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Conserved domains on  [gi|488971989|ref|WP_002882917|]
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MULTISPECIES: HslU--HslV peptidase ATPase subunit [Klebsiella]

Protein Classification

ATP-dependent protease ATPase subunit HslU( domain architecture ID 11480440)

ATP-dependent protease ATPase subunit HslU is the ATPase component of a proteasome-like degradation complex and has chaperone activity

CATH:  1.10.8.10|3.40.50.300|1.10.8.60
Gene Ontology:  GO:0006508|GO:0004176|GO:0005524|GO:0016887|GO:0036402
SCOP:  4000283

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
hslU PRK05201
ATP-dependent protease ATPase subunit HslU;
1-444 0e+00

ATP-dependent protease ATPase subunit HslU;


:

Pssm-ID: 235364 [Multi-domain]  Cd Length: 443  Bit Score: 932.95  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488971989   1 MSEMTPREIVSELDKHIIGQDAAKRSVAIALRNRWRRMQLNEELRHEVTPKNILMIGPTGVGKTEIARRLAKLANAPFIK 80
Cdd:PRK05201   1 MSELTPREIVSELDKYIIGQDDAKRAVAIALRNRWRRMQLPEELRDEVTPKNILMIGPTGVGKTEIARRLAKLANAPFIK 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488971989  81 VEATKFTEVGYVGKEVDSIIRDLTDAAIKMVRMQSIDKNRYRAEELAEERVLDVLIPPAKNNWGQTEPSQEPSAARQAFR 160
Cdd:PRK05201  81 VEATKFTEVGYVGRDVESIIRDLVEIAVKMVREEKREKVREKAEEAAEERILDALLPPAKNNWGEEEEKEEISATRQKFR 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488971989 161 KKLREGQLDDKEIEIDLAAAPMGVEIMSPPGMEEMTSQLQSMFQNLGGQKQKPRKLKIKDAMKLLIEEEAAKLVNPEELK 240
Cdd:PRK05201 161 KKLREGELDDKEIEIEVAEAAPMMEIMGPPGMEEMTIQLQDMFGNLGPKKKKKRKLKVKEARKILIEEEAAKLIDMEEIK 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488971989 241 QEAIDAVEQHGIVFIDEIDKICKRGGNtSGPDVSREGVQRDLLPLVEGCTVSTKHGMVKTDHILFIASGAFQVASPSDLI 320
Cdd:PRK05201 241 QEAIERVEQNGIVFIDEIDKIAARGGS-SGPDVSREGVQRDLLPLVEGSTVSTKYGMVKTDHILFIASGAFHVSKPSDLI 319

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488971989 321 PELQGRLPIRVELKALTTHDFERILTEPNASITVQYKALMATEGVNIEFTEDGIKRIAQAAWQVNETTENIGARRLHTVL 400
Cdd:PRK05201 320 PELQGRFPIRVELDALTEEDFVRILTEPKASLIKQYQALLATEGVTLEFTDDAIRRIAEIAYQVNEKTENIGARRLHTVM 399

                        410       420       430       440
                 ....*....|....*....|....*....|....*....|....
gi 488971989 401 ERLVEDISYDASEMNGQTVTIDAEYVSKHLDVLVADEDLSRFIL 444
Cdd:PRK05201 400 EKLLEDISFEAPDMSGETVTIDAAYVDEKLGDLVKDEDLSRYIL 443
 
Name Accession Description Interval E-value
hslU PRK05201
ATP-dependent protease ATPase subunit HslU;
1-444 0e+00

ATP-dependent protease ATPase subunit HslU;


Pssm-ID: 235364 [Multi-domain]  Cd Length: 443  Bit Score: 932.95  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488971989   1 MSEMTPREIVSELDKHIIGQDAAKRSVAIALRNRWRRMQLNEELRHEVTPKNILMIGPTGVGKTEIARRLAKLANAPFIK 80
Cdd:PRK05201   1 MSELTPREIVSELDKYIIGQDDAKRAVAIALRNRWRRMQLPEELRDEVTPKNILMIGPTGVGKTEIARRLAKLANAPFIK 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488971989  81 VEATKFTEVGYVGKEVDSIIRDLTDAAIKMVRMQSIDKNRYRAEELAEERVLDVLIPPAKNNWGQTEPSQEPSAARQAFR 160
Cdd:PRK05201  81 VEATKFTEVGYVGRDVESIIRDLVEIAVKMVREEKREKVREKAEEAAEERILDALLPPAKNNWGEEEEKEEISATRQKFR 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488971989 161 KKLREGQLDDKEIEIDLAAAPMGVEIMSPPGMEEMTSQLQSMFQNLGGQKQKPRKLKIKDAMKLLIEEEAAKLVNPEELK 240
Cdd:PRK05201 161 KKLREGELDDKEIEIEVAEAAPMMEIMGPPGMEEMTIQLQDMFGNLGPKKKKKRKLKVKEARKILIEEEAAKLIDMEEIK 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488971989 241 QEAIDAVEQHGIVFIDEIDKICKRGGNtSGPDVSREGVQRDLLPLVEGCTVSTKHGMVKTDHILFIASGAFQVASPSDLI 320
Cdd:PRK05201 241 QEAIERVEQNGIVFIDEIDKIAARGGS-SGPDVSREGVQRDLLPLVEGSTVSTKYGMVKTDHILFIASGAFHVSKPSDLI 319

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488971989 321 PELQGRLPIRVELKALTTHDFERILTEPNASITVQYKALMATEGVNIEFTEDGIKRIAQAAWQVNETTENIGARRLHTVL 400
Cdd:PRK05201 320 PELQGRFPIRVELDALTEEDFVRILTEPKASLIKQYQALLATEGVTLEFTDDAIRRIAEIAYQVNEKTENIGARRLHTVM 399

                        410       420       430       440
                 ....*....|....*....|....*....|....*....|....
gi 488971989 401 ERLVEDISYDASEMNGQTVTIDAEYVSKHLDVLVADEDLSRFIL 444
Cdd:PRK05201 400 EKLLEDISFEAPDMSGETVTIDAAYVDEKLGDLVKDEDLSRYIL 443
HslU COG1220
ATP-dependent protease HslVU (ClpYQ), ATPase subunit HslU [Posttranslational modification, ...
 1-444 0e+00

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


Pssm-ID: 440833 [Multi-domain]  Cd Length: 454  Bit Score: 904.03  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488971989   1 MSEMTPREIVSELDKHIIGQDAAKRSVAIALRNRWRRMQLNEELRHEVTPKNILMIGPTGVGKTEIARRLAKLANAPFIK 80
Cdd:COG1220    1 MSELTPREIVAELDKYIIGQDEAKRAVAIALRNRWRRQQLPEELRDEITPKNILMIGPTGVGKTEIARRLAKLANAPFIK 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488971989  81 VEATKFTEVGYVGKEVDSIIRDLTDAAIKMVRMQSIDKNRYRAEELAEERVLDVLIPPAKNNWGQ----------TEPSQ 150
Cdd:COG1220   81 VEATKFTEVGYVGRDVESMIRDLVEIAVKMVREEKMEKVREKAEEAAEERILDLLLPPPKKKAGSnnpfeeeeeeEEEEE 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488971989 151 EPSAARQAFRKKLREGQLDDKEIEIDLAAAP-MGVEIMSPPGMEEMTSQLQSMFQNLGGQKQKPRKLKIKDAMKLLIEEE 229
Cdd:COG1220  161 EISRTREKFRKKLREGELDDREIEIEVEESSsPGVEIMGPPGMEEMGMNLQDMFGNLMPKKKKKRKVKVKEARKILTQEE 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488971989 230 AAKLVNPEELKQEAIDAVEQHGIVFIDEIDKICKRGGnTSGPDVSREGVQRDLLPLVEGCTVSTKHGMVKTDHILFIASG 309
Cdd:COG1220  241 AAKLIDMDEVKQEAIERAEQNGIIFIDEIDKIASRGG-GSGPDVSREGVQRDLLPIVEGSTVNTKYGMVKTDHILFIAAG 319

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488971989 310 AFQVASPSDLIPELQGRLPIRVELKALTTHDFERILTEPNASITVQYKALMATEGVNIEFTEDGIKRIAQAAWQVNETTE 389
Cdd:COG1220  320 AFHVSKPSDLIPELQGRFPIRVELDSLTEEDFVRILTEPKNALTKQYQALLATEGVELEFTDDAIREIAEIAFEVNERTE 399

                        410       420       430       440       450
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 488971989 390 NIGARRLHTVLERLVEDISYDASEMNGQTVTIDAEYVSKHLDVLVADEDLSRFIL 444
Cdd:COG1220  400 NIGARRLHTVMEKLLEDISFEAPDLSGKTVVIDAAYVDEKLGDIVKDEDLSRYIL 454
hslU TIGR00390
ATP-dependent protease HslVU, ATPase subunit; This model represents the ATPase subunit of ...
 4-444 0e+00

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: 752.80  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488971989    4 MTPREIVSELDKHIIGQDAAKRSVAIALRNRWRRMQLNEELRHEVTPKNILMIGPTGVGKTEIARRLAKLANAPFIKVEA 83
Cdd:TIGR00390   1 MTPREIVAELDKYIIGQDNAKKSVAIALRNRYRRSQLNEELKDEVTPKNILMIGPTGVGKTEIARRLAKLANAPFIKVEA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488971989   84 TKFTEVGYVGKEVDSIIRDLTDAAIKMVRMQSIDKNRYRAEELAEERVLDVLIPPAKNNWGQTEPSQEPSAARQAFRKKL 163
Cdd:TIGR00390  81 TKFTEVGYVGRDVESMVRDLTDAAVKLVKEEAIEKVRDRAEELAEERIVDVLLPPAKNQWGQTEQQQEPESAREAFRKKL 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488971989  164 REGQLDDKEIEIDLAAA-PMGVEIMSPPGMEEMTSQLQSMFQNLGGQKQKPRKLKIKDAMKLLIEEEAAKLVNPEELKQE 242
Cdd:TIGR00390 161 REGELDDKEIEIDVSAKmPSGIEIMAPPGMEEMTMQLQSLFQNLGGQKKKKRKLKIKDAKKALIAEEAAKLVDPEEIKQE 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488971989  243 AIDAVEQHGIVFIDEIDKICKRGgNTSGPDVSREGVQRDLLPLVEGCTVSTKHGMVKTDHILFIASGAFQVASPSDLIPE 322
Cdd:TIGR00390 241 AIDAVEQSGIIFIDEIDKIAKKG-ESSGADVSREGVQRDLLPIVEGSTVNTKYGMVKTDHILFIAAGAFQLAKPSDLIPE 319

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488971989  323 LQGRLPIRVELKALTTHDFERILTEPNASITVQYKALMATEGVNIEFTEDGIKRIAQAAWQVNETTENIGARRLHTVLER 402
Cdd:TIGR00390 320 LQGRFPIRVELQALTTDDFERILTEPKNSLIKQYKALMKTEGVNIEFSDEAIKRIAELAYNVNEKTENIGARRLHTVLER 399

                         410       420       430       440
                  ....*....|....*....|....*....|....*....|..
gi 488971989  403 LVEDISYDASEMNGQTVTIDAEYVSKHLDVLVADEDLSRFIL 444
Cdd:TIGR00390 400 LLEDISFEAPDLSGQNITIDADYVSKKLGALVADEDLSRFIL 441
RecA-like_HslU cd19498
ATP-dependent protease ATPase subunit HslU; HslU is a component of the ATP-dependent protease ...
 5-333 5.30e-107

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: 314.32  E-value: 5.30e-107
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488971989   5 TPREIVSELDKHIIGQDAAKRSVAIALRNRWRRMQLNEELRHEVTPKNILMIGPTGVGKTEIARRLAKLANAPFIKVEAT 84
Cdd:cd19498    1 TPREIVSELDKYIIGQDEAKRAVAIALRNRWRRMQLPEELRDEVTPKNILMIGPTGVGKTEIARRLAKLAGAPFIKVEAT 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488971989  85 KFTEVGYVGKEVDSIIRDLTDaaikmvrmqsidknryraeelaeervldvlippaknnwgqtepsqepsaarqafrkklr 164
Cdd:cd19498   81 KFTEVGYVGRDVESIIRDLVE----------------------------------------------------------- 101

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488971989 165 egqlddkeieidlaaapmgveimsppgmeemtsqlqsmfqnlggqkqkprklkikdamkllieeeaaklvnpeelkqeai 244
Cdd:cd19498      --------------------------------------------------------------------------------

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488971989 245 daveqhGIVFIDEIDKICKRGGnTSGPDVSREGVQRDLLPLVEGCTVSTKHGMVKTDHILFIASGAFQVASPSDLIPELQ 324
Cdd:cd19498  102 ------GIVFIDEIDKIAKRGG-SSGPDVSREGVQRDLLPIVEGSTVSTKYGPVKTDHILFIAAGAFHVAKPSDLIPELQ 174


                 ....*....
gi 488971989 325 GRLPIRVEL 333
Cdd:cd19498  175 GRFPIRVEL 183
AAA_2 pfam07724
AAA domain (Cdc48 subfamily); This Pfam entry includes some of the AAA proteins not detected ...
 170-330 1.60e-28

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: 110.36  E-value: 1.60e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488971989  170 DKEIEIDLAAaPMGVeimSPPGMEEMTSQLQSMFQnlggqkqkpRKLKIKDAMKLLIEeeaaKLVNPEELKQEAIDAVEQ 249
Cdd:pfam07724   1 RPIGSFLFLG-PTGV---GKTELAKALAELLFGDE---------RALIRIDMSEYMEE----HSVSRLIGAPPGYVGYEE 63

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488971989  250 HG------------IVFIDEIDKICKrggntsgpdvsreGVQRDLLPLVEGCTVSTKHG-MVKTDHILFIASGAFQVASP 316
Cdd:pfam07724  64 GGqlteavrrkpysIVLIDEIEKAHP-------------GVQNDLLQILEGGTLTDKQGrTVDFKNTLFIMTGNFGSEKI 130

                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 488971989  317 SD------------------------LIPELQGRLPIR 330
Cdd:pfam07724 131 SDasrlgdspdyellkeevmdllkkgFIPEFLGRLPII 168
ClpB_D2-small smart01086
C-terminal, D2-small domain, of ClpB protein; This is the C-terminal domain of ClpB protein, ...
 336-424 1.24e-12

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: 63.23  E-value: 1.24e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488971989   336 LTTHDFERILTEPNASITVQYkalmATEGVNIEFTEDGIKRIAQAAWQvnettENIGARRLHTVLERLVEDISYDA---- 411
Cdd:smart01086   1 LDKEDLVRIVDLPLNALQKRL----AEKGITLEFTDEALDWLAEKGYD-----PKYGARPLRRIIQRELEDPLAELilsg 71

                           90
                   ....*....|...
gi 488971989   412 SEMNGQTVTIDAE 424
Cdd:smart01086  72 ELKDGDTVVVDVD 84
 
Name Accession Description Interval E-value
hslU PRK05201
ATP-dependent protease ATPase subunit HslU;
1-444 0e+00

ATP-dependent protease ATPase subunit HslU;


Pssm-ID: 235364 [Multi-domain]  Cd Length: 443  Bit Score: 932.95  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488971989   1 MSEMTPREIVSELDKHIIGQDAAKRSVAIALRNRWRRMQLNEELRHEVTPKNILMIGPTGVGKTEIARRLAKLANAPFIK 80
Cdd:PRK05201   1 MSELTPREIVSELDKYIIGQDDAKRAVAIALRNRWRRMQLPEELRDEVTPKNILMIGPTGVGKTEIARRLAKLANAPFIK 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488971989  81 VEATKFTEVGYVGKEVDSIIRDLTDAAIKMVRMQSIDKNRYRAEELAEERVLDVLIPPAKNNWGQTEPSQEPSAARQAFR 160
Cdd:PRK05201  81 VEATKFTEVGYVGRDVESIIRDLVEIAVKMVREEKREKVREKAEEAAEERILDALLPPAKNNWGEEEEKEEISATRQKFR 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488971989 161 KKLREGQLDDKEIEIDLAAAPMGVEIMSPPGMEEMTSQLQSMFQNLGGQKQKPRKLKIKDAMKLLIEEEAAKLVNPEELK 240
Cdd:PRK05201 161 KKLREGELDDKEIEIEVAEAAPMMEIMGPPGMEEMTIQLQDMFGNLGPKKKKKRKLKVKEARKILIEEEAAKLIDMEEIK 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488971989 241 QEAIDAVEQHGIVFIDEIDKICKRGGNtSGPDVSREGVQRDLLPLVEGCTVSTKHGMVKTDHILFIASGAFQVASPSDLI 320
Cdd:PRK05201 241 QEAIERVEQNGIVFIDEIDKIAARGGS-SGPDVSREGVQRDLLPLVEGSTVSTKYGMVKTDHILFIASGAFHVSKPSDLI 319

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488971989 321 PELQGRLPIRVELKALTTHDFERILTEPNASITVQYKALMATEGVNIEFTEDGIKRIAQAAWQVNETTENIGARRLHTVL 400
Cdd:PRK05201 320 PELQGRFPIRVELDALTEEDFVRILTEPKASLIKQYQALLATEGVTLEFTDDAIRRIAEIAYQVNEKTENIGARRLHTVM 399

                        410       420       430       440
                 ....*....|....*....|....*....|....*....|....
gi 488971989 401 ERLVEDISYDASEMNGQTVTIDAEYVSKHLDVLVADEDLSRFIL 444
Cdd:PRK05201 400 EKLLEDISFEAPDMSGETVTIDAAYVDEKLGDLVKDEDLSRYIL 443
HslU COG1220
ATP-dependent protease HslVU (ClpYQ), ATPase subunit HslU [Posttranslational modification, ...
 1-444 0e+00

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


Pssm-ID: 440833 [Multi-domain]  Cd Length: 454  Bit Score: 904.03  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488971989   1 MSEMTPREIVSELDKHIIGQDAAKRSVAIALRNRWRRMQLNEELRHEVTPKNILMIGPTGVGKTEIARRLAKLANAPFIK 80
Cdd:COG1220    1 MSELTPREIVAELDKYIIGQDEAKRAVAIALRNRWRRQQLPEELRDEITPKNILMIGPTGVGKTEIARRLAKLANAPFIK 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488971989  81 VEATKFTEVGYVGKEVDSIIRDLTDAAIKMVRMQSIDKNRYRAEELAEERVLDVLIPPAKNNWGQ----------TEPSQ 150
Cdd:COG1220   81 VEATKFTEVGYVGRDVESMIRDLVEIAVKMVREEKMEKVREKAEEAAEERILDLLLPPPKKKAGSnnpfeeeeeeEEEEE 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488971989 151 EPSAARQAFRKKLREGQLDDKEIEIDLAAAP-MGVEIMSPPGMEEMTSQLQSMFQNLGGQKQKPRKLKIKDAMKLLIEEE 229
Cdd:COG1220  161 EISRTREKFRKKLREGELDDREIEIEVEESSsPGVEIMGPPGMEEMGMNLQDMFGNLMPKKKKKRKVKVKEARKILTQEE 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488971989 230 AAKLVNPEELKQEAIDAVEQHGIVFIDEIDKICKRGGnTSGPDVSREGVQRDLLPLVEGCTVSTKHGMVKTDHILFIASG 309
Cdd:COG1220  241 AAKLIDMDEVKQEAIERAEQNGIIFIDEIDKIASRGG-GSGPDVSREGVQRDLLPIVEGSTVNTKYGMVKTDHILFIAAG 319

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488971989 310 AFQVASPSDLIPELQGRLPIRVELKALTTHDFERILTEPNASITVQYKALMATEGVNIEFTEDGIKRIAQAAWQVNETTE 389
Cdd:COG1220  320 AFHVSKPSDLIPELQGRFPIRVELDSLTEEDFVRILTEPKNALTKQYQALLATEGVELEFTDDAIREIAEIAFEVNERTE 399

                        410       420       430       440       450
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 488971989 390 NIGARRLHTVLERLVEDISYDASEMNGQTVTIDAEYVSKHLDVLVADEDLSRFIL 444
Cdd:COG1220  400 NIGARRLHTVMEKLLEDISFEAPDLSGKTVVIDAAYVDEKLGDIVKDEDLSRYIL 454
hslU TIGR00390
ATP-dependent protease HslVU, ATPase subunit; This model represents the ATPase subunit of ...
 4-444 0e+00

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: 752.80  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488971989    4 MTPREIVSELDKHIIGQDAAKRSVAIALRNRWRRMQLNEELRHEVTPKNILMIGPTGVGKTEIARRLAKLANAPFIKVEA 83
Cdd:TIGR00390   1 MTPREIVAELDKYIIGQDNAKKSVAIALRNRYRRSQLNEELKDEVTPKNILMIGPTGVGKTEIARRLAKLANAPFIKVEA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488971989   84 TKFTEVGYVGKEVDSIIRDLTDAAIKMVRMQSIDKNRYRAEELAEERVLDVLIPPAKNNWGQTEPSQEPSAARQAFRKKL 163
Cdd:TIGR00390  81 TKFTEVGYVGRDVESMVRDLTDAAVKLVKEEAIEKVRDRAEELAEERIVDVLLPPAKNQWGQTEQQQEPESAREAFRKKL 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488971989  164 REGQLDDKEIEIDLAAA-PMGVEIMSPPGMEEMTSQLQSMFQNLGGQKQKPRKLKIKDAMKLLIEEEAAKLVNPEELKQE 242
Cdd:TIGR00390 161 REGELDDKEIEIDVSAKmPSGIEIMAPPGMEEMTMQLQSLFQNLGGQKKKKRKLKIKDAKKALIAEEAAKLVDPEEIKQE 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488971989  243 AIDAVEQHGIVFIDEIDKICKRGgNTSGPDVSREGVQRDLLPLVEGCTVSTKHGMVKTDHILFIASGAFQVASPSDLIPE 322
Cdd:TIGR00390 241 AIDAVEQSGIIFIDEIDKIAKKG-ESSGADVSREGVQRDLLPIVEGSTVNTKYGMVKTDHILFIAAGAFQLAKPSDLIPE 319

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488971989  323 LQGRLPIRVELKALTTHDFERILTEPNASITVQYKALMATEGVNIEFTEDGIKRIAQAAWQVNETTENIGARRLHTVLER 402
Cdd:TIGR00390 320 LQGRFPIRVELQALTTDDFERILTEPKNSLIKQYKALMKTEGVNIEFSDEAIKRIAELAYNVNEKTENIGARRLHTVLER 399

                         410       420       430       440
                  ....*....|....*....|....*....|....*....|..
gi 488971989  403 LVEDISYDASEMNGQTVTIDAEYVSKHLDVLVADEDLSRFIL 444
Cdd:TIGR00390 400 LLEDISFEAPDLSGQNITIDADYVSKKLGALVADEDLSRFIL 441
RecA-like_HslU cd19498
ATP-dependent protease ATPase subunit HslU; HslU is a component of the ATP-dependent protease ...
 5-333 5.30e-107

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: 314.32  E-value: 5.30e-107
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488971989   5 TPREIVSELDKHIIGQDAAKRSVAIALRNRWRRMQLNEELRHEVTPKNILMIGPTGVGKTEIARRLAKLANAPFIKVEAT 84
Cdd:cd19498    1 TPREIVSELDKYIIGQDEAKRAVAIALRNRWRRMQLPEELRDEVTPKNILMIGPTGVGKTEIARRLAKLAGAPFIKVEAT 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488971989  85 KFTEVGYVGKEVDSIIRDLTDaaikmvrmqsidknryraeelaeervldvlippaknnwgqtepsqepsaarqafrkklr 164
Cdd:cd19498   81 KFTEVGYVGRDVESIIRDLVE----------------------------------------------------------- 101

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488971989 165 egqlddkeieidlaaapmgveimsppgmeemtsqlqsmfqnlggqkqkprklkikdamkllieeeaaklvnpeelkqeai 244
Cdd:cd19498      --------------------------------------------------------------------------------

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488971989 245 daveqhGIVFIDEIDKICKRGGnTSGPDVSREGVQRDLLPLVEGCTVSTKHGMVKTDHILFIASGAFQVASPSDLIPELQ 324
Cdd:cd19498  102 ------GIVFIDEIDKIAKRGG-SSGPDVSREGVQRDLLPIVEGSTVSTKYGPVKTDHILFIAAGAFHVAKPSDLIPELQ 174


                 ....*....
gi 488971989 325 GRLPIRVEL 333
Cdd:cd19498  175 GRFPIRVEL 183
clpX PRK05342
ATP-dependent Clp protease ATP-binding subunit ClpX;
5-429 8.72e-65

ATP-dependent Clp protease ATP-binding subunit ClpX;


Pssm-ID: 235422 [Multi-domain]  Cd Length: 412  Bit Score: 213.87  E-value: 8.72e-65
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488971989   5 TPREIVSELDKHIIGQDAAKRSVAIALRNRWRRMQLNEELRHEV--TPKNILMIGPTGVGKTEIARRLAKLANAPFIKVE 82
Cdd:PRK05342  61 TPKEIKAHLDQYVIGQERAKKVLSVAVYNHYKRLRHGDKKDDDVelQKSNILLIGPTGSGKTLLAQTLARILDVPFAIAD 140

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488971989  83 ATKFTEVGYVGKEVDSIIRDLTDAAikmvrmqsidknryraeelaeervldvlippaknnwgqtepsqepsaarqafrkk 162
Cdd:PRK05342 141 ATTLTEAGYVGEDVENILLKLLQAA------------------------------------------------------- 165

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488971989 163 lregqlddkeiEIDLAAApmgveimsppgmeemtsqlqsmfqnlggqkqkprklkikdamkllieeeaaklvnpeelkqe 242
Cdd:PRK05342 166 -----------DYDVEKA-------------------------------------------------------------- 172

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488971989 243 aidaveQHGIVFIDEIDKICKRGGNTSG-PDVSREGVQRDLLPLVEGCTVST------KHGM-----VKTDHILFIASGA 310
Cdd:PRK05342 173 ------QRGIVYIDEIDKIARKSENPSItRDVSGEGVQQALLKILEGTVASVppqggrKHPQqefiqVDTTNILFICGGA 246

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488971989 311 F-----------------------------------QVASPSDL-----IPELQGRLPIRVELKALTTHDFERILTEPNA 350
Cdd:PRK05342 247 FdglekiikqrlgkkgigfgaevkskkekrtegellKQVEPEDLikfglIPEFIGRLPVVATLEELDEEALVRILTEPKN 326

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488971989 351 SITVQYKALMATEGVNIEFTEDGIKRIAQAAWQvnettENIGARRLHTVLERLVEDISYDA-SEMNGQTVTIDAEYVSKH 429
Cdd:PRK05342 327 ALVKQYQKLFEMDGVELEFTDEALEAIAKKAIE-----RKTGARGLRSILEEILLDVMFELpSREDVEKVVITKEVVEGK 401
ClpX COG1219
ATP-dependent protease Clp, ATPase subunit ClpX [Posttranslational modification, protein ...
 5-434 8.05e-61

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


Pssm-ID: 440832 [Multi-domain]  Cd Length: 409  Bit Score: 203.36  E-value: 8.05e-61
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488971989   5 TPREIVSELDKHIIGQDAAKRSVAIALRNRWRRMQLNEELRHEVT-PK-NILMIGPTGVGKTEIARRLAKLANAPFIKVE 82
Cdd:COG1219   62 KPKEIKAFLDEYVIGQERAKKVLSVAVYNHYKRLNSGSKDDDDVElEKsNILLIGPTGSGKTLLAQTLARILDVPFAIAD 141

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488971989  83 ATKFTEVGYVGKEVDSIIRDLTDAAikmvrmqsidknryraeelaeervldvlippaknnwgqtepsqepsaarqafrkk 162
Cdd:COG1219  142 ATTLTEAGYVGEDVENILLKLLQAA------------------------------------------------------- 166

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488971989 163 lregqlddkeiEIDLAAApmgveimsppgmeemtsqlqsmfqnlggqkqkprklkikdamkllieeeaaklvnpeelkqe 242
Cdd:COG1219  167 -----------DYDVEKA-------------------------------------------------------------- 173

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488971989 243 aidaveQHGIVFIDEIDKICKRGGNTSGP-DVSREGVQRDLLPLVEGCTVST------KHGM-----VKTDHILFIASGA 310
Cdd:COG1219  174 ------ERGIIYIDEIDKIARKSENPSITrDVSGEGVQQALLKILEGTVANVppqggrKHPQqefiqIDTTNILFICGGA 247

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488971989 311 F--------------------QVASPSD-------------------LIPELQGRLPIRVELKALTTHDFERILTEPNAS 351
Cdd:COG1219  248 FdglekiierrlgkksigfgaEVKSKKEkdegellkqvepedlikfgLIPEFIGRLPVIATLEELDEEALVRILTEPKNA 327

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488971989 352 ITVQYKALMATEGVNIEFTEDGIKRIAQAAWQvnettENIGARRLHTVLERLVEDISYDA-SEMNGQTVTIDAEYVSKHL 430
Cdd:COG1219  328 LVKQYQKLFEMDGVELEFTDEALEAIAKKAIE-----RKTGARGLRSILEEILLDVMYELpSRKDVKKVVITKEVVEGKA 402


                 ....
gi 488971989 431 DVLV 434
Cdd:COG1219  403 KPIL 406
clpX TIGR00382
endopeptidase Clp ATP-binding regulatory subunit (clpX); A member of the ATP-dependent ...
 5-428 1.02e-38

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: 144.52  E-value: 1.02e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488971989    5 TPREIVSELDKHIIGQDAAKRSVAIALRNRWRRMQLNEELRH----EVTPKNILMIGPTGVGKTEIARRLAKLANAPFIK 80
Cdd:TIGR00382  67 TPKEIKAHLDEYVIGQEQAKKVLSVAVYNHYKRLNFEKNKKSdngvELSKSNILLIGPTGSGKTLLAQTLARILNVPFAI 146

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488971989   81 VEATKFTEVGYVGKEVDSIirdltdaaikmvrmqsidknryraeelaeervldvlippaknnwgqtepsqepsaarqafr 160
Cdd:TIGR00382 147 ADATTLTEAGYVGEDVENI------------------------------------------------------------- 165

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488971989  161 kklregqlddkeieidlaaapmgveimsppgmeemtsqLQSMFQNLGGQKQKPRKlkikdamkllieeeaaklvnpeelk 240
Cdd:TIGR00382 166 --------------------------------------LLKLLQAADYDVEKAQK------------------------- 182

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488971989  241 qeaidaveqhGIVFIDEIDKICKRGGNTS-GPDVSREGVQRDLLPLVEGCTVST------KHG-----MVKTDHILFIAS 308
Cdd:TIGR00382 183 ----------GIIYIDEIDKISRKSENPSiTRDVSGEGVQQALLKIIEGTVANVppqggrKHPyqefiQIDTSNILFICG 252

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488971989  309 GAF---------------------------------QVASPSD-----LIPELQGRLPIRVELKALTTHDFERILTEPNA 350
Cdd:TIGR00382 253 GAFvglekiikkrtgkssigfgaevkkkskekadllRQVEPEDlvkfgLIPEFIGRLPVIATLEKLDEEALIAILTKPKN 332

                         410       420       430       440       450       460       470
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 488971989  351 SITVQYKALMATEGVNIEFTEDGIKRIAQAAWQvnettENIGARRLHTVLERLVEDISYDASEM-NGQTVTIDAEYVSK 428
Cdd:TIGR00382 333 ALVKQYQALFKMDNVELDFEEEALKAIAKKALE-----RKTGARGLRSIVEGLLLDVMFDLPSLeDLEKVVITKETVLK 406
RecA-like_ClpX cd19497
ATP-dependent Clp protease ATP-binding subunit ClpX; ClpX is a component of the ATP-dependent ...
 5-333 3.02e-35

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: 131.18  E-value: 3.02e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488971989   5 TPREIVSELDKHIIGQDAAKRSVAIALRNRWRRMQLNEELRH---EVTPKNILMIGPTGVGKTEIARRLAKLANAPFIKV 81
Cdd:cd19497    2 TPKEIKEHLDKYVIGQERAKKVLSVAVYNHYKRIRNNLKQKDddvELEKSNILLIGPTGSGKTLLAQTLAKILDVPFAIA 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488971989  82 EATKFTEVGYVGKEVDSIIRDLTDAAikmvrmqsidknryraeelaeervldvlippaknnwgqtepsqepsaarqafrk 161
Cdd:cd19497   82 DATTLTEAGYVGEDVENILLKLLQAA------------------------------------------------------ 107

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488971989 162 klregqlddkeiEIDLAAApmgveimsppgmeemtsqlqsmfqnlggqkqkprklkikdamkllieeeaaklvnpeelkq 241
Cdd:cd19497  108 ------------DYDVERA------------------------------------------------------------- 114

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488971989 242 eaidaveQHGIVFIDEIDKICKRGGNTSGP-DVSREGVQRDLLPLVEGCTVST------KHG-----MVKTDHILFIASG 309
Cdd:cd19497  115 -------QRGIVYIDEIDKIARKSENPSITrDVSGEGVQQALLKILEGTVANVppqggrKHPqqefiQVDTTNILFICGG 187

                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 488971989 310 AF-----------------------------------QVASPSDL-----IPELQGRLPIRVEL 333
Cdd:cd19497  188 AFvglekiiarrlgkkslgfgaetssekdekerdellSKVEPEDLikfglIPEFVGRLPVIVTL 251
AAA_2 pfam07724
AAA domain (Cdc48 subfamily); This Pfam entry includes some of the AAA proteins not detected ...
 170-330 1.60e-28

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: 110.36  E-value: 1.60e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488971989  170 DKEIEIDLAAaPMGVeimSPPGMEEMTSQLQSMFQnlggqkqkpRKLKIKDAMKLLIEeeaaKLVNPEELKQEAIDAVEQ 249
Cdd:pfam07724   1 RPIGSFLFLG-PTGV---GKTELAKALAELLFGDE---------RALIRIDMSEYMEE----HSVSRLIGAPPGYVGYEE 63

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488971989  250 HG------------IVFIDEIDKICKrggntsgpdvsreGVQRDLLPLVEGCTVSTKHG-MVKTDHILFIASGAFQVASP 316
Cdd:pfam07724  64 GGqlteavrrkpysIVLIDEIEKAHP-------------GVQNDLLQILEGGTLTDKQGrTVDFKNTLFIMTGNFGSEKI 130

                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 488971989  317 SD------------------------LIPELQGRLPIR 330
Cdd:pfam07724 131 SDasrlgdspdyellkeevmdllkkgFIPEFLGRLPII 168
RecA-like_protease cd19481
proteases similar to RecA; RecA-like NTPases. This family includes the NTP binding domain of ...
 23-137 2.25e-16

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: 76.17  E-value: 2.25e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488971989  23 AKRSVAIALRNRWRRMQLNEelRHEVTPKNILMIGPTGVGKTEIARRLAKLANAPFIKVEATKFTE--VGYVGKEVDSII 100
Cdd:cd19481    1 LKASLREAVEAPRRGSRLRR--YGLGLPKGILLYGPPGTGKTLLAKALAGELGLPLIVVKLSSLLSkyVGESEKNLRKIF 78

                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 488971989 101 RDLTDAAIKMVRMQSIDKNRYRAEELAEERVLDVLIP 137
Cdd:cd19481   79 ERARRLAPCILFIDEIDAIGRKRDSSGESGELRRVLN 115
ClpB_D2-small smart01086
C-terminal, D2-small domain, of ClpB protein; This is the C-terminal domain of ClpB protein, ...
 336-424 1.24e-12

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: 63.23  E-value: 1.24e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488971989   336 LTTHDFERILTEPNASITVQYkalmATEGVNIEFTEDGIKRIAQAAWQvnettENIGARRLHTVLERLVEDISYDA---- 411
Cdd:smart01086   1 LDKEDLVRIVDLPLNALQKRL----AEKGITLEFTDEALDWLAEKGYD-----PKYGARPLRRIIQRELEDPLAELilsg 71

                           90
                   ....*....|...
gi 488971989   412 SEMNGQTVTIDAE 424
Cdd:smart01086  72 ELKDGDTVVVDVD 84
AAA cd00009
The AAA+ (ATPases Associated with a wide variety of cellular Activities) superfamily ...
 18-110 1.44e-08

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: 53.69  E-value: 1.44e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488971989  18 IGQDAAKRSVAIALRNRwrrmqlneelrhevTPKNILMIGPTGVGKTEIARRLAKLA---NAPFIKVEATKFTEVGYVGK 94
Cdd:cd00009    1 VGQEEAIEALREALELP--------------PPKNLLLYGPPGTGKTTLARAIANELfrpGAPFLYLNASDLLEGLVVAE 66

                         90
                 ....*....|....*.
gi 488971989  95 EVDSIIRDLTDAAIKM 110
Cdd:cd00009   67 LFGHFLVRLLFELAEK 82
RecA-like_ClpB_Hsp104-like cd19499
Chaperone protein ClpB/Hsp104 subfamily; Bacterial Caseinolytic peptidase B (ClpB) and ...
 12-95 4.56e-08

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: 52.56  E-value: 4.56e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488971989  12 ELDKHIIGQDAAKRSVAIALRNRwrRMQLNEELRHevtPKNILMIGPTGVGKTEIARRLAKL---ANAPFIKVEATKFTE 88
Cdd:cd19499    8 RLHERVVGQDEAVKAVSDAIRRA--RAGLSDPNRP---IGSFLFLGPTGVGKTELAKALAELlfgDEDNLIRIDMSEYME 82

                         90
                 ....*....|....*...
gi 488971989  89 -----------VGYVGKE 95
Cdd:cd19499   83 khsvsrligapPGYVGYT 100
MoxR COG0714
MoxR-like ATPase [General function prediction only]; MoxR-like ATPase is part of the Pathway ...
 4-84 5.29e-08

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: 54.02  E-value: 5.29e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488971989   4 MTPREIVSELDKHIIGQDAAKRSVAIALRNRwrrmqlneelRHevtpknILMIGPTGVGKTEIARRLAKLANAPFIKVEA 83
Cdd:COG0714    1 MTEARLRAEIGKVYVGQEELIELVLIALLAG----------GH------LLLEGVPGVGKTTLAKALARALGLPFIRIQF 64


                 .
gi 488971989  84 T 84
Cdd:COG0714   65 T 65
AAA pfam00004
ATPase family associated with various cellular activities (AAA); AAA family proteins often ...
 53-137 1.65e-07

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: 49.90  E-value: 1.65e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488971989   53 ILMIGPTGVGKTEIARRLAKLANAPFIKVEATKFTEvGYVGkEVDSIIRDLTDAAIKMVR----MQSID---KNRYRAEE 125
Cdd:pfam00004   1 LLLYGPPGTGKTTLAKAVAKELGAPFIEISGSELVS-KYVG-ESEKRLRELFEAAKKLAPcvifIDEIDalaGSRGSGGD 78

                          90
                  ....*....|..
gi 488971989  126 LAEERVLDVLIP 137
Cdd:pfam00004  79 SESRRVVNQLLT 90
RecA-like_FtsH cd19501
ATP-dependent zinc metalloprotease FtsH; FtsH ATPase is a processive, ATP-dependent zinc ...
 15-107 3.11e-07

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


Pssm-ID: 410909 [Multi-domain]  Cd Length: 171  Bit Score: 49.92  E-value: 3.11e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488971989  15 KHIIGQDAAKRSVAIA---LRNRWRRMQLNEELrhevtPKNILMIGPTGVGKTEIARRLAKLANAPFIKVEATKFTEVgY 91
Cdd:cd19501    4 KDVAGCEEAKEELKEVvefLKNPEKFTKLGAKI-----PKGVLLVGPPGTGKTLLAKAVAGEAGVPFFSISGSDFVEM-F 77

                         90
                 ....*....|....*.
gi 488971989  92 VGKEVdSIIRDLTDAA 107
Cdd:cd19501   78 VGVGA-SRVRDLFEQA 92
RPT1 COG1222
ATP-dependent 26S proteasome regulatory subunit [Posttranslational modification, protein ...
 3-107 1.06e-06

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


Pssm-ID: 440835 [Multi-domain]  Cd Length: 326  Bit Score: 50.39  E-value: 1.06e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488971989   3 EMTPREIVSELDKHIIGQDAAKR----SVAIALRNRwrrmqlnEELRHE--VTPKNILMIGPTGVGKTEIARRLAKLANA 76
Cdd:COG1222   66 TAVPAESPDVTFDDIGGLDEQIEeireAVELPLKNP-------ELFRKYgiEPPKGVLLYGPPGTGKTLLAKAVAGELGA 138

                         90       100       110
                 ....*....|....*....|....*....|.
gi 488971989  77 PFIKVEATKFTEvGYVGkEVDSIIRDLTDAA 107
Cdd:COG1222  139 PFIRVRGSELVS-KYIG-EGARNVREVFELA 167
SpoVK COG0464
AAA+-type ATPase, SpoVK/Ycf46/Vps4 family [Cell wall/membrane/envelope biogenesis, Cell cycle ...
 17-93 3.54e-06

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: 49.14  E-value: 3.54e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488971989  17 IIGQDAAKRsvaiALRNRWRRMQLNEELRHE---VTPKNILMIGPTGVGKTEIARRLAKLANAPFIKVEATKFTEvGYVG 93
Cdd:COG0464  159 LGGLEEVKE----ELRELVALPLKRPELREEyglPPPRGLLLYGPPGTGKTLLARALAGELGLPLIEVDLSDLVS-KYVG 233
AAA pfam00004
ATPase family associated with various cellular activities (AAA); AAA family proteins often ...
 252-333 8.00e-06

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: 45.28  E-value: 8.00e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488971989  252 IVFIDEIDKICKRGGNTSGPDVSRegVQRDLLPLVEGCTvstkhgmVKTDHILFIASGafqvASPSDLIPELQGRLPIRV 331
Cdd:pfam00004  60 VIFIDEIDALAGSRGSGGDSESRR--VVNQLLTELDGFT-------SSNSKVIVIAAT----NRPDKLDPALLGRFDRII 126


                  ..
gi 488971989  332 EL 333
Cdd:pfam00004 127 EF 128
hflB PRK10733
ATP-dependent zinc metalloprotease FtsH;
17-109 1.41e-05

ATP-dependent zinc metalloprotease FtsH;


Pssm-ID: 182683 [Multi-domain]  Cd Length: 644  Bit Score: 47.34  E-value: 1.41e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488971989  17 IIGQDAAKRSVAIA---LRNRWRRMQLNEELrhevtPKNILMIGPTGVGKTEIARRLAKLANAPFIKVEATKFTEVgYVG 93
Cdd:PRK10733 154 VAGCDEAKEEVAELveyLREPSRFQKLGGKI-----PKGVLMVGPPGTGKTLLAKAIAGEAKVPFFTISGSDFVEM-FVG 227

                         90
                 ....*....|....*.
gi 488971989  94 KEVdSIIRDLTDAAIK 109
Cdd:PRK10733 228 VGA-SRVRDMFEQAKK 242
RecA-like_NVL_r1-like cd19518
first of two ATPase domains of NVL (nuclear VCP-like protein) and similar ATPase domains; NVL ...
 50-136 1.93e-05

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: 44.70  E-value: 1.93e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488971989  50 PKNILMIGPTGVGKTEIARRLAKLANAPFIKVEATKFteVGYVGKEVDSIIRDLTDAAIK----MVRMQSIDK---NRYR 122
Cdd:cd19518   34 PRGVLLHGPPGCGKTMLANAIAGELKVPFLKISATEI--VSGVSGESEEKIRELFDQAISnapcIVFIDEIDAitpKRES 111

                         90
                 ....*....|....
gi 488971989 123 AEELAEERVLDVLI 136
Cdd:cd19518  112 AQREMERRIVSQLL 125
AAA smart00382
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ...
 49-136 5.74e-05

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


Pssm-ID: 214640 [Multi-domain]  Cd Length: 148  Bit Score: 43.13  E-value: 5.74e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488971989    49 TPKNILMIGPTGVGKTEIARRLAKLANAP---FIKVEATKFTEVGYVGKEVDSIIRDLTDAaikmVRMQSIDKnryrAEE 125
Cdd:smart00382   1 PGEVILIVGPPGSGKTTLARALARELGPPgggVIYIDGEDILEEVLDQLLLIIVGGKKASG----SGELRLRL----ALA 72

                           90
                   ....*....|.
gi 488971989   126 LAEERVLDVLI 136
Cdd:smart00382  73 LARKLKPDVLI 83
AAA_5 pfam07728
AAA domain (dynein-related subfamily); This Pfam entry includes some of the AAA proteins not ...
 52-88 5.84e-05

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


Pssm-ID: 400191 [Multi-domain]  Cd Length: 135  Bit Score: 42.66  E-value: 5.84e-05
                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 488971989   52 NILMIGPTGVGKTEIARRLAK-LANAPFIKVEATKFTE 88
Cdd:pfam07728   1 GVLLVGPPGTGKTELAERLAAaLSNRPVFYVQLTRDTT 38
YifB COG0606
Predicted Mg-chelatase, contains ChlI-like and ATPase domains, YifB family [Posttranslational ...
 3-70 8.34e-05

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


Pssm-ID: 440371 [Multi-domain]  Cd Length: 502  Bit Score: 44.65  E-value: 8.34e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 488971989   3 EMTPREIVSELD-KHIIGQDAAKRSVAIAlrnrwrrmqlneelRHevtpkNILMIGPTGVGKTEIARRL 70
Cdd:COG0606  179 DAPPAEPPYEPDlADVKGQEQAKRALEIAaa-----------gGH-----NLLMIGPPGSGKTMLARRL 231
RecA-like_PAN_like cd19502
proteasome activating nucleotidase PAN and related proteasome subunits; This subfamily ...
 50-103 1.40e-04

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


Pssm-ID: 410910 [Multi-domain]  Cd Length: 171  Bit Score: 42.32  E-value: 1.40e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....
gi 488971989  50 PKNILMIGPTGVGKTEIARRLAKLANAPFIKVEATKFTEvGYVGkEVDSIIRDL 103
Cdd:cd19502   37 PKGVLLYGPPGTGKTLLAKAVANHTDATFIRVVGSELVQ-KYIG-EGARLVREL 88
ftsH CHL00176
cell division protein; Validated
 50-103 1.51e-04

cell division protein; Validated


Pssm-ID: 214386 [Multi-domain]  Cd Length: 638  Bit Score: 44.27  E-value: 1.51e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 488971989  50 PKNILMIGPTGVGKTEIARRLAKLANAPFIKVEATKFTE--VGyVGKevdSIIRDL 103
Cdd:CHL00176 216 PKGVLLVGPPGTGKTLLAKAIAGEAEVPFFSISGSEFVEmfVG-VGA---ARVRDL 267
RecA-like_spastin cd19524
ATPase domain of spastin; Spastin is an ATP-dependent microtubule-severing protein involved in ...
 17-110 1.91e-04

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: 41.76  E-value: 1.91e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488971989  17 IIGQDAAKRSVAIALRNRWRRMQLNEELRheVTPKNILMIGPTGVGKTEIARRLAKLANAPFIKVEATKFTEvGYVGkEV 96
Cdd:cd19524    2 IAGQDLAKQALQEMVILPSLRPELFTGLR--APARGLLLFGPPGNGKTMLAKAVAAESNATFFNISAASLTS-KYVG-EG 77

                         90
                 ....*....|....
gi 488971989  97 DSIIRDLTDAAIKM 110
Cdd:cd19524   78 EKLVRALFAVAREL 91
clpC CHL00095
Clp protease ATP binding subunit
 12-93 2.60e-04

Clp protease ATP binding subunit


Pssm-ID: 214361 [Multi-domain]  Cd Length: 821  Bit Score: 43.51  E-value: 2.60e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488971989  12 ELDKHIIGQDAAKRSVAIALRnrwrrmqlneelRHEVTPKNI-------LMIGPTGVGKTEIARRLAKL---ANAPFIKV 81
Cdd:CHL00095 506 TLHKRIIGQDEAVVAVSKAIR------------RARVGLKNPnrpiasfLFSGPTGVGKTELTKALASYffgSEDAMIRL 573

                         90       100
                 ....*....|....*....|...
gi 488971989  82 EATKFTE-----------VGYVG 93
Cdd:CHL00095 574 DMSEYMEkhtvskligspPGYVG 596
Mg_chelatase pfam01078
Magnesium chelatase, subunit ChlI; Magnesium-chelatase is a three-component enzyme that ...
 17-70 2.68e-04

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


Pssm-ID: 426032 [Multi-domain]  Cd Length: 207  Bit Score: 42.14  E-value: 2.68e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 488971989   17 IIGQDAAKRSVAIALRNRwrrmqlneelrHevtpkNILMIGPTGVGKTEIARRL 70
Cdd:pfam01078   5 VKGQEQAKRALEIAAAGG-----------H-----NLLMIGPPGSGKTMLAKRL 42
RecA-like_VCP_r2 cd19529
second of two ATPase domains of Valosin-containing protein-like ATPase (VAT) and similar ...
 50-117 2.71e-04

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


Pssm-ID: 410937 [Multi-domain]  Cd Length: 159  Bit Score: 41.33  E-value: 2.71e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488971989  50 PKNILMIGPTGVGKTEIARRLAKLANAPFIKVEATKFTE--VGYVGKEVDSIIRDLTDAAIKMVRMQSID 117
Cdd:cd19529   27 PKGILLYGPPGTGKTLLAKAVATESNANFISVKGPELLSkwVGESEKAIREIFRKARQVAPCVIFFDEID 96
RecA-like_CDC48_NLV2_r1-like cd19503
first of two ATPase domains of CDC48 and NLV2, and similar ATPase domains; CDC48 in yeast and ...
 50-83 3.55e-04

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: 41.12  E-value: 3.55e-04
                         10        20        30
                 ....*....|....*....|....*....|....
gi 488971989  50 PKNILMIGPTGVGKTEIARRLAKLANAPFIKVEA 83
Cdd:cd19503   34 PRGVLLHGPPGTGKTLLARAVANEAGANFLSISG 67
RecA-like_CDC48_r2-like cd19511
second of two ATPase domains of CDC48/p97, PEX1 and -6, VAT and NVL, and similar ATPase ...
 49-107 3.59e-04

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


Pssm-ID: 410919 [Multi-domain]  Cd Length: 159  Bit Score: 41.11  E-value: 3.59e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 488971989  49 TPKNILMIGPTGVGKTEIARRLAKLANAPFIkveATKFTEV--GYVGkEVDSIIRDLTDAA 107
Cdd:cd19511   26 PPKGVLLYGPPGCGKTLLAKALASEAGLNFI---SVKGPELfsKYVG-ESERAVREIFQKA 82
RecA-like_VPS4-like cd19509
ATPase domain of VPS4, ATAD1, K, KTNA1, Spastin, FIGL-1 and similar ATPase domains; This ...
 50-110 5.03e-04

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: 40.41  E-value: 5.03e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 488971989  50 PKNILMIGPTGVGKTEIARRLAKLANAPFIKVEATKFTeVGYVGkEVDSIIRDLTDAAIKM 110
Cdd:cd19509   32 PRGILLYGPPGTGKTLLARAVASESGSTFFSISASSLV-SKWVG-ESEKIVRALFALAREL 90
RecA-like_ATAD1 cd19520
ATPase domain of ATPase family AAA domain-containing protein 1 and similar ATPase domains; ...
 50-91 6.23e-04

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


Pssm-ID: 410928 [Multi-domain]  Cd Length: 166  Bit Score: 40.49  E-value: 6.23e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|..
gi 488971989  50 PKNILMIGPTGVGKTEIARRLAKLANAPFIKVEATKFTEVGY 91
Cdd:cd19520   35 PKGVLLYGPPGCGKTMLAKATAKEAGARFINLQVSSLTDKWY 76
SK cd00464
Shikimate kinase (SK) is the fifth enzyme in the shikimate pathway, a seven-step biosynthetic ...
 52-79 7.02e-04

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: 39.85  E-value: 7.02e-04
                         10        20
                 ....*....|....*....|....*...
gi 488971989  52 NILMIGPTGVGKTEIARRLAKLANAPFI 79
Cdd:cd00464    1 NIVLIGMMGAGKTTVGRLLAKALGLPFV 28
RecA-like_Figl-1 cd19525
ATPase domain of Fidgetin-Like 1 (FIGL-1); FIGL-1 may participate in DNA repair in the nucleus; ...
 50-163 7.06e-04

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


Pssm-ID: 410933 [Multi-domain]  Cd Length: 186  Bit Score: 40.36  E-value: 7.06e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488971989  50 PKNILMIGPTGVGKTEIARRLAKLANAPFIKVEATKFTEvGYVGkEVDSIIRDLTDAA-------IKMVRMQSIDKNRYR 122
Cdd:cd19525   55 PKGILLFGPPGTGKTLIGKCIASQSGATFFSISASSLTS-KWVG-EGEKMVRALFSVArckqpavIFIDEIDSLLSQRGE 132

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 488971989 123 AEELAEERV-------LD---------VLIPPAKNnwgqtEPSQEPSAARQAFRKKL 163
Cdd:cd19525  133 GEHESSRRIkteflvqLDgattssedrILVVGATN-----RPQEIDEAARRRLVKRL 184
ClpA COG0542
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ...
 11-71 7.48e-04

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


Pssm-ID: 440308 [Multi-domain]  Cd Length: 836  Bit Score: 41.99  E-value: 7.48e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 488971989  11 SELDKHIIGQDAAKRSVAIALRnrwR-RMQLNEELRhevtPknI---LMIGPTGVGKTEIARRLA 71
Cdd:COG0542  545 EELHERVIGQDEAVEAVADAIR---RsRAGLKDPNR----P--IgsfLFLGPTGVGKTELAKALA 600
Sigma54_activat pfam00158
Sigma-54 interaction domain;
17-81 8.72e-04

Sigma-54 interaction domain;


Pssm-ID: 425491 [Multi-domain]  Cd Length: 168  Bit Score: 40.08  E-value: 8.72e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 488971989   17 IIGQDAAkrsvaialrnrwrrMQlneELRHEV-----TPKNILMIGPTGVGKTEIAR---RLAKLANAPFIKV 81
Cdd:pfam00158   1 IIGESPA--------------MQ---EVLEQAkrvapTDAPVLITGESGTGKELFARaihQLSPRADGPFVAV 56
aroK PRK00131
shikimate kinase; Reviewed
 50-79 1.34e-03

shikimate kinase; Reviewed


Pssm-ID: 234654 [Multi-domain]  Cd Length: 175  Bit Score: 39.40  E-value: 1.34e-03
                         10        20        30
                 ....*....|....*....|....*....|
gi 488971989  50 PKNILMIGPTGVGKTEIARRLAKLANAPFI 79
Cdd:PRK00131   4 GPNIVLIGFMGAGKSTIGRLLAKRLGYDFI 33
clpA PRK11034
ATP-dependent Clp protease ATP-binding subunit; Provisional
 54-109 1.78e-03

ATP-dependent Clp protease ATP-binding subunit; Provisional


Pssm-ID: 236828 [Multi-domain]  Cd Length: 758  Bit Score: 40.59  E-value: 1.78e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 488971989  54 LMIGPTGVGKTEIARRLAKLANAPFIKVEATKFTE-----------VGYVGKEVDSIirdLTDAAIK 109
Cdd:PRK11034 492 LFAGPTGVGKTEVTVQLSKALGIELLRFDMSEYMErhtvsrligapPGYVGFDQGGL---LTDAVIK 555
PRK03992 PRK03992
proteasome-activating nucleotidase; Provisional
 50-81 2.44e-03

proteasome-activating nucleotidase; Provisional


Pssm-ID: 179699 [Multi-domain]  Cd Length: 389  Bit Score: 39.82  E-value: 2.44e-03
                         10        20        30
                 ....*....|....*....|....*....|..
gi 488971989  50 PKNILMIGPTGVGKTEIARRLAKLANAPFIKV 81
Cdd:PRK03992 165 PKGVLLYGPPGTGKTLLAKAVAHETNATFIRV 196
AAA cd00009
The AAA+ (ATPases Associated with a wide variety of cellular Activities) superfamily ...
 220-333 2.89e-03

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: 38.28  E-value: 2.89e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488971989 220 DAMKLLIEEEAAKLVNPEELKQE-AIDAVEQHGIVFIDEIDKIckrggntsgpdvsREGVQRDLLPLVEGCTVstkhGMV 298
Cdd:cd00009   54 NASDLLEGLVVAELFGHFLVRLLfELAEKAKPGVLFIDEIDSL-------------SRGAQNALLRVLETLND----LRI 116

                         90       100       110
                 ....*....|....*....|....*....|....*
gi 488971989 299 KTDHILFIASGAFqvASPSDLIPELQGRLPIRVEL 333
Cdd:cd00009  117 DRENVRVIGATNR--PLLGDLDRALYDRLDIRIVI 149
PRK13342 PRK13342
recombination factor protein RarA; Reviewed
 4-84 3.15e-03

recombination factor protein RarA; Reviewed


Pssm-ID: 237355 [Multi-domain]  Cd Length: 413  Bit Score: 39.68  E-value: 3.15e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488971989   4 MTPR---EIVSEldKHIIGQDAAkrsvaiaLRnrwrRMQLNEELRHevtpknilMI--GPTGVGKTEIARRLAKLANAPF 78
Cdd:PRK13342   6 MRPKtldEVVGQ--EHLLGPGKP-------LR----RMIEAGRLSS--------MIlwGPPGTGKTTLARIIAGATDAPF 64


                 ....*.
gi 488971989  79 IKVEAT 84
Cdd:PRK13342  65 EALSAV 70
PRK10865 PRK10865
ATP-dependent chaperone ClpB;
12-95 3.40e-03

ATP-dependent chaperone ClpB;


Pssm-ID: 182791 [Multi-domain]  Cd Length: 857  Bit Score: 39.83  E-value: 3.40e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488971989  12 ELDKHIIGQDAAKRSVAIALRNRwrRMQLNEELRhevTPKNILMIGPTGVGKTEIARRLAKL---ANAPFIKVEATKFTE 88
Cdd:PRK10865 565 ELHHRVIGQNEAVEAVSNAIRRS--RAGLSDPNR---PIGSFLFLGPTGVGKTELCKALANFmfdSDDAMVRIDMSEFME 639

                         90
                 ....*....|....*...
gi 488971989  89 V-----------GYVGKE 95
Cdd:PRK10865 640 KhsvsrlvgappGYVGYE 657
RecA-like_CDC48_r2-like cd19528
second of two ATPase domains of CDC48 and similar ATPase domains; CDC48 in yeast and p97 or ...
 44-107 4.42e-03

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: 37.87  E-value: 4.42e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 488971989  44 LRHEVTP-KNILMIGPTGVGKTEIARRLAKLANAPFIKVEATKFTEVGYvgKEVDSIIRDLTDAA 107
Cdd:cd19528   20 LKFGMTPsKGVLFYGPPGCGKTLLAKAIANECQANFISVKGPELLTMWF--GESEANVRDIFDKA 82
AroK COG0703
Shikimate kinase [Amino acid transport and metabolism]; Shikimate kinase is part of the ...
 53-79 4.50e-03

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


Pssm-ID: 440467 [Multi-domain]  Cd Length: 165  Bit Score: 37.80  E-value: 4.50e-03
                         10        20
                 ....*....|....*....|....*..
gi 488971989  53 ILMIGPTGVGKTEIARRLAKLANAPFI 79
Cdd:COG0703    1 IVLIGMMGAGKSTVGRLLAKRLGLPFV 27
PTZ00454 PTZ00454
26S protease regulatory subunit 6B-like protein; Provisional
 50-136 5.63e-03

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


Pssm-ID: 240423 [Multi-domain]  Cd Length: 398  Bit Score: 38.98  E-value: 5.63e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488971989  50 PKNILMIGPTGVGKTEIARRLAKLANAPFIKVEATKFTEvGYVG------KEVDSIIRDLTDAAIKMVRMQSIDKNRYRA 123
Cdd:PTZ00454 179 PRGVLLYGPPGTGKTMLAKAVAHHTTATFIRVVGSEFVQ-KYLGegprmvRDVFRLARENAPSIIFIDEVDSIATKRFDA 257

                         90
                 ....*....|...
gi 488971989 124 EELAEERVLDVLI 136
Cdd:PTZ00454 258 QTGADREVQRILL 270
HflB COG0465
ATP-dependent Zn proteases [Posttranslational modification, protein turnover, chaperones];
50-103 6.10e-03

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


Pssm-ID: 440233 [Multi-domain]  Cd Length: 583  Bit Score: 38.86  E-value: 6.10e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 488971989  50 PKNILMIGPTGVGKTEIARRLAKLANAPFIKVEATKFTE--VGyVGKevdSIIRDL 103
Cdd:COG0465  175 PKGVLLVGPPGTGKTLLAKAVAGEAGVPFFSISGSDFVEmfVG-VGA---SRVRDL 226
COG0645 COG0645
Predicted kinase, contains AAA domain [General function prediction only];
53-79 7.70e-03

Predicted kinase, contains AAA domain [General function prediction only];


Pssm-ID: 440410 [Multi-domain]  Cd Length: 164  Bit Score: 37.20  E-value: 7.70e-03
                         10        20
                 ....*....|....*....|....*..
gi 488971989  53 ILMIGPTGVGKTEIARRLAKLANAPFI 79
Cdd:COG0645    2 ILVCGLPGSGKSTLARALAERLGAVRL 28
FlhF COG1419
Flagellar biosynthesis GTPase FlhF [Cell motility];
1-74 9.45e-03

Flagellar biosynthesis GTPase FlhF [Cell motility];


Pssm-ID: 441029 [Multi-domain]  Cd Length: 361  Bit Score: 37.92  E-value: 9.45e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 488971989   1 MSEMTPREIVSELDKHIiGQDAAKRSVAIALRnrwRRMQLNEELRHEvTPKNILMIGPTGVGKTEIarrLAKLA 74
Cdd:COG1419  120 VSPELARELLEKLPEDL-SAEEAWRALLEALA---RRLPVAEDPLLD-EGGVIALVGPTGVGKTTT---IAKLA 185
 
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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