-value: 2.10e-161
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1780585657 159 PTPKEICKGLNKFVIGQERAKKVLSVAVYNHYKRIYHESSQKrsagetdstaakpadDDMVELEKSNILLMGPTGSGKTL 238
Cdd:cd19497     1 PTPKEIKEHLDKYVIGQERAKKVLSVAVYNHYKRIRNNLKQK---------------DDDVELEKSNILLIGPTGSGKTL 65
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1780585657 239 LAKTLARFVNVPFVIADATTLTQAGYVGEDVESILYKLLTVADYNVAAAQQGIVYIDEVDKITKKAESLNISRDVSGEGV 318
Cdd:cd19497    66 LAQTLAKILDVPFAIADATTLTEAGYVGEDVENILLKLLQAADYDVERAQRGIVYIDEIDKIARKSENPSITRDVSGEGV 145
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1780585657 319 QQALLKMLEGTIVNVPEKGARKHPRGDNIQIDTKDILFICGGAFVDIEKTISERRHDSSIGFGAPVRAnmraggVTNAAV 398
Cdd:cd19497   146 QQALLKILEGTVANVPPQGGRKHPQQEFIQVDTTNILFICGGAFVGLEKIIARRLGKKSLGFGAETSS------EKDEKE 219
                         250       260       270
                  ....*....|....*....|....*....|..
gi 1780585657 399 ASNLMETVESSDLIAYGLIPEFVGRFPVLVSL 430
Cdd:cd19497   220 RDELLSKVEPEDLIKFGLIPEFVGRLPVIVTL 251
hslU PRK05201
ATP-dependent protease ATPase subunit HslU;
160-524 1.13e-51

ATP-dependent protease ATPase subunit HslU;


Pssm-ID: 235364 [Multi-domain]  Cd Length: 443  Bit Score: 183.35  E-value: 1.13e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1780585657 160 TPKEICKGLNKFVIGQERAKKVLSVAVYNHYKRiyhessQKrsagetdstaakpADDDMVE--LEKsNILLMGPTGSGKT 237
Cdd:PRK05201    5 TPREIVSELDKYIIGQDDAKRAVAIALRNRWRR------MQ-------------LPEELRDevTPK-NILMIGPTGVGKT 64
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1780585657 238 LLAKTLARFVNVPFVIADATTLTQAGYVGEDVESIL-------------------------------------------- 273
Cdd:PRK05201   65 EIARRLAKLANAPFIKVEATKFTEVGYVGRDVESIIrdlveiavkmvreekrekvrekaeeaaeerildallppaknnwg 144
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1780585657 274 -----------------------------------------------------------------------------YKL 276
Cdd:PRK05201  145 eeeekeeisatrqkfrkklregelddkeieievaeaapmmeimgppgmeemtiqlqdmfgnlgpkkkkkrklkvkeaRKI 224
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1780585657 277 LT------------VADYNVAAAQQ-GIVYIDEVDKITKKAESlnISRDVSGEGVQQALLKMLEGTIVNVpekgarKHpr 343
Cdd:PRK05201  225 LIeeeaaklidmeeIKQEAIERVEQnGIVFIDEIDKIAARGGS--SGPDVSREGVQRDLLPLVEGSTVST------KY-- 294
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1780585657 344 GdniQIDTKDILFICGGAFvdiektiserrHDSSigfgaPvranmraggvtnaavasnlmetvesSDLIaygliPEFVGR 423
Cdd:PRK05201  295 G---MVKTDHILFIASGAF-----------HVSK-----P-------------------------SDLI-----PELQGR 325
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1780585657 424 FPVLVSLSALTENQLMQVLTEPKNALGKQYKKMYQMNSVKLHFTESALRLIARKAI-----TKNTGARGLRALLESILMD 498
Cdd:PRK05201  326 FPIRVELDALTEEDFVRILTEPKASLIKQYQALLATEGVTLEFTDDAIRRIAEIAYqvnekTENIGARRLHTVMEKLLED 405
                         490       500
                  ....*....|....*....|....*.
gi 1780585657 499 SMYEIPDEgtgsdMIEAVVVDEEAVE 524
Cdd:PRK05201  406 ISFEAPDM-----SGETVTIDAAYVD 426
HslU COG1220
ATP-dependent protease HslVU (ClpYQ), ATPase subunit HslU [Posttranslational modification, ...
160-524 1.43e-48

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


Pssm-ID: 440833 [Multi-domain]  Cd Length: 454  Bit Score: 175.24  E-value: 1.43e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1780585657 160 TPKEICKGLNKFVIGQERAKKVLSVAVYNHYKRiyhesSQkrsagetdstaakpADDDMVElE---KsNILLMGPTGSGK 236
Cdd:COG1220     5 TPREIVAELDKYIIGQDEAKRAVAIALRNRWRR-----QQ--------------LPEELRD-EitpK-NILMIGPTGVGK 63
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1780585657 237 TLLAKTLARFVNVPFVIADATTLTQAGYVGEDVESIL------------------------------------------- 273
Cdd:COG1220    64 TEIARRLAKLANAPFIKVEATKFTEVGYVGRDVESMIrdlveiavkmvreekmekvrekaeeaaeerildlllpppkkka 143
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1780585657     --------------------------------------------------------------------------------
Cdd:COG1220   144 gsnnpfeeeeeeeeeeeeisrtrekfrkklregelddreieieveessspgveimgppgmeemgmnlqdmfgnlmpkkkk 223
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1780585657 274 ---------YKLLT------------VADYNVAAAQQ-GIVYIDEVDKITKKAESlniSR-DVSGEGVQQALLKMLEGTI 330
Cdd:COG1220   224 krkvkvkeaRKILTqeeaaklidmdeVKQEAIERAEQnGIIFIDEIDKIASRGGG---SGpDVSREGVQRDLLPIVEGST 300
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1780585657 331 VNVpekgarKHprGdniQIDTKDILFICGGAFvdiektiserrHDSSigfgaPvranmraggvtnaavasnlmetvesSD 410
Cdd:COG1220   301 VNT------KY--G---MVKTDHILFIAAGAF-----------HVSK-----P-------------------------SD 328
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1780585657 411 LIaygliPEFVGRFPVLVSLSALTENQLMQVLTEPKNALGKQYKKMYQMNSVKLHFTESALRLIARKAI-----TKNTGA 485
Cdd:COG1220   329 LI-----PELQGRFPIRVELDSLTEEDFVRILTEPKNALTKQYQALLATEGVELEFTDDAIREIAEIAFevnerTENIGA 403
                         490       500       510
                  ....*....|....*....|....*....|....*....
gi 1780585657 486 RGLRALLESILMDSMYEIPDEGTgsdmiEAVVVDEEAVE 524
Cdd:COG1220   404 RRLHTVMEKLLEDISFEAPDLSG-----KTVVIDAAYVD 437
hslU TIGR00390
ATP-dependent protease HslVU, ATPase subunit; This model represents the ATPase subunit of ...
160-505 1.31e-43

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: 161.14  E-value: 1.31e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1780585657 160 TPKEICKGLNKFVIGQERAKKVLSVAVYNHYKRIYHESSQKRsagetdstaakpadddmvELEKSNILLMGPTGSGKTLL 239
Cdd:TIGR00390   2 TPREIVAELDKYIIGQDNAKKSVAIALRNRYRRSQLNEELKD------------------EVTPKNILMIGPTGVGKTEI 63
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1780585657 240 AKTLARFVNVPFVIADATTLTQAGYVGEDVESILYKLLTVA--------------------------------------- 280
Cdd:TIGR00390  64 ARRLAKLANAPFIKVEATKFTEVGYVGRDVESMVRDLTDAAvklvkeeaiekvrdraeelaeerivdvllppaknqwgqt 143
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1780585657 281 -----------------------DYNV----------------------------------------------------- 284
Cdd:TIGR00390 144 eqqqepesareafrkklregeldDKEIeidvsakmpsgieimappgmeemtmqlqslfqnlggqkkkkrklkikdakkal 223
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1780585657 285 --------------------AAAQQGIVYIDEVDKITKKAESlnISRDVSGEGVQQALLKMLEGTIVNVpekgarKHPrg 344
Cdd:TIGR00390 224 iaeeaaklvdpeeikqeaidAVEQSGIIFIDEIDKIAKKGES--SGADVSREGVQRDLLPIVEGSTVNT------KYG-- 293
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1780585657 345 dniQIDTKDILFICGGAFvdiektiserrhdssigfgapvranmraggvtnaavasnlmETVESSDLIaygliPEFVGRF 424
Cdd:TIGR00390 294 ---MVKTDHILFIAAGAF-----------------------------------------QLAKPSDLI-----PELQGRF 324
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1780585657 425 PVLVSLSALTENQLMQVLTEPKNALGKQYKKMYQMNSVKLHFTESALRLIARKAI-----TKNTGARGLRALLESILMDS 499
Cdd:TIGR00390 325 PIRVELQALTTDDFERILTEPKNSLIKQYKALMKTEGVNIEFSDEAIKRIAELAYnvnekTENIGARRLHTVLERLLEDI 404

                  ....*.
gi 1780585657 500 MYEIPD 505
Cdd:TIGR00390 405 SFEAPD 410
RecA-like_HslU cd19498
ATP-dependent protease ATPase subunit HslU; HslU is a component of the ATP-dependent protease ...
160-430 1.72e-42

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: 150.61  E-value: 1.72e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1780585657 160 TPKEICKGLNKFVIGQERAKKVLSVAVYNHYKRIYHESSQKRsagetdstaakpadddmvELEKSNILLMGPTGSGKTLL 239
Cdd:cd19498     1 TPREIVSELDKYIIGQDEAKRAVAIALRNRWRRMQLPEELRD------------------EVTPKNILMIGPTGVGKTEI 62
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1780585657 240 AKTLARFVNVPFVIADATTLTQAGYVGEDVESILYKLLtvadynvaaaqQGIVYIDEVDKITKKAESlnISRDVSGEGVQ 319
Cdd:cd19498    63 ARRLAKLAGAPFIKVEATKFTEVGYVGRDVESIIRDLV-----------EGIVFIDEIDKIAKRGGS--SGPDVSREGVQ 129
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1780585657 320 QALLKMLEGTIVNVpekgarKHprgdnIQIDTKDILFICGGAFvdiektiserrhdssigfgapvranmraggvtnaava 399
Cdd:cd19498   130 RDLLPIVEGSTVST------KY-----GPVKTDHILFIAAGAF------------------------------------- 161
                         250       260       270
                  ....*....|....*....|....*....|.
gi 1780585657 400 snlmETVESSDliaygLIPEFVGRFPVLVSL 430
Cdd:cd19498   162 ----HVAKPSD-----LIPELQGRFPIRVEL 183
AAA_2 pfam07724
AAA domain (Cdc48 subfamily); This Pfam entry includes some of the AAA proteins not detected ...
222-426 6.49e-34

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: 126.54  E-value: 6.49e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1780585657 222 EKSNILLMGPTGSGKTLLAKTLARFVNV---PFVIADATTLTQagyvgedvESILYKLLTVADYNVAAAQQG-------- 290
Cdd:pfam07724   2 PIGSFLFLGPTGVGKTELAKALAELLFGderALIRIDMSEYME--------EHSVSRLIGAPPGYVGYEEGGqlteavrr 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1780585657 291 ----IVYIDEVDKITKkaeslnisrdvsgeGVQQALLKMLEGTIVNvPEKGarkhprgdnIQIDTKDILFICGGAFVDIE 366
Cdd:pfam07724  74 kpysIVLIDEIEKAHP--------------GVQNDLLQILEGGTLT-DKQG---------RTVDFKNTLFIMTGNFGSEK 129
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1780585657 367 KTISERRHDSsigfgapvranmraggvtnaavASNLMETVESSDLIAYGLIPEFVGRFPV 426
Cdd:pfam07724 130 ISDASRLGDS----------------------PDYELLKEEVMDLLKKGFIPEFLGRLPI 167
ClpB_D2-small smart01086
C-terminal, D2-small domain, of ClpB protein; This is the C-terminal domain of ClpB protein, ...
433-526 7.05e-21

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


Pssm-ID: 198154 [Multi-domain]  Cd Length: 90  Bit Score: 87.11  E-value: 7.05e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1780585657  433 LTENQLMQVLTEPKNALGKQYKkmyqMNSVKLHFTESALRLIARKAITKNTGARGLRALLESILMDSMYEIPDEGTGSDm 512
Cdd:smart01086   1 LDKEDLVRIVDLPLNALQKRLA----EKGITLEFTDEALDWLAEKGYDPKYGARPLRRIIQRELEDPLAELILSGELKD- 75
                           90
                   ....*....|....
gi 1780585657  513 IEAVVVDEEAVEGE 526
Cdd:smart01086  76 GDTVVVDVDDGELV 89
RecA-like_protease cd19481
proteases similar to RecA; RecA-like NTPases. This family includes the NTP binding domain of ...
223-328 6.16e-18

proteases similar to RecA; RecA-like NTPases. This family includes the NTP binding domain of F1 and V1 H(+)ATPases, DnaB and related helicases as well as bacterial RecA and related eukaryotic and archaeal recombinases. This group also includes bacterial conjugation proteins and related DNA transfer proteins involved in type II and type IV secretion.


Pssm-ID: 410889 [Multi-domain]  Cd Length: 158  Bit Score: 81.18  E-value: 6.16e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1780585657 223 KSNILLMGPTGSGKTLLAKTLARFVNVPFVIADATTLTqAGYVGEdVESILYKLLTVADynvaAAQQGIVYIDEVDKITK 302
Cdd:cd19481    26 PKGILLYGPPGTGKTLLAKALAGELGLPLIVVKLSSLL-SKYVGE-SEKNLRKIFERAR----RLAPCILFIDEIDAIGR 99
                          90       100
                  ....*....|....*....|....*.
gi 1780585657 303 KAESLNISRDVSgeGVQQALLKMLEG 328
Cdd:cd19481   100 KRDSSGESGELR--RVLNQLLTELDG 123
AAA cd00009
The AAA+ (ATPases Associated with a wide variety of cellular Activities) superfamily ...
223-381 7.19e-15

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


Pssm-ID: 99707 [Multi-domain]  Cd Length: 151  Bit Score: 72.18  E-value: 7.19e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1780585657 223 KSNILLMGPTGSGKTLLAKTLARFV---NVPFVIADATTLTQAGYVGEDVESILYKLLTVAdynVAAAQQGIVYIDEVDK 299
Cdd:cd00009    19 PKNLLLYGPPGTGKTTLARAIANELfrpGAPFLYLNASDLLEGLVVAELFGHFLVRLLFEL---AEKAKPGVLFIDEIDS 95
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1780585657 300 ItkkaeslnisrdvsGEGVQQALLKMLEGTIVNVPEKGARKhprgdniqidtkdILFICGGAFVDIEKTISERRHDSSIG 379
Cdd:cd00009    96 L--------------SRGAQNALLRVLETLNDLRIDRENVR-------------VIGATNRPLLGDLDRALYDRLDIRIV 148

                  ..
gi 1780585657 380 FG 381
Cdd:cd00009   149 IP 150
AAA pfam00004
ATPase family associated with various cellular activities (AAA); AAA family proteins often ...
226-328 4.74e-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: 4.74e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1780585657 226 ILLMGPTGSGKTLLAKTLARFVNVPFVIADATTLTQaGYVGEDVESILyKLLTVADynvaAAQQGIVYIDEVDKITKKAE 305
Cdd:pfam00004   1 LLLYGPPGTGKTTLAKAVAKELGAPFIEISGSELVS-KYVGESEKRLR-ELFEAAK----KLAPCVIFIDEIDALAGSRG 74
                          90       100
                  ....*....|....*....|...
gi 1780585657 306 SlniSRDVSGEGVQQALLKMLEG 328
Cdd:pfam00004  75 S---GGDSESRRVVNQLLTELDG 94
SpoVK COG0464
AAA+-type ATPase, SpoVK/Ycf46/Vps4 family [Cell wall/membrane/envelope biogenesis, Cell cycle ...
226-328 6.65e-12

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


Pssm-ID: 440232 [Multi-domain]  Cd Length: 397  Bit Score: 67.63  E-value: 6.65e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1780585657 226 ILLMGPTGSGKTLLAKTLARFVNVPFVIADATTLTqAGYVGEdVESILYKLLTVAdynvAAAQQGIVYIDEVDKITKKAE 305
Cdd:COG0464   194 LLLYGPPGTGKTLLARALAGELGLPLIEVDLSDLV-SKYVGE-TEKNLREVFDKA----RGLAPCVLFIDEADALAGKRG 267
                          90       100
                  ....*....|....*....|...
gi 1780585657 306 SlniSRDVSGEGVQQALLKMLEG 328
Cdd:COG0464   268 E---VGDGVGRRVVNTLLTEMEE 287
ClpB_D2-small pfam10431
C-terminal, D2-small domain, of ClpB protein; This is the C-terminal domain of ClpB protein, ...
433-502 2.63e-10

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: 56.65  E-value: 2.63e-10
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1780585657 433 LTENQLMQVLTEpknALGKQYKKMYQMNsVKLHFTESALRLIARKAITKNTGARGLRALLESILMDSMYE 502
Cdd:pfam10431   1 LSKEELRKIVDL---QLKELQKRLAERG-ITLELTDAAKDWLAEKGYDPEYGARPLRRAIQREIEDPLAE 66
RecA-like_CDC48_NLV2_r1-like cd19503
first of two ATPase domains of CDC48 and NLV2, and similar ATPase domains; CDC48 in yeast and ...
226-328 1.37e-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: 57.30  E-value: 1.37e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1780585657 226 ILLMGPTGSGKTLLAKTLARFVNVPFVIADATTLtQAGYVGEDvESILYKLLTVAdynvAAAQQGIVYIDEVDKITKKAE 305
Cdd:cd19503    37 VLLHGPPGTGKTLLARAVANEAGANFLSISGPSI-VSKYLGES-EKNLREIFEEA----RSHAPSIIFIDEIDALAPKRE 110
                          90       100
                  ....*....|....*....|...
gi 1780585657 306 SlnISRDVSGEGVQQaLLKMLEG 328
Cdd:cd19503   111 E--DQREVERRVVAQ-LLTLMDG 130
RecA-like_NVL_r1-like cd19518
first of two ATPase domains of NVL (nuclear VCP-like protein) and similar ATPase domains; NVL ...
226-339 2.27e-09

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: 56.64  E-value: 2.27e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1780585657 226 ILLMGPTGSGKTLLAKTLARFVNVPFVIADATTLTqAGYVGEDVEsilyKLLTVADYNVAAAqQGIVYIDEVDKITKKAE 305
Cdd:cd19518    37 VLLHGPPGCGKTMLANAIAGELKVPFLKISATEIV-SGVSGESEE----KIRELFDQAISNA-PCIVFIDEIDAITPKRE 110
                          90       100       110
                  ....*....|....*....|....*....|....
gi 1780585657 306 SlnISRDVSGEGVQQALLKMLEgtIVNVPEKGAR 339
Cdd:cd19518   111 S--AQREMERRIVSQLLTCMDE--LNNEKTAGGP 140
RPT1 COG1222
ATP-dependent 26S proteasome regulatory subunit [Posttranslational modification, protein ...
226-328 3.79e-08

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


Pssm-ID: 440835 [Multi-domain]  Cd Length: 326  Bit Score: 55.40  E-value: 3.79e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1780585657 226 ILLMGPTGSGKTLLAKTLARFVNVPFVIADATTLTQAgYVGEDvESILYKLLTVAdynvAAAQQGIVYIDEVDKITKKAE 305
Cdd:COG1222   115 VLLYGPPGTGKTLLAKAVAGELGAPFIRVRGSELVSK-YIGEG-ARNVREVFELA----REKAPSIIFIDEIDAIAARRT 188
                          90       100
                  ....*....|....*....|....*
gi 1780585657 306 SlniSRDvSGEG--VQQALLKMLEG 328
Cdd:COG1222   189 D---DGT-SGEVqrTVNQLLAELDG 209
AAA smart00382
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ...
223-309 1.86e-07

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


Pssm-ID: 214640 [Multi-domain]  Cd Length: 148  Bit Score: 50.83  E-value: 1.86e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1780585657  223 KSNILLMGPTGSGKTLLAKTLARFVNVP---FVIADATTLTQA------------GYVGEDVESILYKLLTVADYNvaaa 287
Cdd:smart00382   2 GEVILIVGPPGSGKTTLARALARELGPPgggVIYIDGEDILEEvldqllliivggKKASGSGELRLRLALALARKL---- 77
                           90       100
                   ....*....|....*....|..
gi 1780585657  288 QQGIVYIDEVDKITKKAESLNI 309
Cdd:smart00382  78 KPDVLILDEITSLLDAEQEALL 99
RecA-like_VPS4-like cd19509
ATPase domain of VPS4, ATAD1, K, KTNA1, Spastin, FIGL-1 and similar ATPase domains; This ...
226-337 2.77e-07

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


Pssm-ID: 410917 [Multi-domain]  Cd Length: 163  Bit Score: 50.43  E-value: 2.77e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1780585657 226 ILLMGPTGSGKTLLAKTLARFVNVPFVIADATTLTqAGYVGEDvESILYKLLTVADYNvaaaQQGIVYIDEVDKITKK-- 303
Cdd:cd19509    35 ILLYGPPGTGKTLLARAVASESGSTFFSISASSLV-SKWVGES-EKIVRALFALAREL----QPSIIFIDEIDSLLSErg 108
                          90       100       110
                  ....*....|....*....|....*....|....
gi 1780585657 304 AESLNISRDVSGEgvqqaLLKMLEGtIVNVPEKG 337
Cdd:cd19509   109 SGEHEASRRVKTE-----FLVQMDG-VLNKPEDR 136
RecA-like_spastin cd19524
ATPase domain of spastin; Spastin is an ATP-dependent microtubule-severing protein involved in ...
226-300 2.77e-07

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


Pssm-ID: 410932 [Multi-domain]  Cd Length: 164  Bit Score: 50.62  E-value: 2.77e-07
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1780585657 226 ILLMGPTGSGKTLLAKTLARFVNVPFVIADATTLTqAGYVGEDvESILYKLLTVAdynvAAAQQGIVYIDEVDKI 300
Cdd:cd19524    36 LLLFGPPGNGKTMLAKAVAAESNATFFNISAASLT-SKYVGEG-EKLVRALFAVA----RELQPSIIFIDEVDSL 104
CDC48 TIGR01243
AAA family ATPase, CDC48 subfamily; This subfamily of the AAA family ATPases includes two ...
226-328 3.16e-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: 53.37  E-value: 3.16e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1780585657 226 ILLMGPTGSGKTLLAKTLARFVNVPFVIADATTLtQAGYVGEDvESILYKLLTVADYNVAAaqqgIVYIDEVDKITKKAE 305
Cdd:TIGR01243 215 VLLYGPPGTGKTLLAKAVANEAGAYFISINGPEI-MSKYYGES-EERLREIFKEAEENAPS----IIFIDEIDAIAPKRE 288
                          90       100
                  ....*....|....*....|....*.
gi 1780585657 306 slnisrDVSGE---GVQQALLKMLEG 328
Cdd:TIGR01243 289 ------EVTGEvekRVVAQLLTLMDG 308
RecA-like_PAN_like cd19502
proteasome activating nucleotidase PAN and related proteasome subunits; This subfamily ...
226-326 9.64e-07

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: 49.26  E-value: 9.64e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1780585657 226 ILLMGPTGSGKTLLAKTLARFVNVPFVIADATTLTQAgYVGEDvESILYKLLTVADYNVAAaqqgIVYIDEVDKITKKAE 305
Cdd:cd19502    40 VLLYGPPGTGKTLLAKAVANHTDATFIRVVGSELVQK-YIGEG-ARLVRELFEMAREKAPS----IIFIDEIDAIGAKRF 113
                          90       100
                  ....*....|....*....|.
gi 1780585657 306 SLNISRDvsgEGVQQALLKML 326
Cdd:cd19502   114 DSGTGGD---REVQRTMLELL 131
RecA-like_CDC48_r1-like cd19519
first of two ATPase domains of CDC48 and similar ATPase domains; CDC48 in yeast and p97 or VCP ...
226-328 1.08e-06

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


Pssm-ID: 410927 [Multi-domain]  Cd Length: 166  Bit Score: 48.97  E-value: 1.08e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1780585657 226 ILLMGPTGSGKTLLAKTLARFVNVPFVIADATTLtQAGYVGEDvESILYKLLTVADYNVAAaqqgIVYIDEVDKITKKAE 305
Cdd:cd19519    37 ILLYGPPGTGKTLIARAVANETGAFFFLINGPEI-MSKLAGES-ESNLRKAFEEAEKNAPA----IIFIDEIDAIAPKRE 110
                          90       100
                  ....*....|....*....|....*.
gi 1780585657 306 slnisrDVSGE---GVQQALLKMLEG 328
Cdd:cd19519   111 ------KTHGEverRIVSQLLTLMDG 130
RecA-like_NSF-SEC18_r1-like cd19504
first of two ATPase domains of NSF and SEC18, and similar ATPase domains; ...
226-325 4.62e-06

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


Pssm-ID: 410912 [Multi-domain]  Cd Length: 177  Bit Score: 47.10  E-value: 4.62e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1780585657 226 ILLMGPTGSGKTLLAKTLARFVNV--PFVIADATTLTQagYVGEDVESIlYKLLTVA--DYNVAAAQQG--IVYIDEVDK 299
Cdd:cd19504    38 ILLYGPPGTGKTLMARQIGKMLNArePKIVNGPEILNK--YVGESEANI-RKLFADAeeEQRRLGANSGlhIIIFDEIDA 114
                          90       100
                  ....*....|....*....|....*.
gi 1780585657 300 ITKKAESLNISRDVSGEGVQQALLKM 325
Cdd:cd19504   115 ICKQRGSMAGSTGVHDTVVNQLLSKI 140
RecA-like_ClpB_Hsp104-like cd19499
Chaperone protein ClpB/Hsp104 subfamily; Bacterial Caseinolytic peptidase B (ClpB) and ...
166-299 1.01e-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: 46.40  E-value: 1.01e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1780585657 166 KGLNKFVIGQERAKKVLSVAVynhykRIYHessqkrsAGETDSTaaKPaddDMVeleksnILLMGPTGSGKTLLAKTLAR 245
Cdd:cd19499     7 ERLHERVVGQDEAVKAVSDAI-----RRAR-------AGLSDPN--RP---IGS------FLFLGPTGVGKTELAKALAE 63
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1780585657 246 FV---NVPFVIAD---------ATTLTQA--GYVGEDVESILYKLLTVADYNVaaaqqgiVYIDEVDK 299
Cdd:cd19499    64 LLfgdEDNLIRIDmseymekhsVSRLIGAppGYVGYTEGGQLTEAVRRKPYSV-------VLLDEIEK 124
RecA-like_ATAD1 cd19520
ATPase domain of ATPase family AAA domain-containing protein 1 and similar ATPase domains; ...
226-298 1.16e-05

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


Pssm-ID: 410928 [Multi-domain]  Cd Length: 166  Bit Score: 45.88  E-value: 1.16e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1780585657 226 ILLMGPTGSGKTLLAKTLARFVNVPFVIADATTLTQAGYvGEDvesilyKLLTVADYNVAAA-QQGIVYIDEVD 298
Cdd:cd19520    38 VLLYGPPGCGKTMLAKATAKEAGARFINLQVSSLTDKWY-GES------QKLVAAVFSLASKlQPSIIFIDEID 104
AAA_22 pfam13401
AAA domain;
219-322 1.48e-05

AAA domain;


Pssm-ID: 379165 [Multi-domain]  Cd Length: 129  Bit Score: 44.64  E-value: 1.48e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1780585657 219 VELEKSNILLMGPTGSGKTLLAKTLARF---VNVPFVIADAT-------------TLTQAGYVGEDVESILYKLLTvaDY 282
Cdd:pfam13401   1 IRFGAGILVLTGESGTGKTTLLRRLLEQlpeVRDSVVFVDLPsgtspkdllrallRALGLPLSGRLSKEELLAALQ--QL 78
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 1780585657 283 NVAAAQQGIVYIDEVDKITKKA-ESLNISRDVSGEGVQQAL 322
Cdd:pfam13401  79 LLALAVAVVLIIDEAQHLSLEAlEELRDLLNLSSKLLQLIL 119
RecA-like_Figl-1 cd19525
ATPase domain of Fidgetin-Like 1 (FIGL-1); FIGL-1 may participate in DNA repair in the nucleus; ...
226-306 1.90e-05

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


Pssm-ID: 410933 [Multi-domain]  Cd Length: 186  Bit Score: 45.75  E-value: 1.90e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1780585657 226 ILLMGPTGSGKTLLAKTLARFVNVPFVIADATTLTqAGYVGEDvESILYKLLTVAdynvAAAQQGIVYIDEVDK-ITKKA 304
Cdd:cd19525    58 ILLFGPPGTGKTLIGKCIASQSGATFFSISASSLT-SKWVGEG-EKMVRALFSVA----RCKQPAVIFIDEIDSlLSQRG 131

                  ..
gi 1780585657 305 ES 306
Cdd:cd19525   132 EG 133
RecA-like_KTNA1 cd19522
Katanin p60 ATPase-containing subunit A1; Katanin p60 ATPase-containing subunit A1 (KTNA1) is ...
226-340 1.97e-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: 45.36  E-value: 1.97e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1780585657 226 ILLMGPTGSGKTLLAKTLARFVNVPFVIADATTLTqAGYVGEDvESILYKLLTVADYNVAAAqqgiVYIDEVDKITKK-- 303
Cdd:cd19522    36 VLMVGPPGTGKTLLAKAVATECGTTFFNVSSSTLT-SKYRGES-EKLVRLLFEMARFYAPTT----IFIDEIDSICSRrg 109
                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 1780585657 304 -AESLNISRDVSGEgvqqaLLKMLEGTIVNVPEKGARK 340
Cdd:cd19522   110 tSEEHEASRRVKSE-----LLVQMDGVGGASENDDPSK 142
PTZ00361 PTZ00361
26 proteosome regulatory subunit 4-like protein; Provisional
226-326 1.98e-05

26 proteosome regulatory subunit 4-like protein; Provisional


Pssm-ID: 185575 [Multi-domain]  Cd Length: 438  Bit Score: 47.07  E-value: 1.98e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1780585657 226 ILLMGPTGSGKTLLAKTLARFVNVPFVIADATTLTQAgYVGEDvESILYKLLTVADYNVAAaqqgIVYIDEVDKI-TKKA 304
Cdd:PTZ00361  220 VILYGPPGTGKTLLAKAVANETSATFLRVVGSELIQK-YLGDG-PKLVRELFRVAEENAPS----IVFIDEIDAIgTKRY 293
                          90       100
                  ....*....|....*....|...
gi 1780585657 305 ESlnisrDVSGEG-VQQALLKML 326
Cdd:PTZ00361  294 DA-----TSGGEKeIQRTMLELL 311
RecA-like_FtsH cd19501
ATP-dependent zinc metalloprotease FtsH; FtsH ATPase is a processive, ATP-dependent zinc ...
226-303 3.89e-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: 44.53  E-value: 3.89e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1780585657 226 ILLMGPTGSGKTLLAKTLARFVNVPFVIADATTLTQAgYVGEDVeSILYKLLTVADYNVAAaqqgIVYIDEVDKITKK 303
Cdd:cd19501    40 VLLVGPPGTGKTLLAKAVAGEAGVPFFSISGSDFVEM-FVGVGA-SRVRDLFEQAKKNAPC----IVFIDEIDAVGRK 111
RecA-like_Ycf46-like cd19507
ATPase domain of Ycf46 and similar ATPase domains; Ycf46 may play a role in the regulation of ...
226-299 5.23e-05

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: 43.90  E-value: 5.23e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1780585657 226 ILLMGPTGSGKTLLAKTLARFVNVPFVIADATTLTqAGYVGEDvESILYKLLTVADynvaAAQQGIVYIDEVDK 299
Cdd:cd19507    34 LLLVGIQGTGKSLTAKAIAGVWQLPLLRLDMGRLF-GGLVGES-ESRLRQMIQTAE----AIAPCVLWIDEIEK 101
AAA_5 pfam07728
AAA domain (dynein-related subfamily); This Pfam entry includes some of the AAA proteins not ...
225-308 6.82e-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: 43.05  E-value: 6.82e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1780585657 225 NILLMGPTGSGKTLLAKTLA-RFVNVPFVI----ADATT--LTQ----AGYVGEDVESILyklltvadynVAAAQQG-IV 292
Cdd:pfam07728   1 GVLLVGPPGTGKTELAERLAaALSNRPVFYvqltRDTTEedLFGrrniDPGGASWVDGPL----------VRAAREGeIA 70
                          90
                  ....*....|....*..
gi 1780585657 293 YIDEVDKITKKA-ESLN 308
Cdd:pfam07728  71 VLDEINRANPDVlNSLL 87
PRK13342 PRK13342
recombination factor protein RarA; Reviewed
218-331 9.23e-05

recombination factor protein RarA; Reviewed


Pssm-ID: 237355 [Multi-domain]  Cd Length: 413  Bit Score: 45.08  E-value: 9.23e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1780585657 218 MVELEK-SNILLMGPTGSGKTLLAKTLARFVNVPFVIADATTltqAGyVgEDVESILYKlltvADYNVAAAQQGIVYIDE 296
Cdd:PRK13342   30 MIEAGRlSSMILWGPPGTGKTTLARIIAGATDAPFEALSAVT---SG-V-KDLREVIEE----ARQRRSAGRRTILFIDE 100
                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 1780585657 297 VDKITKKaeslnisrdvsgegvQQ-ALLKMLE-GTIV 331
Cdd:PRK13342  101 IHRFNKA---------------QQdALLPHVEdGTIT 122
PTZ00454 PTZ00454
26S protease regulatory subunit 6B-like protein; Provisional
226-326 1.06e-04

26S protease regulatory subunit 6B-like protein; Provisional


Pssm-ID: 240423 [Multi-domain]  Cd Length: 398  Bit Score: 44.75  E-value: 1.06e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1780585657 226 ILLMGPTGSGKTLLAKTLARFVNVPFVIADATTLTQAgYVGEDVESI--LYKLltvADYNVAAaqqgIVYIDEVDKITKK 303
Cdd:PTZ00454  182 VLLYGPPGTGKTMLAKAVAHHTTATFIRVVGSEFVQK-YLGEGPRMVrdVFRL---ARENAPS----IIFIDEVDSIATK 253
                          90       100
                  ....*....|....*....|...
gi 1780585657 304 AESLNISRDvsgEGVQQALLKML 326
Cdd:PTZ00454  254 RFDAQTGAD---REVQRILLELL 273
RecA-like_ATAD3-like cd19512
ATPase domains of ATPase AAA-domain protein 3A (ATAD3A), -3B, and -3C, and similar ATPase ...
225-312 1.13e-04

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


Pssm-ID: 410920 [Multi-domain]  Cd Length: 150  Bit Score: 42.51  E-value: 1.13e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1780585657 225 NILLMGPTGSGKTLLAKTLARFVNVPFVIadaTTLTQAGYVGEDVESILYKLLtvaDYNVAAAQQGIVYIDEVDKITKKA 304
Cdd:cd19512    24 NILFYGPPGTGKTLFAKKLALHSGMDYAI---MTGGDVAPMGREGVTAIHKVF---DWANTSRRGLLLFVDEADAFLRKR 97

                  ....*...
gi 1780585657 305 ESLNISRD 312
Cdd:cd19512    98 STEKISED 105
RecA-like_CDC48_r2-like cd19528
second of two ATPase domains of CDC48 and similar ATPase domains; CDC48 in yeast and p97 or ...
226-325 3.46e-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: 3.46e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1780585657 226 ILLMGPTGSGKTLLAKTLARFVNVPFVIADATTLTQAgYVGEDvESILYKLLTVAdynvAAAQQGIVYIDEVDKITK-KA 304
Cdd:cd19528    30 VLFYGPPGCGKTLLAKAIANECQANFISVKGPELLTM-WFGES-EANVRDIFDKA----RAAAPCVLFFDELDSIAKaRG 103
                          90       100
                  ....*....|....*....|.
gi 1780585657 305 ESLNISRDVSGEGVQQALLKM 325
Cdd:cd19528   104 GNIGDAGGAADRVINQILTEM 124
PRK03992 PRK03992
proteasome-activating nucleotidase; Provisional
224-326 3.78e-04

proteasome-activating nucleotidase; Provisional


Pssm-ID: 179699 [Multi-domain]  Cd Length: 389  Bit Score: 42.90  E-value: 3.78e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1780585657 224 SNILLMGPTGSGKTLLAKTLARFVNVPFVIADATTLTQAgYVGEDVeSILYKLLTVADYNVAAaqqgIVYIDEVDKI-TK 302
Cdd:PRK03992  166 KGVLLYGPPGTGKTLLAKAVAHETNATFIRVVGSELVQK-FIGEGA-RLVRELFELAREKAPS----IIFIDEIDAIaAK 239
                          90       100
                  ....*....|....*....|....*
gi 1780585657 303 KAESLNisrdvSGEG-VQQALLKML 326
Cdd:PRK03992  240 RTDSGT-----SGDReVQRTLMQLL 259
ruvB PRK00080
Holliday junction branch migration DNA helicase RuvB;
173-305 3.99e-04

Holliday junction branch migration DNA helicase RuvB;


Pssm-ID: 234619 [Multi-domain]  Cd Length: 328  Bit Score: 42.81  E-value: 3.99e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1780585657 173 IGQERAKKVLSVAVynhykriyhESSQKRSagetdstaaKPADddmveleksNILLMGPTGSGKTLLAKTLARFVNVPFV 252
Cdd:PRK00080   28 IGQEKVKENLKIFI---------EAAKKRG---------EALD---------HVLLYGPPGLGKTTLANIIANEMGVNIR 80
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1780585657 253 IADATTLTQAGyvgeDVESILYKLltvadynvaaaQQG-IVYIDEVDKITKKAE 305
Cdd:PRK00080   81 ITSGPALEKPG----DLAAILTNL-----------EEGdVLFIDEIHRLSPVVE 119
ClpA COG0542
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ...
168-246 4.26e-04

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


Pssm-ID: 440308 [Multi-domain]  Cd Length: 836  Bit Score: 43.15  E-value: 4.26e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1780585657 168 LNKFVIGQERAKKVLSVAVynhykriyhessqKRS-AGETDstAAKPadddmveleksnI---LLMGPTGSGKTLLAKTL 243
Cdd:COG0542   547 LHERVIGQDEAVEAVADAI-------------RRSrAGLKD--PNRP------------IgsfLFLGPTGVGKTELAKAL 599

                  ...
gi 1780585657 244 ARF 246
Cdd:COG0542   600 AEF 602
ycf46 CHL00195
Ycf46; Provisional
226-306 6.71e-04

Ycf46; Provisional


Pssm-ID: 177094 [Multi-domain]  Cd Length: 489  Bit Score: 42.31  E-value: 6.71e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1780585657 226 ILLMGPTGSGKTLLAKTLARFVNVPFVIADATTLTqAGYVGEDvESILYKLLTVADynvaAAQQGIVYIDEVDKITKKAE 305
Cdd:CHL00195  262 LLLVGIQGTGKSLTAKAIANDWQLPLLRLDVGKLF-GGIVGES-ESRMRQMIRIAE----ALSPCILWIDEIDKAFSNSE 335

                  .
gi 1780585657 306 S 306
Cdd:CHL00195  336 S 336
RecA-like_PEX1_r2 cd19526
second of two ATPase domains of Peroxisomal biogenesis factor 1 (PEX1); PEX1(also known as ...
223-303 7.34e-04

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


Pssm-ID: 410934 [Multi-domain]  Cd Length: 158  Bit Score: 40.49  E-value: 7.34e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1780585657 223 KSNILLMGPTGSGKTLLAKTLARFVNVPFVIADATTLTqAGYVG---EDVESILYKlltvadynVAAAQQGIVYIDEVDK 299
Cdd:cd19526    27 RSGILLYGPPGCGKTLLASAIASECGLNFISVKGPELL-NKYIGaseQNVRDLFSR--------AQSAKPCILFFDEFDS 97

                  ....
gi 1780585657 300 ITKK 303
Cdd:cd19526    98 IAPK 101
hflB PRK10733
ATP-dependent zinc metalloprotease FtsH;
226-331 8.05e-04

ATP-dependent zinc metalloprotease FtsH;


Pssm-ID: 182683 [Multi-domain]  Cd Length: 644  Bit Score: 42.33  E-value: 8.05e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1780585657 226 ILLMGPTGSGKTLLAKTLARFVNVPFVIADATTLTQAgYVGEDVESI--LYKlltvadyNVAAAQQGIVYIDEVDKITK- 302
Cdd:PRK10733  188 VLMVGPPGTGKTLLAKAIAGEAKVPFFTISGSDFVEM-FVGVGASRVrdMFE-------QAKKAAPCIIFIDEIDAVGRq 259
                          90       100       110
                  ....*....|....*....|....*....|....
gi 1780585657 303 KAESLNISRDVSGEGVQQALLKM-----LEGTIV 331
Cdd:PRK10733  260 RGAGLGGGHDEREQTLNQMLVEMdgfegNEGIIV 293
RecA-like_VPS4 cd19521
ATPase domain of vacuolar protein sorting-associated protein 4; Vacuolar protein ...
224-301 9.70e-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: 9.70e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1780585657 224 SNILLMGPTGSGKTLLAKTLARFVNVPFVIADATTLTqAGYVGEDvESILYKLLTVADYNvaaaQQGIVYIDEVDKIT 301
Cdd:cd19521    41 SGILLYGPPGTGKSYLAKAVATEANSTFFSVSSSDLV-SKWMGES-EKLVKQLFAMAREN----KPSIIFIDEVDSLC 112
SK cd00464
Shikimate kinase (SK) is the fifth enzyme in the shikimate pathway, a seven-step biosynthetic ...
225-255 1.41e-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: 39.46  E-value: 1.41e-03
                          10        20        30
                  ....*....|....*....|....*....|.
gi 1780585657 225 NILLMGPTGSGKTLLAKTLARFVNVPFVIAD 255
Cdd:cd00464     1 NIVLIGMMGAGKTTVGRLLAKALGLPFVDLD 31
RecA-like_VCP_r2 cd19529
second of two ATPase domains of Valosin-containing protein-like ATPase (VAT) and similar ...
226-328 1.42e-03

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


Pssm-ID: 410937 [Multi-domain]  Cd Length: 159  Bit Score: 39.79  E-value: 1.42e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1780585657 226 ILLMGPTGSGKTLLAKTLARFVNVPFVIADATTLTqAGYVGED---VESILYKLLTVAdynvaaaqQGIVYIDEVDKITK 302
Cdd:cd19529    30 ILLYGPPGTGKTLLAKAVATESNANFISVKGPELL-SKWVGESekaIREIFRKARQVA--------PCVIFFDEIDSIAP 100
                          90       100
                  ....*....|....*....|....*.
gi 1780585657 303 KaESLNISRDVSGEGVQQaLLKMLEG 328
Cdd:cd19529   101 R-RGTTGDSGVTERVVNQ-LLTELDG 124
RecA-like_CDC48_r2-like cd19511
second of two ATPase domains of CDC48/p97, PEX1 and -6, VAT and NVL, and similar ATPase ...
226-328 1.72e-03

second of two ATPase domains of CDC48/p97, PEX1 and -6, VAT and NVL, and similar ATPase domains; This subfamily includes the second of two ATPase domains of the molecular chaperone CDC48 in yeast and p97 or VCP in metazoans, Peroxisomal biogenesis factor 1 (PEX1) and -6 (PEX6), Valosin-containing protein-like ATPase (VAT), and nuclear VCP-like protein (NVL). This subfamily belongs to the RecA-like NTPase family which includes the NTP binding domain of F1 and V1 H(+)ATPases, DnaB and related helicases as well as bacterial RecA and related eukaryotic and archaeal recombinases. The RecA-like NTPase family also includes bacterial conjugation proteins and related DNA transfer proteins involved in type II and type IV secretion.


Pssm-ID: 410919 [Multi-domain]  Cd Length: 159  Bit Score: 39.19  E-value: 1.72e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1780585657 226 ILLMGPTGSGKTLLAKTLARFVNVPFV-IADATTLTQagYVGEDvESILYKLLTVAdynvAAAQQGIVYIDEVDKITKKa 304
Cdd:cd19511    30 VLLYGPPGCGKTLLAKALASEAGLNFIsVKGPELFSK--YVGES-ERAVREIFQKA----RQAAPCIIFFDEIDSLAPR- 101
                          90       100
                  ....*....|....*....|....*....
gi 1780585657 305 eslnisRDVSGEG-----VQQALLKMLEG 328
Cdd:cd19511   102 ------RGQSDSSgvtdrVVSQLLTELDG 124
ftsH CHL00176
cell division protein; Validated
226-303 2.08e-03

cell division protein; Validated


Pssm-ID: 214386 [Multi-domain]  Cd Length: 638  Bit Score: 41.19  E-value: 2.08e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1780585657 226 ILLMGPTGSGKTLLAKTLARFVNVPFV-IADATTLTQAGYVGEDVESILYKlltvadynvaAAQQG---IVYIDEVDKIT 301
Cdd:CHL00176  219 VLLVGPPGTGKTLLAKAIAGEAEVPFFsISGSEFVEMFVGVGAARVRDLFK----------KAKENspcIVFIDEIDAVG 288

                  ..
gi 1780585657 302 KK 303
Cdd:CHL00176  289 RQ 290
HflB COG0465
ATP-dependent Zn proteases [Posttranslational modification, protein turnover, chaperones];
226-251 2.38e-03

ATP-dependent Zn proteases [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 440233 [Multi-domain]  Cd Length: 583  Bit Score: 40.79  E-value: 2.38e-03
                          10        20
                  ....*....|....*....|....*.
gi 1780585657 226 ILLMGPTGSGKTLLAKTLARFVNVPF 251
Cdd:COG0465   178 VLLVGPPGTGKTLLAKAVAGEAGVPF 203
RecA-like_PEX6_r2 cd19527
second of two ATPase domains of Peroxisomal biogenesis factor 6 (PEX6); PEX6(also known as ...
222-328 2.52e-03

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: 39.03  E-value: 2.52e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1780585657 222 EKSNILLMGPTGSGKTLLAKTLARFVNVPFVIADATTLTQAgYVGE---DVESILYKlltvadynVAAAQQGIVYIDEVD 298
Cdd:cd19527    25 KRSGILLYGPPGTGKTLLAKAIATECSLNFLSVKGPELINM-YIGEseaNVREVFQK--------ARDAKPCVIFFDELD 95
                          90       100       110
                  ....*....|....*....|....*....|
gi 1780585657 299 KITKKAESLNISRDVSGEGVQQaLLKMLEG 328
Cdd:cd19527    96 SLAPSRGNSGDSGGVMDRVVSQ-LLAELDG 124
FlhF TIGR03499
flagellar biosynthetic protein FlhF; [Cellular processes, Chemotaxis and motility]
212-247 3.59e-03

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


Pssm-ID: 274609 [Multi-domain]  Cd Length: 282  Bit Score: 39.63  E-value: 3.59e-03
                          10        20        30
                  ....*....|....*....|....*....|....*..
gi 1780585657 212 KPADDDMVElEKSNILLMGPTGSGKTL-LAKTLARFV 247
Cdd:TIGR03499 184 KPEEDPILE-QGGVIALVGPTGVGKTTtLAKLAARFA 219
RecA-like_NVL_r2-like cd19530
second of two ATPase domains of NVL (nuclear VCP-like protein) and similar ATPase domains; NVL ...
226-326 3.85e-03

second 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: 410938 [Multi-domain]  Cd Length: 161  Bit Score: 38.24  E-value: 3.85e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1780585657 226 ILLMGPTGSGKTLLAKTLARFVNVPFVIADATTLTQAgYVGEDvESILYKLLTVAdynvAAAQQGIVYIDEVDKITKKae 305
Cdd:cd19530    33 VLLYGPPGCGKTLLAKAVANESGANFISVKGPELLNK-YVGES-ERAVRQVFQRA----RASAPCVIFFDEVDALVPK-- 104
                          90       100
                  ....*....|....*....|.
gi 1780585657 306 slnisRDVSGEGVQQALLKML 326
Cdd:cd19530   105 -----RGDGGSWASERVVNQL 120
PspF COG1221
Transcriptional regulators containing an AAA-type ATPase domain and a DNA-binding domain ...
225-255 5.74e-03

Transcriptional regulators containing an AAA-type ATPase domain and a DNA-binding domain [Transcription, Signal transduction mechanisms];


Pssm-ID: 440834 [Multi-domain]  Cd Length: 835  Bit Score: 39.71  E-value: 5.74e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 1780585657 225 NILLMGPTGSGKTLLAKTLARFV--------NVPFVI---AD 255
Cdd:COG1221   132 HTLILGPTGVGKSFFAELMYEYAieigvlpeDAPFVVfncAD 173
YifB COG0606
Predicted Mg-chelatase, contains ChlI-like and ATPase domains, YifB family [Posttranslational ...
172-243 5.85e-03

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: 39.25  E-value: 5.85e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1780585657 172 VIGQERAKKVLSVAVynhykriyhessqkrsAGetdstaakpadddmveleKSNILLMGPTGSGKTLLAKTL 243
Cdd:COG0606   194 VKGQEQAKRALEIAA----------------AG------------------GHNLLMIGPPGSGKTMLARRL 231
CDC6 COG1474
Cdc6-related protein, AAA superfamily ATPase [Replication, recombination and repair];
224-306 5.93e-03

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


Pssm-ID: 441083 [Multi-domain]  Cd Length: 389  Bit Score: 39.06  E-value: 5.93e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1780585657 224 SNILLMGPTGSGKTLLAKTL-------ARFVNVPFVIA-----DATTLTQA-----------------GYVGEDVESILY 274
Cdd:COG1474    52 SNVLIYGPTGTGKTAVAKYVleeleeeAEERGVDVRVVyvncrQASTRYRVlsrileelgsgedipstGLSTDELFDRLY 131
                          90       100       110
                  ....*....|....*....|....*....|..
gi 1780585657 275 KLLTVADYNVaaaqqgIVYIDEVDKITKKAES 306
Cdd:COG1474   132 EALDERDGVL------VVVLDEIDYLVDDEGD 157
TIGR02928 TIGR02928
orc1/cdc6 family replication initiation protein; Members of this protein family are found ...
224-311 6.60e-03

orc1/cdc6 family replication initiation protein; Members of this protein family are found exclusively in the archaea. This set of DNA binding proteins shows homology to the origin recognition complex subunit 1/cell division control protein 6 family in eukaryotes. Several members may be found in genome and interact with each other. [DNA metabolism, DNA replication, recombination, and repair]


Pssm-ID: 274354 [Multi-domain]  Cd Length: 365  Bit Score: 39.15  E-value: 6.60e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1780585657 224 SNILLMGPTGSGKTLLAKTLARFVN-------VPFVIA-----DATTLTQA--------GYVGEDV------ESILYKLL 277
Cdd:TIGR02928  41 SNVFIYGKTGTGKTAVTKYVMKELEeaaedrdVRVVTVyvncqILDTLYQVlvelanqlRGSGEEVpttglsTSEVFRRL 120
                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 1780585657 278 TvaDYNVAAAQQGIVYIDEVDKITKKAESL--NISR 311
Cdd:TIGR02928 121 Y--KELNERGDSLIIVLDEIDYLVGDDDDLlyQLSR 154
CDC48 TIGR01243
AAA family ATPase, CDC48 subfamily; This subfamily of the AAA family ATPases includes two ...
226-325 6.68e-03

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


Pssm-ID: 273521 [Multi-domain]  Cd Length: 733  Bit Score: 39.51  E-value: 6.68e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1780585657 226 ILLMGPTGSGKTLLAKTLARFVNVPFVIADATTLTqAGYVGEDvESILYKLLTVAdynvAAAQQGIVYIDEVDKITkKAE 305
Cdd:TIGR01243 490 VLLFGPPGTGKTLLAKAVATESGANFIAVRGPEIL-SKWVGES-EKAIREIFRKA----RQAAPAIIFFDEIDAIA-PAR 562
                          90       100
                  ....*....|....*....|
gi 1780585657 306 SLNISRDVSGEGVQQALLKM 325
Cdd:TIGR01243 563 GARFDTSVTDRIVNQLLTEM 582
GntK cd02021
Gluconate kinase (GntK) catalyzes the phosphoryl transfer from ATP to gluconate. The resulting ...
226-256 7.67e-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: 37.23  E-value: 7.67e-03
                          10        20        30
                  ....*....|....*....|....*....|.
gi 1780585657 226 ILLMGPTGSGKTLLAKTLARFVNVPFVIADA 256
Cdd:cd02021     2 IVVMGVSGSGKSTVGKALAERLGAPFIDGDD 32
ClpA COG0542
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ...
418-498 8.03e-03

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


Pssm-ID: 440308 [Multi-domain]  Cd Length: 836  Bit Score: 39.29  E-value: 8.03e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1780585657 418 PEFVGRFPVLVSLSALTENQLMQVLtepKNALGKQYKKMYQMNsVKLHFTESALRLIARKAITKNTGARGLRALLESILM 497
Cdd:COG0542   733 PEFLNRIDEIIVFHPLSKEELRKIV---DLQLKRLRKRLAERG-ITLELTDAAKDFLAEKGYDPEYGARPLKRAIQRELE 808

                  .
gi 1780585657 498 D 498
Cdd:COG0542   809 D 809
MoxR COG0714
MoxR-like ATPase [General function prediction only]; MoxR-like ATPase is part of the Pathway ...
226-251 9.41e-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: 38.22  E-value: 9.41e-03
                          10        20
                  ....*....|....*....|....*.
gi 1780585657 226 ILLMGPTGSGKTLLAKTLARFVNVPF 251
Cdd:COG0714    34 LLLEGVPGVGKTTLAKALARALGLPF 59
 
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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