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Conserved domains on  [gi|332007407|gb|AED94790|]
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FtsH extracellular protease family [Arabidopsis thaliana]

Protein Classification

ATP-dependent metallopeptidase FtsH/Yme1/Tma family protein( domain architecture ID 11422021)

ATP-dependent metallopeptidase FtsH/Yme1/Tma family protein such as ATP-dependent zinc metalloprotease FtsH, which targets both cytoplasmic and membrane proteins and plays a role in quality control of integral membrane proteins

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
HflB COG0465
ATP-dependent Zn proteases [Posttranslational modification, protein turnover, chaperones];
104-694 0e+00

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


:

Pssm-ID: 440233 [Multi-domain]  Cd Length: 583  Bit Score: 931.37  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332007407 104 VLMTAPNPQAQSSDLPdgtqwrYSEFLNAVKKGKVERVKFskDGSVLQLTAVDNRRA--TVIVPNDPDLIDILAMNGVDI 181
Cdd:COG0465    8 LFNLFSSSSSSVKEIS------YSEFLQLVEAGKVKSVTI--QGDRITGTLKDGTKTrfTTYRVNDPELVDLLEEKGVEV 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332007407 182 SVSEGEGGNGLFDFIGNLLFPLLAFGGLFYLFRGGQGGAGGpgglggPMDFGRSKSKFQEVPETGVTFGDVAGADQAKLE 261
Cdd:COG0465   80 TAKPPEESSWLLSLLISLLPILLLIGLWIFFMRRMQGGGGG------AMSFGKSKAKLYDEDKPKVTFDDVAGVDEAKEE 153
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332007407 262 LQEVVDFLKNPDKYTALGAKIPKGCLLVGPPGTGKTLLARAVAGEAGVPFFSCAASEFVELFVGVGASRVRDLFEKAKSK 341
Cdd:COG0465  154 LQEIVDFLKDPEKFTRLGAKIPKGVLLVGPPGTGKTLLAKAVAGEAGVPFFSISGSDFVEMFVGVGASRVRDLFEQAKKN 233
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332007407 342 APCIVFIDEIDAVGRQRGAGMGGGNDEREQTINQLLTEMDGFSGNSGVIVLAATNRPDVLDSALLRPGRFDRQVTVDRPD 421
Cdd:COG0465  234 APCIIFIDEIDAVGRQRGAGLGGGHDEREQTLNQLLVEMDGFEGNEGVIVIAATNRPDVLDPALLRPGRFDRQVVVDLPD 313
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332007407 422 VAGRVQILKVHSRGKAIGKDVDYEKVARRTPGFTGADLQNLMNEAAILAARRELKEISKDEISDALERIIAGPEKKNAVV 501
Cdd:COG0465  314 VKGREAILKVHARKKPLAPDVDLEVIARRTPGFSGADLANLVNEAALLAARRNKKAVTMEDFEEAIDRVIAGPERKSRVI 393
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332007407 502 SEEKKRLVAYHEAGHALVGALMPEYDPVAKISIIPRGQAGGLTFFAPSEERLesgLYSRSYLENQMAVALGGRVAEEVIF 581
Cdd:COG0465  394 SEKEKKITAYHEAGHALVAALLPGADPVHKVTIIPRGRALGYTMQLPEEDRY---LYTKEELLDRIAVLLGGRAAEELVF 470
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332007407 582 GDenVTTGASNDFMQVSRVARQMVERFGFSKKIGQVAVGGAGGNPFLGQSMSSQKDYSMATADVVDAEVRELVEKAYVRA 661
Cdd:COG0465  471 GE--VTTGASNDLERATKIARAMVTEYGMSEKLGPVAYGESEGEVFLGRDIGQSRNYSEETAREIDEEVRRIIDEAYERA 548
                        570       580       590
                 ....*....|....*....|....*....|...
gi 332007407 662 KEIITTQIDILHKLAQLLIEKETVDGEEFMSLF 694
Cdd:COG0465  549 KEILTENRDKLDALAEALLEKETLDGEELEEIL 581
 
Name Accession Description Interval E-value
HflB COG0465
ATP-dependent Zn proteases [Posttranslational modification, protein turnover, chaperones];
104-694 0e+00

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


Pssm-ID: 440233 [Multi-domain]  Cd Length: 583  Bit Score: 931.37  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332007407 104 VLMTAPNPQAQSSDLPdgtqwrYSEFLNAVKKGKVERVKFskDGSVLQLTAVDNRRA--TVIVPNDPDLIDILAMNGVDI 181
Cdd:COG0465    8 LFNLFSSSSSSVKEIS------YSEFLQLVEAGKVKSVTI--QGDRITGTLKDGTKTrfTTYRVNDPELVDLLEEKGVEV 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332007407 182 SVSEGEGGNGLFDFIGNLLFPLLAFGGLFYLFRGGQGGAGGpgglggPMDFGRSKSKFQEVPETGVTFGDVAGADQAKLE 261
Cdd:COG0465   80 TAKPPEESSWLLSLLISLLPILLLIGLWIFFMRRMQGGGGG------AMSFGKSKAKLYDEDKPKVTFDDVAGVDEAKEE 153
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332007407 262 LQEVVDFLKNPDKYTALGAKIPKGCLLVGPPGTGKTLLARAVAGEAGVPFFSCAASEFVELFVGVGASRVRDLFEKAKSK 341
Cdd:COG0465  154 LQEIVDFLKDPEKFTRLGAKIPKGVLLVGPPGTGKTLLAKAVAGEAGVPFFSISGSDFVEMFVGVGASRVRDLFEQAKKN 233
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332007407 342 APCIVFIDEIDAVGRQRGAGMGGGNDEREQTINQLLTEMDGFSGNSGVIVLAATNRPDVLDSALLRPGRFDRQVTVDRPD 421
Cdd:COG0465  234 APCIIFIDEIDAVGRQRGAGLGGGHDEREQTLNQLLVEMDGFEGNEGVIVIAATNRPDVLDPALLRPGRFDRQVVVDLPD 313
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332007407 422 VAGRVQILKVHSRGKAIGKDVDYEKVARRTPGFTGADLQNLMNEAAILAARRELKEISKDEISDALERIIAGPEKKNAVV 501
Cdd:COG0465  314 VKGREAILKVHARKKPLAPDVDLEVIARRTPGFSGADLANLVNEAALLAARRNKKAVTMEDFEEAIDRVIAGPERKSRVI 393
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332007407 502 SEEKKRLVAYHEAGHALVGALMPEYDPVAKISIIPRGQAGGLTFFAPSEERLesgLYSRSYLENQMAVALGGRVAEEVIF 581
Cdd:COG0465  394 SEKEKKITAYHEAGHALVAALLPGADPVHKVTIIPRGRALGYTMQLPEEDRY---LYTKEELLDRIAVLLGGRAAEELVF 470
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332007407 582 GDenVTTGASNDFMQVSRVARQMVERFGFSKKIGQVAVGGAGGNPFLGQSMSSQKDYSMATADVVDAEVRELVEKAYVRA 661
Cdd:COG0465  471 GE--VTTGASNDLERATKIARAMVTEYGMSEKLGPVAYGESEGEVFLGRDIGQSRNYSEETAREIDEEVRRIIDEAYERA 548
                        570       580       590
                 ....*....|....*....|....*....|...
gi 332007407 662 KEIITTQIDILHKLAQLLIEKETVDGEEFMSLF 694
Cdd:COG0465  549 KEILTENRDKLDALAEALLEKETLDGEELEEIL 581
FtsH_fam TIGR01241
ATP-dependent metalloprotease FtsH; HflB(FtsH) is a pleiotropic protein required for correct ...
192-694 0e+00

ATP-dependent metalloprotease FtsH; HflB(FtsH) is a pleiotropic protein required for correct cell division in bacteria. It has ATP-dependent zinc metalloprotease activity. It was formerly designated cell division protein FtsH. [Cellular processes, Cell division, Protein fate, Degradation of proteins, peptides, and glycopeptides]


Pssm-ID: 273520 [Multi-domain]  Cd Length: 495  Bit Score: 784.55  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332007407  192 LFDFIGNLLFPLLAFGGLFYLFRGGQGGAGGPGglggpMDFGRSKSKFQEVPETGVTFGDVAGADQAKLELQEVVDFLKN 271
Cdd:TIGR01241   2 LLGFLFSLLPPILLLVGVWFFFRRQMQGGGGRA-----FSFGKSKAKLLNEEKPKVTFKDVAGIDEAKEELMEIVDFLKN 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332007407  272 PDKYTALGAKIPKGCLLVGPPGTGKTLLARAVAGEAGVPFFSCAASEFVELFVGVGASRVRDLFEKAKSKAPCIVFIDEI 351
Cdd:TIGR01241  77 PSKFTKLGAKIPKGVLLVGPPGTGKTLLAKAVAGEAGVPFFSISGSDFVEMFVGVGASRVRDLFEQAKKNAPCIIFIDEI 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332007407  352 DAVGRQRGAGMGGGNDEREQTINQLLTEMDGFSGNSGVIVLAATNRPDVLDSALLRPGRFDRQVTVDRPDVAGRVQILKV 431
Cdd:TIGR01241 157 DAVGRQRGAGLGGGNDEREQTLNQLLVEMDGFGTNTGVIVIAATNRPDVLDPALLRPGRFDRQVVVDLPDIKGREEILKV 236
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332007407  432 HSRGKAIGKDVDYEKVARRTPGFTGADLQNLMNEAAILAARRELKEISKDEISDALERIIAGPEKKNAVVSEEKKRLVAY 511
Cdd:TIGR01241 237 HAKNKKLAPDVDLKAVARRTPGFSGADLANLLNEAALLAARKNKTEITMNDIEEAIDRVIAGPEKKSRVISEKEKKLVAY 316
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332007407  512 HEAGHALVGALMPEYDPVAKISIIPRGQAGGLTFFAPSEERlesGLYSRSYLENQMAVALGGRVAEEVIFGDenVTTGAS 591
Cdd:TIGR01241 317 HEAGHALVGLLLKDADPVHKVTIIPRGQALGYTQFLPEEDK---YLYTKSQLLAQIAVLLGGRAAEEIIFGE--VTTGAS 391
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332007407  592 NDFMQVSRVARQMVERFGFSKKIGQVAVGGAGGNPFLGQSMSSQKDYSMATADVVDAEVRELVEKAYVRAKEIITTQIDI 671
Cdd:TIGR01241 392 NDIKQATNIARAMVTEWGMSDKLGPVAYGSDGGDVFLGRGFAKAKEYSEETAREIDEEVKRIIEEAYKRAKQILTENRDE 471
                         490       500
                  ....*....|....*....|...
gi 332007407  672 LHKLAQLLIEKETVDGEEFMSLF 694
Cdd:TIGR01241 472 LELLAKALLEKETITREEIKELL 494
ftsH CHL00176
cell division protein; Validated
93-693 0e+00

cell division protein; Validated


Pssm-ID: 214386 [Multi-domain]  Cd Length: 638  Bit Score: 703.35  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332007407  93 QSPNLSTFGQNVlmtapnpqaQSSdlpdgtQWRYSEFLNAVKKGKVERVKFSKDG--SVLQLTAVDN----RRATVIVP- 165
Cdd:CHL00176  36 KSPNNPDVVQNK---------ASS------RMTYGRFLEYLDMGWIKKVDLYDNGrtAIVEASSPELgnrpQRIRVELPv 100
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332007407 166 NDPDLIDILAMNGVDISVSEGEGGNGLFDFIGNLLFPLLAFGGLFYLFRGGQGGAGGPGGLggPMDFGRSKSKFQEVPET 245
Cdd:CHL00176 101 GASELIQKLKEANIDFDAHPPVLKSNIVTILSNLLLPLILIGVLWFFFQRSSNFKGGPGQN--LMNFGKSKARFQMEADT 178
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332007407 246 GVTFGDVAGADQAKLELQEVVDFLKNPDKYTALGAKIPKGCLLVGPPGTGKTLLARAVAGEAGVPFFSCAASEFVELFVG 325
Cdd:CHL00176 179 GITFRDIAGIEEAKEEFEEVVSFLKKPERFTAVGAKIPKGVLLVGPPGTGKTLLAKAIAGEAEVPFFSISGSEFVEMFVG 258
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332007407 326 VGASRVRDLFEKAKSKAPCIVFIDEIDAVGRQRGAGMGGGNDEREQTINQLLTEMDGFSGNSGVIVLAATNRPDVLDSAL 405
Cdd:CHL00176 259 VGAARVRDLFKKAKENSPCIVFIDEIDAVGRQRGAGIGGGNDEREQTLNQLLTEMDGFKGNKGVIVIAATNRVDILDAAL 338
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332007407 406 LRPGRFDRQVTVDRPDVAGRVQILKVHSRGKAIGKDVDYEKVARRTPGFTGADLQNLMNEAAILAARRELKEISKDEISD 485
Cdd:CHL00176 339 LRPGRFDRQITVSLPDREGRLDILKVHARNKKLSPDVSLELIARRTPGFSGADLANLLNEAAILTARRKKATITMKEIDT 418
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332007407 486 ALERIIAGPEKKNAVVSeEKKRLVAYHEAGHALVGALMPEYDPVAKISIIPRGQAGGLTFFAPSEERLesgLYSRSYLEN 565
Cdd:CHL00176 419 AIDRVIAGLEGTPLEDS-KNKRLIAYHEVGHAIVGTLLPNHDPVQKVTLIPRGQAKGLTWFTPEEDQS---LVSRSQILA 494
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332007407 566 QMAVALGGRVAEEVIFGDENVTTGASNDFMQVSRVARQMVERFGFSKKIGQVAVGGAGGNPFLGQSMSSQKDYSMATADV 645
Cdd:CHL00176 495 RIVGALGGRAAEEVVFGSTEVTTGASNDLQQVTNLARQMVTRFGMSSIGPISLESNNSTDPFLGRFMQRNSEYSEEIADK 574
                        570       580       590       600
                 ....*....|....*....|....*....|....*....|....*...
gi 332007407 646 VDAEVRELVEKAYVRAKEIITTQIDILHKLAQLLIEKETVDGEEFMSL 693
Cdd:CHL00176 575 IDMEVRSILHTCYQYAYQILKDNRVLIDLLVELLLQKETIDGDEFREI 622
RecA-like_FtsH cd19501
ATP-dependent zinc metalloprotease FtsH; FtsH ATPase is a processive, ATP-dependent zinc ...
247-417 2.85e-120

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: 356.54  E-value: 2.85e-120
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332007407 247 VTFGDVAGADQAKLELQEVVDFLKNPDKYTALGAKIPKGCLLVGPPGTGKTLLARAVAGEAGVPFFSCAASEFVELFVGV 326
Cdd:cd19501    1 VTFKDVAGCEEAKEELKEVVEFLKNPEKFTKLGAKIPKGVLLVGPPGTGKTLLAKAVAGEAGVPFFSISGSDFVEMFVGV 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332007407 327 GASRVRDLFEKAKSKAPCIVFIDEIDAVGRQRGAGMGGGNDEREQTINQLLTEMDGFSGNSGVIVLAATNRPDVLDSALL 406
Cdd:cd19501   81 GASRVRDLFEQAKKNAPCIVFIDEIDAVGRKRGAGLGGGHDEREQTLNQLLVEMDGFESNTGVIVIAATNRPDVLDPALL 160
                        170
                 ....*....|.
gi 332007407 407 RPGRFDRQVTV 417
Cdd:cd19501  161 RPGRFDRQVYV 171
Peptidase_M41 pfam01434
Peptidase family M41;
499-693 3.72e-94

Peptidase family M41;


Pssm-ID: 460210 [Multi-domain]  Cd Length: 190  Bit Score: 289.89  E-value: 3.72e-94
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332007407  499 AVVSEEKKRLVAYHEAGHALVGALMPEYDPVAKISIIPRGQAGGLTFFAPSEERLesgLYSRSYLENQMAVALGGRVAEE 578
Cdd:pfam01434   1 RVISEEEKKIVAYHEAGHALVGLLLPGADPVHKVTIIPRGQALGYTQFLPEEDKL---LYTKEQLLARIAVLLGGRAAEE 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332007407  579 VIFGdeNVTTGASNDFMQVSRVARQMVERFGFSKKIGQVAVGGAGGNPFLGQSMSSQKDYSMATADVVDAEVRELVEKAY 658
Cdd:pfam01434  78 LIFG--EVTTGASNDLEKATKIARQMVTEFGMSDKLGPVSLEESDGNVFLGRGMGKRKPYSEETADIIDEEVKRLLEEAY 155
                         170       180       190
                  ....*....|....*....|....*....|....*
gi 332007407  659 VRAKEIITTQIDILHKLAQLLIEKETVDGEEFMSL 693
Cdd:pfam01434 156 ERAKEILTEHRDELEALAEALLEKETLDAEEIREL 190
AAA smart00382
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ...
283-421 3.64e-18

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: 81.65  E-value: 3.64e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332007407   283 PKGCLLVGPPGTGKTLLARAVAGEA---GVPFFSCAASEFVE--------------LFVGVGASRVRDLFEKAKSKAPCI 345
Cdd:smart00382   2 GEVILIVGPPGSGKTTLARALARELgppGGGVIYIDGEDILEevldqllliivggkKASGSGELRLRLALALARKLKPDV 81
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 332007407   346 VFIDEIDAVGRQRGagmgggndEREQTINQLLTEMDGFSGNSGVIVLAATNRPDVLDSALLRPgRFDRQVTVDRPD 421
Cdd:smart00382  82 LILDEITSLLDAEQ--------EALLLLLEELRLLLLLKSEKNLTVILTTNDEKDLGPALLRR-RFDRRIVLLLIL 148
 
Name Accession Description Interval E-value
HflB COG0465
ATP-dependent Zn proteases [Posttranslational modification, protein turnover, chaperones];
104-694 0e+00

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


Pssm-ID: 440233 [Multi-domain]  Cd Length: 583  Bit Score: 931.37  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332007407 104 VLMTAPNPQAQSSDLPdgtqwrYSEFLNAVKKGKVERVKFskDGSVLQLTAVDNRRA--TVIVPNDPDLIDILAMNGVDI 181
Cdd:COG0465    8 LFNLFSSSSSSVKEIS------YSEFLQLVEAGKVKSVTI--QGDRITGTLKDGTKTrfTTYRVNDPELVDLLEEKGVEV 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332007407 182 SVSEGEGGNGLFDFIGNLLFPLLAFGGLFYLFRGGQGGAGGpgglggPMDFGRSKSKFQEVPETGVTFGDVAGADQAKLE 261
Cdd:COG0465   80 TAKPPEESSWLLSLLISLLPILLLIGLWIFFMRRMQGGGGG------AMSFGKSKAKLYDEDKPKVTFDDVAGVDEAKEE 153
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332007407 262 LQEVVDFLKNPDKYTALGAKIPKGCLLVGPPGTGKTLLARAVAGEAGVPFFSCAASEFVELFVGVGASRVRDLFEKAKSK 341
Cdd:COG0465  154 LQEIVDFLKDPEKFTRLGAKIPKGVLLVGPPGTGKTLLAKAVAGEAGVPFFSISGSDFVEMFVGVGASRVRDLFEQAKKN 233
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332007407 342 APCIVFIDEIDAVGRQRGAGMGGGNDEREQTINQLLTEMDGFSGNSGVIVLAATNRPDVLDSALLRPGRFDRQVTVDRPD 421
Cdd:COG0465  234 APCIIFIDEIDAVGRQRGAGLGGGHDEREQTLNQLLVEMDGFEGNEGVIVIAATNRPDVLDPALLRPGRFDRQVVVDLPD 313
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332007407 422 VAGRVQILKVHSRGKAIGKDVDYEKVARRTPGFTGADLQNLMNEAAILAARRELKEISKDEISDALERIIAGPEKKNAVV 501
Cdd:COG0465  314 VKGREAILKVHARKKPLAPDVDLEVIARRTPGFSGADLANLVNEAALLAARRNKKAVTMEDFEEAIDRVIAGPERKSRVI 393
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332007407 502 SEEKKRLVAYHEAGHALVGALMPEYDPVAKISIIPRGQAGGLTFFAPSEERLesgLYSRSYLENQMAVALGGRVAEEVIF 581
Cdd:COG0465  394 SEKEKKITAYHEAGHALVAALLPGADPVHKVTIIPRGRALGYTMQLPEEDRY---LYTKEELLDRIAVLLGGRAAEELVF 470
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332007407 582 GDenVTTGASNDFMQVSRVARQMVERFGFSKKIGQVAVGGAGGNPFLGQSMSSQKDYSMATADVVDAEVRELVEKAYVRA 661
Cdd:COG0465  471 GE--VTTGASNDLERATKIARAMVTEYGMSEKLGPVAYGESEGEVFLGRDIGQSRNYSEETAREIDEEVRRIIDEAYERA 548
                        570       580       590
                 ....*....|....*....|....*....|...
gi 332007407 662 KEIITTQIDILHKLAQLLIEKETVDGEEFMSLF 694
Cdd:COG0465  549 KEILTENRDKLDALAEALLEKETLDGEELEEIL 581
FtsH_fam TIGR01241
ATP-dependent metalloprotease FtsH; HflB(FtsH) is a pleiotropic protein required for correct ...
192-694 0e+00

ATP-dependent metalloprotease FtsH; HflB(FtsH) is a pleiotropic protein required for correct cell division in bacteria. It has ATP-dependent zinc metalloprotease activity. It was formerly designated cell division protein FtsH. [Cellular processes, Cell division, Protein fate, Degradation of proteins, peptides, and glycopeptides]


Pssm-ID: 273520 [Multi-domain]  Cd Length: 495  Bit Score: 784.55  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332007407  192 LFDFIGNLLFPLLAFGGLFYLFRGGQGGAGGPGglggpMDFGRSKSKFQEVPETGVTFGDVAGADQAKLELQEVVDFLKN 271
Cdd:TIGR01241   2 LLGFLFSLLPPILLLVGVWFFFRRQMQGGGGRA-----FSFGKSKAKLLNEEKPKVTFKDVAGIDEAKEELMEIVDFLKN 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332007407  272 PDKYTALGAKIPKGCLLVGPPGTGKTLLARAVAGEAGVPFFSCAASEFVELFVGVGASRVRDLFEKAKSKAPCIVFIDEI 351
Cdd:TIGR01241  77 PSKFTKLGAKIPKGVLLVGPPGTGKTLLAKAVAGEAGVPFFSISGSDFVEMFVGVGASRVRDLFEQAKKNAPCIIFIDEI 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332007407  352 DAVGRQRGAGMGGGNDEREQTINQLLTEMDGFSGNSGVIVLAATNRPDVLDSALLRPGRFDRQVTVDRPDVAGRVQILKV 431
Cdd:TIGR01241 157 DAVGRQRGAGLGGGNDEREQTLNQLLVEMDGFGTNTGVIVIAATNRPDVLDPALLRPGRFDRQVVVDLPDIKGREEILKV 236
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332007407  432 HSRGKAIGKDVDYEKVARRTPGFTGADLQNLMNEAAILAARRELKEISKDEISDALERIIAGPEKKNAVVSEEKKRLVAY 511
Cdd:TIGR01241 237 HAKNKKLAPDVDLKAVARRTPGFSGADLANLLNEAALLAARKNKTEITMNDIEEAIDRVIAGPEKKSRVISEKEKKLVAY 316
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332007407  512 HEAGHALVGALMPEYDPVAKISIIPRGQAGGLTFFAPSEERlesGLYSRSYLENQMAVALGGRVAEEVIFGDenVTTGAS 591
Cdd:TIGR01241 317 HEAGHALVGLLLKDADPVHKVTIIPRGQALGYTQFLPEEDK---YLYTKSQLLAQIAVLLGGRAAEEIIFGE--VTTGAS 391
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332007407  592 NDFMQVSRVARQMVERFGFSKKIGQVAVGGAGGNPFLGQSMSSQKDYSMATADVVDAEVRELVEKAYVRAKEIITTQIDI 671
Cdd:TIGR01241 392 NDIKQATNIARAMVTEWGMSDKLGPVAYGSDGGDVFLGRGFAKAKEYSEETAREIDEEVKRIIEEAYKRAKQILTENRDE 471
                         490       500
                  ....*....|....*....|...
gi 332007407  672 LHKLAQLLIEKETVDGEEFMSLF 694
Cdd:TIGR01241 472 LELLAKALLEKETITREEIKELL 494
ftsH CHL00176
cell division protein; Validated
93-693 0e+00

cell division protein; Validated


Pssm-ID: 214386 [Multi-domain]  Cd Length: 638  Bit Score: 703.35  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332007407  93 QSPNLSTFGQNVlmtapnpqaQSSdlpdgtQWRYSEFLNAVKKGKVERVKFSKDG--SVLQLTAVDN----RRATVIVP- 165
Cdd:CHL00176  36 KSPNNPDVVQNK---------ASS------RMTYGRFLEYLDMGWIKKVDLYDNGrtAIVEASSPELgnrpQRIRVELPv 100
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332007407 166 NDPDLIDILAMNGVDISVSEGEGGNGLFDFIGNLLFPLLAFGGLFYLFRGGQGGAGGPGGLggPMDFGRSKSKFQEVPET 245
Cdd:CHL00176 101 GASELIQKLKEANIDFDAHPPVLKSNIVTILSNLLLPLILIGVLWFFFQRSSNFKGGPGQN--LMNFGKSKARFQMEADT 178
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332007407 246 GVTFGDVAGADQAKLELQEVVDFLKNPDKYTALGAKIPKGCLLVGPPGTGKTLLARAVAGEAGVPFFSCAASEFVELFVG 325
Cdd:CHL00176 179 GITFRDIAGIEEAKEEFEEVVSFLKKPERFTAVGAKIPKGVLLVGPPGTGKTLLAKAIAGEAEVPFFSISGSEFVEMFVG 258
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332007407 326 VGASRVRDLFEKAKSKAPCIVFIDEIDAVGRQRGAGMGGGNDEREQTINQLLTEMDGFSGNSGVIVLAATNRPDVLDSAL 405
Cdd:CHL00176 259 VGAARVRDLFKKAKENSPCIVFIDEIDAVGRQRGAGIGGGNDEREQTLNQLLTEMDGFKGNKGVIVIAATNRVDILDAAL 338
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332007407 406 LRPGRFDRQVTVDRPDVAGRVQILKVHSRGKAIGKDVDYEKVARRTPGFTGADLQNLMNEAAILAARRELKEISKDEISD 485
Cdd:CHL00176 339 LRPGRFDRQITVSLPDREGRLDILKVHARNKKLSPDVSLELIARRTPGFSGADLANLLNEAAILTARRKKATITMKEIDT 418
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332007407 486 ALERIIAGPEKKNAVVSeEKKRLVAYHEAGHALVGALMPEYDPVAKISIIPRGQAGGLTFFAPSEERLesgLYSRSYLEN 565
Cdd:CHL00176 419 AIDRVIAGLEGTPLEDS-KNKRLIAYHEVGHAIVGTLLPNHDPVQKVTLIPRGQAKGLTWFTPEEDQS---LVSRSQILA 494
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332007407 566 QMAVALGGRVAEEVIFGDENVTTGASNDFMQVSRVARQMVERFGFSKKIGQVAVGGAGGNPFLGQSMSSQKDYSMATADV 645
Cdd:CHL00176 495 RIVGALGGRAAEEVVFGSTEVTTGASNDLQQVTNLARQMVTRFGMSSIGPISLESNNSTDPFLGRFMQRNSEYSEEIADK 574
                        570       580       590       600
                 ....*....|....*....|....*....|....*....|....*...
gi 332007407 646 VDAEVRELVEKAYVRAKEIITTQIDILHKLAQLLIEKETVDGEEFMSL 693
Cdd:CHL00176 575 IDMEVRSILHTCYQYAYQILKDNRVLIDLLVELLLQKETIDGDEFREI 622
hflB PRK10733
ATP-dependent zinc metalloprotease FtsH;
120-693 0e+00

ATP-dependent zinc metalloprotease FtsH;


Pssm-ID: 182683 [Multi-domain]  Cd Length: 644  Bit Score: 579.30  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332007407 120 DGTQWRYSEFLNAVKKGKVERVKFSkdGSVLQLTAVDNRRATVIVP-NDPDLIDILAMNGVDIsVSEGEGGNGLFDFIGN 198
Cdd:PRK10733  28 NGRKVDYSTFLQEVNQDQVREARIN--GREINVTKKDSNRYTTYIPvNDPKLLDNLLTKNVKV-VGEPPEEPSLLASIFI 104
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332007407 199 LLFPLLAFGGLFYLFrggqGGAGGPGGLGGPMDFGRSKSKFQEVPETGVTFGDVAGADQAKLELQEVVDFLKNPDKYTAL 278
Cdd:PRK10733 105 SWFPMLLLIGVWIFF----MRQMQGGGGKGAMSFGKSKARMLTEDQIKTTFADVAGCDEAKEEVAELVEYLREPSRFQKL 180
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332007407 279 GAKIPKGCLLVGPPGTGKTLLARAVAGEAGVPFFSCAASEFVELFVGVGASRVRDLFEKAKSKAPCIVFIDEIDAVGRQR 358
Cdd:PRK10733 181 GGKIPKGVLMVGPPGTGKTLLAKAIAGEAKVPFFTISGSDFVEMFVGVGASRVRDMFEQAKKAAPCIIFIDEIDAVGRQR 260
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332007407 359 GAGMGGGNDEREQTINQLLTEMDGFSGNSGVIVLAATNRPDVLDSALLRPGRFDRQVTVDRPDVAGRVQILKVHSRGKAI 438
Cdd:PRK10733 261 GAGLGGGHDEREQTLNQMLVEMDGFEGNEGIIVIAATNRPDVLDPALLRPGRFDRQVVVGLPDVRGREQILKVHMRRVPL 340
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332007407 439 GKDVDYEKVARRTPGFTGADLQNLMNEAAILAARRELKEISKDEISDALERIIAGPEKKNAVVSEEKKRLVAYHEAGHAL 518
Cdd:PRK10733 341 APDIDAAIIARGTPGFSGADLANLVNEAALFAARGNKRVVSMVEFEKAKDKIMMGAERRSMVMTEAQKESTAYHEAGHAI 420
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332007407 519 VGALMPEYDPVAKISIIPRGQAGGLTFFAPSEERLESglySRSYLENQMAVALGGRVAEEVIFGDENVTTGASNDFMQVS 598
Cdd:PRK10733 421 IGRLVPEHDPVHKVTIIPRGRALGVTFFLPEGDAISA---SRQKLESQISTLYGGRLAEEIIYGPEHVSTGASNDIKVAT 497
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332007407 599 RVARQMVERFGFSKKIGQVAVGGAGGNPFLGQSMSSQKDYSMATADVVDAEVRELVEKAYVRAKEIITTQIDILHKLAQL 678
Cdd:PRK10733 498 NLARNMVTQWGFSEKLGPLLYAEEEGEVFLGRSVAKAKHMSDETARIIDQEVKALIERNYNRARQLLTDNMDILHAMKDA 577
                        570
                 ....*....|....*
gi 332007407 679 LIEKETVDGEEFMSL 693
Cdd:PRK10733 578 LMKYETIDAPQIDDL 592
RecA-like_FtsH cd19501
ATP-dependent zinc metalloprotease FtsH; FtsH ATPase is a processive, ATP-dependent zinc ...
247-417 2.85e-120

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: 356.54  E-value: 2.85e-120
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332007407 247 VTFGDVAGADQAKLELQEVVDFLKNPDKYTALGAKIPKGCLLVGPPGTGKTLLARAVAGEAGVPFFSCAASEFVELFVGV 326
Cdd:cd19501    1 VTFKDVAGCEEAKEELKEVVEFLKNPEKFTKLGAKIPKGVLLVGPPGTGKTLLAKAVAGEAGVPFFSISGSDFVEMFVGV 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332007407 327 GASRVRDLFEKAKSKAPCIVFIDEIDAVGRQRGAGMGGGNDEREQTINQLLTEMDGFSGNSGVIVLAATNRPDVLDSALL 406
Cdd:cd19501   81 GASRVRDLFEQAKKNAPCIVFIDEIDAVGRKRGAGLGGGHDEREQTLNQLLVEMDGFESNTGVIVIAATNRPDVLDPALL 160
                        170
                 ....*....|.
gi 332007407 407 RPGRFDRQVTV 417
Cdd:cd19501  161 RPGRFDRQVYV 171
RPT1 COG1222
ATP-dependent 26S proteasome regulatory subunit [Posttranslational modification, protein ...
241-497 4.14e-110

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


Pssm-ID: 440835 [Multi-domain]  Cd Length: 326  Bit Score: 336.21  E-value: 4.14e-110
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332007407 241 EVPEtgVTFGDVAGADQAKLELQEVV-DFLKNPDKYTALGAKIPKGCLLVGPPGTGKTLLARAVAGEAGVPFFSCAASEF 319
Cdd:COG1222   71 ESPD--VTFDDIGGLDEQIEEIREAVeLPLKNPELFRKYGIEPPKGVLLYGPPGTGKTLLAKAVAGELGAPFIRVRGSEL 148
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332007407 320 VELFVGVGASRVRDLFEKAKSKAPCIVFIDEIDAVGRQRGAGMGGGndEREQTINQLLTEMDGFSGNSGVIVLAATNRPD 399
Cdd:COG1222  149 VSKYIGEGARNVREVFELAREKAPSIIFIDEIDAIAARRTDDGTSG--EVQRTVNQLLAELDGFESRGDVLIIAATNRPD 226
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332007407 400 VLDSALLRPGRFDRQVTVDRPDVAGRVQILKVHSRGKAIGKDVDYEKVARRTPGFTGADLQNLMNEAAILAARRELKEIS 479
Cdd:COG1222  227 LLDPALLRPGRFDRVIEVPLPDEEAREEILKIHLRDMPLADDVDLDKLAKLTEGFSGADLKAIVTEAGMFAIREGRDTVT 306
                        250
                 ....*....|....*...
gi 332007407 480 KDEISDALERIIAGPEKK 497
Cdd:COG1222  307 MEDLEKAIEKVKKKTETA 324
Peptidase_M41 pfam01434
Peptidase family M41;
499-693 3.72e-94

Peptidase family M41;


Pssm-ID: 460210 [Multi-domain]  Cd Length: 190  Bit Score: 289.89  E-value: 3.72e-94
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332007407  499 AVVSEEKKRLVAYHEAGHALVGALMPEYDPVAKISIIPRGQAGGLTFFAPSEERLesgLYSRSYLENQMAVALGGRVAEE 578
Cdd:pfam01434   1 RVISEEEKKIVAYHEAGHALVGLLLPGADPVHKVTIIPRGQALGYTQFLPEEDKL---LYTKEQLLARIAVLLGGRAAEE 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332007407  579 VIFGdeNVTTGASNDFMQVSRVARQMVERFGFSKKIGQVAVGGAGGNPFLGQSMSSQKDYSMATADVVDAEVRELVEKAY 658
Cdd:pfam01434  78 LIFG--EVTTGASNDLEKATKIARQMVTEFGMSDKLGPVSLEESDGNVFLGRGMGKRKPYSEETADIIDEEVKRLLEEAY 155
                         170       180       190
                  ....*....|....*....|....*....|....*
gi 332007407  659 VRAKEIITTQIDILHKLAQLLIEKETVDGEEFMSL 693
Cdd:pfam01434 156 ERAKEILTEHRDELEALAEALLEKETLDAEEIREL 190
PRK03992 PRK03992
proteasome-activating nucleotidase; Provisional
241-498 9.22e-92

proteasome-activating nucleotidase; Provisional


Pssm-ID: 179699 [Multi-domain]  Cd Length: 389  Bit Score: 290.97  E-value: 9.22e-92
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332007407 241 EVPEtgVTFGDVAGADQAKLELQEVVDF-LKNPDKYTALGAKIPKGCLLVGPPGTGKTLLARAVAGEAGVPFFSCAASEF 319
Cdd:PRK03992 124 ESPN--VTYEDIGGLEEQIREVREAVELpLKKPELFEEVGIEPPKGVLLYGPPGTGKTLLAKAVAHETNATFIRVVGSEL 201
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332007407 320 VELFVGVGASRVRDLFEKAKSKAPCIVFIDEIDAVGRQRGAGMGGGNDEREQTINQLLTEMDGFSGNSGVIVLAATNRPD 399
Cdd:PRK03992 202 VQKFIGEGARLVRELFELAREKAPSIIFIDEIDAIAAKRTDSGTSGDREVQRTLMQLLAEMDGFDPRGNVKIIAATNRID 281
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332007407 400 VLDSALLRPGRFDRQVTVDRPDVAGRVQILKVHSRGKAIGKDVDYEKVARRTPGFTGADLQNLMNEAAILAARRELKEIS 479
Cdd:PRK03992 282 ILDPAILRPGRFDRIIEVPLPDEEGRLEILKIHTRKMNLADDVDLEELAELTEGASGADLKAICTEAGMFAIRDDRTEVT 361
                        250
                 ....*....|....*....
gi 332007407 480 KDEISDALERIIAGPEKKN 498
Cdd:PRK03992 362 MEDFLKAIEKVMGKEEKDS 380
26Sp45 TIGR01242
26S proteasome subunit P45 family; Many proteins may score above the trusted cutoff because an ...
240-491 5.60e-80

26S proteasome subunit P45 family; Many proteins may score above the trusted cutoff because an internal


Pssm-ID: 130309 [Multi-domain]  Cd Length: 364  Bit Score: 259.35  E-value: 5.60e-80
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332007407  240 QEVPEtgVTFGDVAGADQAKLELQEVVDF-LKNPDKYTALGAKIPKGCLLVGPPGTGKTLLARAVAGEAGVPFFSCAASE 318
Cdd:TIGR01242 114 EERPN--VSYEDIGGLEEQIREIREAVELpLKHPELFEEVGIEPPKGVLLYGPPGTGKTLLAKAVAHETNATFIRVVGSE 191
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332007407  319 FVELFVGVGASRVRDLFEKAKSKAPCIVFIDEIDAVGRQRGAGMGGGNDEREQTINQLLTEMDGFSGNSGVIVLAATNRP 398
Cdd:TIGR01242 192 LVRKYIGEGARLVREIFELAKEKAPSIIFIDEIDAIAAKRTDSGTSGDREVQRTLMQLLAELDGFDPRGNVKVIAATNRP 271
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332007407  399 DVLDSALLRPGRFDRQVTVDRPDVAGRVQILKVHSRGKAIGKDVDYEKVARRTPGFTGADLQNLMNEAAILAARRELKEI 478
Cdd:TIGR01242 272 DILDPALLRPGRFDRIIEVPLPDFEGRLEILKIHTRKMKLAEDVDLEAIAKMTEGASGADLKAICTEAGMFAIREERDYV 351
                         250
                  ....*....|...
gi 332007407  479 SKDEISDALERII 491
Cdd:TIGR01242 352 TMDDFIKAVEKVL 364
SpoVK COG0464
AAA+-type ATPase, SpoVK/Ycf46/Vps4 family [Cell wall/membrane/envelope biogenesis, Cell cycle ...
158-490 1.29e-78

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: 256.76  E-value: 1.29e-78
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332007407 158 RRATVIVPNDPDLIDILAMNGVDISVSEGEGGNGLFDFIGNLLFPLLAFGGLFYLFRGGQGGAGGPGGLGGPMDFGRSKS 237
Cdd:COG0464   67 ALLLLALLLLALLALLAALLSALELLLLGELLLLLLLLLLLLLLLLDLERALLELLRESAEALALAAPLVTYEDIGGLEE 146
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332007407 238 KFQEVPEtgVTFGDVAGADQAKLELQEVVD-FLKNPDKYTALGAKIPKGCLLVGPPGTGKTLLARAVAGEAGVPFFSCAA 316
Cdd:COG0464  147 ELLELRE--AILDDLGGLEEVKEELRELVAlPLKRPELREEYGLPPPRGLLLYGPPGTGKTLLARALAGELGLPLIEVDL 224
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332007407 317 SEFVELFVGVGASRVRDLFEKAKSKAPCIVFIDEIDAVGRQRGaGMGGGNDEREqtINQLLTEMDGFsgNSGVIVLAATN 396
Cdd:COG0464  225 SDLVSKYVGETEKNLREVFDKARGLAPCVLFIDEADALAGKRG-EVGDGVGRRV--VNTLLTEMEEL--RSDVVVIAATN 299
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332007407 397 RPDVLDSALLRpgRFDRQVTVDRPDVAGRVQILKVHSRGKAIGKDVDYEKVARRTPGFTGADLQNLMNEAAILAARRELK 476
Cdd:COG0464  300 RPDLLDPALLR--RFDEIIFFPLPDAEERLEIFRIHLRKRPLDEDVDLEELAEATEGLSGADIRNVVRRAALQALRLGRE 377
                        330
                 ....*....|....
gi 332007407 477 EISKDEISDALERI 490
Cdd:COG0464  378 PVTTEDLLEALERE 391
CDC48 TIGR01243
AAA family ATPase, CDC48 subfamily; This subfamily of the AAA family ATPases includes two ...
241-491 4.18e-73

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: 251.36  E-value: 4.18e-73
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332007407  241 EVPEtgVTFGDVAGADQAKLELQEVVDF-LKNPDKYTALGAKIPKGCLLVGPPGTGKTLLARAVAGEAGVPFFSCAASEF 319
Cdd:TIGR01243 446 EVPN--VRWSDIGGLEEVKQELREAVEWpLKHPEIFEKMGIRPPKGVLLFGPPGTGKTLLAKAVATESGANFIAVRGPEI 523
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332007407  320 VELFVGVGASRVRDLFEKAKSKAPCIVFIDEIDAVGRQRGAGMGGGNDEReqTINQLLTEMDGFSGNSGVIVLAATNRPD 399
Cdd:TIGR01243 524 LSKWVGESEKAIREIFRKARQAAPAIIFFDEIDAIAPARGARFDTSVTDR--IVNQLLTEMDGIQELSNVVVIAATNRPD 601
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332007407  400 VLDSALLRPGRFDRQVTVDRPDVAGRVQILKVHSRGKAIGKDVDYEKVARRTPGFTGADLQNLMNEAAILAARRELKEIS 479
Cdd:TIGR01243 602 ILDPALLRPGRFDRLILVPPPDEEARKEIFKIHTRSMPLAEDVDLEELAEMTEGYTGADIEAVCREAAMAALRESIGSPA 681
                         250
                  ....*....|..
gi 332007407  480 KDEISDALERII 491
Cdd:TIGR01243 682 KEKLEVGEEEFL 693
RecA-like_PAN_like cd19502
proteasome activating nucleotidase PAN and related proteasome subunits; This subfamily ...
248-417 1.13e-65

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: 214.51  E-value: 1.13e-65
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332007407 248 TFGDVAGADQAKLELQEVVDF-LKNPDKYTALGAKIPKGCLLVGPPGTGKTLLARAVAGEAGVPFFSCAASEFVELFVGV 326
Cdd:cd19502    1 TYEDIGGLDEQIREIREVVELpLKHPELFEELGIEPPKGVLLYGPPGTGKTLLAKAVANHTDATFIRVVGSELVQKYIGE 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332007407 327 GASRVRDLFEKAKSKAPCIVFIDEIDAVGRQRGAGMGGGNDEREQTINQLLTEMDGFSGNSGVIVLAATNRPDVLDSALL 406
Cdd:cd19502   81 GARLVRELFEMAREKAPSIIFIDEIDAIGAKRFDSGTGGDREVQRTMLELLNQLDGFDPRGNIKVIMATNRPDILDPALL 160
                        170
                 ....*....|.
gi 332007407 407 RPGRFDRQVTV 417
Cdd:cd19502  161 RPGRFDRKIEF 171
CDC48 TIGR01243
AAA family ATPase, CDC48 subfamily; This subfamily of the AAA family ATPases includes two ...
242-481 8.36e-63

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: 222.86  E-value: 8.36e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332007407  242 VPEtgVTFGDVAGADQAKLELQEVVDF-LKNPDKYTALGAKIPKGCLLVGPPGTGKTLLARAVAGEAGVPFFSCAASEFV 320
Cdd:TIGR01243 172 VPK--VTYEDIGGLKEAKEKIREMVELpMKHPELFEHLGIEPPKGVLLYGPPGTGKTLLAKAVANEAGAYFISINGPEIM 249
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332007407  321 ELFVGVGASRVRDLFEKAKSKAPCIVFIDEIDAVGRQRGAGMGggnDEREQTINQLLTEMDGFSGNSGVIVLAATNRPDV 400
Cdd:TIGR01243 250 SKYYGESEERLREIFKEAEENAPSIIFIDEIDAIAPKREEVTG---EVEKRVVAQLLTLMDGLKGRGRVIVIGATNRPDA 326
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332007407  401 LDSALLRPGRFDRQVTVDRPDVAGRVQILKVHSRGKAIGKDVDYEKVARRTPGFTGADLQNLMNEAAILAARRELKEISK 480
Cdd:TIGR01243 327 LDPALRRPGRFDREIVIRVPDKRARKEILKVHTRNMPLAEDVDLDKLAEVTHGFVGADLAALAKEAAMAALRRFIREGKI 406

                  .
gi 332007407  481 D 481
Cdd:TIGR01243 407 N 407
COG1223 COG1223
Predicted ATPase, AAA+ superfamily [General function prediction only];
249-492 7.25e-62

Predicted ATPase, AAA+ superfamily [General function prediction only];


Pssm-ID: 440836 [Multi-domain]  Cd Length: 246  Bit Score: 207.04  E-value: 7.25e-62
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332007407 249 FGDVAGADQAKLELQEVVDFLKNPDKYTALGAKIPKGCLLVGPPGTGKTLLARAVAGEAGVPFFSCAASEFVELFVGVGA 328
Cdd:COG1223    1 LDDVVGQEEAKKKLKLIIKELRRRENLRKFGLWPPRKILFYGPPGTGKTMLAEALAGELKLPLLTVRLDSLIGSYLGETA 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332007407 329 SRVRDLFEKAKSkAPCIVFIDEIDAVGRQRGAGMGGGndEREQTINQLLTEMDGFsgNSGVIVLAATNRPDVLDSALLRp 408
Cdd:COG1223   81 RNLRKLFDFARR-APCVIFFDEFDAIAKDRGDQNDVG--EVKRVVNALLQELDGL--PSGSVVIAATNHPELLDSALWR- 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332007407 409 gRFDRQVTVDRPDVAGRVQILKVHSRGKAIGKDVDYEKVARRTPGFTGADLQNLMNEAAILAARRELKEISKDEISDALE 488
Cdd:COG1223  155 -RFDEVIEFPLPDKEERKEILELNLKKFPLPFELDLKKLAKKLEGLSGADIEKVLKTALKKAILEDREKVTKEDLEEALK 233

                 ....
gi 332007407 489 RIIA 492
Cdd:COG1223  234 QRKE 237
RecA-like_protease cd19481
proteases similar to RecA; RecA-like NTPases. This family includes the NTP binding domain of ...
258-417 1.24e-59

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: 197.89  E-value: 1.24e-59
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332007407 258 AKLELQEVVDFLKNPDKYTALGAKIPKGCLLVGPPGTGKTLLARAVAGEAGVPFFSCAASEFVELFVGVGASRVRDLFEK 337
Cdd:cd19481    1 LKASLREAVEAPRRGSRLRRYGLGLPKGILLYGPPGTGKTLLAKALAGELGLPLIVVKLSSLLSKYVGESEKNLRKIFER 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332007407 338 AKSKAPCIVFIDEIDAVGRQRGAgmGGGNDEREQTINQLLTEMDGFSGNSGVIVLAATNRPDVLDSALLRPGRFDRQVTV 417
Cdd:cd19481   81 ARRLAPCILFIDEIDAIGRKRDS--SGESGELRRVLNQLLTELDGVNSRSKVLVIAATNRPDLLDPALLRPGRFDEVIEF 158
RecA-like_CDC48_r2-like cd19511
second of two ATPase domains of CDC48/p97, PEX1 and -6, VAT and NVL, and similar ATPase ...
258-417 8.95e-59

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: 195.58  E-value: 8.95e-59
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332007407 258 AKLELQEVVDF-LKNPDKYTALGAKIPKGCLLVGPPGTGKTLLARAVAGEAGVPFFSCAASEFVELFVGVGASRVRDLFE 336
Cdd:cd19511    1 VKRELKEAVEWpLKHPDAFKRLGIRPPKGVLLYGPPGCGKTLLAKALASEAGLNFISVKGPELFSKYVGESERAVREIFQ 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332007407 337 KAKSKAPCIVFIDEIDAVGRQRGAGMGGGNDEReqTINQLLTEMDGFSGNSGVIVLAATNRPDVLDSALLRPGRFDRQVT 416
Cdd:cd19511   81 KARQAAPCIIFFDEIDSLAPRRGQSDSSGVTDR--VVSQLLTELDGIESLKGVVVIAATNRPDMIDPALLRPGRLDKLIY 158

                 .
gi 332007407 417 V 417
Cdd:cd19511  159 V 159
RecA-like_CDC48_NLV2_r1-like cd19503
first of two ATPase domains of CDC48 and NLV2, and similar ATPase domains; CDC48 in yeast and ...
251-415 9.65e-58

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: 192.89  E-value: 9.65e-58
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332007407 251 DVAGADQAKLELQEVVDF-LKNPDKYTALGAKIPKGCLLVGPPGTGKTLLARAVAGEAGVPFFSCAASEFVELFVGVGAS 329
Cdd:cd19503    1 DIGGLDEQIASLKELIELpLKYPELFRALGLKPPRGVLLHGPPGTGKTLLARAVANEAGANFLSISGPSIVSKYLGESEK 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332007407 330 RVRDLFEKAKSKAPCIVFIDEIDAVGRQRGAgmggGNDEREQTI-NQLLTEMDGFSGNSGVIVLAATNRPDVLDSALLRP 408
Cdd:cd19503   81 NLREIFEEARSHAPSIIFIDEIDALAPKREE----DQREVERRVvAQLLTLMDGMSSRGKVVVIAATNRPDAIDPALRRP 156

                 ....*..
gi 332007407 409 GRFDRQV 415
Cdd:cd19503  157 GRFDREV 163
PTZ00454 PTZ00454
26S protease regulatory subunit 6B-like protein; Provisional
240-491 3.12e-55

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


Pssm-ID: 240423 [Multi-domain]  Cd Length: 398  Bit Score: 194.21  E-value: 3.12e-55
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332007407 240 QEVPEtgVTFGDVAGADQAKLELQEVVDF-LKNPDKYTALGAKIPKGCLLVGPPGTGKTLLARAVAGEAGVPFFSCAASE 318
Cdd:PTZ00454 137 SEKPD--VTYSDIGGLDIQKQEIREAVELpLTCPELYEQIGIDPPRGVLLYGPPGTGKTMLAKAVAHHTTATFIRVVGSE 214
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332007407 319 FVELFVGVGASRVRDLFEKAKSKAPCIVFIDEIDAVGRQRGAGMGGGNDEREQTINQLLTEMDGFSGNSGVIVLAATNRP 398
Cdd:PTZ00454 215 FVQKYLGEGPRMVRDVFRLARENAPSIIFIDEVDSIATKRFDAQTGADREVQRILLELLNQMDGFDQTTNVKVIMATNRA 294
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332007407 399 DVLDSALLRPGRFDRQVTVDRPDVAGRVQILKVHSRGKAIGKDVDYEKVARRTPGFTGADLQNLMNEAAILAARRELKEI 478
Cdd:PTZ00454 295 DTLDPALLRPGRLDRKIEFPLPDRRQKRLIFQTITSKMNLSEEVDLEDFVSRPEKISAADIAAICQEAGMQAVRKNRYVI 374
                        250
                 ....*....|...
gi 332007407 479 SKDEISDALERII 491
Cdd:PTZ00454 375 LPKDFEKGYKTVV 387
PTZ00361 PTZ00361
26 proteosome regulatory subunit 4-like protein; Provisional
248-491 1.45e-54

26 proteosome regulatory subunit 4-like protein; Provisional


Pssm-ID: 185575 [Multi-domain]  Cd Length: 438  Bit Score: 193.45  E-value: 1.45e-54
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332007407 248 TFGDVAGADQAKLELQEVVDF-LKNPDKYTALGAKIPKGCLLVGPPGTGKTLLARAVAGEAGVPFFSCAASEFVELFVGV 326
Cdd:PTZ00361 181 SYADIGGLEQQIQEIKEAVELpLTHPELYDDIGIKPPKGVILYGPPGTGKTLLAKAVANETSATFLRVVGSELIQKYLGD 260
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332007407 327 GASRVRDLFEKAKSKAPCIVFIDEIDAVGRQRGAGMGGGNDEREQTINQLLTEMDGFSGNSGVIVLAATNRPDVLDSALL 406
Cdd:PTZ00361 261 GPKLVRELFRVAEENAPSIVFIDEIDAIGTKRYDATSGGEKEIQRTMLELLNQLDGFDSRGDVKVIMATNRIESLDPALI 340
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332007407 407 RPGRFDRQVTVDRPDVAGRVQILKVHSRGKAIGKDVDYEKVARRTPGFTGADLQNLMNEAAILAARRELKEISKDEISDA 486
Cdd:PTZ00361 341 RPGRIDRKIEFPNPDEKTKRRIFEIHTSKMTLAEDVDLEEFIMAKDELSGADIKAICTEAGLLALRERRMKVTQADFRKA 420

                 ....*
gi 332007407 487 LERII 491
Cdd:PTZ00361 421 KEKVL 425
RecA-like_VCP_r2 cd19529
second of two ATPase domains of Valosin-containing protein-like ATPase (VAT) and similar ...
258-417 1.42e-53

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: 181.54  E-value: 1.42e-53
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332007407 258 AKLELQEVVDF-LKNPDKYTALGAKIPKGCLLVGPPGTGKTLLARAVAGEAGVPFFSCAASEFVELFVGVGASRVRDLFE 336
Cdd:cd19529    1 VKQELKEAVEWpLLKPEVFKRLGIRPPKGILLYGPPGTGKTLLAKAVATESNANFISVKGPELLSKWVGESEKAIREIFR 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332007407 337 KAKSKAPCIVFIDEIDAVGRQRGAGMGGGNDEReqTINQLLTEMDGFSGNSGVIVLAATNRPDVLDSALLRPGRFDRQVT 416
Cdd:cd19529   81 KARQVAPCVIFFDEIDSIAPRRGTTGDSGVTER--VVNQLLTELDGLEEMNGVVVIAATNRPDIIDPALLRAGRFDRLIY 158

                 .
gi 332007407 417 V 417
Cdd:cd19529  159 I 159
RecA-like_CDC48_r2-like cd19528
second of two ATPase domains of CDC48 and similar ATPase domains; CDC48 in yeast and p97 or ...
259-417 2.98e-53

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: 180.78  E-value: 2.98e-53
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332007407 259 KLELQEVVDF-LKNPDKYTALGAKIPKGCLLVGPPGTGKTLLARAVAGEAGVPFFSCAASEFVELFVGVGASRVRDLFEK 337
Cdd:cd19528    2 KRELQELVQYpVEHPDKFLKFGMTPSKGVLFYGPPGCGKTLLAKAIANECQANFISVKGPELLTMWFGESEANVRDIFDK 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332007407 338 AKSKAPCIVFIDEIDAVGRQRGAGMGGGNDEREQTINQLLTEMDGFSGNSGVIVLAATNRPDVLDSALLRPGRFDRQVTV 417
Cdd:cd19528   82 ARAAAPCVLFFDELDSIAKARGGNIGDAGGAADRVINQILTEMDGMNTKKNVFIIGATNRPDIIDPAILRPGRLDQLIYI 161
AAA pfam00004
ATPase family associated with various cellular activities (AAA); AAA family proteins often ...
287-419 2.22e-52

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: 177.02  E-value: 2.22e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332007407  287 LLVGPPGTGKTLLARAVAGEAGVPFFSCAASEFVELFVGVGASRVRDLFEKAKSKAPCIVFIDEIDAVGRQRGagmGGGN 366
Cdd:pfam00004   2 LLYGPPGTGKTTLAKAVAKELGAPFIEISGSELVSKYVGESEKRLRELFEAAKKLAPCVIFIDEIDALAGSRG---SGGD 78
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 332007407  367 DEREQTINQLLTEMDGFSGN-SGVIVLAATNRPDVLDSALLrpGRFDRQVTVDR 419
Cdd:pfam00004  79 SESRRVVNQLLTELDGFTSSnSKVIVIAATNRPDKLDPALL--GRFDRIIEFPL 130
RecA-like_NVL_r1-like cd19518
first of two ATPase domains of NVL (nuclear VCP-like protein) and similar ATPase domains; NVL ...
251-415 6.03e-50

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: 172.20  E-value: 6.03e-50
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332007407 251 DVAGADQAKLELQEVVDFLK-NPDKYTALGAKIPKGCLLVGPPGTGKTLLARAVAGEAGVPFFSCAASEFVELFVGVGAS 329
Cdd:cd19518    1 DIGGMDSTLKELCELLIHPIlPPEYFQHLGVEPPRGVLLHGPPGCGKTMLANAIAGELKVPFLKISATEIVSGVSGESEE 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332007407 330 RVRDLFEKAKSKAPCIVFIDEIDAVGRQRgagmGGGNDEREQTI-NQLLTEMDGFSGNS----GVIVLAATNRPDVLDSA 404
Cdd:cd19518   81 KIRELFDQAISNAPCIVFIDEIDAITPKR----ESAQREMERRIvSQLLTCMDELNNEKtaggPVLVIGATNRPDSLDPA 156
                        170
                 ....*....|.
gi 332007407 405 LLRPGRFDRQV 415
Cdd:cd19518  157 LRRAGRFDREI 167
RecA-like_NVL_r2-like cd19530
second of two ATPase domains of NVL (nuclear VCP-like protein) and similar ATPase domains; NVL ...
256-417 5.55e-49

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: 169.21  E-value: 5.55e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332007407 256 DQAKLELQ-EVVDFLKNPDKYTALGAKIPKGCLLVGPPGTGKTLLARAVAGEAGVPFFSCAASEFVELFVGVGASRVRDL 334
Cdd:cd19530    2 DHVREELTmSILRPIKRPDIYKALGIDLPTGVLLYGPPGCGKTLLAKAVANESGANFISVKGPELLNKYVGESERAVRQV 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332007407 335 FEKAKSKAPCIVFIDEIDAVGRQRGagmGGGNDEREQTINQLLTEMDGFSGNSGVIVLAATNRPDVLDSALLRPGRFDRQ 414
Cdd:cd19530   82 FQRARASAPCVIFFDEVDALVPKRG---DGGSWASERVVNQLLTEMDGLEERSNVFVIAATNRPDIIDPAMLRPGRLDKT 158

                 ...
gi 332007407 415 VTV 417
Cdd:cd19530  159 LYV 161
RecA-like_CDC48_r1-like cd19519
first of two ATPase domains of CDC48 and similar ATPase domains; CDC48 in yeast and p97 or VCP ...
251-417 1.22e-48

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: 168.38  E-value: 1.22e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332007407 251 DVAGADQAKLELQEVVDF-LKNPDKYTALGAKIPKGCLLVGPPGTGKTLLARAVAGEAGVPFFSCAASEFVELFVGVGAS 329
Cdd:cd19519    1 DIGGCRKQLAQIREMVELpLRHPELFKAIGIKPPRGILLYGPPGTGKTLIARAVANETGAFFFLINGPEIMSKLAGESES 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332007407 330 RVRDLFEKAKSKAPCIVFIDEIDAVGRQRGAGMGggndEREQTI-NQLLTEMDGFSGNSGVIVLAATNRPDVLDSALLRP 408
Cdd:cd19519   81 NLRKAFEEAEKNAPAIIFIDEIDAIAPKREKTHG----EVERRIvSQLLTLMDGLKQRAHVIVMAATNRPNSIDPALRRF 156

                 ....*....
gi 332007407 409 GRFDRQVTV 417
Cdd:cd19519  157 GRFDREIDI 165
RecA-like_PEX1_r2 cd19526
second of two ATPase domains of Peroxisomal biogenesis factor 1 (PEX1); PEX1(also known as ...
258-415 3.35e-44

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: 155.66  E-value: 3.35e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332007407 258 AKLELQEVVDF-LKNPDKYTALGAKIPKGCLLVGPPGTGKTLLARAVAGEAGVPFFSCAASEFVELFVGVGASRVRDLFE 336
Cdd:cd19526    1 VKKALEETIEWpSKYPKIFASSPLRLRSGILLYGPPGCGKTLLASAIASECGLNFISVKGPELLNKYIGASEQNVRDLFS 80
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 332007407 337 KAKSKAPCIVFIDEIDAVGRQRGAGMGGGNDereQTINQLLTEMDGFSGNSGVIVLAATNRPDVLDSALLRPGRFDRQV 415
Cdd:cd19526   81 RAQSAKPCILFFDEFDSIAPKRGHDSTGVTD---RVVNQLLTQLDGVEGLDGVYVLAATSRPDLIDPALLRPGRLDKLV 156
RecA-like_PEX6_r2 cd19527
second of two ATPase domains of Peroxisomal biogenesis factor 6 (PEX6); PEX6(also known as ...
259-417 5.71e-41

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: 146.89  E-value: 5.71e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332007407 259 KLELQEVVDF-LKNPDKYtALGAKIPKGCLLVGPPGTGKTLLARAVAGEAGVPFFSCAASEFVELFVGVGASRVRDLFEK 337
Cdd:cd19527    2 KKEILDTIQLpLEHPELF-SSGLRKRSGILLYGPPGTGKTLLAKAIATECSLNFLSVKGPELINMYIGESEANVREVFQK 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332007407 338 AKSKAPCIVFIDEIDAVGRQRGA-GMGGGNDEReqTINQLLTEMDGFS-GNSGVIVLAATNRPDVLDSALLRPGRFDRQV 415
Cdd:cd19527   81 ARDAKPCVIFFDELDSLAPSRGNsGDSGGVMDR--VVSQLLAELDGMSsSGQDVFVIGATNRPDLLDPALLRPGRFDKLL 158

                 ..
gi 332007407 416 TV 417
Cdd:cd19527  159 YL 160
RecA-like_VPS4-like cd19509
ATPase domain of VPS4, ATAD1, K, KTNA1, Spastin, FIGL-1 and similar ATPase domains; This ...
252-417 3.21e-39

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: 142.11  E-value: 3.21e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332007407 252 VAGADQAKLELQEVVDF-LKNPDKYTaLGAKIPKGCLLVGPPGTGKTLLARAVAGEAGVPFFSCAASEFVELFVGVGASR 330
Cdd:cd19509    1 IAGLDDAKEALKEAVILpSLRPDLFP-GLRGPPRGILLYGPPGTGKTLLARAVASESGSTFFSISASSLVSKWVGESEKI 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332007407 331 VRDLFEKAKSKAPCIVFIDEIDAVGRQRGAgmggGNDEREQTI-NQLLTEMDGF--SGNSGVIVLAATNRPDVLDSALLR 407
Cdd:cd19509   80 VRALFALARELQPSIIFIDEIDSLLSERGS----GEHEASRRVkTEFLVQMDGVlnKPEDRVLVLGATNRPWELDEAFLR 155
                        170
                 ....*....|
gi 332007407 408 pgRFDRQVTV 417
Cdd:cd19509  156 --RFEKRIYI 163
pup_AAA TIGR03689
proteasome ATPase; In the Actinobacteria, as shown for Mycobacterium tuberculosis, some ...
240-432 1.81e-38

proteasome ATPase; In the Actinobacteria, as shown for Mycobacterium tuberculosis, some proteins are modified by ligation between an epsilon-amino group of a lysine side chain and the C-terminal carboxylate of the ubiquitin-like protein Pup. This modification leads to protein degradation by the archaeal-like proteasome found in the Actinobacteria. Members of this protein family belong to the AAA family of ATPases and tend to be clustered with the genes for Pup, the Pup ligase PafA, and structural components of the proteasome. This protein forms hexameric rings with ATPase activity. [Protein fate, Degradation of proteins, peptides, and glycopeptides]


Pssm-ID: 200312 [Multi-domain]  Cd Length: 512  Bit Score: 149.86  E-value: 1.81e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332007407  240 QEVPEtgVTFGDVAGADQAKLELQEVVD--FLkNPDKYTALGAKIPKGCLLVGPPGTGKTLLARAVA--------GEAGV 309
Cdd:TIGR03689 174 EEVPD--VTYADIGGLGSQIEQIRDAVElpFL-HPELYREYGLKPPKGVLLYGPPGCGKTLIAKAVAnslaarigAEGGG 250
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332007407  310 P--FFSCAASEFVELFVGVGASRVRDLFEKAKSKA----PCIVFIDEIDAVGRQRGAGMgggNDEREQTI-NQLLTEMDG 382
Cdd:TIGR03689 251 KsyFLNIKGPELLNKYVGETERQIRLIFQRAREKAsegrPVIVFFDEMDSLFRTRGSGV---SSDVETTVvPQLLAEIDG 327
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 332007407  383 FSGNSGVIVLAATNRPDVLDSALLRPGRFDRQVTVDRPDVAGRVQILKVH 432
Cdd:TIGR03689 328 VESLDNVIVIGASNREDMIDPAILRPGRLDVKIRIERPDAEAAADIFAKY 377
RecA-like_VPS4 cd19521
ATPase domain of vacuolar protein sorting-associated protein 4; Vacuolar protein ...
247-417 6.36e-35

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: 130.37  E-value: 6.36e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332007407 247 VTFGDVAGADQAKLELQEVVDF-LKNPDKYTalGAKIP-KGCLLVGPPGTGKTLLARAVAGEAGVPFFSCAASEFVELFV 324
Cdd:cd19521    4 VKWEDVAGLEGAKEALKEAVILpVKFPHLFT--GNRKPwSGILLYGPPGTGKSYLAKAVATEANSTFFSVSSSDLVSKWM 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332007407 325 GVGASRVRDLFEKAKSKAPCIVFIDEIDAVGRQRGAGMgggNDEREQTINQLLTEMDGFSGNS-GVIVLAATNRPDVLDS 403
Cdd:cd19521   82 GESEKLVKQLFAMARENKPSIIFIDEVDSLCGTRGEGE---SEASRRIKTELLVQMNGVGNDSqGVLVLGATNIPWQLDS 158
                        170
                 ....*....|....
gi 332007407 404 ALLRpgRFDRQVTV 417
Cdd:cd19521  159 AIRR--RFEKRIYI 170
RecA-like_spastin cd19524
ATPase domain of spastin; Spastin is an ATP-dependent microtubule-severing protein involved in ...
251-417 6.51e-33

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: 124.58  E-value: 6.51e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332007407 251 DVAGADQAKLELQEVVDF-LKNPDKYTALGAKiPKGCLLVGPPGTGKTLLARAVAGEAGVPFFSCAASEFVELFVGVGAS 329
Cdd:cd19524    1 DIAGQDLAKQALQEMVILpSLRPELFTGLRAP-ARGLLLFGPPGNGKTMLAKAVAAESNATFFNISAASLTSKYVGEGEK 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332007407 330 RVRDLFEKAKSKAPCIVFIDEIDAVGRQRGAGMgggNDEREQTINQLLTEMDGFSGNSG--VIVLAATNRPDVLDSALLR 407
Cdd:cd19524   80 LVRALFAVARELQPSIIFIDEVDSLLSERSEGE---HEASRRLKTEFLIEFDGVQSNGDdrVLVMGATNRPQELDDAVLR 156
                        170
                 ....*....|
gi 332007407 408 pgRFDRQVTV 417
Cdd:cd19524  157 --RFTKRVYV 164
RecA-like_Figl-1 cd19525
ATPase domain of Fidgetin-Like 1 (FIGL-1); FIGL-1 may participate in DNA repair in the nucleus; ...
247-417 7.09e-33

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: 125.10  E-value: 7.09e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332007407 247 VTFGDVAGADQAKLELQEVVDF-LKNPDKYTALGAKiPKGCLLVGPPGTGKTLLARAVAGEAGVPFFSCAASEFVELFVG 325
Cdd:cd19525   19 INWADIAGLEFAKKTIKEIVVWpMLRPDIFTGLRGP-PKGILLFGPPGTGKTLIGKCIASQSGATFFSISASSLTSKWVG 97
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332007407 326 VGASRVRDLFEKAKSKAPCIVFIDEIDAVGRQRGAGMgggNDEREQTINQLLTEMDGFSGNSG--VIVLAATNRPDVLDS 403
Cdd:cd19525   98 EGEKMVRALFSVARCKQPAVIFIDEIDSLLSQRGEGE---HESSRRIKTEFLVQLDGATTSSEdrILVVGATNRPQEIDE 174
                        170
                 ....*....|....
gi 332007407 404 ALLRpgRFDRQVTV 417
Cdd:cd19525  175 AARR--RLVKRLYI 186
RecA-like_Yta7-like cd19517
ATPase domain of Saccharomyces cerevisiae Yta7 and similar ATPase domains; Saccharomyces ...
251-414 2.46e-32

ATPase domain of Saccharomyces cerevisiae Yta7 and similar ATPase domains; Saccharomyces cerevisiae Yta7 is a chromatin-associated AAA-ATPase involved in regulation of chromatin dynamics. Its human ortholog ANCCA/ATAD2 transcriptionally activates pathways of malignancy in a broad range of cancers. The RecA-like_Yta7 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: 410925 [Multi-domain]  Cd Length: 170  Bit Score: 123.00  E-value: 2.46e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332007407 251 DVAGADQAKLELQEVVDF-LKNPDKYTALGAKIPKGCLLVGPPGTGKTLLARAVAGEAG-----VPFFSCAASEFVELFV 324
Cdd:cd19517    1 DIGGLSHYINQLKEMVFFpLLYPEVFAKFKITPPRGVLFHGPPGTGKTLMARALAAECSkggqkVSFFMRKGADCLSKWV 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332007407 325 GVGASRVRDLFEKAKSKAPCIVFIDEIDAVGRQRGAgmgggndEREQT----INQLLTEMDGFSGNSGVIVLAATNRPDV 400
Cdd:cd19517   81 GEAERQLRLLFEEAYRMQPSIIFFDEIDGLAPVRSS-------KQEQIhasiVSTLLALMDGLDNRGQVVVIGATNRPDA 153
                        170
                 ....*....|....
gi 332007407 401 LDSALLRPGRFDRQ 414
Cdd:cd19517  154 LDPALRRPGRFDRE 167
RecA-like_KTNA1 cd19522
Katanin p60 ATPase-containing subunit A1; Katanin p60 ATPase-containing subunit A1 (KTNA1) is ...
251-417 6.84e-32

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: 121.63  E-value: 6.84e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332007407 251 DVAGADQAKLELQE-VVDFLKNPDKYTalGAKIP-KGCLLVGPPGTGKTLLARAVAGEAGVPFFSCAASEFVELFVGVGA 328
Cdd:cd19522    1 DIADLEEAKKLLEEaVVLPMWMPEFFK--GIRRPwKGVLMVGPPGTGKTLLAKAVATECGTTFFNVSSSTLTSKYRGESE 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332007407 329 SRVRDLFEKAKSKAPCIVFIDEIDAVGRQRGAgmGGGNDEREQTINQLLTEMDGFSGNSG-------VIVLAATNRPDVL 401
Cdd:cd19522   79 KLVRLLFEMARFYAPTTIFIDEIDSICSRRGT--SEEHEASRRVKSELLVQMDGVGGASEnddpskmVMVLAATNFPWDI 156
                        170
                 ....*....|....*.
gi 332007407 402 DSALLRpgRFDRQVTV 417
Cdd:cd19522  157 DEALRR--RLEKRIYI 170
RecA-like_ATAD1 cd19520
ATPase domain of ATPase family AAA domain-containing protein 1 and similar ATPase domains; ...
251-411 1.79e-30

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: 117.53  E-value: 1.79e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332007407 251 DVAGADQAKLELQEVVDF-LKNPDKYTALG-AKIPKGCLLVGPPGTGKTLLARAVAGEAGVPFFSCAASEFVELFVGVGA 328
Cdd:cd19520    1 DIGGLDEVITELKELVILpLQRPELFDNSRlLQPPKGVLLYGPPGCGKTMLAKATAKEAGARFINLQVSSLTDKWYGESQ 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332007407 329 SRVRDLFEKAKSKAPCIVFIDEIDAVGRQRGAGmgggndEREQTI---NQLLTEMDGFS--GNSGVIVLAATNRPDVLDS 403
Cdd:cd19520   81 KLVAAVFSLASKLQPSIIFIDEIDSFLRQRSST------DHEATAmmkAEFMSLWDGLStdGNCRVIVMGATNRPQDLDE 154
                        170
                 ....*....|
gi 332007407 404 ALLR--PGRF 411
Cdd:cd19520  155 AILRrmPKRF 164
RecA-like_NSF-SEC18_r1-like cd19504
first of two ATPase domains of NSF and SEC18, and similar ATPase domains; ...
272-417 1.47e-28

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: 112.58  E-value: 1.47e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332007407 272 PDKYTALGAKIPKGCLLVGPPGTGKTLLARAV-----AGEAGVpffsCAASEFVELFVGVGASRVRDLFEKA----KSKA 342
Cdd:cd19504   24 PEIVEQLGCKHVKGILLYGPPGTGKTLMARQIgkmlnAREPKI----VNGPEILNKYVGESEANIRKLFADAeeeqRRLG 99
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 332007407 343 PC----IVFIDEIDAVGRQRGAgMGGGNDEREQTINQLLTEMDGFSGNSGVIVLAATNRPDVLDSALLRPGRFDRQVTV 417
Cdd:cd19504  100 ANsglhIIIFDEIDAICKQRGS-MAGSTGVHDTVVNQLLSKIDGVEQLNNILVIGMTNRKDLIDEALLRPGRLEVQMEI 177
ycf46 CHL00195
Ycf46; Provisional
247-491 6.37e-27

Ycf46; Provisional


Pssm-ID: 177094 [Multi-domain]  Cd Length: 489  Bit Score: 115.12  E-value: 6.37e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332007407 247 VTFGDVAGADQAKLELQEVVD-FLKNPDKYtalGAKIPKGCLLVGPPGTGKTLLARAVAGEAGVPFFSCaasEFVELF-- 323
Cdd:CHL00195 225 EKISDIGGLDNLKDWLKKRSTsFSKQASNY---GLPTPRGLLLVGIQGTGKSLTAKAIANDWQLPLLRL---DVGKLFgg 298
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332007407 324 -VGVGASRVRDLFEKAKSKAPCIVFIDEID-AVGRQRGAGMGGGNDEREQTINQLLTEMdgfsgNSGVIVLAATNRPDVL 401
Cdd:CHL00195 299 iVGESESRMRQMIRIAEALSPCILWIDEIDkAFSNSESKGDSGTTNRVLATFITWLSEK-----KSPVFVVATANNIDLL 373
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332007407 402 DSALLRPGRFDRQVTVDRPDVAGRVQILKVH---SRGKAIgKDVDYEKVARRTPGFTGADLQNLMNEaAILAARRELKEI 478
Cdd:CHL00195 374 PLEILRKGRFDEIFFLDLPSLEEREKIFKIHlqkFRPKSW-KKYDIKKLSKLSNKFSGAEIEQSIIE-AMYIAFYEKREF 451
                        250
                 ....*....|...
gi 332007407 479 SKDEISDALERII 491
Cdd:CHL00195 452 TTDDILLALKQFI 464
AAA cd00009
The AAA+ (ATPases Associated with a wide variety of cellular Activities) superfamily ...
253-418 3.76e-25

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: 101.84  E-value: 3.76e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332007407 253 AGADQAKLELQEVVDflknpdkytalgAKIPKGCLLVGPPGTGKTLLARAVAGEA---GVPFFSCAASEFVELFVG---V 326
Cdd:cd00009    1 VGQEEAIEALREALE------------LPPPKNLLLYGPPGTGKTTLARAIANELfrpGAPFLYLNASDLLEGLVVaelF 68
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332007407 327 GASRVRDLFEKAKSKAPCIVFIDEIDAVGRqrgagmgggnDEREQTINQLLTEMDGFSGNSGVIVLAATNRPDVLDSALL 406
Cdd:cd00009   69 GHFLVRLLFELAEKAKPGVLFIDEIDSLSR----------GAQNALLRVLETLNDLRIDRENVRVIGATNRPLLGDLDRA 138
                        170
                 ....*....|..
gi 332007407 407 RPGRFDRQVTVD 418
Cdd:cd00009  139 LYDRLDIRIVIP 150
RecA-like_fidgetin cd19523
ATPase domain of fidgetin; Fidgetin (FIGN) is a ATP-dependent microtubule severing protein. ...
251-407 6.59e-21

ATPase domain of fidgetin; Fidgetin (FIGN) is a ATP-dependent microtubule severing protein. This subfamily belongs to the RecA-like NTPase family which includes the NTP binding domain of F1 and V1 H(+)ATPases, DnaB and related helicases as well as bacterial RecA and related eukaryotic and archaeal recombinases. The RecA-like NTPase family also includes bacterial conjugation proteins and related DNA transfer proteins involved in type II and type IV secretion.


Pssm-ID: 410931 [Multi-domain]  Cd Length: 163  Bit Score: 89.94  E-value: 6.59e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332007407 251 DVAGADQAKLELQ-EVVDFLKNPDKYTALgAKIPKGCLLVGPPGTGKTLLARAVAGEAGVPFFSCAASEFVELFVGVGAS 329
Cdd:cd19523    1 DIAGLGALKAAIKeEVLWPLLRPDAFSGL-LRLPRSILLFGPRGTGKTLLGRCLASQLGATFLRLRGSTLVAKWAGEGEK 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332007407 330 RVRDLFEKAKSKAPCIVFIDEIDAVGRQRGAGMGGGNdeREQTinQLLTEMDGF--SGNSGVIVLAATNRPDVLDSALLR 407
Cdd:cd19523   80 ILQASFLAARCRQPSVLFISDLDALLSSQDDEASPVG--RLQV--ELLAQLDGVlgSGEDGVLVVCTTSKPEEIDESLRR 155
RecA-like_Ycf46-like cd19507
ATPase domain of Ycf46 and similar ATPase domains; Ycf46 may play a role in the regulation of ...
251-413 9.55e-21

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: 89.74  E-value: 9.55e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332007407 251 DVAGADQAKLELQE-VVDFLKNPDKYtalGAKIPKGCLLVGPPGTGKTLLARAVAGEAGVPFFSCAASEFVELFVGVGAS 329
Cdd:cd19507    1 DVGGLDNLKDWLKKrKAAFSKQASAY---GLPTPKGLLLVGIQGTGKSLTAKAIAGVWQLPLLRLDMGRLFGGLVGESES 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332007407 330 RVRDLFEKAKSKAPCIVFIDEID-AVGRQRGAGMGGGNderEQTINQLLTEMDgfSGNSGVIVLAATNRPDVLDSALLRP 408
Cdd:cd19507   78 RLRQMIQTAEAIAPCVLWIDEIEkGFSNADSKGDSGTS---SRVLGTFLTWLQ--EKKKPVFVVATANNVQSLPPELLRK 152

                 ....*
gi 332007407 409 GRFDR 413
Cdd:cd19507  153 GRFDE 157
RecA-like_BCS1 cd19510
Mitochondrial chaperone BCS1; Mitochondrial chaperone BCS1 is necessary for the assembly of ...
262-417 3.40e-19

Mitochondrial chaperone BCS1; Mitochondrial chaperone BCS1 is necessary for the assembly of mitochondrial respiratory chain complex III and plays an important role in the maintenance of mitochondrial tubular networks, respiratory chain assembly and formation of the LETM1 complex. 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: 410918 [Multi-domain]  Cd Length: 153  Bit Score: 84.71  E-value: 3.40e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332007407 262 LQEVVDFLKNPDKYTALGAKIPKGCLLVGPPGTGKTLLARAVAGEAGVPFFSCAASEfvelfVGVGASRVRDLFEKAKSK 341
Cdd:cd19510    2 IDDLKDFIKNEDWYNDRGIPYRRGYLLYGPPGTGKSSFIAALAGELDYDICDLNLSE-----VVLTDDRLNHLLNTAPKQ 76
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 332007407 342 ApcIVFIDEIDAV---GRQRGAGMGGGNDEREQTINQLLTEMDGFSGNSGVIVLAATNRPDVLDSALLRPGRFDRQVTV 417
Cdd:cd19510   77 S--IILLEDIDAAfesREHNKKNPSAYGGLSRVTFSGLLNALDGVASSEERIVFMTTNHIERLDPALIRPGRVDMKIYM 153
AAA smart00382
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ...
283-421 3.64e-18

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: 81.65  E-value: 3.64e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332007407   283 PKGCLLVGPPGTGKTLLARAVAGEA---GVPFFSCAASEFVE--------------LFVGVGASRVRDLFEKAKSKAPCI 345
Cdd:smart00382   2 GEVILIVGPPGSGKTTLARALARELgppGGGVIYIDGEDILEevldqllliivggkKASGSGELRLRLALALARKLKPDV 81
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 332007407   346 VFIDEIDAVGRQRGagmgggndEREQTINQLLTEMDGFSGNSGVIVLAATNRPDVLDSALLRPgRFDRQVTVDRPD 421
Cdd:smart00382  82 LILDEITSLLDAEQ--------EALLLLLEELRLLLLLKSEKNLTVILTTNDEKDLGPALLRR-RFDRRIVLLLIL 148
AAA_lid_3 pfam17862
AAA+ lid domain; This entry represents the alpha helical AAA+ lid domain that is found to the ...
441-485 3.56e-14

AAA+ lid domain; This entry represents the alpha helical AAA+ lid domain that is found to the C-terminus of AAA domains.


Pssm-ID: 465537 [Multi-domain]  Cd Length: 45  Bit Score: 66.79  E-value: 3.56e-14
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 332007407  441 DVDYEKVARRTPGFTGADLQNLMNEAAILAARRELKEISKDEISD 485
Cdd:pfam17862   1 DVDLEELAERTEGFSGADLEALCREAALAALRRGLEAVTQEDLEE 45
RecA-like_HslU cd19498
ATP-dependent protease ATPase subunit HslU; HslU is a component of the ATP-dependent protease ...
282-382 7.00e-11

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: 61.63  E-value: 7.00e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332007407 282 IPKGCLLVGPPGTGKTLLARAVAGEAGVPFFSCAASEFVEL-FVGVGA-SRVRDLFEKakskapcIVFIDEIDAVGRQRG 359
Cdd:cd19498   45 TPKNILMIGPTGVGKTEIARRLAKLAGAPFIKVEATKFTEVgYVGRDVeSIIRDLVEG-------IVFIDEIDKIAKRGG 117
                         90       100
                 ....*....|....*....|...
gi 332007407 360 AgmGGGNDEREQTINQLLTEMDG 382
Cdd:cd19498  118 S--SGPDVSREGVQRDLLPIVEG 138
RecA-like_Ycf2 cd19505
ATPase domain of plant YCF2; Ycf2 is a chloroplast ATPase which has an essential function; ...
278-413 2.68e-10

ATPase domain of plant YCF2; Ycf2 is a chloroplast ATPase which has an essential function; however, its function remains unclear. The gene encoding YCF2 is the largest known plastid gene in angiosperms and has been used to predict phylogenetic relationships. 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: 410913 [Multi-domain]  Cd Length: 161  Bit Score: 59.31  E-value: 2.68e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332007407 278 LGAKIPKGCLLVGPPGTGKTLLARAVAGEAGVPFFSCAASEFV--------------ELFVGVGASRVRDLFEKAKSKAP 343
Cdd:cd19505    7 LGLSPSKGILLIGSIETGRSYLIKSLAANSYVPLIRISLNKLLynkpdfgnddwidgMLILKESLHRLNLQFELAKAMSP 86
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 332007407 344 CIVFIDEIDAVGRQRGAGMGGGNdeREQTINQLLTEM-DGFSGNS--GVIVLAATNRPDVLDSALLRPGRFDR 413
Cdd:cd19505   87 CIIWIPNIHELNVNRSTQNLEED--PKLLLGLLLNYLsRDFEKSStrNILVIASTHIPQKVDPALIAPNRLDT 157
RecA-like_ATAD3-like cd19512
ATPase domains of ATPase AAA-domain protein 3A (ATAD3A), -3B, and -3C, and similar ATPase ...
287-415 6.10e-10

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: 58.31  E-value: 6.10e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332007407 287 LLVGPPGTGKTLLARAVAGEAGVPFFSCAASEFVELfvGV-GASRVRDLFEKA-KSKAPCIVFIDEIDAVGRQRgAGMGG 364
Cdd:cd19512   26 LFYGPPGTGKTLFAKKLALHSGMDYAIMTGGDVAPM--GReGVTAIHKVFDWAnTSRRGLLLFVDEADAFLRKR-STEKI 102
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 332007407 365 GNDEReQTINQLLTEMdGFSGNSGVIVLaATNRPDVLDSALlrPGRFDRQV 415
Cdd:cd19512  103 SEDLR-AALNAFLYRT-GEQSNKFMLVL-ASNQPEQFDWAI--NDRIDEMV 148
PRK04195 PRK04195
replication factor C large subunit; Provisional
248-352 1.38e-08

replication factor C large subunit; Provisional


Pssm-ID: 235250 [Multi-domain]  Cd Length: 482  Bit Score: 57.62  E-value: 1.38e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332007407 248 TFGDVAGADQAKLELQEVVD-FLKNpdkytalgaKIPKGCLLVGPPGTGKTLLARAVAGEAGVPFFSCAASEF-----VE 321
Cdd:PRK04195  12 TLSDVVGNEKAKEQLREWIEsWLKG---------KPKKALLLYGPPGVGKTSLAHALANDYGWEVIELNASDQrtadvIE 82
                         90       100       110
                 ....*....|....*....|....*....|.
gi 332007407 322 LFVGvGASRVRDLFEKAKSkapcIVFIDEID 352
Cdd:PRK04195  83 RVAG-EAATSGSLFGARRK----LILLDEVD 108
RarA COG2256
Replication-associated recombination protein RarA (DNA-dependent ATPase) [Replication, ...
290-351 1.38e-08

Replication-associated recombination protein RarA (DNA-dependent ATPase) [Replication, recombination and repair];


Pssm-ID: 441857 [Multi-domain]  Cd Length: 439  Bit Score: 57.76  E-value: 1.38e-08
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 332007407 290 GPPGTGKTLLARAVAGEAGvpffscaaSEFVEL---FVGVgaSRVRDLFEKAKSKA----PCIVFIDEI 351
Cdd:COG2256   56 GPPGTGKTTLARLIANATD--------AEFVALsavTSGV--KDIREVIEEARERRaygrRTILFVDEI 114
PRK13342 PRK13342
recombination factor protein RarA; Reviewed
286-351 2.13e-08

recombination factor protein RarA; Reviewed


Pssm-ID: 237355 [Multi-domain]  Cd Length: 413  Bit Score: 57.02  E-value: 2.13e-08
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332007407 286 CLLVGPPGTGKTLLARAVAGEAGVPFFSCAASefvelFVGVgaSRVRDLFEKAKSKA----PCIVFIDEI 351
Cdd:PRK13342  39 MILWGPPGTGKTTLARIIAGATDAPFEALSAV-----TSGV--KDLREVIEEARQRRsagrRTILFIDEI 101
RecA-like_Pch2-like cd19508
ATPase domain of Pachytene checkpoint 2 (Pch2) and similar ATPase domains; Pch2 (known as ...
287-422 1.55e-07

ATPase domain of Pachytene checkpoint 2 (Pch2) and similar ATPase domains; Pch2 (known as Thyroid hormone receptor interactor 13 (TRIP13) and 16E1BP) is a key regulator of specific chromosomal events, like the control of G2/prophase processes such as DNA break formation and recombination, checkpoint signaling, and chromosome synapsis. 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: 410916 [Multi-domain]  Cd Length: 199  Bit Score: 52.45  E-value: 1.55e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332007407 287 LLVGPPGTGKTLLARAVAGEAGVPF-FSCAASEFVEL--------FVGVGASRVRDLFEKAKS-----KAPCIVFIDEID 352
Cdd:cd19508   56 LLHGPPGTGKTSLCKALAQKLSIRLsSRYRYGQLIEInshslfskWFSESGKLVTKMFQKIQEliddkDALVFVLIDEVE 135
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 332007407 353 AVGRQRGAgMGGGNDERE--QTINQLLTEMDGFSGNSGVIVLAATNRPDVLDSALlrpgrfdrqvtVDRPDV 422
Cdd:cd19508  136 SLAAARSA-SSSGTEPSDaiRVVNAVLTQIDRIKRYHNNVILLTSNLLEKIDVAF-----------VDRADI 195
AAA_5 pfam07728
AAA domain (dynein-related subfamily); This Pfam entry includes some of the AAA proteins not ...
287-411 8.01e-07

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: 48.83  E-value: 8.01e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332007407  287 LLVGPPGTGKTLLARAVAgEA--GVPFFSCAASEFV---ELF----VGVGASRVRD--LFEKAKSKapCIVFIDEIDAVG 355
Cdd:pfam07728   3 LLVGPPGTGKTELAERLA-AAlsNRPVFYVQLTRDTteeDLFgrrnIDPGGASWVDgpLVRAAREG--EIAVLDEINRAN 79
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 332007407  356 RQRGAGMGGGNDEREQTINQLLTEMDgfSGNSGVIVLAATNRPD----VLDSALLRpgRF 411
Cdd:pfam07728  80 PDVLNSLLSLLDERRLLLPDGGELVK--AAPDGFRLIATMNPLDrglnELSPALRS--RF 135
DnaA COG0593
Chromosomal replication initiation ATPase DnaA [Replication, recombination and repair];
287-512 8.81e-07

Chromosomal replication initiation ATPase DnaA [Replication, recombination and repair];


Pssm-ID: 440358 [Multi-domain]  Cd Length: 303  Bit Score: 51.35  E-value: 8.81e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332007407 287 LLVGPPGTGKTLLARAVAGEAGVPFFS-----CAASEFVELFvgVGASRVRDLFE-KAKSKAPCIVFIDEIdavgrQRGA 360
Cdd:COG0593   38 FLYGGVGLGKTHLLHAIGNEALENNPGarvvyLTAEEFTNDF--INAIRNNTIEEfKEKYRSVDVLLIDDI-----QFLA 110
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332007407 361 GmgggnDEREQ-----TINQLLtemdgfsgNSGV-IVLAATNRPDVLDSAL--LRpGRFDRQVTVD--RPDVAGRVQIL- 429
Cdd:COG0593  111 G-----KEATQeeffhTFNALR--------EAGKqIVLTSDRPPKELPGLEerLR-SRLEWGLVVDiqPPDLETRIAILr 176
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332007407 430 -KVHSRGKAIGKDV-DYekVARRTPGfTGADLQNLMNeAAILAARRELKEISKDEISDALERIIAGPEKKnaVVSEEKKR 507
Cdd:COG0593  177 kKAADRGLELPDEVlEY--LARRIER-NVRELEGALN-RLDAYALLTGRPITLELAREVLKDLLRAQKKE--ITIEDIQK 250

                 ....*
gi 332007407 508 LVAYH 512
Cdd:COG0593  251 AVAEY 255
RecA-like_superfamily cd01120
RecA-like_NTPases; RecA-like NTPases. This superfamily includes the NTP binding domain of F1 ...
287-402 3.85e-06

RecA-like_NTPases; RecA-like NTPases. This superfamily 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: 410865 [Multi-domain]  Cd Length: 119  Bit Score: 46.34  E-value: 3.85e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332007407 287 LLVGPPGTGKTLLARAVAGEAgvpffscAASEfvelFVGVGASRVRDLFEKAKS----KAPCIVFIDEIDAVGRQRgagm 362
Cdd:cd01120    2 LITGPPGSGKTTLLLQFAEQA-------LLSD----EPVIFISFLDTILEAIEDlieeKKLDIIIIDSLSSLARAS---- 66
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 332007407 363 ggGNDEREQTINQLLTEMdGFSGNSGVIVLAATNRPDVLD 402
Cdd:cd01120   67 --QGDRSSELLEDLAKLL-RAARNTGITVIATIHSDKFDI 103
TIP49 COG1224
DNA helicase TIP49, TBP-interacting protein [Transcription];
284-319 4.31e-06

DNA helicase TIP49, TBP-interacting protein [Transcription];


Pssm-ID: 440837 [Multi-domain]  Cd Length: 452  Bit Score: 49.58  E-value: 4.31e-06
                         10        20        30
                 ....*....|....*....|....*....|....*...
gi 332007407 284 KGCLLVGPPGTGKTLLARAVAGEAG--VPFFSCAASEF 319
Cdd:COG1224   65 KGILIVGPPGTGKTALAVAIARELGedTPFVAISGSEI 102
AAA_2 pfam07724
AAA domain (Cdc48 subfamily); This Pfam entry includes some of the AAA proteins not detected ...
287-352 5.40e-06

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: 47.19  E-value: 5.40e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 332007407  287 LLVGPPGTGKTLLARAVAGEAGV---PFFSCAASEFVE-----LFVG-----VGASRVRDLFEKAKSKAPCIVFIDEID 352
Cdd:pfam07724   7 LFLGPTGVGKTELAKALAELLFGderALIRIDMSEYMEehsvsRLIGappgyVGYEEGGQLTEAVRRKPYSIVLIDEIE 85
MoxR COG0714
MoxR-like ATPase [General function prediction only]; MoxR-like ATPase is part of the Pathway ...
286-492 6.15e-06

MoxR-like ATPase [General function prediction only]; MoxR-like ATPase is part of the Pathway/BioSystem: Cobalamine/B12 biosynthesis


Pssm-ID: 440478 [Multi-domain]  Cd Length: 292  Bit Score: 48.63  E-value: 6.15e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332007407 286 CLLVGPPGTGKTLLARAVAGEAGVPFF----------------SCAASEFVELFVGVGAsrvrdLFEkakskapCIVFID 349
Cdd:COG0714   34 LLLEGVPGVGKTTLAKALARALGLPFIriqftpdllpsdilgtYIYDQQTGEFEFRPGP-----LFA-------NVLLAD 101
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332007407 350 EIDavgrqRGagmgggndeREQTINQLLTEM-------DG--FSGNSGVIVLAATNRPDV-----LDSALLRpgRFDRQV 415
Cdd:COG0714  102 EIN-----RA---------PPKTQSALLEAMeerqvtiPGgtYKLPEPFLVIATQNPIEQegtypLPEAQLD--RFLLKL 165
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 332007407 416 TVDRPDVAGRVQILkvhsrgkaigkdvdyekvaRRTPGFTGADLQNLMNEAAILAARRELKEIskdEISDALERIIA 492
Cdd:COG0714  166 YIGYPDAEEEREIL-------------------RRHTGRHLAEVEPVLSPEELLALQELVRQV---HVSEAVLDYIV 220
CDC6 COG1474
Cdc6-related protein, AAA superfamily ATPase [Replication, recombination and repair];
261-490 1.11e-05

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


Pssm-ID: 441083 [Multi-domain]  Cd Length: 389  Bit Score: 48.31  E-value: 1.11e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332007407 261 ELQEVVDFLKnpdkyTALGAKIPKGCLLVGPPGTGKTLLARAV-------AGEAGVPFFSC------------AASEFVE 321
Cdd:COG1474   34 EIEELASALR-----PALRGERPSNVLIYGPTGTGKTAVAKYVleeleeeAEERGVDVRVVyvncrqastryrVLSRILE 108
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332007407 322 LFV--------GVGASRVRDLFEKA--KSKAPCIVFIDEIDAVGRqrgagmgggnDEREQTINQLLTEMDGFSGNS-GVI 390
Cdd:COG1474  109 ELGsgedipstGLSTDELFDRLYEAldERDGVLVVVLDEIDYLVD----------DEGDDLLYQLLRANEELEGARvGVI 178
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332007407 391 vlAATNRPDV---LDSALLRpgRF-DRQVTVDRPDVAGRVQILKVHS----RGKAIGKDVdYEKVARRTPGFTGaDLQ-- 460
Cdd:COG1474  179 --GISNDLEFlenLDPRVKS--SLgEEEIVFPPYDADELRDILEDRAelafYDGVLSDEV-IPLIAALAAQEHG-DARka 252
                        250       260       270
                 ....*....|....*....|....*....|.
gi 332007407 461 -NLMNEAAILAARRELKEISKDEISDALERI 490
Cdd:COG1474  253 iDLLRVAGEIAEREGSDRVTEEHVREAREKI 283
RecA-like_ClpX cd19497
ATP-dependent Clp protease ATP-binding subunit ClpX; ClpX is a component of the ATP-dependent ...
287-356 1.29e-05

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: 47.21  E-value: 1.29e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 332007407 287 LLVGPPGTGKTLLARAVAGEAGVPFFSCAASEFVEL-FVG--VGASRVRDL------FEKAKSKapcIVFIDEIDAVGR 356
Cdd:cd19497   54 LLIGPTGSGKTLLAQTLAKILDVPFAIADATTLTEAgYVGedVENILLKLLqaadydVERAQRG---IVYIDEIDKIAR 129
TIP49 pfam06068
TIP49 P-loop domain; This family consists of the C-terminal region of several eukaryotic and ...
284-319 4.28e-05

TIP49 P-loop domain; This family consists of the C-terminal region of several eukaryotic and archaeal RuvB-like 1 (Pontin or TIP49a) and RuvB-like 2 (Reptin or TIP49b) proteins. The N-terminal domain contains the pfam00004 domain. In zebrafish, the liebeskummer (lik) mutation, causes development of hyperplastic embryonic hearts. lik encodes Reptin, a component of a DNA-stimulated ATPase complex. Beta-catenin and Pontin, a DNA-stimulated ATPase that is often part of complexes with Reptin, are in the same genetic pathways. The Reptin/Pontin ratio serves to regulate heart growth during development, at least in part via the beta-catenin pathway. TBP-interacting protein 49 (TIP49) was originally identified as a TBP-binding protein, and two related proteins are encoded by individual genes, tip49a and b. Although the function of this gene family has not been elucidated, they are supposed to play a critical role in nuclear events because they interact with various kinds of nuclear factors and have DNA helicase activities.TIP49a has been suggested to act as an autoantigen in some patients with autoimmune diseases.


Pssm-ID: 399217 [Multi-domain]  Cd Length: 347  Bit Score: 46.15  E-value: 4.28e-05
                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 332007407  284 KGCLLVGPPGTGKTLLARAVAGEAG--VPFFSCAASEF 319
Cdd:pfam06068  51 RAVLIAGPPGTGKTALAIAISKELGedTPFTSISGSEV 88
ABCC_Protease_Secretion cd03246
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ...
282-404 5.09e-05

ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of the protease secretion system PrtD, a 60-kDa integral membrane protein sharing 37% identity with HlyB, the ABC component of the alpha-hemolysin secretion pathway, in the C-terminal domain. They export degradative enzymes by using a type I protein secretion system and lack an N-terminal signal peptide, but contain a C-terminal secretion signal. The Type I secretion apparatus is made up of three components, an ABC transporter, a membrane fusion protein (MFP), and an outer membrane protein (OMP). For the HlyA transporter complex, HlyB (ABC transporter) and HlyD (MFP) reside in the inner membrane of E. coli. The OMP component is TolC, which is thought to interact with the MFP to form a continuous channel across the periplasm from the cytoplasm to the exterior. HlyB belongs to the family of ABC transporters, which are ubiquitous, ATP-dependent transmembrane pumps or channels. The spectrum of transport substrates ranges from inorganic ions, nutrients such as amino acids, sugars, or peptides, hydrophobic drugs, to large polypeptides, such as HlyA.


Pssm-ID: 213213 [Multi-domain]  Cd Length: 173  Bit Score: 44.51  E-value: 5.09e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332007407 282 IPKGCLL--VGPPGTGKTLLARAVAGEA----------GVPFFSCAASEF----------VELFVGV-------GASRVR 332
Cdd:cd03246   25 IEPGESLaiIGPSGSGKSTLARLILGLLrptsgrvrldGADISQWDPNELgdhvgylpqdDELFSGSiaenilsGGQRQR 104
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 332007407 333 DLFEKAKSKAPCIVFIDEIDAvgrqrgagmgGGNDEREQTINQLLTEMDGfsgnSGVIVLAATNRPDVLDSA 404
Cdd:cd03246  105 LGLARALYGNPRILVLDEPNS----------HLDVEGERALNQAIAALKA----AGATRIVIAHRPETLASA 162
RecA-like_Lon cd19500
lon protease homolog 2 peroxisomal; Lon protease (also known as Lon peptidase) is an ...
287-356 6.05e-05

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


Pssm-ID: 410908 [Multi-domain]  Cd Length: 182  Bit Score: 44.47  E-value: 6.05e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 332007407 287 LLVGPPGTGKTLLARAVAGEAGVPFFSCA---ASEFVEL------FVGVGASRVRDLFEKAKSKAPCIVfIDEIDAVGR 356
Cdd:cd19500   41 CLVGPPGVGKTSLGKSIARALGRKFVRISlggVRDEAEIrghrrtYVGAMPGRIIQALKKAGTNNPVFL-LDEIDKIGS 118
clpX PRK05342
ATP-dependent Clp protease ATP-binding subunit ClpX;
287-356 7.83e-05

ATP-dependent Clp protease ATP-binding subunit ClpX;


Pssm-ID: 235422 [Multi-domain]  Cd Length: 412  Bit Score: 45.53  E-value: 7.83e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 332007407 287 LLVGPPGTGKTLLARAVAGEAGVPFFSCAASEFVEL-FVG--VGASRVRDLF------EKAKSKapcIVFIDEIDAVGR 356
Cdd:PRK05342 112 LLIGPTGSGKTLLAQTLARILDVPFAIADATTLTEAgYVGedVENILLKLLQaadydvEKAQRG---IVYIDEIDKIAR 187
NACHT COG5635
Predicted NTPase, NACHT family domain [Signal transduction mechanisms];
263-407 1.05e-04

Predicted NTPase, NACHT family domain [Signal transduction mechanisms];


Pssm-ID: 444362 [Multi-domain]  Cd Length: 935  Bit Score: 45.57  E-value: 1.05e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332007407 263 QEVVDFLKNPDKYTALGAKIPKgCLLVGPPGTGKTLLARAVA---------GEAGVPFF----SCAAS----EFVELFVG 325
Cdd:COG5635  161 LNLLERIESLKRLELLEAKKKR-LLILGEPGSGKTTLLRYLAlelaeryldAEDPIPILielrDLAEEasleDLLAEALE 239
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332007407 326 VGASRVRDLFEKAKSKAPCIVFIDEIDAVGRQrgagmgggnDEREQTINQLLTEMDGFSGNSGVIvlaaTNRPDVLDSAL 405
Cdd:COG5635  240 KRGGEPEDALERLLRNGRLLLLLDGLDEVPDE---------ADRDEVLNQLRRFLERYPKARVII----TSRPEGYDSSE 306

                 ..
gi 332007407 406 LR 407
Cdd:COG5635  307 LE 308
HolB COG0470
DNA polymerase III, delta prime subunit [Replication, recombination and repair];
262-353 2.13e-04

DNA polymerase III, delta prime subunit [Replication, recombination and repair];


Pssm-ID: 440238 [Multi-domain]  Cd Length: 289  Bit Score: 43.81  E-value: 2.13e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332007407 262 LQEVVDFLKNpdkyTALGAKIPKGCLLVGPPGTGKTLLARAVA-------GEAGVPFFSCAA--------SEFVELFVGV 326
Cdd:COG0470    1 QEEAWEQLLA----AAESGRLPHALLLHGPPGIGKTTLALALArdllcenPEGGKACGQCHSrlmaagnhPDLLELNPEE 76
                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 332007407 327 -----GASRVRDLFEKAKSKAPC----IVFIDEIDA 353
Cdd:COG0470   77 ksdqiGIDQIRELGEFLSLTPLEggrkVVIIDEADA 112
Sigma54_activat pfam00158
Sigma-54 interaction domain;
280-351 3.33e-04

Sigma-54 interaction domain;


Pssm-ID: 425491 [Multi-domain]  Cd Length: 168  Bit Score: 42.00  E-value: 3.33e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332007407  280 AKIPKGCLLVGPPGTGKTLLARAV---AGEAGVPF--FSCAA-------SefvELFvGV------GASRVRD-LFEKAKS 340
Cdd:pfam00158  19 APTDAPVLITGESGTGKELFARAIhqlSPRADGPFvaVNCAAipeelleS---ELF-GHekgaftGADSDRKgLFELADG 94
                          90
                  ....*....|.
gi 332007407  341 KapcIVFIDEI 351
Cdd:pfam00158  95 G---TLFLDEI 102
T7SS_EccA TIGR03922
type VII secretion AAA-ATPase EccA; This model represents the AAA family ATPase, EccA, of the ...
287-381 4.35e-04

type VII secretion AAA-ATPase EccA; This model represents the AAA family ATPase, EccA, of the actinobacterial flavor of type VII secretion systems. Species such as Mycobacterium tuberculosis have several instances of this system per genome, designated EccA1, EccA2, etc. [Protein fate, Protein and peptide secretion and trafficking]


Pssm-ID: 188437 [Multi-domain]  Cd Length: 557  Bit Score: 43.68  E-value: 4.35e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332007407  287 LLVGPPGTGKTLLARAVAGE-AGVPFFS------CAASEFVELFVGVGASRVRDLFEKAKSKapcIVFIDEIDAVGRQRG 359
Cdd:TIGR03922 316 LFAGPPGTGKTTIARVVAKIyCGLGVLRkplvreVSRADLIGQYIGESEAKTNEIIDSALGG---VLFLDEAYTLVETGY 392
                          90       100
                  ....*....|....*....|..
gi 332007407  360 agmGGGNDEREQTINQLLTEMD 381
Cdd:TIGR03922 393 ---GQKDPFGLEAIDTLLARME 411
AcoR COG3284
Transcriptional regulator DhaR of acetoin/glycerol metabolism [Transcription];
243-352 4.85e-04

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


Pssm-ID: 442514 [Multi-domain]  Cd Length: 625  Bit Score: 43.35  E-value: 4.85e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332007407 243 PETGVTFGDVAGADQAkleLQEVVDFLKnpdkyTALGAKIPkgCLLVGPPGTGKTLLARAVAGE---AGVPF--FSCAA- 316
Cdd:COG3284  314 APAPAALAALAGGDPA---MRRALRRAR-----RLADRDIP--VLILGETGTGKELFARAIHAAsprADGPFvaVNCAAi 383
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 332007407 317 -SEFV--ELFVGV-----GASRV--RDLFEKAKSKapcIVFIDEID 352
Cdd:COG3284  384 pEELIesELFGYEpgaftGARRKgrPGKIEQADGG---TLFLDEIG 426
RecA-like_ClpB_Hsp104-like cd19499
Chaperone protein ClpB/Hsp104 subfamily; Bacterial Caseinolytic peptidase B (ClpB) and ...
287-352 7.74e-04

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: 41.01  E-value: 7.74e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332007407 287 LLVGPPGTGKTLLARAVA-----GEAGVPFFSCaaSEFVELFVG----------VGASRVRDLFEKAKSKAPCIVFIDEI 351
Cdd:cd19499   45 LFLGPTGVGKTELAKALAellfgDEDNLIRIDM--SEYMEKHSVsrligappgyVGYTEGGQLTEAVRRKPYSVVLLDEI 122

                 .
gi 332007407 352 D 352
Cdd:cd19499  123 E 123
ClpX COG1219
ATP-dependent protease Clp, ATPase subunit ClpX [Posttranslational modification, protein ...
287-356 1.56e-03

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


Pssm-ID: 440832 [Multi-domain]  Cd Length: 409  Bit Score: 41.57  E-value: 1.56e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332007407 287 LLVGPPGTGKTLLARAVAGEAGVPFFSCAAS---------EFVElfvgvgaSRVRDLFEKAK---SKAPC-IVFIDEIDA 353
Cdd:COG1219  113 LLIGPTGSGKTLLAQTLARILDVPFAIADATtlteagyvgEDVE-------NILLKLLQAADydvEKAERgIIYIDEIDK 185

                 ...
gi 332007407 354 VGR 356
Cdd:COG1219  186 IAR 188
PspF COG1221
Transcriptional regulators containing an AAA-type ATPase domain and a DNA-binding domain ...
283-351 2.09e-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: 41.63  E-value: 2.09e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332007407 283 PKG--CLLVGPPGTGKTLLARAV---AGEAGV-----PF--FSCAasEFVE--------LFvGV------GASRVRD-LF 335
Cdd:COG1221  128 PKGlhTLILGPTGVGKSFFAELMyeyAIEIGVlpedaPFvvFNCA--DYANnpqllmsqLF-GYvkgaftGADKDKEgLI 204
                         90
                 ....*....|....*.
gi 332007407 336 EKAKSKapcIVFIDEI 351
Cdd:COG1221  205 EKADGG---ILFLDEV 217
DnaC COG1484
DNA replication protein DnaC [Replication, recombination and repair];
284-351 2.10e-03

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


Pssm-ID: 441093 [Multi-domain]  Cd Length: 242  Bit Score: 40.53  E-value: 2.10e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 332007407 284 KGCLLVGPPGTGKTLLARAVAGEA---GVP--FFScaASEFV-ELFVGVGASRVRDLFEKAKsKAPCIVfIDEI 351
Cdd:COG1484  100 ENLILLGPPGTGKTHLAIALGHEAcraGYRvrFTT--APDLVnELKEARADGRLERLLKRLA-KVDLLI-LDEL 169
YifB COG0606
Predicted Mg-chelatase, contains ChlI-like and ATPase domains, YifB family [Posttranslational ...
287-305 3.78e-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: 40.41  E-value: 3.78e-03
                         10
                 ....*....|....*....
gi 332007407 287 LLVGPPGTGKTLLARAVAG 305
Cdd:COG0606  215 LMIGPPGSGKTMLARRLPG 233
AAA_16 pfam13191
AAA ATPase domain; This family of domains contain a P-loop motif that is characteriztic of the ...
283-407 3.96e-03

AAA ATPase domain; This family of domains contain a P-loop motif that is characteriztic of the AAA superfamily.


Pssm-ID: 433025 [Multi-domain]  Cd Length: 167  Bit Score: 38.64  E-value: 3.96e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332007407  283 PKGCLLVGPPGTGKTLLARAV---AGEAGVPFFSCAASEFVELFVGVGASRVRDLFEKAKSKAPCIVFIDEIDAVGRQRG 359
Cdd:pfam13191  24 PPSVLLTGEAGTGKTTLLRELlraLERDGGYFLRGKCDENLPYSPLLEALTREGLLRQLLDELESSLLEAWRAALLEALA 103
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 332007407  360 AGMGGGNDEREQTINQLLTEMDGFSGNSG--VIVLAATNRPDVLDSALLR 407
Cdd:pfam13191 104 PVPELPGDLAERLLDLLLRLLDLLARGERplVLVLDDLQWADEASLQLLA 153
ruvB PRK00080
Holliday junction branch migration DNA helicase RuvB;
286-311 4.26e-03

Holliday junction branch migration DNA helicase RuvB;


Pssm-ID: 234619 [Multi-domain]  Cd Length: 328  Bit Score: 39.73  E-value: 4.26e-03
                         10        20
                 ....*....|....*....|....*.
gi 332007407 286 CLLVGPPGTGKTLLARAVAGEAGVPF 311
Cdd:PRK00080  54 VLLYGPPGLGKTTLANIIANEMGVNI 79
RuvB COG2255
Holliday junction resolvasome RuvABC, ATP-dependent DNA helicase subunit RuvB [Replication, ...
286-311 4.47e-03

Holliday junction resolvasome RuvABC, ATP-dependent DNA helicase subunit RuvB [Replication, recombination and repair];


Pssm-ID: 441856 [Multi-domain]  Cd Length: 337  Bit Score: 39.68  E-value: 4.47e-03
                         10        20
                 ....*....|....*....|....*.
gi 332007407 286 CLLVGPPGTGKTLLARAVAGEAGVPF 311
Cdd:COG2255   57 VLLYGPPGLGKTTLAHIIANEMGVNI 82
McrB COG1401
5-methylcytosine-specific restriction endonuclease McrBC, GTP-binding regulatory subunit McrB ...
243-351 7.17e-03

5-methylcytosine-specific restriction endonuclease McrBC, GTP-binding regulatory subunit McrB [Defense mechanisms];


Pssm-ID: 441011 [Multi-domain]  Cd Length: 477  Bit Score: 39.37  E-value: 7.17e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332007407 243 PETGVTFGDVAGADQAKLELQEVVDFLKNPDK------YTALgaKIPKGCLLVGPPGTGKTLLARAVAGEAG-------- 308
Cdd:COG1401  177 LAAELSAAEELYSEDLESEDDYLKDLLREKFEetleafLAAL--KTKKNVILAGPPGTGKTYLARRLAEALGgedngrie 254
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 332007407 309 -VPF---FScaASEFVE-LFVGVGASRVR-------DLFEKAK--SKAPCIVFIDEI 351
Cdd:COG1401  255 fVQFhpsWS--YEDFLLgYRPSLDEGKYEptpgiflRFCLKAEknPDKPYVLIIDEI 309
RuvB_N pfam05496
Holliday junction DNA helicase RuvB P-loop domain; The RuvB protein makes up part of the ...
287-311 7.22e-03

Holliday junction DNA helicase RuvB P-loop domain; The RuvB protein makes up part of the RuvABC revolvasome which catalyzes the resolution of Holliday junctions that arise during genetic recombination and DNA repair. Branch migration is catalyzed by the RuvB protein that is targeted to the Holliday junction by the structure specific RuvA protein. This family contains the N-terminal region of the protein.


Pssm-ID: 398900 [Multi-domain]  Cd Length: 159  Bit Score: 37.86  E-value: 7.22e-03
                          10        20
                  ....*....|....*....|....*
gi 332007407  287 LLVGPPGTGKTLLARAVAGEAGVPF 311
Cdd:pfam05496  37 LLYGPPGLGKTTLANIIANEMGVNI 61
DnaX COG2812
DNA polymerase III, gamma/tau subunits [Replication, recombination and repair];
248-304 7.55e-03

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


Pssm-ID: 442061 [Multi-domain]  Cd Length: 340  Bit Score: 39.02  E-value: 7.55e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 332007407 248 TFGDVAGadqaklelQE-VVDFLKNpdkytALGA-KIPKGCLLVGPPGTGKTLLARAVA 304
Cdd:COG2812    8 TFDDVVG--------QEhVVRTLKN-----ALASgRLAHAYLFTGPRGVGKTTLARILA 53
ruvB TIGR00635
Holliday junction DNA helicase, RuvB subunit; All proteins in this family for which functions ...
286-357 8.72e-03

Holliday junction DNA helicase, RuvB subunit; All proteins in this family for which functions are known are 5'-3' DNA helicases that, as part of a complex with RuvA homologs serve as a 5'-3' Holliday junction helicase. RuvA specifically binds Holliday junctions as a sandwich of two tetramers and maintains the configuration of the junction. It forms a complex with two hexameric rings of RuvB, the subunit that contains helicase activity. The complex drives ATP-dependent branch migration of the Holliday junction recombination intermediate. The endonuclease RuvC resolves junctions. [DNA metabolism, DNA replication, recombination, and repair]


Pssm-ID: 129721 [Multi-domain]  Cd Length: 305  Bit Score: 38.82  E-value: 8.72e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 332007407  286 CLLVGPPGTGKTLLARAVAGEAGVPFFSCAASEFVelfvgvgasRVRDLFEKAKS-KAPCIVFIDEIDAVGRQ 357
Cdd:TIGR00635  33 LLLYGPPGLGKTTLAHIIANEMGVNLKITSGPALE---------KPGDLAAILTNlEEGDVLFIDEIHRLSPA 96
44 PHA02544
clamp loader, small subunit; Provisional
281-355 9.00e-03

clamp loader, small subunit; Provisional


Pssm-ID: 222866 [Multi-domain]  Cd Length: 316  Bit Score: 38.82  E-value: 9.00e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 332007407 281 KIPKGCLLVGPPGTGKTLLARAVAGEAGVPFFSCAAS----EFVELFVGVGASRVrDLFEKAKskapcIVFIDEIDAVG 355
Cdd:PHA02544  41 RIPNMLLHSPSPGTGKTTVAKALCNEVGAEVLFVNGSdcriDFVRNRLTRFASTV-SLTGGGK-----VIIIDEFDRLG 113
 
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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