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Conserved domains on  [gi|1732943972|gb|TYS20788|]
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ATP-dependent zinc metalloprotease FtsH [Bacillus subtilis]

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];
14-602 0e+00

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


:

Pssm-ID: 440233 [Multi-domain]  Cd Length: 583  Bit Score: 1050.01  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943972  14 ILLVVIGVVSYFQTSNPKTENMSYSTFIKNLDDGKVDSVSVQPvrgvYEVKGQLKNyDKDQYFLTHVPEGkgaDQIFNAL 93
Cdd:COG0465     1 IALLLVLLFNLFSSSSSSVKEISYSEFLQLVEAGKVKSVTIQG----DRITGTLKD-GTKTRFTTYRVND---PELVDLL 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943972  94 --KKTDVKVEPAQETSGWVTFLTTIIPFVIIFILFFFLLNQAQGGGSRVMNFGKSKAKLYTEEKKRVKFKDVAGADEEKQ 171
Cdd:COG0465    73 eeKGVEVTAKPPEESSWLLSLLISLLPILLLIGLWIFFMRRMQGGGGGAMSFGKSKAKLYDEDKPKVTFDDVAGVDEAKE 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943972 172 ELVEVVEFLKDPRKFAELGARIPKGVLLVGPPGTGKTLLAKACAGEAGVPFFSISGSDFVEMFVGVGASRVRDLFENAKK 251
Cdd:COG0465   153 ELQEIVDFLKDPEKFTRLGAKIPKGVLLVGPPGTGKTLLAKAVAGEAGVPFFSISGSDFVEMFVGVGASRVRDLFEQAKK 232
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943972 252 NAPCLIFIDEIDAVGRQRGAGLGGGHDEREQTLNQLLVEMDGFSANEGIIIIAATNRADILDPALLRPGRFDRQITVDRP 331
Cdd:COG0465   233 NAPCIIFIDEIDAVGRQRGAGLGGGHDEREQTLNQLLVEMDGFEGNEGVIVIAATNRPDVLDPALLRPGRFDRQVVVDLP 312
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943972 332 DVIGREAVLKVHARNKPLDETVNLKSIAMRTPGFSGADLENLLNEAALVAARQNKKKIDARDIDEATDRVIAGPAKKSRV 411
Cdd:COG0465   313 DVKGREAILKVHARKKPLAPDVDLEVIARRTPGFSGADLANLVNEAALLAARRNKKAVTMEDFEEAIDRVIAGPERKSRV 392
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943972 412 ISKKERNIVAYHEGGHTVIGLVLDEADMVHKVTIVPRGQAGGYAVMLPREDRYFQTKPELLDKIVGLLGGRVAEEIIFGE 491
Cdd:COG0465   393 ISEKEKKITAYHEAGHALVAALLPGADPVHKVTIIPRGRALGYTMQLPEEDRYLYTKEELLDRIAVLLGGRAAEELVFGE 472
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943972 492 VSTGAHNDFQRATNIARRMVTEFGMSEKLGPLQFGQSQgGQVFLGRDFNNEQNYSDQIAYEIDQEIQRIIKECYERAKQI 571
Cdd:COG0465   473 VTTGASNDLERATKIARAMVTEYGMSEKLGPVAYGESE-GEVFLGRDIGQSRNYSEETAREIDEEVRRIIDEAYERAKEI 551
                         570       580       590
                  ....*....|....*....|....*....|.
gi 1732943972 572 LTENRDKLELIAQTLLKVETLDAEQIKHLVD 602
Cdd:COG0465   552 LTENRDKLDALAEALLEKETLDGEELEEILA 582
 
Name Accession Description Interval E-value
HflB COG0465
ATP-dependent Zn proteases [Posttranslational modification, protein turnover, chaperones];
14-602 0e+00

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


Pssm-ID: 440233 [Multi-domain]  Cd Length: 583  Bit Score: 1050.01  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943972  14 ILLVVIGVVSYFQTSNPKTENMSYSTFIKNLDDGKVDSVSVQPvrgvYEVKGQLKNyDKDQYFLTHVPEGkgaDQIFNAL 93
Cdd:COG0465     1 IALLLVLLFNLFSSSSSSVKEISYSEFLQLVEAGKVKSVTIQG----DRITGTLKD-GTKTRFTTYRVND---PELVDLL 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943972  94 --KKTDVKVEPAQETSGWVTFLTTIIPFVIIFILFFFLLNQAQGGGSRVMNFGKSKAKLYTEEKKRVKFKDVAGADEEKQ 171
Cdd:COG0465    73 eeKGVEVTAKPPEESSWLLSLLISLLPILLLIGLWIFFMRRMQGGGGGAMSFGKSKAKLYDEDKPKVTFDDVAGVDEAKE 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943972 172 ELVEVVEFLKDPRKFAELGARIPKGVLLVGPPGTGKTLLAKACAGEAGVPFFSISGSDFVEMFVGVGASRVRDLFENAKK 251
Cdd:COG0465   153 ELQEIVDFLKDPEKFTRLGAKIPKGVLLVGPPGTGKTLLAKAVAGEAGVPFFSISGSDFVEMFVGVGASRVRDLFEQAKK 232
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943972 252 NAPCLIFIDEIDAVGRQRGAGLGGGHDEREQTLNQLLVEMDGFSANEGIIIIAATNRADILDPALLRPGRFDRQITVDRP 331
Cdd:COG0465   233 NAPCIIFIDEIDAVGRQRGAGLGGGHDEREQTLNQLLVEMDGFEGNEGVIVIAATNRPDVLDPALLRPGRFDRQVVVDLP 312
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943972 332 DVIGREAVLKVHARNKPLDETVNLKSIAMRTPGFSGADLENLLNEAALVAARQNKKKIDARDIDEATDRVIAGPAKKSRV 411
Cdd:COG0465   313 DVKGREAILKVHARKKPLAPDVDLEVIARRTPGFSGADLANLVNEAALLAARRNKKAVTMEDFEEAIDRVIAGPERKSRV 392
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943972 412 ISKKERNIVAYHEGGHTVIGLVLDEADMVHKVTIVPRGQAGGYAVMLPREDRYFQTKPELLDKIVGLLGGRVAEEIIFGE 491
Cdd:COG0465   393 ISEKEKKITAYHEAGHALVAALLPGADPVHKVTIIPRGRALGYTMQLPEEDRYLYTKEELLDRIAVLLGGRAAEELVFGE 472
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943972 492 VSTGAHNDFQRATNIARRMVTEFGMSEKLGPLQFGQSQgGQVFLGRDFNNEQNYSDQIAYEIDQEIQRIIKECYERAKQI 571
Cdd:COG0465   473 VTTGASNDLERATKIARAMVTEYGMSEKLGPVAYGESE-GEVFLGRDIGQSRNYSEETAREIDEEVRRIIDEAYERAKEI 551
                         570       580       590
                  ....*....|....*....|....*....|.
gi 1732943972 572 LTENRDKLELIAQTLLKVETLDAEQIKHLVD 602
Cdd:COG0465   552 LTENRDKLDALAEALLEKETLDGEELEEILA 582
FtsH_fam TIGR01241
ATP-dependent metalloprotease FtsH; HflB(FtsH) is a pleiotropic protein required for correct ...
131-602 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: 903.19  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943972 131 NQAQGGGSRVMNFGKSKAKLYTEEKKRVKFKDVAGADEEKQELVEVVEFLKDPRKFAELGARIPKGVLLVGPPGTGKTLL 210
Cdd:TIGR01241  25 RQMQGGGGRAFSFGKSKAKLLNEEKPKVTFKDVAGIDEAKEELMEIVDFLKNPSKFTKLGAKIPKGVLLVGPPGTGKTLL 104
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943972 211 AKACAGEAGVPFFSISGSDFVEMFVGVGASRVRDLFENAKKNAPCLIFIDEIDAVGRQRGAGLGGGHDEREQTLNQLLVE 290
Cdd:TIGR01241 105 AKAVAGEAGVPFFSISGSDFVEMFVGVGASRVRDLFEQAKKNAPCIIFIDEIDAVGRQRGAGLGGGNDEREQTLNQLLVE 184
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943972 291 MDGFSANEGIIIIAATNRADILDPALLRPGRFDRQITVDRPDVIGREAVLKVHARNKPLDETVNLKSIAMRTPGFSGADL 370
Cdd:TIGR01241 185 MDGFGTNTGVIVIAATNRPDVLDPALLRPGRFDRQVVVDLPDIKGREEILKVHAKNKKLAPDVDLKAVARRTPGFSGADL 264
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943972 371 ENLLNEAALVAARQNKKKIDARDIDEATDRVIAGPAKKSRVISKKERNIVAYHEGGHTVIGLVLDEADMVHKVTIVPRGQ 450
Cdd:TIGR01241 265 ANLLNEAALLAARKNKTEITMNDIEEAIDRVIAGPEKKSRVISEKEKKLVAYHEAGHALVGLLLKDADPVHKVTIIPRGQ 344
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943972 451 AGGYAVMLPREDRYFQTKPELLDKIVGLLGGRVAEEIIFGEVSTGAHNDFQRATNIARRMVTEFGMSEKLGPLQFGqSQG 530
Cdd:TIGR01241 345 ALGYTQFLPEEDKYLYTKSQLLAQIAVLLGGRAAEEIIFGEVTTGASNDIKQATNIARAMVTEWGMSDKLGPVAYG-SDG 423
                         410       420       430       440       450       460       470
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1732943972 531 GQVFLGRDFNNEQNYSDQIAYEIDQEIQRIIKECYERAKQILTENRDKLELIAQTLLKVETLDAEQIKHLVD 602
Cdd:TIGR01241 424 GDVFLGRGFAKAKEYSEETAREIDEEVKRIIEEAYKRAKQILTENRDELELLAKALLEKETITREEIKELLA 495
ftsH CHL00176
cell division protein; Validated
7-610 0e+00

cell division protein; Validated


Pssm-ID: 214386 [Multi-domain]  Cd Length: 638  Bit Score: 671.76  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943972   7 NTIFYLLILLVVIGVVSYFQTS---------------------NPKTENMSYSTFIKNLDDGKVDSVSVQPVRGVYEVKG 65
Cdd:CHL00176    3 EQSKYAILISLPLIVEKFTVWDvfyyssvedglkspnnpdvvqNKASSRMTYGRFLEYLDMGWIKKVDLYDNGRTAIVEA 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943972  66 QLKNY-DKDQYFLTHVPEGKgADQIFNALK-KTDVKVEPAQETSGWVT----FLTTIIPFVIIFILFFFLLNQAQGGGSR 139
Cdd:CHL00176   83 SSPELgNRPQRIRVELPVGA-SELIQKLKEaNIDFDAHPPVLKSNIVTilsnLLLPLILIGVLWFFFQRSSNFKGGPGQN 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943972 140 VMNFGKSKAKLYTEEKKRVKFKDVAGADEEKQELVEVVEFLKDPRKFAELGARIPKGVLLVGPPGTGKTLLAKACAGEAG 219
Cdd:CHL00176  162 LMNFGKSKARFQMEADTGITFRDIAGIEEAKEEFEEVVSFLKKPERFTAVGAKIPKGVLLVGPPGTGKTLLAKAIAGEAE 241
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943972 220 VPFFSISGSDFVEMFVGVGASRVRDLFENAKKNAPCLIFIDEIDAVGRQRGAGLGGGHDEREQTLNQLLVEMDGFSANEG 299
Cdd:CHL00176  242 VPFFSISGSEFVEMFVGVGAARVRDLFKKAKENSPCIVFIDEIDAVGRQRGAGIGGGNDEREQTLNQLLTEMDGFKGNKG 321
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943972 300 IIIIAATNRADILDPALLRPGRFDRQITVDRPDVIGREAVLKVHARNKPLDETVNLKSIAMRTPGFSGADLENLLNEAAL 379
Cdd:CHL00176  322 VIVIAATNRVDILDAALLRPGRFDRQITVSLPDREGRLDILKVHARNKKLSPDVSLELIARRTPGFSGADLANLLNEAAI 401
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943972 380 VAARQNKKKIDARDIDEATDRVIAGPAKKSRVISKKERnIVAYHEGGHTVIGLVLDEADMVHKVTIVPRGQAGGYAVMLP 459
Cdd:CHL00176  402 LTARRKKATITMKEIDTAIDRVIAGLEGTPLEDSKNKR-LIAYHEVGHAIVGTLLPNHDPVQKVTLIPRGQAKGLTWFTP 480
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943972 460 REDRYFQTKPELLDKIVGLLGGRVAEEIIFG--EVSTGAHNDFQRATNIARRMVTEFGMSeKLGPLQFGQSQGGQVFLGR 537
Cdd:CHL00176  481 EEDQSLVSRSQILARIVGALGGRAAEEVVFGstEVTTGASNDLQQVTNLARQMVTRFGMS-SIGPISLESNNSTDPFLGR 559
                         570       580       590       600       610       620       630
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1732943972 538 DFNNEQNYSDQIAYEIDQEIQRIIKECYERAKQILTENRDKLELIAQTLLKVETLDAEQIKHLV-DHGTLPERN 610
Cdd:CHL00176  560 FMQRNSEYSEEIADKIDMEVRSILHTCYQYAYQILKDNRVLIDLLVELLLQKETIDGDEFREIVnSYTILPPKK 633
RecA-like_FtsH cd19501
ATP-dependent zinc metalloprotease FtsH; FtsH ATPase is a processive, ATP-dependent zinc ...
158-328 1.04e-127

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: 373.49  E-value: 1.04e-127
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943972 158 VKFKDVAGADEEKQELVEVVEFLKDPRKFAELGARIPKGVLLVGPPGTGKTLLAKACAGEAGVPFFSISGSDFVEMFVGV 237
Cdd:cd19501     1 VTFKDVAGCEEAKEELKEVVEFLKNPEKFTKLGAKIPKGVLLVGPPGTGKTLLAKAVAGEAGVPFFSISGSDFVEMFVGV 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943972 238 GASRVRDLFENAKKNAPCLIFIDEIDAVGRQRGAGLGGGHDEREQTLNQLLVEMDGFSANEGIIIIAATNRADILDPALL 317
Cdd:cd19501    81 GASRVRDLFEQAKKNAPCIVFIDEIDAVGRKRGAGLGGGHDEREQTLNQLLVEMDGFESNTGVIVIAATNRPDVLDPALL 160
                         170
                  ....*....|.
gi 1732943972 318 RPGRFDRQITV 328
Cdd:cd19501   161 RPGRFDRQVYV 171
Peptidase_M41 pfam01434
Peptidase family M41;
410-600 1.77e-107

Peptidase family M41;


Pssm-ID: 460210 [Multi-domain]  Cd Length: 190  Bit Score: 322.24  E-value: 1.77e-107
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943972 410 RVISKKERNIVAYHEGGHTVIGLVLDEADMVHKVTIVPRGQAGGYAVMLPREDRYFQTKPELLDKIVGLLGGRVAEEIIF 489
Cdd:pfam01434   1 RVISEEEKKIVAYHEAGHALVGLLLPGADPVHKVTIIPRGQALGYTQFLPEEDKLLYTKEQLLARIAVLLGGRAAEELIF 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943972 490 GEVSTGAHNDFQRATNIARRMVTEFGMSEKLGPLQFGQSQgGQVFLGRDFNNEQNYSDQIAYEIDQEIQRIIKECYERAK 569
Cdd:pfam01434  81 GEVTTGASNDLEKATKIARQMVTEFGMSDKLGPVSLEESD-GNVFLGRGMGKRKPYSEETADIIDEEVKRLLEEAYERAK 159
                         170       180       190
                  ....*....|....*....|....*....|.
gi 1732943972 570 QILTENRDKLELIAQTLLKVETLDAEQIKHL 600
Cdd:pfam01434 160 EILTEHRDELEALAEALLEKETLDAEEIREL 190
AAA smart00382
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ...
194-332 2.27e-20

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: 87.81  E-value: 2.27e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943972  194 PKGVLLVGPPGTGKTLLAKACAGEA---GVPFFSISGSDFVE--------------MFVGVGASRVRDLFENAKKNAPCL 256
Cdd:smart00382   2 GEVILIVGPPGSGKTTLARALARELgppGGGVIYIDGEDILEevldqllliivggkKASGSGELRLRLALALARKLKPDV 81
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1732943972  257 IFIDEIDAvgrqrgagLGGGHDEREQTLNQLLVEMDGFSANEGIIIIAATNRADILDPALLRPgRFDRQITVDRPD 332
Cdd:smart00382  82 LILDEITS--------LLDAEQEALLLLLEELRLLLLLKSEKNLTVILTTNDEKDLGPALLRR-RFDRRIVLLLIL 148
 
Name Accession Description Interval E-value
HflB COG0465
ATP-dependent Zn proteases [Posttranslational modification, protein turnover, chaperones];
14-602 0e+00

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


Pssm-ID: 440233 [Multi-domain]  Cd Length: 583  Bit Score: 1050.01  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943972  14 ILLVVIGVVSYFQTSNPKTENMSYSTFIKNLDDGKVDSVSVQPvrgvYEVKGQLKNyDKDQYFLTHVPEGkgaDQIFNAL 93
Cdd:COG0465     1 IALLLVLLFNLFSSSSSSVKEISYSEFLQLVEAGKVKSVTIQG----DRITGTLKD-GTKTRFTTYRVND---PELVDLL 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943972  94 --KKTDVKVEPAQETSGWVTFLTTIIPFVIIFILFFFLLNQAQGGGSRVMNFGKSKAKLYTEEKKRVKFKDVAGADEEKQ 171
Cdd:COG0465    73 eeKGVEVTAKPPEESSWLLSLLISLLPILLLIGLWIFFMRRMQGGGGGAMSFGKSKAKLYDEDKPKVTFDDVAGVDEAKE 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943972 172 ELVEVVEFLKDPRKFAELGARIPKGVLLVGPPGTGKTLLAKACAGEAGVPFFSISGSDFVEMFVGVGASRVRDLFENAKK 251
Cdd:COG0465   153 ELQEIVDFLKDPEKFTRLGAKIPKGVLLVGPPGTGKTLLAKAVAGEAGVPFFSISGSDFVEMFVGVGASRVRDLFEQAKK 232
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943972 252 NAPCLIFIDEIDAVGRQRGAGLGGGHDEREQTLNQLLVEMDGFSANEGIIIIAATNRADILDPALLRPGRFDRQITVDRP 331
Cdd:COG0465   233 NAPCIIFIDEIDAVGRQRGAGLGGGHDEREQTLNQLLVEMDGFEGNEGVIVIAATNRPDVLDPALLRPGRFDRQVVVDLP 312
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943972 332 DVIGREAVLKVHARNKPLDETVNLKSIAMRTPGFSGADLENLLNEAALVAARQNKKKIDARDIDEATDRVIAGPAKKSRV 411
Cdd:COG0465   313 DVKGREAILKVHARKKPLAPDVDLEVIARRTPGFSGADLANLVNEAALLAARRNKKAVTMEDFEEAIDRVIAGPERKSRV 392
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943972 412 ISKKERNIVAYHEGGHTVIGLVLDEADMVHKVTIVPRGQAGGYAVMLPREDRYFQTKPELLDKIVGLLGGRVAEEIIFGE 491
Cdd:COG0465   393 ISEKEKKITAYHEAGHALVAALLPGADPVHKVTIIPRGRALGYTMQLPEEDRYLYTKEELLDRIAVLLGGRAAEELVFGE 472
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943972 492 VSTGAHNDFQRATNIARRMVTEFGMSEKLGPLQFGQSQgGQVFLGRDFNNEQNYSDQIAYEIDQEIQRIIKECYERAKQI 571
Cdd:COG0465   473 VTTGASNDLERATKIARAMVTEYGMSEKLGPVAYGESE-GEVFLGRDIGQSRNYSEETAREIDEEVRRIIDEAYERAKEI 551
                         570       580       590
                  ....*....|....*....|....*....|.
gi 1732943972 572 LTENRDKLELIAQTLLKVETLDAEQIKHLVD 602
Cdd:COG0465   552 LTENRDKLDALAEALLEKETLDGEELEEILA 582
FtsH_fam TIGR01241
ATP-dependent metalloprotease FtsH; HflB(FtsH) is a pleiotropic protein required for correct ...
131-602 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: 903.19  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943972 131 NQAQGGGSRVMNFGKSKAKLYTEEKKRVKFKDVAGADEEKQELVEVVEFLKDPRKFAELGARIPKGVLLVGPPGTGKTLL 210
Cdd:TIGR01241  25 RQMQGGGGRAFSFGKSKAKLLNEEKPKVTFKDVAGIDEAKEELMEIVDFLKNPSKFTKLGAKIPKGVLLVGPPGTGKTLL 104
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943972 211 AKACAGEAGVPFFSISGSDFVEMFVGVGASRVRDLFENAKKNAPCLIFIDEIDAVGRQRGAGLGGGHDEREQTLNQLLVE 290
Cdd:TIGR01241 105 AKAVAGEAGVPFFSISGSDFVEMFVGVGASRVRDLFEQAKKNAPCIIFIDEIDAVGRQRGAGLGGGNDEREQTLNQLLVE 184
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943972 291 MDGFSANEGIIIIAATNRADILDPALLRPGRFDRQITVDRPDVIGREAVLKVHARNKPLDETVNLKSIAMRTPGFSGADL 370
Cdd:TIGR01241 185 MDGFGTNTGVIVIAATNRPDVLDPALLRPGRFDRQVVVDLPDIKGREEILKVHAKNKKLAPDVDLKAVARRTPGFSGADL 264
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943972 371 ENLLNEAALVAARQNKKKIDARDIDEATDRVIAGPAKKSRVISKKERNIVAYHEGGHTVIGLVLDEADMVHKVTIVPRGQ 450
Cdd:TIGR01241 265 ANLLNEAALLAARKNKTEITMNDIEEAIDRVIAGPEKKSRVISEKEKKLVAYHEAGHALVGLLLKDADPVHKVTIIPRGQ 344
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943972 451 AGGYAVMLPREDRYFQTKPELLDKIVGLLGGRVAEEIIFGEVSTGAHNDFQRATNIARRMVTEFGMSEKLGPLQFGqSQG 530
Cdd:TIGR01241 345 ALGYTQFLPEEDKYLYTKSQLLAQIAVLLGGRAAEEIIFGEVTTGASNDIKQATNIARAMVTEWGMSDKLGPVAYG-SDG 423
                         410       420       430       440       450       460       470
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1732943972 531 GQVFLGRDFNNEQNYSDQIAYEIDQEIQRIIKECYERAKQILTENRDKLELIAQTLLKVETLDAEQIKHLVD 602
Cdd:TIGR01241 424 GDVFLGRGFAKAKEYSEETAREIDEEVKRIIEEAYKRAKQILTENRDELELLAKALLEKETITREEIKELLA 495
ftsH CHL00176
cell division protein; Validated
7-610 0e+00

cell division protein; Validated


Pssm-ID: 214386 [Multi-domain]  Cd Length: 638  Bit Score: 671.76  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943972   7 NTIFYLLILLVVIGVVSYFQTS---------------------NPKTENMSYSTFIKNLDDGKVDSVSVQPVRGVYEVKG 65
Cdd:CHL00176    3 EQSKYAILISLPLIVEKFTVWDvfyyssvedglkspnnpdvvqNKASSRMTYGRFLEYLDMGWIKKVDLYDNGRTAIVEA 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943972  66 QLKNY-DKDQYFLTHVPEGKgADQIFNALK-KTDVKVEPAQETSGWVT----FLTTIIPFVIIFILFFFLLNQAQGGGSR 139
Cdd:CHL00176   83 SSPELgNRPQRIRVELPVGA-SELIQKLKEaNIDFDAHPPVLKSNIVTilsnLLLPLILIGVLWFFFQRSSNFKGGPGQN 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943972 140 VMNFGKSKAKLYTEEKKRVKFKDVAGADEEKQELVEVVEFLKDPRKFAELGARIPKGVLLVGPPGTGKTLLAKACAGEAG 219
Cdd:CHL00176  162 LMNFGKSKARFQMEADTGITFRDIAGIEEAKEEFEEVVSFLKKPERFTAVGAKIPKGVLLVGPPGTGKTLLAKAIAGEAE 241
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943972 220 VPFFSISGSDFVEMFVGVGASRVRDLFENAKKNAPCLIFIDEIDAVGRQRGAGLGGGHDEREQTLNQLLVEMDGFSANEG 299
Cdd:CHL00176  242 VPFFSISGSEFVEMFVGVGAARVRDLFKKAKENSPCIVFIDEIDAVGRQRGAGIGGGNDEREQTLNQLLTEMDGFKGNKG 321
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943972 300 IIIIAATNRADILDPALLRPGRFDRQITVDRPDVIGREAVLKVHARNKPLDETVNLKSIAMRTPGFSGADLENLLNEAAL 379
Cdd:CHL00176  322 VIVIAATNRVDILDAALLRPGRFDRQITVSLPDREGRLDILKVHARNKKLSPDVSLELIARRTPGFSGADLANLLNEAAI 401
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943972 380 VAARQNKKKIDARDIDEATDRVIAGPAKKSRVISKKERnIVAYHEGGHTVIGLVLDEADMVHKVTIVPRGQAGGYAVMLP 459
Cdd:CHL00176  402 LTARRKKATITMKEIDTAIDRVIAGLEGTPLEDSKNKR-LIAYHEVGHAIVGTLLPNHDPVQKVTLIPRGQAKGLTWFTP 480
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943972 460 REDRYFQTKPELLDKIVGLLGGRVAEEIIFG--EVSTGAHNDFQRATNIARRMVTEFGMSeKLGPLQFGQSQGGQVFLGR 537
Cdd:CHL00176  481 EEDQSLVSRSQILARIVGALGGRAAEEVVFGstEVTTGASNDLQQVTNLARQMVTRFGMS-SIGPISLESNNSTDPFLGR 559
                         570       580       590       600       610       620       630
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1732943972 538 DFNNEQNYSDQIAYEIDQEIQRIIKECYERAKQILTENRDKLELIAQTLLKVETLDAEQIKHLV-DHGTLPERN 610
Cdd:CHL00176  560 FMQRNSEYSEEIADKIDMEVRSILHTCYQYAYQILKDNRVLIDLLVELLLQKETIDGDEFREIVnSYTILPPKK 633
hflB PRK10733
ATP-dependent zinc metalloprotease FtsH;
6-619 0e+00

ATP-dependent zinc metalloprotease FtsH;


Pssm-ID: 182683 [Multi-domain]  Cd Length: 644  Bit Score: 626.68  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943972   6 RNTIFYLLILLVVIGVVSYFQTSNPKTENMSYSTFIKNLDDGKVDSVSVQPvrgvYEVKGQLKNYDKdqyFLTHVPEGKg 85
Cdd:PRK10733    3 KNLILWLVIAVVLMSVFQSFGPSESNGRKVDYSTFLQEVNQDQVREARING----REINVTKKDSNR---YTTYIPVND- 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943972  86 aDQIFNALKKTDVKV--EPAQETSGWVTFLTTIIPFVIIFILFFFLLNQAQGGGSR-VMNFGKSKAKLYTEEKKRVKFKD 162
Cdd:PRK10733   75 -PKLLDNLLTKNVKVvgEPPEEPSLLASIFISWFPMLLLIGVWIFFMRQMQGGGGKgAMSFGKSKARMLTEDQIKTTFAD 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943972 163 VAGADEEKQELVEVVEFLKDPRKFAELGARIPKGVLLVGPPGTGKTLLAKACAGEAGVPFFSISGSDFVEMFVGVGASRV 242
Cdd:PRK10733  154 VAGCDEAKEEVAELVEYLREPSRFQKLGGKIPKGVLMVGPPGTGKTLLAKAIAGEAKVPFFTISGSDFVEMFVGVGASRV 233
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943972 243 RDLFENAKKNAPCLIFIDEIDAVGRQRGAGLGGGHDEREQTLNQLLVEMDGFSANEGIIIIAATNRADILDPALLRPGRF 322
Cdd:PRK10733  234 RDMFEQAKKAAPCIIFIDEIDAVGRQRGAGLGGGHDEREQTLNQMLVEMDGFEGNEGIIVIAATNRPDVLDPALLRPGRF 313
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943972 323 DRQITVDRPDVIGREAVLKVHARNKPLDETVNLKSIAMRTPGFSGADLENLLNEAALVAARQNKKKIDARDIDEATDRVI 402
Cdd:PRK10733  314 DRQVVVGLPDVRGREQILKVHMRRVPLAPDIDAAIIARGTPGFSGADLANLVNEAALFAARGNKRVVSMVEFEKAKDKIM 393
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943972 403 AGPAKKSRVISKKERNIVAYHEGGHTVIGLVLDEADMVHKVTIVPRGQAGGYAVMLPREDRYFQTKPELLDKIVGLLGGR 482
Cdd:PRK10733  394 MGAERRSMVMTEAQKESTAYHEAGHAIIGRLVPEHDPVHKVTIIPRGRALGVTFFLPEGDAISASRQKLESQISTLYGGR 473
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943972 483 VAEEIIFG--EVSTGAHNDFQRATNIARRMVTEFGMSEKLGPLQFGQSQgGQVFLGRDFNNEQNYSDQIAYEIDQEIQRI 560
Cdd:PRK10733  474 LAEEIIYGpeHVSTGASNDIKVATNLARNMVTQWGFSEKLGPLLYAEEE-GEVFLGRSVAKAKHMSDETARIIDQEVKAL 552
                         570       580       590       600       610       620
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943972 561 IKECYERAKQILTENRDKLELIAQTLLKVETLDAEQIKHLVDHGTL-PERNFSDDEKNDD 619
Cdd:PRK10733  553 IERNYNRARQLLTDNMDILHAMKDALMKYETIDAPQIDDLMARRDVrPPAGWEEPGASNN 612
RecA-like_FtsH cd19501
ATP-dependent zinc metalloprotease FtsH; FtsH ATPase is a processive, ATP-dependent zinc ...
158-328 1.04e-127

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: 373.49  E-value: 1.04e-127
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943972 158 VKFKDVAGADEEKQELVEVVEFLKDPRKFAELGARIPKGVLLVGPPGTGKTLLAKACAGEAGVPFFSISGSDFVEMFVGV 237
Cdd:cd19501     1 VTFKDVAGCEEAKEELKEVVEFLKNPEKFTKLGAKIPKGVLLVGPPGTGKTLLAKAVAGEAGVPFFSISGSDFVEMFVGV 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943972 238 GASRVRDLFENAKKNAPCLIFIDEIDAVGRQRGAGLGGGHDEREQTLNQLLVEMDGFSANEGIIIIAATNRADILDPALL 317
Cdd:cd19501    81 GASRVRDLFEQAKKNAPCIVFIDEIDAVGRKRGAGLGGGHDEREQTLNQLLVEMDGFESNTGVIVIAATNRPDVLDPALL 160
                         170
                  ....*....|.
gi 1732943972 318 RPGRFDRQITV 328
Cdd:cd19501   161 RPGRFDRQVYV 171
RPT1 COG1222
ATP-dependent 26S proteasome regulatory subunit [Posttranslational modification, protein ...
151-410 1.28e-111

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


Pssm-ID: 440835 [Multi-domain]  Cd Length: 326  Bit Score: 338.13  E-value: 1.28e-111
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943972 151 YTEEKKRVKFKDVAGADEEKQELVEVVE-FLKDPRKFAELGARIPKGVLLVGPPGTGKTLLAKACAGEAGVPFFSISGSD 229
Cdd:COG1222    68 VPAESPDVTFDDIGGLDEQIEEIREAVElPLKNPELFRKYGIEPPKGVLLYGPPGTGKTLLAKAVAGELGAPFIRVRGSE 147
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943972 230 FVEMFVGVGASRVRDLFENAKKNAPCLIFIDEIDAVGRQRGAGlgGGHDEREQTLNQLLVEMDGFSANEGIIIIAATNRA 309
Cdd:COG1222   148 LVSKYIGEGARNVREVFELAREKAPSIIFIDEIDAIAARRTDD--GTSGEVQRTVNQLLAELDGFESRGDVLIIAATNRP 225
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943972 310 DILDPALLRPGRFDRQITVDRPDVIGREAVLKVHARNKPLDETVNLKSIAMRTPGFSGADLENLLNEAALVAARQNKKKI 389
Cdd:COG1222   226 DLLDPALLRPGRFDRVIEVPLPDEEAREEILKIHLRDMPLADDVDLDKLAKLTEGFSGADLKAIVTEAGMFAIREGRDTV 305
                         250       260
                  ....*....|....*....|.
gi 1732943972 390 DARDIDEATDRVIAGPAKKSR 410
Cdd:COG1222   306 TMEDLEKAIEKVKKKTETATN 326
Peptidase_M41 pfam01434
Peptidase family M41;
410-600 1.77e-107

Peptidase family M41;


Pssm-ID: 460210 [Multi-domain]  Cd Length: 190  Bit Score: 322.24  E-value: 1.77e-107
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943972 410 RVISKKERNIVAYHEGGHTVIGLVLDEADMVHKVTIVPRGQAGGYAVMLPREDRYFQTKPELLDKIVGLLGGRVAEEIIF 489
Cdd:pfam01434   1 RVISEEEKKIVAYHEAGHALVGLLLPGADPVHKVTIIPRGQALGYTQFLPEEDKLLYTKEQLLARIAVLLGGRAAEELIF 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943972 490 GEVSTGAHNDFQRATNIARRMVTEFGMSEKLGPLQFGQSQgGQVFLGRDFNNEQNYSDQIAYEIDQEIQRIIKECYERAK 569
Cdd:pfam01434  81 GEVTTGASNDLEKATKIARQMVTEFGMSDKLGPVSLEESD-GNVFLGRGMGKRKPYSEETADIIDEEVKRLLEEAYERAK 159
                         170       180       190
                  ....*....|....*....|....*....|.
gi 1732943972 570 QILTENRDKLELIAQTLLKVETLDAEQIKHL 600
Cdd:pfam01434 160 EILTEHRDELEALAEALLEKETLDAEEIREL 190
PRK03992 PRK03992
proteasome-activating nucleotidase; Provisional
153-409 7.52e-96

proteasome-activating nucleotidase; Provisional


Pssm-ID: 179699 [Multi-domain]  Cd Length: 389  Bit Score: 299.44  E-value: 7.52e-96
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943972 153 EEKKRVKFKDVAGADEEKQELVEVVEF-LKDPRKFAELGARIPKGVLLVGPPGTGKTLLAKACAGEAGVPFFSISGSDFV 231
Cdd:PRK03992  123 IESPNVTYEDIGGLEEQIREVREAVELpLKKPELFEEVGIEPPKGVLLYGPPGTGKTLLAKAVAHETNATFIRVVGSELV 202
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943972 232 EMFVGVGASRVRDLFENAKKNAPCLIFIDEIDAVGRQRGAGLGGGHDEREQTLNQLLVEMDGFSANEGIIIIAATNRADI 311
Cdd:PRK03992  203 QKFIGEGARLVRELFELAREKAPSIIFIDEIDAIAAKRTDSGTSGDREVQRTLMQLLAEMDGFDPRGNVKIIAATNRIDI 282
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943972 312 LDPALLRPGRFDRQITVDRPDVIGREAVLKVHARNKPLDETVNLKSIAMRTPGFSGADLENLLNEAALVAARQNKKKIDA 391
Cdd:PRK03992  283 LDPAILRPGRFDRIIEVPLPDEEGRLEILKIHTRKMNLADDVDLEELAELTEGASGADLKAICTEAGMFAIRDDRTEVTM 362
                         250
                  ....*....|....*...
gi 1732943972 392 RDIDEATDRVIAGPAKKS 409
Cdd:PRK03992  363 EDFLKAIEKVMGKEEKDS 380
26Sp45 TIGR01242
26S proteasome subunit P45 family; Many proteins may score above the trusted cutoff because an ...
153-402 7.16e-82

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: 262.43  E-value: 7.16e-82
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943972 153 EEKKRVKFKDVAGADEEKQELVEVVEF-LKDPRKFAELGARIPKGVLLVGPPGTGKTLLAKACAGEAGVPFFSISGSDFV 231
Cdd:TIGR01242 114 EERPNVSYEDIGGLEEQIREIREAVELpLKHPELFEEVGIEPPKGVLLYGPPGTGKTLLAKAVAHETNATFIRVVGSELV 193
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943972 232 EMFVGVGASRVRDLFENAKKNAPCLIFIDEIDAVGRQRGAGLGGGHDEREQTLNQLLVEMDGFSANEGIIIIAATNRADI 311
Cdd:TIGR01242 194 RKYIGEGARLVREIFELAKEKAPSIIFIDEIDAIAAKRTDSGTSGDREVQRTLMQLLAELDGFDPRGNVKVIAATNRPDI 273
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943972 312 LDPALLRPGRFDRQITVDRPDVIGREAVLKVHARNKPLDETVNLKSIAMRTPGFSGADLENLLNEAALVAARQNKKKIDA 391
Cdd:TIGR01242 274 LDPALLRPGRFDRIIEVPLPDFEGRLEILKIHTRKMKLAEDVDLEAIAKMTEGASGADLKAICTEAGMFAIREERDYVTM 353
                         250
                  ....*....|.
gi 1732943972 392 RDIDEATDRVI 402
Cdd:TIGR01242 354 DDFIKAVEKVL 364
SpoVK COG0464
AAA+-type ATPase, SpoVK/Ycf46/Vps4 family [Cell wall/membrane/envelope biogenesis, Cell cycle ...
160-401 7.36e-82

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: 263.70  E-value: 7.36e-82
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943972 160 FKDVAGADEEKQELVEVVE-FLKDPRKFAELGARIPKGVLLVGPPGTGKTLLAKACAGEAGVPFFSISGSDFVEMFVGVG 238
Cdd:COG0464   156 LDDLGGLEEVKEELRELVAlPLKRPELREEYGLPPPRGLLLYGPPGTGKTLLARALAGELGLPLIEVDLSDLVSKYVGET 235
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943972 239 ASRVRDLFENAKKNAPCLIFIDEIDAVGRQRGaGLGGGHDEREqtLNQLLVEMDGFsaNEGIIIIAATNRADILDPALLR 318
Cdd:COG0464   236 EKNLREVFDKARGLAPCVLFIDEADALAGKRG-EVGDGVGRRV--VNTLLTEMEEL--RSDVVVIAATNRPDLLDPALLR 310
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943972 319 pgRFDRQITVDRPDVIGREAVLKVHARNKPLDETVNLKSIAMRTPGFSGADLENLLNEAALVAARQNKKKIDARDIDEAT 398
Cdd:COG0464   311 --RFDEIIFFPLPDAEERLEIFRIHLRKRPLDEDVDLEELAEATEGLSGADIRNVVRRAALQALRLGREPVTTEDLLEAL 388

                  ...
gi 1732943972 399 DRV 401
Cdd:COG0464   389 ERE 391
CDC48 TIGR01243
AAA family ATPase, CDC48 subfamily; This subfamily of the AAA family ATPases includes two ...
154-402 4.13e-71

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: 244.05  E-value: 4.13e-71
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943972 154 EKKRVKFKDVAGADEEKQELVEVVEF-LKDPRKFAELGARIPKGVLLVGPPGTGKTLLAKACAGEAGVPFFSISGSDFVE 232
Cdd:TIGR01243 446 EVPNVRWSDIGGLEEVKQELREAVEWpLKHPEIFEKMGIRPPKGVLLFGPPGTGKTLLAKAVATESGANFIAVRGPEILS 525
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943972 233 MFVGVGASRVRDLFENAKKNAPCLIFIDEIDAVGRQRGAGLGGGHDEReqTLNQLLVEMDGFSANEGIIIIAATNRADIL 312
Cdd:TIGR01243 526 KWVGESEKAIREIFRKARQAAPAIIFFDEIDAIAPARGARFDTSVTDR--IVNQLLTEMDGIQELSNVVVIAATNRPDIL 603
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943972 313 DPALLRPGRFDRQITVDRPDVIGREAVLKVHARNKPLDETVNLKSIAMRTPGFSGADLENLLNEAALVAARQNKKKIDAR 392
Cdd:TIGR01243 604 DPALLRPGRFDRLILVPPPDEEARKEIFKIHTRSMPLAEDVDLEELAEMTEGYTGADIEAVCREAAMAALRESIGSPAKE 683
                         250
                  ....*....|
gi 1732943972 393 DIDEATDRVI 402
Cdd:TIGR01243 684 KLEVGEEEFL 693
RecA-like_PAN_like cd19502
proteasome activating nucleotidase PAN and related proteasome subunits; This subfamily ...
160-328 1.46e-67

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: 217.98  E-value: 1.46e-67
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943972 160 FKDVAGADEEKQELVEVVEF-LKDPRKFAELGARIPKGVLLVGPPGTGKTLLAKACAGEAGVPFFSISGSDFVEMFVGVG 238
Cdd:cd19502     2 YEDIGGLDEQIREIREVVELpLKHPELFEELGIEPPKGVLLYGPPGTGKTLLAKAVANHTDATFIRVVGSELVQKYIGEG 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943972 239 ASRVRDLFENAKKNAPCLIFIDEIDAVGRQRGAGLGGGHDEREQTLNQLLVEMDGFSANEGIIIIAATNRADILDPALLR 318
Cdd:cd19502    82 ARLVRELFEMAREKAPSIIFIDEIDAIGAKRFDSGTGGDREVQRTMLELLNQLDGFDPRGNIKVIMATNRPDILDPALLR 161
                         170
                  ....*....|
gi 1732943972 319 PGRFDRQITV 328
Cdd:cd19502   162 PGRFDRKIEF 171
RecA-like_protease cd19481
proteases similar to RecA; RecA-like NTPases. This family includes the NTP binding domain of ...
170-328 2.28e-63

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: 206.36  E-value: 2.28e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943972 170 KQELVEVVEFLKDPRKFAELGARIPKGVLLVGPPGTGKTLLAKACAGEAGVPFFSISGSDFVEMFVGVGASRVRDLFENA 249
Cdd:cd19481     2 KASLREAVEAPRRGSRLRRYGLGLPKGILLYGPPGTGKTLLAKALAGELGLPLIVVKLSSLLSKYVGESEKNLRKIFERA 81
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1732943972 250 KKNAPCLIFIDEIDAVGRQRGAglGGGHDEREQTLNQLLVEMDGFSANEGIIIIAATNRADILDPALLRPGRFDRQITV 328
Cdd:cd19481    82 RRLAPCILFIDEIDAIGRKRDS--SGESGELRRVLNQLLTELDGVNSRSKVLVIAATNRPDLLDPALLRPGRFDEVIEF 158
CDC48 TIGR01243
AAA family ATPase, CDC48 subfamily; This subfamily of the AAA family ATPases includes two ...
153-390 8.91e-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: 221.32  E-value: 8.91e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943972 153 EEKK--RVKFKDVAGADEEKQELVEVVEF-LKDPRKFAELGARIPKGVLLVGPPGTGKTLLAKACAGEAGVPFFSISGSD 229
Cdd:TIGR01243 168 IERKvpKVTYEDIGGLKEAKEKIREMVELpMKHPELFEHLGIEPPKGVLLYGPPGTGKTLLAKAVANEAGAYFISINGPE 247
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943972 230 FVEMFVGVGASRVRDLFENAKKNAPCLIFIDEIDAVGRQRGAGLGgghDEREQTLNQLLVEMDGFSANEGIIIIAATNRA 309
Cdd:TIGR01243 248 IMSKYYGESEERLREIFKEAEENAPSIIFIDEIDAIAPKREEVTG---EVEKRVVAQLLTLMDGLKGRGRVIVIGATNRP 324
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943972 310 DILDPALLRPGRFDRQITVDRPDVIGREAVLKVHARNKPLDETVNLKSIAMRTPGFSGADLENLLNEAALVAARQ--NKK 387
Cdd:TIGR01243 325 DALDPALRRPGRFDREIVIRVPDKRARKEILKVHTRNMPLAEDVDLDKLAEVTHGFVGADLAALAKEAAMAALRRfiREG 404

                  ...
gi 1732943972 388 KID 390
Cdd:TIGR01243 405 KIN 407
RecA-like_CDC48_r2-like cd19511
second of two ATPase domains of CDC48/p97, PEX1 and -6, VAT and NVL, and similar ATPase ...
170-328 3.89e-62

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: 203.28  E-value: 3.89e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943972 170 KQELVEVVEF-LKDPRKFAELGARIPKGVLLVGPPGTGKTLLAKACAGEAGVPFFSISGSDFVEMFVGVGASRVRDLFEN 248
Cdd:cd19511     2 KRELKEAVEWpLKHPDAFKRLGIRPPKGVLLYGPPGCGKTLLAKALASEAGLNFISVKGPELFSKYVGESERAVREIFQK 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943972 249 AKKNAPCLIFIDEIDAVGRQRGAGLGGGHDEReqTLNQLLVEMDGFSANEGIIIIAATNRADILDPALLRPGRFDRQITV 328
Cdd:cd19511    82 ARQAAPCIIFFDEIDSLAPRRGQSDSSGVTDR--VVSQLLTELDGIESLKGVVVIAATNRPDMIDPALLRPGRLDKLIYV 159
COG1223 COG1223
Predicted ATPase, AAA+ superfamily [General function prediction only];
160-400 1.19e-61

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


Pssm-ID: 440836 [Multi-domain]  Cd Length: 246  Bit Score: 205.12  E-value: 1.19e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943972 160 FKDVAGADEEKQELVEVVEFLKDPRKFAELGARIPKGVLLVGPPGTGKTLLAKACAGEAGVPFFSISGSDFVEMFVGVGA 239
Cdd:COG1223     1 LDDVVGQEEAKKKLKLIIKELRRRENLRKFGLWPPRKILFYGPPGTGKTMLAEALAGELKLPLLTVRLDSLIGSYLGETA 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943972 240 SRVRDLFENAkKNAPCLIFIDEIDAVGRQRGAglGGGHDEREQTLNQLLVEMDGFsaNEGIIIIAATNRADILDPALLRp 319
Cdd:COG1223    81 RNLRKLFDFA-RRAPCVIFFDEFDAIAKDRGD--QNDVGEVKRVVNALLQELDGL--PSGSVVIAATNHPELLDSALWR- 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943972 320 gRFDRQITVDRPDVIGREAVLKVHARNKPLDETVNLKSIAMRTPGFSGADLENLLNEAALVAARQNKKKIDARDIDEATD 399
Cdd:COG1223   155 -RFDEVIEFPLPDKEERKEILELNLKKFPLPFELDLKKLAKKLEGLSGADIEKVLKTALKKAILEDREKVTKEDLEEALK 233

                  .
gi 1732943972 400 R 400
Cdd:COG1223   234 Q 234
PTZ00454 PTZ00454
26S protease regulatory subunit 6B-like protein; Provisional
150-402 4.22e-61

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


Pssm-ID: 240423 [Multi-domain]  Cd Length: 398  Bit Score: 208.85  E-value: 4.22e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943972 150 LYTEEKKRVKFKDVAGADEEKQELVEVVEF-LKDPRKFAELGARIPKGVLLVGPPGTGKTLLAKACAGEAGVPFFSISGS 228
Cdd:PTZ00454  134 LQMSEKPDVTYSDIGGLDIQKQEIREAVELpLTCPELYEQIGIDPPRGVLLYGPPGTGKTMLAKAVAHHTTATFIRVVGS 213
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943972 229 DFVEMFVGVGASRVRDLFENAKKNAPCLIFIDEIDAVGRQRGAGLGGGHDEREQTLNQLLVEMDGFSANEGIIIIAATNR 308
Cdd:PTZ00454  214 EFVQKYLGEGPRMVRDVFRLARENAPSIIFIDEVDSIATKRFDAQTGADREVQRILLELLNQMDGFDQTTNVKVIMATNR 293
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943972 309 ADILDPALLRPGRFDRQITVDRPDVIGREAVLKVHARNKPLDETVNLKSIAMRTPGFSGADLENLLNEAALVAARQNKKK 388
Cdd:PTZ00454  294 ADTLDPALLRPGRLDRKIEFPLPDRRQKRLIFQTITSKMNLSEEVDLEDFVSRPEKISAADIAAICQEAGMQAVRKNRYV 373
                         250
                  ....*....|....
gi 1732943972 389 IDARDIDEATDRVI 402
Cdd:PTZ00454  374 ILPKDFEKGYKTVV 387
RecA-like_CDC48_NLV2_r1-like cd19503
first of two ATPase domains of CDC48 and NLV2, and similar ATPase domains; CDC48 in yeast and ...
162-326 7.24e-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: 192.12  E-value: 7.24e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943972 162 DVAGADEEKQELVEVVEF-LKDPRKFAELGARIPKGVLLVGPPGTGKTLLAKACAGEAGVPFFSISGSDFVEMFVGVGAS 240
Cdd:cd19503     1 DIGGLDEQIASLKELIELpLKYPELFRALGLKPPRGVLLHGPPGTGKTLLARAVANEAGANFLSISGPSIVSKYLGESEK 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943972 241 RVRDLFENAKKNAPCLIFIDEIDAVGRQRGAglggGHDEREQTL-NQLLVEMDGFSANEGIIIIAATNRADILDPALLRP 319
Cdd:cd19503    81 NLREIFEEARSHAPSIIFIDEIDALAPKREE----DQREVERRVvAQLLTLMDGMSSRGKVVVIAATNRPDAIDPALRRP 156

                  ....*..
gi 1732943972 320 GRFDRQI 326
Cdd:cd19503   157 GRFDREV 163
PTZ00361 PTZ00361
26 proteosome regulatory subunit 4-like protein; Provisional
160-402 7.36e-58

26 proteosome regulatory subunit 4-like protein; Provisional


Pssm-ID: 185575 [Multi-domain]  Cd Length: 438  Bit Score: 201.15  E-value: 7.36e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943972 160 FKDVAGADEEKQELVEVVEF-LKDPRKFAELGARIPKGVLLVGPPGTGKTLLAKACAGEAGVPFFSISGSDFVEMFVGVG 238
Cdd:PTZ00361  182 YADIGGLEQQIQEIKEAVELpLTHPELYDDIGIKPPKGVILYGPPGTGKTLLAKAVANETSATFLRVVGSELIQKYLGDG 261
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943972 239 ASRVRDLFENAKKNAPCLIFIDEIDAVGRQRGAGLGGGHDEREQTLNQLLVEMDGFSANEGIIIIAATNRADILDPALLR 318
Cdd:PTZ00361  262 PKLVRELFRVAEENAPSIVFIDEIDAIGTKRYDATSGGEKEIQRTMLELLNQLDGFDSRGDVKVIMATNRIESLDPALIR 341
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943972 319 PGRFDRQITVDRPDVIGREAVLKVHARNKPLDETVNLKSIAMRTPGFSGADLENLLNEAALVAARQNKKKIDARDIDEAT 398
Cdd:PTZ00361  342 PGRIDRKIEFPNPDEKTKRRIFEIHTSKMTLAEDVDLEEFIMAKDELSGADIKAICTEAGLLALRERRMKVTQADFRKAK 421

                  ....
gi 1732943972 399 DRVI 402
Cdd:PTZ00361  422 EKVL 425
AAA pfam00004
ATPase family associated with various cellular activities (AAA); AAA family proteins often ...
197-330 1.29e-55

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: 184.72  E-value: 1.29e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943972 197 VLLVGPPGTGKTLLAKACAGEAGVPFFSISGSDFVEMFVGVGASRVRDLFENAKKNAPCLIFIDEIDAVGRQRGaglGGG 276
Cdd:pfam00004   1 LLLYGPPGTGKTTLAKAVAKELGAPFIEISGSELVSKYVGESEKRLRELFEAAKKLAPCVIFIDEIDALAGSRG---SGG 77
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1732943972 277 HDEREQTLNQLLVEMDGFSANEG-IIIIAATNRADILDPALLrpGRFDRQITVDR 330
Cdd:pfam00004  78 DSESRRVVNQLLTELDGFTSSNSkVIVIAATNRPDKLDPALL--GRFDRIIEFPL 130
RecA-like_VCP_r2 cd19529
second of two ATPase domains of Valosin-containing protein-like ATPase (VAT) and similar ...
170-328 1.67e-55

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: 185.78  E-value: 1.67e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943972 170 KQELVEVVEF-LKDPRKFAELGARIPKGVLLVGPPGTGKTLLAKACAGEAGVPFFSISGSDFVEMFVGVGASRVRDLFEN 248
Cdd:cd19529     2 KQELKEAVEWpLLKPEVFKRLGIRPPKGILLYGPPGTGKTLLAKAVATESNANFISVKGPELLSKWVGESEKAIREIFRK 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943972 249 AKKNAPCLIFIDEIDAVGRQRGAGLGGGHDEReqTLNQLLVEMDGFSANEGIIIIAATNRADILDPALLRPGRFDRQITV 328
Cdd:cd19529    82 ARQVAPCVIFFDEIDSIAPRRGTTGDSGVTER--VVNQLLTELDGLEEMNGVVVIAATNRPDIIDPALLRAGRFDRLIYI 159
RecA-like_CDC48_r2-like cd19528
second of two ATPase domains of CDC48 and similar ATPase domains; CDC48 in yeast and p97 or ...
170-328 1.85e-54

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: 183.10  E-value: 1.85e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943972 170 KQELVEVVEF-LKDPRKFAELGARIPKGVLLVGPPGTGKTLLAKACAGEAGVPFFSISGSDFVEMFVGVGASRVRDLFEN 248
Cdd:cd19528     2 KRELQELVQYpVEHPDKFLKFGMTPSKGVLFYGPPGCGKTLLAKAIANECQANFISVKGPELLTMWFGESEANVRDIFDK 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943972 249 AKKNAPCLIFIDEIDAVGRQRGAGLGGGHDEREQTLNQLLVEMDGFSANEGIIIIAATNRADILDPALLRPGRFDRQITV 328
Cdd:cd19528    82 ARAAAPCVLFFDELDSIAKARGGNIGDAGGAADRVINQILTEMDGMNTKKNVFIIGATNRPDIIDPAILRPGRLDQLIYI 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 ...
162-328 1.88e-49

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: 169.54  E-value: 1.88e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943972 162 DVAGADEEKQELVEVVEF-LKDPRKFAELGARIPKGVLLVGPPGTGKTLLAKACAGEAGVPFFSISGSDFVEMFVGVGAS 240
Cdd:cd19519     1 DIGGCRKQLAQIREMVELpLRHPELFKAIGIKPPRGILLYGPPGTGKTLIARAVANETGAFFFLINGPEIMSKLAGESES 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943972 241 RVRDLFENAKKNAPCLIFIDEIDAVGRQRGAglggGHDEREQTL-NQLLVEMDGFSANEGIIIIAATNRADILDPALLRP 319
Cdd:cd19519    81 NLRKAFEEAEKNAPAIIFIDEIDAIAPKREK----THGEVERRIvSQLLTLMDGLKQRAHVIVMAATNRPNSIDPALRRF 156

                  ....*....
gi 1732943972 320 GRFDRQITV 328
Cdd:cd19519   157 GRFDREIDI 165
RecA-like_NVL_r1-like cd19518
first of two ATPase domains of NVL (nuclear VCP-like protein) and similar ATPase domains; NVL ...
162-326 8.54e-49

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: 167.97  E-value: 8.54e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943972 162 DVAGADEEKQELVEVVEFLKDPRK-FAELGARIPKGVLLVGPPGTGKTLLAKACAGEAGVPFFSISGSDFVEMFVGVGAS 240
Cdd:cd19518     1 DIGGMDSTLKELCELLIHPILPPEyFQHLGVEPPRGVLLHGPPGCGKTMLANAIAGELKVPFLKISATEIVSGVSGESEE 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943972 241 RVRDLFENAKKNAPCLIFIDEIDAVGRQRGaglGGGHDEREQTLNQLLVEMDGFSANE----GIIIIAATNRADILDPAL 316
Cdd:cd19518    81 KIRELFDQAISNAPCIVFIDEIDAITPKRE---SAQREMERRIVSQLLTCMDELNNEKtaggPVLVIGATNRPDSLDPAL 157
                         170
                  ....*....|
gi 1732943972 317 LRPGRFDRQI 326
Cdd:cd19518   158 RRAGRFDREI 167
RecA-like_NVL_r2-like cd19530
second of two ATPase domains of NVL (nuclear VCP-like protein) and similar ATPase domains; NVL ...
176-328 1.02e-48

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: 167.66  E-value: 1.02e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943972 176 VVEFLKDPRKFAELGARIPKGVLLVGPPGTGKTLLAKACAGEAGVPFFSISGSDFVEMFVGVGASRVRDLFENAKKNAPC 255
Cdd:cd19530    12 ILRPIKRPDIYKALGIDLPTGVLLYGPPGCGKTLLAKAVANESGANFISVKGPELLNKYVGESERAVRQVFQRARASAPC 91
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1732943972 256 LIFIDEIDAVGRQRGAGLGGGhdeREQTLNQLLVEMDGFSANEGIIIIAATNRADILDPALLRPGRFDRQITV 328
Cdd:cd19530    92 VIFFDEVDALVPKRGDGGSWA---SERVVNQLLTEMDGLEERSNVFVIAATNRPDIIDPAMLRPGRLDKTLYV 161
RecA-like_PEX1_r2 cd19526
second of two ATPase domains of Peroxisomal biogenesis factor 1 (PEX1); PEX1(also known as ...
170-326 1.24e-43

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: 153.74  E-value: 1.24e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943972 170 KQELVEVVEF-LKDPRKFAELGARIPKGVLLVGPPGTGKTLLAKACAGEAGVPFFSISGSDFVEMFVGVGASRVRDLFEN 248
Cdd:cd19526     2 KKALEETIEWpSKYPKIFASSPLRLRSGILLYGPPGCGKTLLASAIASECGLNFISVKGPELLNKYIGASEQNVRDLFSR 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943972 249 AKKNAPCLIFIDEIDAVGRQRgaglggGHDER---EQTLNQLLVEMDGFSANEGIIIIAATNRADILDPALLRPGRFDRQ 325
Cdd:cd19526    82 AQSAKPCILFFDEFDSIAPKR------GHDSTgvtDRVVNQLLTQLDGVEGLDGVYVLAATSRPDLIDPALLRPGRLDKL 155

                  .
gi 1732943972 326 I 326
Cdd:cd19526   156 V 156
RecA-like_PEX6_r2 cd19527
second of two ATPase domains of Peroxisomal biogenesis factor 6 (PEX6); PEX6(also known as ...
170-328 1.21e-42

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: 151.13  E-value: 1.21e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943972 170 KQELVEVVEF-LKDPRKFAeLGARIPKGVLLVGPPGTGKTLLAKACAGEAGVPFFSISGSDFVEMFVGVGASRVRDLFEN 248
Cdd:cd19527     2 KKEILDTIQLpLEHPELFS-SGLRKRSGILLYGPPGTGKTLLAKAIATECSLNFLSVKGPELINMYIGESEANVREVFQK 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943972 249 AKKNAPCLIFIDEIDAVGRQRGA-GLGGGHDEReqTLNQLLVEMDGFS-ANEGIIIIAATNRADILDPALLRPGRFDRQI 326
Cdd:cd19527    81 ARDAKPCVIFFDELDSLAPSRGNsGDSGGVMDR--VVSQLLAELDGMSsSGQDVFVIGATNRPDLLDPALLRPGRFDKLL 158

                  ..
gi 1732943972 327 TV 328
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 ...
163-328 6.57e-41

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: 146.34  E-value: 6.57e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943972 163 VAGADEEKQELVEVVEFlkdPRKFAEL---GARIPKGVLLVGPPGTGKTLLAKACAGEAGVPFFSISGSDFVEMFVGVGA 239
Cdd:cd19509     1 IAGLDDAKEALKEAVIL---PSLRPDLfpgLRGPPRGILLYGPPGTGKTLLARAVASESGSTFFSISASSLVSKWVGESE 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943972 240 SRVRDLFENAKKNAPCLIFIDEIDAVGRQRGAglgGGHDEREQTLNQLLVEMDGF--SANEGIIIIAATNRADILDPALL 317
Cdd:cd19509    78 KIVRALFALARELQPSIIFIDEIDSLLSERGS---GEHEASRRVKTEFLVQMDGVlnKPEDRVLVLGATNRPWELDEAFL 154
                         170
                  ....*....|.
gi 1732943972 318 RpgRFDRQITV 328
Cdd:cd19509   155 R--RFEKRIYI 163
pup_AAA TIGR03689
proteasome ATPase; In the Actinobacteria, as shown for Mycobacterium tuberculosis, some ...
150-351 3.28e-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: 148.32  E-value: 3.28e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943972 150 LYTEEKKRVKFKDVAGADEEKQELVEVVE--FLKdPRKFAELGARIPKGVLLVGPPGTGKTLLAKACA--------GEAG 219
Cdd:TIGR03689 171 LVLEEVPDVTYADIGGLGSQIEQIRDAVElpFLH-PELYREYGLKPPKGVLLYGPPGCGKTLIAKAVAnslaarigAEGG 249
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943972 220 VP--FFSISGSDFVEMFVGVGASRVRDLFENAKKNA----PCLIFIDEIDAVGRQRGAGLGGghDEREQTLNQLLVEMDG 293
Cdd:TIGR03689 250 GKsyFLNIKGPELLNKYVGETERQIRLIFQRAREKAsegrPVIVFFDEMDSLFRTRGSGVSS--DVETTVVPQLLAEIDG 327
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1732943972 294 FSANEGIIIIAATNRADILDPALLRPGRFDRQITVDRPDVIGREAVLKVH-ARNKPLDE 351
Cdd:TIGR03689 328 VESLDNVIVIGASNREDMIDPAILRPGRLDVKIRIERPDAEAAADIFAKYlTDDLPLPE 386
RecA-like_VPS4 cd19521
ATPase domain of vacuolar protein sorting-associated protein 4; Vacuolar protein ...
155-328 1.11e-37

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: 137.69  E-value: 1.11e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943972 155 KKRVKFKDVAGADEEKQELVEVVEFlkdPRKFAEL--GARIP-KGVLLVGPPGTGKTLLAKACAGEAGVPFFSISGSDFV 231
Cdd:cd19521     1 KPNVKWEDVAGLEGAKEALKEAVIL---PVKFPHLftGNRKPwSGILLYGPPGTGKSYLAKAVATEANSTFFSVSSSDLV 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943972 232 EMFVGVGASRVRDLFENAKKNAPCLIFIDEIDAVGRQRGAglgGGHDEREQTLNQLLVEMDGFSAN-EGIIIIAATNRAD 310
Cdd:cd19521    78 SKWMGESEKLVKQLFAMARENKPSIIFIDEVDSLCGTRGE---GESEASRRIKTELLVQMNGVGNDsQGVLVLGATNIPW 154
                         170
                  ....*....|....*...
gi 1732943972 311 ILDPALLRpgRFDRQITV 328
Cdd:cd19521   155 QLDSAIRR--RFEKRIYI 170
RecA-like_Yta7-like cd19517
ATPase domain of Saccharomyces cerevisiae Yta7 and similar ATPase domains; Saccharomyces ...
162-325 8.94e-35

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: 129.55  E-value: 8.94e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943972 162 DVAGADEEKQELVEVVEF-LKDPRKFAELGARIPKGVLLVGPPGTGKTLLAKACAGEAG-----VPFFSISGSDFVEMFV 235
Cdd:cd19517     1 DIGGLSHYINQLKEMVFFpLLYPEVFAKFKITPPRGVLFHGPPGTGKTLMARALAAECSkggqkVSFFMRKGADCLSKWV 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943972 236 GVGASRVRDLFENAKKNAPCLIFIDEIDAVGRQRGAglggghdEREQT----LNQLLVEMDGFSANEGIIIIAATNRADI 311
Cdd:cd19517    81 GEAERQLRLLFEEAYRMQPSIIFFDEIDGLAPVRSS-------KQEQIhasiVSTLLALMDGLDNRGQVVVIGATNRPDA 153
                         170
                  ....*....|....
gi 1732943972 312 LDPALLRPGRFDRQ 325
Cdd:cd19517   154 LDPALRRPGRFDRE 167
RecA-like_ATAD1 cd19520
ATPase domain of ATPase family AAA domain-containing protein 1 and similar ATPase domains; ...
162-322 6.00e-33

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: 124.46  E-value: 6.00e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943972 162 DVAGADEEKQELVEVVEFlkdPRKFAELGA-----RIPKGVLLVGPPGTGKTLLAKACAGEAGVPFFSISGSDFVEMFVG 236
Cdd:cd19520     1 DIGGLDEVITELKELVIL---PLQRPELFDnsrllQPPKGVLLYGPPGCGKTMLAKATAKEAGARFINLQVSSLTDKWYG 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943972 237 VGASRVRDLFENAKKNAPCLIFIDEIDAVGRQRGAglgGGHDEREQTLNQLLVEMDGFS--ANEGIIIIAATNRADILDP 314
Cdd:cd19520    78 ESQKLVAAVFSLASKLQPSIIFIDEIDSFLRQRSS---TDHEATAMMKAEFMSLWDGLStdGNCRVIVMGATNRPQDLDE 154
                         170
                  ....*....|
gi 1732943972 315 ALLR--PGRF 322
Cdd:cd19520   155 AILRrmPKRF 164
RecA-like_KTNA1 cd19522
Katanin p60 ATPase-containing subunit A1; Katanin p60 ATPase-containing subunit A1 (KTNA1) is ...
162-328 2.10e-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: 122.79  E-value: 2.10e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943972 162 DVAGADEEKQELVE-VVEFLKDPRKFAelGARIP-KGVLLVGPPGTGKTLLAKACAGEAGVPFFSISGSDFVEMFVGVGA 239
Cdd:cd19522     1 DIADLEEAKKLLEEaVVLPMWMPEFFK--GIRRPwKGVLMVGPPGTGKTLLAKAVATECGTTFFNVSSSTLTSKYRGESE 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943972 240 SRVRDLFENAKKNAPCLIFIDEIDAVGRQRGAglGGGHDEREQTLNQLLVEMDGFS---ANEG----IIIIAATNRADIL 312
Cdd:cd19522    79 KLVRLLFEMARFYAPTTIFIDEIDSICSRRGT--SEEHEASRRVKSELLVQMDGVGgasENDDpskmVMVLAATNFPWDI 156
                         170
                  ....*....|....*.
gi 1732943972 313 DPALLRpgRFDRQITV 328
Cdd:cd19522   157 DEALRR--RLEKRIYI 170
RecA-like_Figl-1 cd19525
ATPase domain of Fidgetin-Like 1 (FIGL-1); FIGL-1 may participate in DNA repair in the nucleus; ...
158-328 5.76e-32

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: 122.40  E-value: 5.76e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943972 158 VKFKDVAGADEEKQELVEVVEF-LKDPRKFAELGARiPKGVLLVGPPGTGKTLLAKACAGEAGVPFFSISGSDFVEMFVG 236
Cdd:cd19525    19 INWADIAGLEFAKKTIKEIVVWpMLRPDIFTGLRGP-PKGILLFGPPGTGKTLIGKCIASQSGATFFSISASSLTSKWVG 97
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943972 237 VGASRVRDLFENAKKNAPCLIFIDEIDAVGRQRGAglgGGHDEREQTLNQLLVEMDGF--SANEGIIIIAATNRADILDP 314
Cdd:cd19525    98 EGEKMVRALFSVARCKQPAVIFIDEIDSLLSQRGE---GEHESSRRIKTEFLVQLDGAttSSEDRILVVGATNRPQEIDE 174
                         170
                  ....*....|....
gi 1732943972 315 ALLRpgRFDRQITV 328
Cdd:cd19525   175 AARR--RLVKRLYI 186
RecA-like_spastin cd19524
ATPase domain of spastin; Spastin is an ATP-dependent microtubule-severing protein involved in ...
162-328 3.46e-31

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: 119.18  E-value: 3.46e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943972 162 DVAGADEEKQELVEVVeFLKDPRKFAELGARIP-KGVLLVGPPGTGKTLLAKACAGEAGVPFFSISGSDFVEMFVGVGAS 240
Cdd:cd19524     1 DIAGQDLAKQALQEMV-ILPSLRPELFTGLRAPaRGLLLFGPPGNGKTMLAKAVAAESNATFFNISAASLTSKYVGEGEK 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943972 241 RVRDLFENAKKNAPCLIFIDEIDAVGRQRGAglgGGHDEREQTLNQLLVEMDGFSAN--EGIIIIAATNRADILDPALLR 318
Cdd:cd19524    80 LVRALFAVARELQPSIIFIDEVDSLLSERSE---GEHEASRRLKTEFLIEFDGVQSNgdDRVLVMGATNRPQELDDAVLR 156
                         170
                  ....*....|
gi 1732943972 319 pgRFDRQITV 328
Cdd:cd19524   157 --RFTKRVYV 164
AAA cd00009
The AAA+ (ATPases Associated with a wide variety of cellular Activities) superfamily ...
164-329 1.67e-27

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: 108.39  E-value: 1.67e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943972 164 AGADEEKQELVEVVEflkdprkfaelgARIPKGVLLVGPPGTGKTLLAKACAGEA---GVPFFSISGSDFVEMFVG---V 237
Cdd:cd00009     1 VGQEEAIEALREALE------------LPPPKNLLLYGPPGTGKTTLARAIANELfrpGAPFLYLNASDLLEGLVVaelF 68
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943972 238 GASRVRDLFENAKKNAPCLIFIDEIDAVGRqrgaglggghDEREQTLNQLLVEMDGFSANEGIIIIAATNRADILDPALL 317
Cdd:cd00009    69 GHFLVRLLFELAEKAKPGVLFIDEIDSLSR----------GAQNALLRVLETLNDLRIDRENVRVIGATNRPLLGDLDRA 138
                         170
                  ....*....|..
gi 1732943972 318 RPGRFDRQITVD 329
Cdd:cd00009   139 LYDRLDIRIVIP 150
RecA-like_NSF-SEC18_r1-like cd19504
first of two ATPase domains of NSF and SEC18, and similar ATPase domains; ...
183-328 7.84e-27

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: 107.19  E-value: 7.84e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943972 183 PRKFAELGARIPKGVLLVGPPGTGKTLLAKAC-----AGEAGVpffsISGSDFVEMFVGVGASRVRDLFENAKKNAPCL- 256
Cdd:cd19504    24 PEIVEQLGCKHVKGILLYGPPGTGKTLMARQIgkmlnAREPKI----VNGPEILNKYVGESEANIRKLFADAEEEQRRLg 99
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1732943972 257 -------IFIDEIDAVGRQRGAGlGGGHDEREQTLNQLLVEMDGFSANEGIIIIAATNRADILDPALLRPGRFDRQITV 328
Cdd:cd19504   100 ansglhiIIFDEIDAICKQRGSM-AGSTGVHDTVVNQLLSKIDGVEQLNNILVIGMTNRKDLIDEALLRPGRLEVQMEI 177
ycf46 CHL00195
Ycf46; Provisional
158-402 1.22e-22

Ycf46; Provisional


Pssm-ID: 177094 [Multi-domain]  Cd Length: 489  Bit Score: 101.63  E-value: 1.22e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943972 158 VKFKDVAGADEEKQELVevveflKDPRKFAE----LGARIPKGVLLVGPPGTGKTLLAKACAGEAGVPFFSIsgsDFVEM 233
Cdd:CHL00195  225 EKISDIGGLDNLKDWLK------KRSTSFSKqasnYGLPTPRGLLLVGIQGTGKSLTAKAIANDWQLPLLRL---DVGKL 295
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943972 234 F---VGVGASRVRDLFENAKKNAPCLIFIDEID-AVGRQRGAGLGGGHDEREQTLNQLLVEmdgfsANEGIIIIAATNRA 309
Cdd:CHL00195  296 FggiVGESESRMRQMIRIAEALSPCILWIDEIDkAFSNSESKGDSGTTNRVLATFITWLSE-----KKSPVFVVATANNI 370
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943972 310 DILDPALLRPGRFDRQITVDRPDVIGREAVLKVH-ARNKPLD-ETVNLKSIAMRTPGFSGADLENLLNEAALVAARQNkK 387
Cdd:CHL00195  371 DLLPLEILRKGRFDEIFFLDLPSLEEREKIFKIHlQKFRPKSwKKYDIKKLSKLSNKFSGAEIEQSIIEAMYIAFYEK-R 449
                         250
                  ....*....|....*
gi 1732943972 388 KIDARDIDEATDRVI 402
Cdd:CHL00195  450 EFTTDDILLALKQFI 464
AAA smart00382
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ...
194-332 2.27e-20

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: 87.81  E-value: 2.27e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943972  194 PKGVLLVGPPGTGKTLLAKACAGEA---GVPFFSISGSDFVE--------------MFVGVGASRVRDLFENAKKNAPCL 256
Cdd:smart00382   2 GEVILIVGPPGSGKTTLARALARELgppGGGVIYIDGEDILEevldqllliivggkKASGSGELRLRLALALARKLKPDV 81
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1732943972  257 IFIDEIDAvgrqrgagLGGGHDEREQTLNQLLVEMDGFSANEGIIIIAATNRADILDPALLRPgRFDRQITVDRPD 332
Cdd:smart00382  82 LILDEITS--------LLDAEQEALLLLLEELRLLLLLKSEKNLTVILTTNDEKDLGPALLRR-RFDRRIVLLLIL 148
RecA-like_Ycf46-like cd19507
ATPase domain of Ycf46 and similar ATPase domains; Ycf46 may play a role in the regulation of ...
190-324 4.51e-20

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: 87.42  E-value: 4.51e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943972 190 GARIPKGVLLVGPPGTGKTLLAKACAGEAGVPFFSISGSDFVEMFVGVGASRVRDLFENAKKNAPCLIFIDEID-AVGrq 268
Cdd:cd19507    27 GLPTPKGLLLVGIQGTGKSLTAKAIAGVWQLPLLRLDMGRLFGGLVGESESRLRQMIQTAEAIAPCVLWIDEIEkGFS-- 104
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1732943972 269 rGAGLGGGHDEREQTLNQLLVEMDGFSANegIIIIAATNRADILDPALLRPGRFDR 324
Cdd:cd19507   105 -NADSKGDSGTSSRVLGTFLTWLQEKKKP--VFVVATANNVQSLPPELLRKGRFDE 157
RecA-like_fidgetin cd19523
ATPase domain of fidgetin; Fidgetin (FIGN) is a ATP-dependent microtubule severing protein. ...
162-328 3.93e-19

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: 84.94  E-value: 3.93e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943972 162 DVAGADEEKQELV-EVVEFLKDPRKFAELgARIPKGVLLVGPPGTGKTLLAKACAGEAGVPFFSISGSDFVEMFVGVGAS 240
Cdd:cd19523     1 DIAGLGALKAAIKeEVLWPLLRPDAFSGL-LRLPRSILLFGPRGTGKTLLGRCLASQLGATFLRLRGSTLVAKWAGEGEK 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943972 241 RVRDLFENAKKNAPCLIFIDEIDAV--GRQRGAGLGGghdeREQTlnQLLVEMDGF--SANEGIIIIAATNRADILDPAL 316
Cdd:cd19523    80 ILQASFLAARCRQPSVLFISDLDALlsSQDDEASPVG----RLQV--ELLAQLDGVlgSGEDGVLVVCTTSKPEEIDESL 153
                         170
                  ....*....|..
gi 1732943972 317 LRpgRFDRQITV 328
Cdd:cd19523   154 RR--YFSKRLLV 163
RecA-like_BCS1 cd19510
Mitochondrial chaperone BCS1; Mitochondrial chaperone BCS1 is necessary for the assembly of ...
175-328 4.76e-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: 84.33  E-value: 4.76e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943972 175 EVVEFLKDPRKFAELGARIPKGVLLVGPPGTGKTLLAKACAGEAGVPFFSISGSDfvemfVGVGASRVRDLFENAKKNAp 254
Cdd:cd19510     4 DLKDFIKNEDWYNDRGIPYRRGYLLYGPPGTGKSSFIAALAGELDYDICDLNLSE-----VVLTDDRLNHLLNTAPKQS- 77
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1732943972 255 cLIFIDEIDAV---GRQRGAGLGGGHDEREQTLNQLLVEMDGFSANEGIIIIAATNRADILDPALLRPGRFDRQITV 328
Cdd:cd19510    78 -IILLEDIDAAfesREHNKKNPSAYGGLSRVTFSGLLNALDGVASSEERIVFMTTNHIERLDPALIRPGRVDMKIYM 153
RecA-like_Ycf2 cd19505
ATPase domain of plant YCF2; Ycf2 is a chloroplast ATPase which has an essential function; ...
188-328 9.61e-13

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: 66.25  E-value: 9.61e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943972 188 ELGARIPKGVLLVGPPGTGKTLLAKACAGEAGVPFFSISGSDFV--------------EMFVGVGASRVRDLFENAKKNA 253
Cdd:cd19505     6 RLGLSPSKGILLIGSIETGRSYLIKSLAANSYVPLIRISLNKLLynkpdfgnddwidgMLILKESLHRLNLQFELAKAMS 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943972 254 PCLIFIDEIDAVGRQRgaglgGGHDEREQT------LNQLLVEMDGFSANEGIIIIAATNRADILDPALLRPGRFDRQIT 327
Cdd:cd19505    86 PCIIWIPNIHELNVNR-----STQNLEEDPklllglLLNYLSRDFEKSSTRNILVIASTHIPQKVDPALIAPNRLDTCIN 160

                  .
gi 1732943972 328 V 328
Cdd:cd19505   161 I 161
AAA_lid_3 pfam17862
AAA+ lid domain; This entry represents the alpha helical AAA+ lid domain that is found to the ...
353-396 1.24e-12

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: 62.56  E-value: 1.24e-12
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 1732943972 353 VNLKSIAMRTPGFSGADLENLLNEAALVAARQNKKKIDARDIDE 396
Cdd:pfam17862   2 VDLEELAERTEGFSGADLEALCREAALAALRRGLEAVTQEDLEE 45
RecA-like_ATAD3-like cd19512
ATPase domains of ATPase AAA-domain protein 3A (ATAD3A), -3B, and -3C, and similar ATPase ...
195-334 7.57e-12

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: 63.70  E-value: 7.57e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943972 195 KGVLLVGPPGTGKTLLAKACAGEAGVPFFSISGSDFVEMFVGvGASRVRDLFENAKK-NAPCLIFIDEIDAVGRQRgAGL 273
Cdd:cd19512    23 RNILFYGPPGTGKTLFAKKLALHSGMDYAIMTGGDVAPMGRE-GVTAIHKVFDWANTsRRGLLLFVDEADAFLRKR-STE 100
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1732943972 274 GGGHDEReQTLNQLLVEMdGFSANEgIIIIAATNradildpallRPGRFDRQITvDRPDVI 334
Cdd:cd19512   101 KISEDLR-AALNAFLYRT-GEQSNK-FMLVLASN----------QPEQFDWAIN-DRIDEM 147
PRK04195 PRK04195
replication factor C large subunit; Provisional
154-263 1.94e-11

replication factor C large subunit; Provisional


Pssm-ID: 235250 [Multi-domain]  Cd Length: 482  Bit Score: 66.48  E-value: 1.94e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943972 154 EKKRVK-FKDVAGADEEKQELVEVVEflkdprkfAELGARIPKGVLLVGPPGTGKTLLAKACAGEAGVPFFSISGSDF-- 230
Cdd:PRK04195    6 EKYRPKtLSDVVGNEKAKEQLREWIE--------SWLKGKPKKALLLYGPPGVGKTSLAHALANDYGWEVIELNASDQrt 77
                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 1732943972 231 ---VEMFVGvGASRVRDLFENAKKnapcLIFIDEID 263
Cdd:PRK04195   78 advIERVAG-EAATSGSLFGARRK----LILLDEVD 108
FtsH_ext pfam06480
FtsH Extracellular; This domain is found in the FtsH family of proteins. FtsH is the only ...
9-105 3.50e-11

FtsH Extracellular; This domain is found in the FtsH family of proteins. FtsH is the only membrane-bound ATP-dependent protease universally conserved in prokaryotes. It only efficiently degrades proteins that have a low thermodynamic stability - e.g. it lacks robust unfoldase activity. This feature may be key and implies that this could be a criterion for degrading a protein. In Oenococcus oeni FtsH is involved in protection against environmental stress, and shows increased expression under heat or osmotic stress. These two lines of evidence suggest that it is a fundamental prokaryotic self-protection mechanism that checks if proteins are correctly folded (personal obs: Yeats C). The precise function of this N-terminal region is unclear.


Pssm-ID: 377663 [Multi-domain]  Cd Length: 103  Bit Score: 60.31  E-value: 3.50e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943972   9 IFYLLILLVVIGVVSYFQ-TSNPKTENMSYSTFIKNLDDGKVDSVSVQPVRGVYEVKGQLKNYDKD---QYFLTHVPE-G 83
Cdd:pfam06480   2 LLWLLILLVLLLLFLLFLlSSSSSTKEISYSEFLEYLEAGKVKKVVVQDDEILPTGVVEGTLKDGSkftTYFIPSLPNvD 81
                          90       100
                  ....*....|....*....|..
gi 1732943972  84 KGADQIFNALKKTDVKVEPAQE 105
Cdd:pfam06480  82 SLLEKLEDALEEKGVKVSVKPP 103
PRK13342 PRK13342
recombination factor protein RarA; Reviewed
197-262 2.14e-09

recombination factor protein RarA; Reviewed


Pssm-ID: 237355 [Multi-domain]  Cd Length: 413  Bit Score: 60.10  E-value: 2.14e-09
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943972 197 VLLVGPPGTGKTLLAKACAGEAGVPFFSISGSDFvemfvgvGASRVRDLFENAKKNA----PCLIFIDEI 262
Cdd:PRK13342   39 MILWGPPGTGKTTLARIIAGATDAPFEALSAVTS-------GVKDLREVIEEARQRRsagrRTILFIDEI 101
RecA-like_HslU cd19498
ATP-dependent protease ATPase subunit HslU; HslU is a component of the ATP-dependent protease ...
193-305 2.69e-09

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: 57.00  E-value: 2.69e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943972 193 IPKGVLLVGPPGTGKTLLAKACAGEAGVPFFSISGSDFVEM-FVGVGA-SRVRDLFENakknapcLIFIDEIDAVGRQRG 270
Cdd:cd19498    45 TPKNILMIGPTGVGKTEIARRLAKLAGAPFIKVEATKFTEVgYVGRDVeSIIRDLVEG-------IVFIDEIDKIAKRGG 117
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 1732943972 271 aglGGGHD-EREQTLNQLLVEMDGFSAN--------EGIIIIAA 305
Cdd:cd19498   118 ---SSGPDvSREGVQRDLLPIVEGSTVStkygpvktDHILFIAA 158
RarA COG2256
Replication-associated recombination protein RarA (DNA-dependent ATPase) [Replication, ...
197-262 1.02e-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: 1.02e-08
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943972 197 VLLVGPPGTGKTLLAKACAGEAGVPFFSISGsdfvemfVGVGASRVRDLFENAKKNA----PCLIFIDEI 262
Cdd:COG2256    52 MILWGPPGTGKTTLARLIANATDAEFVALSA-------VTSGVKDIREVIEEARERRaygrRTILFVDEI 114
ycf2 CHL00206
Ycf2; Provisional
188-400 1.43e-08

Ycf2; Provisional


Pssm-ID: 214396 [Multi-domain]  Cd Length: 2281  Bit Score: 58.38  E-value: 1.43e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943972  188 ELGARIPKGVLLVGPPGTGKTLLAKACAGEAGVPFFS--------------------ISGSDFVE--------------- 232
Cdd:CHL00206  1624 RLALSPSRGILVIGSIGTGRSYLVKYLATNSYVPFITvflnkfldnkpkgfliddidIDDSDDIDdsddidrdldtellt 1703
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943972  233 --------MFVGVGASRVRDLFENAKKNAPCLIFIDEIDAVGRqrgaglgggHDEREQTLNQLLVEMDGFSAN---EGII 301
Cdd:CHL00206  1704 mmnaltmdMMPKIDRFYITLQFELAKAMSPCIIWIPNIHDLNV---------NESNYLSLGLLVNSLSRDCERcstRNIL 1774
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943972  302 IIAATNRADILDPALLRPGRFDRQITVDRPDVIGRE----AVLKV---HARNKPLdETVNLKSIAMrtpGFSGADLENLL 374
Cdd:CHL00206  1775 VIASTHIPQKVDPALIAPNKLNTCIKIRRLLIPQQRkhffTLSYTrgfHLEKKMF-HTNGFGSITM---GSNARDLVALT 1850
                          250       260
                   ....*....|....*....|....*.
gi 1732943972  375 NEAALVAARQNKKKIDARDIDEATDR 400
Cdd:CHL00206  1851 NEALSISITQKKSIIDTNTIRSALHR 1876
AAA_5 pfam07728
AAA domain (dynein-related subfamily); This Pfam entry includes some of the AAA proteins not ...
196-322 1.93e-08

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: 53.45  E-value: 1.93e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943972 196 GVLLVGPPGTGKTLLAK-ACAGEAGVPFFSISGSDF---------VEMFVGVGASRVRDLFENAKKnaPCLIFIDEIDAv 265
Cdd:pfam07728   1 GVLLVGPPGTGKTELAErLAAALSNRPVFYVQLTRDtteedlfgrRNIDPGGASWVDGPLVRAARE--GEIAVLDEINR- 77
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943972 266 grqrgaglggGHDEREQTLNQLLVE-----MDGF----SANEGIIIIAATNRADI----LDPALLRpgRF 322
Cdd:pfam07728  78 ----------ANPDVLNSLLSLLDErrlllPDGGelvkAAPDGFRLIATMNPLDRglneLSPALRS--RF 135
RecA-like_Pch2-like cd19508
ATPase domain of Pachytene checkpoint 2 (Pch2) and similar ATPase domains; Pch2 (known as ...
197-333 2.77e-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: 51.29  E-value: 2.77e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943972 197 VLLVGPPGTGKTLLAKACAGEAGV---------------------PFFSISGSDFVEMFvgvgaSRVRDLFENakKNAPC 255
Cdd:cd19508    55 VLLHGPPGTGKTSLCKALAQKLSIrlssryrygqlieinshslfsKWFSESGKLVTKMF-----QKIQELIDD--KDALV 127
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1732943972 256 LIFIDEIDAVGRQRGAGLGGGH-DEREQTLNQLLVEMDGFSANEGIIIIAATNRADILDPALlrpgrfdrqitVDRPDV 333
Cdd:cd19508   128 FVLIDEVESLAAARSASSSGTEpSDAIRVVNAVLTQIDRIKRYHNNVILLTSNLLEKIDVAF-----------VDRADI 195
TIP49 COG1224
DNA helicase TIP49, TBP-interacting protein [Transcription];
195-230 4.31e-07

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


Pssm-ID: 440837 [Multi-domain]  Cd Length: 452  Bit Score: 52.67  E-value: 4.31e-07
                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 1732943972 195 KGVLLVGPPGTGKTLLAKACAGEAG--VPFFSISGSDF 230
Cdd:COG1224    65 KGILIVGPPGTGKTALAVAIARELGedTPFVAISGSEI 102
RecA-like_superfamily cd01120
RecA-like_NTPases; RecA-like NTPases. This superfamily includes the NTP binding domain of F1 ...
197-313 5.12e-07

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: 48.65  E-value: 5.12e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943972 197 VLLVGPPGTGKTLLAK---ACAGEAGVPFFSISgsdFVEMFVgvgaSRVRDLFENAKknaPCLIFIDEIDAVGRQRGAgl 273
Cdd:cd01120     1 ILITGPPGSGKTTLLLqfaEQALLSDEPVIFIS---FLDTIL----EAIEDLIEEKK---LDIIIIDSLSSLARASQG-- 68
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 1732943972 274 ggghDEREQTLNQLLVEMdGFSANEGIIIIAATNRADILD 313
Cdd:cd01120    69 ----DRSSELLEDLAKLL-RAARNTGITVIATIHSDKFDI 103
RecA-like_Lon cd19500
lon protease homolog 2 peroxisomal; Lon protease (also known as Lon peptidase) is an ...
198-267 3.12e-06

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: 47.94  E-value: 3.12e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1732943972 198 LLVGPPGTGKTLLAKACAGEAGVPFFSIS-G--SDFVEM------FVGVGASRVRDLFENAKKNAPcLIFIDEIDAVGR 267
Cdd:cd19500    41 CLVGPPGVGKTSLGKSIARALGRKFVRISlGgvRDEAEIrghrrtYVGAMPGRIIQALKKAGTNNP-VFLLDEIDKIGS 118
MoxR COG0714
MoxR-like ATPase [General function prediction only]; MoxR-like ATPase is part of the Pathway ...
197-384 6.51e-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: 48.24  E-value: 6.51e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943972 197 VLLVGPPGTGKTLLAKACAGEAGVPFFSISG------------SDFVEMFvgvGASRVRD--LFENakknapcLIFIDEI 262
Cdd:COG0714    34 LLLEGVPGVGKTTLAKALARALGLPFIRIQFtpdllpsdilgtYIYDQQT---GEFEFRPgpLFAN-------VLLADEI 103
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943972 263 DavgrqRGaglggghdeREQTLNQLL-------VEMDG--FSANEGIIIIAATNRADI-----LDPALLRpgRFDRQITV 328
Cdd:COG0714   104 N-----RA---------PPKTQSALLeameerqVTIPGgtYKLPEPFLVIATQNPIEQegtypLPEAQLD--RFLLKLYI 167
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1732943972 329 DRPDvigREAVLKvharnkpldetvnlksIAMRTPGFSGADLENLLNEAALVAARQ 384
Cdd:COG0714   168 GYPD---AEEERE----------------ILRRHTGRHLAEVEPVLSPEELLALQE 204
T7SS_EccA TIGR03922
type VII secretion AAA-ATPase EccA; This model represents the AAA family ATPase, EccA, of the ...
154-352 7.00e-06

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: 49.07  E-value: 7.00e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943972 154 EKKRVKFKDVAGADEEKQELVEV----------------VEFLKDPRKF----AELGARIP---KGVLLVGPPGTGKTLL 210
Cdd:TIGR03922 249 APSRAEFVDPAAAERKAKLLAEAeaelaeqiglervkrqVAALKSSTAMalarAERGLPVAqtsNHMLFAGPPGTGKTTI 328
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943972 211 AKACAGE-AGVPFFS------ISGSDFVEMFVGVGASRVRDLFENAKKNApclIFIDEIDAVGRQRGaglGGGHDEREQT 283
Cdd:TIGR03922 329 ARVVAKIyCGLGVLRkplvreVSRADLIGQYIGESEAKTNEIIDSALGGV---LFLDEAYTLVETGY---GQKDPFGLEA 402
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1732943972 284 LNQLLVEMDgfSANEGIIIIAATNRADIlDPAL-----LRpGRFDRQITVDR--PDVIGREAVLKVHARNKPLDET 352
Cdd:TIGR03922 403 IDTLLARME--NDRDRLVVIGAGYRKDL-DKFLevnegLR-SRFTRVIEFPSysPDELVEIARRMATERDSVLDDA 474
TIP49 pfam06068
TIP49 P-loop domain; This family consists of the C-terminal region of several eukaryotic and ...
195-230 8.19e-06

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: 48.46  E-value: 8.19e-06
                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 1732943972 195 KGVLLVGPPGTGKTLLAKACAGEAG--VPFFSISGSDF 230
Cdd:pfam06068  51 RAVLIAGPPGTGKTALAIAISKELGedTPFTSISGSEV 88
McrB COG1401
5-methylcytosine-specific restriction endonuclease McrBC, GTP-binding regulatory subunit McrB ...
192-262 1.35e-04

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


Pssm-ID: 441011 [Multi-domain]  Cd Length: 477  Bit Score: 44.76  E-value: 1.35e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943972 192 RIPKGVLLVGPPGTGKT----LLAKACAGEAG-----VPFF-SISGSDFVEMFVGVGAS---RVRD-LF----ENAKKN- 252
Cdd:COG1401   219 KTKKNVILAGPPGTGKTylarRLAEALGGEDNgriefVQFHpSWSYEDFLLGYRPSLDEgkyEPTPgIFlrfcLKAEKNp 298
                          90
                  ....*....|.
gi 1732943972 253 -APCLIFIDEI 262
Cdd:COG1401   299 dKPYVLIIDEI 309
ruvB PRK00080
Holliday junction branch migration DNA helicase RuvB;
197-262 1.89e-04

Holliday junction branch migration DNA helicase RuvB;


Pssm-ID: 234619 [Multi-domain]  Cd Length: 328  Bit Score: 43.97  E-value: 1.89e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1732943972 197 VLLVGPPGTGKTLLAKACAGEAGVPFFSISG------SDFVEMFVgvgasrvrdlfeNAKKNApcLIFIDEI 262
Cdd:PRK00080   54 VLLYGPPGLGKTTLANIIANEMGVNIRITSGpalekpGDLAAILT------------NLEEGD--VLFIDEI 111
RuvB_N pfam05496
Holliday junction DNA helicase RuvB P-loop domain; The RuvB protein makes up part of the ...
197-262 3.65e-04

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: 41.33  E-value: 3.65e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1732943972 197 VLLVGPPGTGKTLLAKACAGEAGVPFFSISGSDFvemfvgvgaSRVRDL---FENAKKNApcLIFIDEI 262
Cdd:pfam05496  36 VLLYGPPGLGKTTLANIIANEMGVNIRITSGPAI---------ERPGDLaaiLTNLEPGD--VLFIDEI 93
AAA_2 pfam07724
AAA domain (Cdc48 subfamily); This Pfam entry includes some of the AAA proteins not detected ...
194-263 4.31e-04

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: 41.41  E-value: 4.31e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943972 194 PKGV-LLVGPPGTGKTLLAKACAGEAGV---PFFSISGSDFVE-----MFVG-----VGASRVRDLFENAKKNAPCLIFI 259
Cdd:pfam07724   2 PIGSfLFLGPTGVGKTELAKALAELLFGderALIRIDMSEYMEehsvsRLIGappgyVGYEEGGQLTEAVRRKPYSIVLI 81

                  ....
gi 1732943972 260 DEID 263
Cdd:pfam07724  82 DEIE 85
44 PHA02544
clamp loader, small subunit; Provisional
184-266 5.63e-04

clamp loader, small subunit; Provisional


Pssm-ID: 222866 [Multi-domain]  Cd Length: 316  Bit Score: 42.28  E-value: 5.63e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943972 184 RKFAELGaRIPKGVLLVGPPGTGKTLLAKACAGEAGVPFFSISGS----DFVEMFVGVGASRVrDLFENAKknapcLIFI 259
Cdd:PHA02544   34 KSIVKKG-RIPNMLLHSPSPGTGKTTVAKALCNEVGAEVLFVNGSdcriDFVRNRLTRFASTV-SLTGGGK-----VIII 106

                  ....*..
gi 1732943972 260 DEIDAVG 266
Cdd:PHA02544  107 DEFDRLG 113
HolB COG0470
DNA polymerase III, delta prime subunit [Replication, recombination and repair];
192-264 5.70e-04

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


Pssm-ID: 440238 [Multi-domain]  Cd Length: 289  Bit Score: 42.27  E-value: 5.70e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943972 192 RIPKGVLLVGPPGTGKTLLA---------------KACAGEAGVPFFSISGSDFVEMFVGV-----GASRVRDLFENAKK 251
Cdd:COG0470    16 RLPHALLLHGPPGIGKTTLAlalardllcenpeggKACGQCHSRLMAAGNHPDLLELNPEEksdqiGIDQIRELGEFLSL 95
                          90
                  ....*....|....*..
gi 1732943972 252 NAPC----LIFIDEIDA 264
Cdd:COG0470    96 TPLEggrkVVIIDEADA 112
PRK11331 PRK11331
5-methylcytosine-specific restriction enzyme subunit McrB; Provisional
193-331 1.04e-03

5-methylcytosine-specific restriction enzyme subunit McrB; Provisional


Pssm-ID: 183088 [Multi-domain]  Cd Length: 459  Bit Score: 41.99  E-value: 1.04e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943972 193 IPKGVLLVGPPGTGKTLLAKACA----GEAG------VPFF-SISGSDFVEMFV--GVGASRVRDLFEN---AKKNAPCL 256
Cdd:PRK11331  193 IKKNIILQGPPGVGKTFVARRLAylltGEKApqrvnmVQFHqSYSYEDFIQGYRpnGVGFRRKDGIFYNfcqQAKEQPEK 272
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943972 257 IFIDEIDAVGRQRGAGLGG------GHDEREQTLNQLLV----EMDGFSANEGIIIIAATNRAD----ILDPALLRPGRF 322
Cdd:PRK11331  273 KYVFIIDEINRANLSKVFGevmmlmEHDKRGENWSVPLTysenDEERFYVPENVYIIGLMNTADrslaVVDYALRRRFSF 352
                         170
                  ....*....|
gi 1732943972 323 -DRQITVDRP 331
Cdd:PRK11331  353 iDIEPGFDTP 362
DnaC COG1484
DNA replication protein DnaC [Replication, recombination and repair];
195-262 1.57e-03

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


Pssm-ID: 441093 [Multi-domain]  Cd Length: 242  Bit Score: 40.53  E-value: 1.57e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1732943972 195 KGVLLVGPPGTGKTLLA-----KACagEAGVP--FFSIsgSDFV-EMFVGVGASRVRDLFENAKKnAPCLIfIDEI 262
Cdd:COG1484   100 ENLILLGPPGTGKTHLAialghEAC--RAGYRvrFTTA--PDLVnELKEARADGRLERLLKRLAK-VDLLI-LDEL 169
NACHT COG5635
Predicted NTPase, NACHT family domain [Signal transduction mechanisms];
174-301 1.97e-03

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


Pssm-ID: 444362 [Multi-domain]  Cd Length: 935  Bit Score: 41.33  E-value: 1.97e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943972 174 VEVVEFLKDPRKFAELGARIPKgVLLVGPPGTGKT---------LLAKACAGEAGVPFF--------SISGSDFVEMFVG 236
Cdd:COG5635   161 LNLLERIESLKRLELLEAKKKR-LLILGEPGSGKTtllrylaleLAERYLDAEDPIPILielrdlaeEASLEDLLAEALE 239
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1732943972 237 VGASRVRDLFENAKKNAPCLIFIDEIDAVGRQrgaglggghDEREQTLNQLLVEMDGFSANEGII 301
Cdd:COG5635   240 KRGGEPEDALERLLRNGRLLLLLDGLDEVPDE---------ADRDEVLNQLRRFLERYPKARVII 295
RecA-like_ClpX cd19497
ATP-dependent Clp protease ATP-binding subunit ClpX; ClpX is a component of the ATP-dependent ...
197-267 2.11e-03

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: 40.28  E-value: 2.11e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943972 197 VLLVGPPGTGKTLLAKACAGEAGVPfFSIS-----------GSDfVEmfvgvgaSRVRDLFENA----KKNAPCLIFIDE 261
Cdd:cd19497    53 ILLIGPTGSGKTLLAQTLAKILDVP-FAIAdattlteagyvGED-VE-------NILLKLLQAAdydvERAQRGIVYIDE 123

                  ....*.
gi 1732943972 262 IDAVGR 267
Cdd:cd19497   124 IDKIAR 129
ruvB TIGR00635
Holliday junction DNA helicase, RuvB subunit; All proteins in this family for which functions ...
197-268 2.39e-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: 40.36  E-value: 2.39e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1732943972 197 VLLVGPPGTGKTLLAKACAGEAGVPFFSISG------SDFVEMFVGVGASRVrdlfenakknapclIFIDEIDAVGRQ 268
Cdd:TIGR00635  33 LLLYGPPGLGKTTLAHIIANEMGVNLKITSGpalekpGDLAAILTNLEEGDV--------------LFIDEIHRLSPA 96
YifB COG0606
Predicted Mg-chelatase, contains ChlI-like and ATPase domains, YifB family [Posttranslational ...
197-212 2.46e-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: 40.79  E-value: 2.46e-03
                          10
                  ....*....|....*.
gi 1732943972 197 VLLVGPPGTGKTLLAK 212
Cdd:COG0606   214 LLMIGPPGSGKTMLAR 229
clpX PRK05342
ATP-dependent Clp protease ATP-binding subunit ClpX;
197-222 3.97e-03

ATP-dependent Clp protease ATP-binding subunit ClpX;


Pssm-ID: 235422 [Multi-domain]  Cd Length: 412  Bit Score: 40.14  E-value: 3.97e-03
                          10        20
                  ....*....|....*....|....*.
gi 1732943972 197 VLLVGPPGTGKTLLAKACAGEAGVPF 222
Cdd:PRK05342  111 ILLIGPTGSGKTLLAQTLARILDVPF 136
ClpX COG1219
ATP-dependent protease Clp, ATPase subunit ClpX [Posttranslational modification, protein ...
197-222 4.20e-03

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


Pssm-ID: 440832 [Multi-domain]  Cd Length: 409  Bit Score: 40.03  E-value: 4.20e-03
                          10        20
                  ....*....|....*....|....*.
gi 1732943972 197 VLLVGPPGTGKTLLAKACAGEAGVPF 222
Cdd:COG1219   112 ILLIGPTGSGKTLLAQTLARILDVPF 137
SR_beta cd04105
Signal recognition particle receptor, beta subunit (SR-beta), together with SR-alpha, forms ...
197-312 5.12e-03

Signal recognition particle receptor, beta subunit (SR-beta), together with SR-alpha, forms the heterodimeric signal recognition particle (SRP); Signal recognition particle receptor, beta subunit (SR-beta). SR-beta and SR-alpha form the heterodimeric signal recognition particle (SRP or SR) receptor that binds SRP to regulate protein translocation across the ER membrane. Nascent polypeptide chains are synthesized with an N-terminal hydrophobic signal sequence that binds SRP54, a component of the SRP. SRP directs targeting of the ribosome-nascent chain complex (RNC) to the ER membrane via interaction with the SR, which is localized to the ER membrane. The RNC is then transferred to the protein-conducting channel, or translocon, which facilitates polypeptide translation across the ER membrane or integration into the ER membrane. SR-beta is found only in eukaryotes; it is believed to control the release of the signal sequence from SRP54 upon binding of the ribosome to the translocon. High expression of SR-beta has been observed in human colon cancer, suggesting it may play a role in the development of this type of cancer.


Pssm-ID: 206691 [Multi-domain]  Cd Length: 202  Bit Score: 38.84  E-value: 5.12e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943972 197 VLLVGPPGTGKT-LLAKACAGEA----------GVPFFSISGSDFVEMFVGV-GASRVRD-LFENAKKNAPCLIFIdeID 263
Cdd:cd04105     3 VLLLGPSDSGKTaLFTKLTTGKVrstvtsiepnVASFYSNSSKGKKLTLVDVpGHEKLRDkLLEYLKASLKAIVFV--VD 80
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 1732943972 264 AVGRQRGAglgggHDEREQTLNQLLVEMdgFSANEGIIIIAAtNRADIL 312
Cdd:cd04105    81 SATFQKNI-----RDVAEFLYDILTDLE--KIKNKIPILIAC-NKQDLF 121
RecA-like_ClpB_Hsp104-like cd19499
Chaperone protein ClpB/Hsp104 subfamily; Bacterial Caseinolytic peptidase B (ClpB) and ...
180-263 5.99e-03

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: 38.31  E-value: 5.99e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943972 180 LKDPRKfaelgariPKGVLL-VGPPGTGKTLLAKACAGE---AGVPFFSISGSDFVEMFVG----------VGASRVRDL 245
Cdd:cd19499    34 LSDPNR--------PIGSFLfLGPTGVGKTELAKALAELlfgDEDNLIRIDMSEYMEKHSVsrligappgyVGYTEGGQL 105
                          90
                  ....*....|....*...
gi 1732943972 246 FENAKKNAPCLIFIDEID 263
Cdd:cd19499   106 TEAVRRKPYSVVLLDEIE 123
RuvB COG2255
Holliday junction resolvasome RuvABC, ATP-dependent DNA helicase subunit RuvB [Replication, ...
197-227 6.22e-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: 39.29  E-value: 6.22e-03
                          10        20        30
                  ....*....|....*....|....*....|.
gi 1732943972 197 VLLVGPPGTGKTLLAKACAGEAGVPFFSISG 227
Cdd:COG2255    57 VLLYGPPGLGKTTLAHIIANEMGVNIRITSG 87
IstB_IS21 pfam01695
IstB-like ATP binding protein; This protein contains an ATP/GTP binding P-loop motif. It is ...
182-232 6.23e-03

IstB-like ATP binding protein; This protein contains an ATP/GTP binding P-loop motif. It is found associated with IS21 family insertion sequences. The function of this protein is unknown, but it may perform a transposase function.


Pssm-ID: 426385 [Multi-domain]  Cd Length: 238  Bit Score: 38.58  E-value: 6.23e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1732943972 182 DPRKFAELGA----RIPKGVLLVGPPGTGKTLLAKACAGEA---GVPFFSISGSDFVE 232
Cdd:pfam01695  76 DQRIVAELASlsfiDRAQNVVLLGPPGVGKTHLAIALGVEAcraGYSVRFTSAADLVN 133
DnaA COG0593
Chromosomal replication initiation ATPase DnaA [Replication, recombination and repair];
197-402 6.30e-03

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


Pssm-ID: 440358 [Multi-domain]  Cd Length: 303  Bit Score: 39.02  E-value: 6.30e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943972 197 VLLVGPPGTGKTLLAKACAGEAGVPFFS-----ISGSDFVEMFvgVGASRVRDLFENAKK--NAPCLIfIDEIdavgrQR 269
Cdd:COG0593    37 LFLYGGVGLGKTHLLHAIGNEALENNPGarvvyLTAEEFTNDF--INAIRNNTIEEFKEKyrSVDVLL-IDDI-----QF 108
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943972 270 GAGlggghDEREQ-----TLNQLLvemdgfsaNEGIIIIAATNRA----DILDPALLRpgRFDRQITVD--RPDVIGREA 338
Cdd:COG0593   109 LAG-----KEATQeeffhTFNALR--------EAGKQIVLTSDRPpkelPGLEERLRS--RLEWGLVVDiqPPDLETRIA 173
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1732943972 339 VL--KVHARNKPLDETVnLKSIAMRTPGfSGADLENLLNeaALVA-ARQNKKKID-------ARDIDEATDRVI 402
Cdd:COG0593   174 ILrkKAADRGLELPDEV-LEYLARRIER-NVRELEGALN--RLDAyALLTGRPITlelarevLKDLLRAQKKEI 243
Mg_chelatase pfam01078
Magnesium chelatase, subunit ChlI; Magnesium-chelatase is a three-component enzyme that ...
197-213 6.70e-03

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


Pssm-ID: 426032 [Multi-domain]  Cd Length: 207  Bit Score: 38.29  E-value: 6.70e-03
                          10
                  ....*....|....*..
gi 1732943972 197 VLLVGPPGTGKTLLAKA 213
Cdd:pfam01078  25 LLMIGPPGSGKTMLAKR 41
 
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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