NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|1088032500|gb|OGZ02941|]
View 

MAG: cell division protein FtsH [Candidatus Liptonbacteria bacterium RIFCSPLOWO2_12_FULL_60_15]

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

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

Name Accession Description Interval E-value
HflB COG0465
ATP-dependent Zn proteases [Posttranslational modification, protein turnover, chaperones];
12-601 0e+00

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


:

Pssm-ID: 440233 [Multi-domain]  Cd Length: 583  Bit Score: 915.96  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1088032500  12 VLLAFALLFSFLVENVASSPSLTLNDLARKVSAGEVAKIVIAGDDLEVTLKDGTTA--SAKKEAEAGLSETFKNYGVSqe 89
Cdd:COG0465     1 IALLLVLLFNLFSSSSSSVKEISYSEFLQLVEAGKVKSVTIQGDRITGTLKDGTKTrfTTYRVNDPELVDLLEEKGVE-- 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1088032500  90 alaatsVEVKEESGLRFWASILIpTLVPLLIIGGIFFFMFRQAKSGVNQAFTFGRANLRLSGGEKDRATFKDVAGLKEAK 169
Cdd:COG0465    79 ------VTAKPPEESSWLLSLLI-SLLPILLLIGLWIFFMRRMQGGGGGAMSFGKSKAKLYDEDKPKVTFDDVAGVDEAK 151
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1088032500 170 QELEEVVDFLKNPKKFLDIGARIPRGVLLMGAPGTGKTLLARAVAGEAGVPFFHISASEFVEMFVGVGASRTRDAFQTAK 249
Cdd:COG0465   152 EELQEIVDFLKDPEKFTRLGAKIPKGVLLVGPPGTGKTLLAKAVAGEAGVPFFSISGSDFVEMFVGVGASRVRDLFEQAK 231
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1088032500 250 RAAPSILFIDEIDAVGRERGAGLGGGHDEREQTLNQILVEMDGFDRDTKVIVLAATNRPDILDSALLRPGRFDRRVVLDL 329
Cdd:COG0465   232 KNAPCIIFIDEIDAVGRQRGAGLGGGHDEREQTLNQLLVEMDGFEGNEGVIVIAATNRPDVLDPALLRPGRFDRQVVVDL 311
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1088032500 330 PDINDREAILAIHARGKKLDASVDMRRIAVRTPGFSGADLANLVNEAAISSARKNKKMVGQEELLDSIEKVLLGPERKGR 409
Cdd:COG0465   312 PDVKGREAILKVHARKKPLAPDVDLEVIARRTPGFSGADLANLVNEAALLAARRNKKAVTMEDFEEAIDRVIAGPERKSR 391
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1088032500 410 AISDKEKKITAYHEAGHALVTASLKDADPVQKVSIVSRGRAGGYTLKLPLEEQRLKTKSQFLADLAVMLGGYVSEKLVFG 489
Cdd:COG0465   392 VISEKEKKITAYHEAGHALVAALLPGADPVHKVTIIPRGRALGYTMQLPEEDRYLYTKEELLDRIAVLLGGRAAEELVFG 471
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1088032500 490 DVSTGASNDLEGASELSRNLVVKYGMSEALGPMTFGKSEEMVFLGREIATGKDYSEETASKIDAETRGFIERAHQAAARI 569
Cdd:COG0465   472 EVTTGASNDLERATKIARAMVTEYGMSEKLGPVAYGESEGEVFLGRDIGQSRNYSEETAREIDEEVRRIIDEAYERAKEI 551
                         570       580       590
                  ....*....|....*....|....*....|..
gi 1088032500 570 LKTHRRALDAIAKTLIEKETLEHEDFYALLKG 601
Cdd:COG0465   552 LTENRDKLDALAEALLEKETLDGEELEEILAG 583
 
Name Accession Description Interval E-value
HflB COG0465
ATP-dependent Zn proteases [Posttranslational modification, protein turnover, chaperones];
12-601 0e+00

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


Pssm-ID: 440233 [Multi-domain]  Cd Length: 583  Bit Score: 915.96  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1088032500  12 VLLAFALLFSFLVENVASSPSLTLNDLARKVSAGEVAKIVIAGDDLEVTLKDGTTA--SAKKEAEAGLSETFKNYGVSqe 89
Cdd:COG0465     1 IALLLVLLFNLFSSSSSSVKEISYSEFLQLVEAGKVKSVTIQGDRITGTLKDGTKTrfTTYRVNDPELVDLLEEKGVE-- 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1088032500  90 alaatsVEVKEESGLRFWASILIpTLVPLLIIGGIFFFMFRQAKSGVNQAFTFGRANLRLSGGEKDRATFKDVAGLKEAK 169
Cdd:COG0465    79 ------VTAKPPEESSWLLSLLI-SLLPILLLIGLWIFFMRRMQGGGGGAMSFGKSKAKLYDEDKPKVTFDDVAGVDEAK 151
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1088032500 170 QELEEVVDFLKNPKKFLDIGARIPRGVLLMGAPGTGKTLLARAVAGEAGVPFFHISASEFVEMFVGVGASRTRDAFQTAK 249
Cdd:COG0465   152 EELQEIVDFLKDPEKFTRLGAKIPKGVLLVGPPGTGKTLLAKAVAGEAGVPFFSISGSDFVEMFVGVGASRVRDLFEQAK 231
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1088032500 250 RAAPSILFIDEIDAVGRERGAGLGGGHDEREQTLNQILVEMDGFDRDTKVIVLAATNRPDILDSALLRPGRFDRRVVLDL 329
Cdd:COG0465   232 KNAPCIIFIDEIDAVGRQRGAGLGGGHDEREQTLNQLLVEMDGFEGNEGVIVIAATNRPDVLDPALLRPGRFDRQVVVDL 311
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1088032500 330 PDINDREAILAIHARGKKLDASVDMRRIAVRTPGFSGADLANLVNEAAISSARKNKKMVGQEELLDSIEKVLLGPERKGR 409
Cdd:COG0465   312 PDVKGREAILKVHARKKPLAPDVDLEVIARRTPGFSGADLANLVNEAALLAARRNKKAVTMEDFEEAIDRVIAGPERKSR 391
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1088032500 410 AISDKEKKITAYHEAGHALVTASLKDADPVQKVSIVSRGRAGGYTLKLPLEEQRLKTKSQFLADLAVMLGGYVSEKLVFG 489
Cdd:COG0465   392 VISEKEKKITAYHEAGHALVAALLPGADPVHKVTIIPRGRALGYTMQLPEEDRYLYTKEELLDRIAVLLGGRAAEELVFG 471
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1088032500 490 DVSTGASNDLEGASELSRNLVVKYGMSEALGPMTFGKSEEMVFLGREIATGKDYSEETASKIDAETRGFIERAHQAAARI 569
Cdd:COG0465   472 EVTTGASNDLERATKIARAMVTEYGMSEKLGPVAYGESEGEVFLGRDIGQSRNYSEETAREIDEEVRRIIDEAYERAKEI 551
                         570       580       590
                  ....*....|....*....|....*....|..
gi 1088032500 570 LKTHRRALDAIAKTLIEKETLEHEDFYALLKG 601
Cdd:COG0465   552 LTENRDKLDALAEALLEKETLDGEELEEILAG 583
FtsH_fam TIGR01241
ATP-dependent metalloprotease FtsH; HflB(FtsH) is a pleiotropic protein required for correct ...
106-600 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: 751.04  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1088032500 106 FWASILIPTLVPLLIIGGIFFFMFRQAKSGVNQAFTFGRANLRLSGGEKDRATFKDVAGLKEAKQELEEVVDFLKNPKKF 185
Cdd:TIGR01241   1 SLLGFLFSLLPPILLLVGVWFFFRRQMQGGGGRAFSFGKSKAKLLNEEKPKVTFKDVAGIDEAKEELMEIVDFLKNPSKF 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1088032500 186 LDIGARIPRGVLLMGAPGTGKTLLARAVAGEAGVPFFHISASEFVEMFVGVGASRTRDAFQTAKRAAPSILFIDEIDAVG 265
Cdd:TIGR01241  81 TKLGAKIPKGVLLVGPPGTGKTLLAKAVAGEAGVPFFSISGSDFVEMFVGVGASRVRDLFEQAKKNAPCIIFIDEIDAVG 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1088032500 266 RERGAGLGGGHDEREQTLNQILVEMDGFDRDTKVIVLAATNRPDILDSALLRPGRFDRRVVLDLPDINDREAILAIHARG 345
Cdd:TIGR01241 161 RQRGAGLGGGNDEREQTLNQLLVEMDGFGTNTGVIVIAATNRPDVLDPALLRPGRFDRQVVVDLPDIKGREEILKVHAKN 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1088032500 346 KKLDASVDMRRIAVRTPGFSGADLANLVNEAAISSARKNKKMVGQEELLDSIEKVLLGPERKGRAISDKEKKITAYHEAG 425
Cdd:TIGR01241 241 KKLAPDVDLKAVARRTPGFSGADLANLLNEAALLAARKNKTEITMNDIEEAIDRVIAGPEKKSRVISEKEKKLVAYHEAG 320
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1088032500 426 HALVTASLKDADPVQKVSIVSRGRAGGYTLKLPLEEQRLKTKSQFLADLAVMLGGYVSEKLVFGDVSTGASNDLEGASEL 505
Cdd:TIGR01241 321 HALVGLLLKDADPVHKVTIIPRGQALGYTQFLPEEDKYLYTKSQLLAQIAVLLGGRAAEEIIFGEVTTGASNDIKQATNI 400
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1088032500 506 SRNLVVKYGMSEALGPMTFGKSEEMVFLGREIATGKDYSEETASKIDAETRGFIERAHQAAARILKTHRRALDAIAKTLI 585
Cdd:TIGR01241 401 ARAMVTEWGMSDKLGPVAYGSDGGDVFLGRGFAKAKEYSEETAREIDEEVKRIIEEAYKRAKQILTENRDELELLAKALL 480
                         490
                  ....*....|....*
gi 1088032500 586 EKETLEHEDFYALLK 600
Cdd:TIGR01241 481 EKETITREEIKELLA 495
ftsH CHL00176
cell division protein; Validated
98-602 0e+00

cell division protein; Validated


Pssm-ID: 214386 [Multi-domain]  Cd Length: 638  Bit Score: 583.55  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1088032500  98 VKEESGLRFWASILiptLVPLLIIGGIFFFMFR--QAKSGVNQAF-TFGRANLRLSGGEKDRATFKDVAGLKEAKQELEE 174
Cdd:CHL00176  121 PVLKSNIVTILSNL---LLPLILIGVLWFFFQRssNFKGGPGQNLmNFGKSKARFQMEADTGITFRDIAGIEEAKEEFEE 197
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1088032500 175 VVDFLKNPKKFLDIGARIPRGVLLMGAPGTGKTLLARAVAGEAGVPFFHISASEFVEMFVGVGASRTRDAFQTAKRAAPS 254
Cdd:CHL00176  198 VVSFLKKPERFTAVGAKIPKGVLLVGPPGTGKTLLAKAIAGEAEVPFFSISGSEFVEMFVGVGAARVRDLFKKAKENSPC 277
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1088032500 255 ILFIDEIDAVGRERGAGLGGGHDEREQTLNQILVEMDGFDRDTKVIVLAATNRPDILDSALLRPGRFDRRVVLDLPDIND 334
Cdd:CHL00176  278 IVFIDEIDAVGRQRGAGIGGGNDEREQTLNQLLTEMDGFKGNKGVIVIAATNRVDILDAALLRPGRFDRQITVSLPDREG 357
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1088032500 335 REAILAIHARGKKLDASVDMRRIAVRTPGFSGADLANLVNEAAISSARKNKKMVGQEELLDSIEKVLLGPErkGRAISD- 413
Cdd:CHL00176  358 RLDILKVHARNKKLSPDVSLELIARRTPGFSGADLANLLNEAAILTARRKKATITMKEIDTAIDRVIAGLE--GTPLEDs 435
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1088032500 414 KEKKITAYHEAGHALVTASLKDADPVQKVSIVSRGRAGGYTLKLPLEEQRLKTKSQFLADLAVMLGGYVSEKLVFGD--V 491
Cdd:CHL00176  436 KNKRLIAYHEVGHAIVGTLLPNHDPVQKVTLIPRGQAKGLTWFTPEEDQSLVSRSQILARIVGALGGRAAEEVVFGSteV 515
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1088032500 492 STGASNDLEGASELSRNLVVKYGMSeALGPMTF-GKSEEMVFLGREIATGKDYSEETASKIDAETRGFIERAHQAAARIL 570
Cdd:CHL00176  516 TTGASNDLQQVTNLARQMVTRFGMS-SIGPISLeSNNSTDPFLGRFMQRNSEYSEEIADKIDMEVRSILHTCYQYAYQIL 594
                         490       500       510
                  ....*....|....*....|....*....|..
gi 1088032500 571 KTHRRALDAIAKTLIEKETLEHEDFYALLKGF 602
Cdd:CHL00176  595 KDNRVLIDLLVELLLQKETIDGDEFREIVNSY 626
RecA-like_FtsH cd19501
ATP-dependent zinc metalloprotease FtsH; FtsH ATPase is a processive, ATP-dependent zinc ...
158-326 2.25e-113

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: 335.74  E-value: 2.25e-113
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1088032500 158 TFKDVAGLKEAKQELEEVVDFLKNPKKFLDIGARIPRGVLLMGAPGTGKTLLARAVAGEAGVPFFHISASEFVEMFVGVG 237
Cdd:cd19501     2 TFKDVAGCEEAKEELKEVVEFLKNPEKFTKLGAKIPKGVLLVGPPGTGKTLLAKAVAGEAGVPFFSISGSDFVEMFVGVG 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1088032500 238 ASRTRDAFQTAKRAAPSILFIDEIDAVGRERGAGLGGGHDEREQTLNQILVEMDGFDRDTKVIVLAATNRPDILDSALLR 317
Cdd:cd19501    82 ASRVRDLFEQAKKNAPCIVFIDEIDAVGRKRGAGLGGGHDEREQTLNQLLVEMDGFESNTGVIVIAATNRPDVLDPALLR 161

                  ....*....
gi 1088032500 318 PGRFDRRVV 326
Cdd:cd19501   162 PGRFDRQVY 170
Peptidase_M41 pfam01434
Peptidase family M41;
409-598 3.14e-81

Peptidase family M41;


Pssm-ID: 460210 [Multi-domain]  Cd Length: 190  Bit Score: 253.68  E-value: 3.14e-81
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1088032500 409 RAISDKEKKITAYHEAGHALVTASLKDADPVQKVSIVSRGRAGGYTLKLPLEEQRLKTKSQFLADLAVMLGGYVSEKLVF 488
Cdd:pfam01434   1 RVISEEEKKIVAYHEAGHALVGLLLPGADPVHKVTIIPRGQALGYTQFLPEEDKLLYTKEQLLARIAVLLGGRAAEELIF 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1088032500 489 GDVSTGASNDLEGASELSRNLVVKYGMSEALGPMTFGKSEEMVFLGREIATGKDYSEETASKIDAETRGFIERAHQAAAR 568
Cdd:pfam01434  81 GEVTTGASNDLEKATKIARQMVTEFGMSDKLGPVSLEESDGNVFLGRGMGKRKPYSEETADIIDEEVKRLLEEAYERAKE 160
                         170       180       190
                  ....*....|....*....|....*....|
gi 1088032500 569 ILKTHRRALDAIAKTLIEKETLEHEDFYAL 598
Cdd:pfam01434 161 ILTEHRDELEALAEALLEKETLDAEEIREL 190
AAA smart00382
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ...
193-331 4.60e-16

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: 75.49  E-value: 4.60e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1088032500  193 PRGVLLMGAPGTGKTLLARAVAGEA---GVPFFHISASEFVE--------------MFVGVGASRTRDAFQTAKRAAPSI 255
Cdd:smart00382   2 GEVILIVGPPGSGKTTLARALARELgppGGGVIYIDGEDILEevldqllliivggkKASGSGELRLRLALALARKLKPDV 81
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1088032500  256 LFIDEIDAVGRERGaglggghdEREQTLNQILVEMDGFDRDTKVIVLAATNRPDILDSALLRPgRFDRRVVLDLPD 331
Cdd:smart00382  82 LILDEITSLLDAEQ--------EALLLLLEELRLLLLLKSEKNLTVILTTNDEKDLGPALLRR-RFDRRIVLLLIL 148
 
Name Accession Description Interval E-value
HflB COG0465
ATP-dependent Zn proteases [Posttranslational modification, protein turnover, chaperones];
12-601 0e+00

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


Pssm-ID: 440233 [Multi-domain]  Cd Length: 583  Bit Score: 915.96  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1088032500  12 VLLAFALLFSFLVENVASSPSLTLNDLARKVSAGEVAKIVIAGDDLEVTLKDGTTA--SAKKEAEAGLSETFKNYGVSqe 89
Cdd:COG0465     1 IALLLVLLFNLFSSSSSSVKEISYSEFLQLVEAGKVKSVTIQGDRITGTLKDGTKTrfTTYRVNDPELVDLLEEKGVE-- 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1088032500  90 alaatsVEVKEESGLRFWASILIpTLVPLLIIGGIFFFMFRQAKSGVNQAFTFGRANLRLSGGEKDRATFKDVAGLKEAK 169
Cdd:COG0465    79 ------VTAKPPEESSWLLSLLI-SLLPILLLIGLWIFFMRRMQGGGGGAMSFGKSKAKLYDEDKPKVTFDDVAGVDEAK 151
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1088032500 170 QELEEVVDFLKNPKKFLDIGARIPRGVLLMGAPGTGKTLLARAVAGEAGVPFFHISASEFVEMFVGVGASRTRDAFQTAK 249
Cdd:COG0465   152 EELQEIVDFLKDPEKFTRLGAKIPKGVLLVGPPGTGKTLLAKAVAGEAGVPFFSISGSDFVEMFVGVGASRVRDLFEQAK 231
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1088032500 250 RAAPSILFIDEIDAVGRERGAGLGGGHDEREQTLNQILVEMDGFDRDTKVIVLAATNRPDILDSALLRPGRFDRRVVLDL 329
Cdd:COG0465   232 KNAPCIIFIDEIDAVGRQRGAGLGGGHDEREQTLNQLLVEMDGFEGNEGVIVIAATNRPDVLDPALLRPGRFDRQVVVDL 311
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1088032500 330 PDINDREAILAIHARGKKLDASVDMRRIAVRTPGFSGADLANLVNEAAISSARKNKKMVGQEELLDSIEKVLLGPERKGR 409
Cdd:COG0465   312 PDVKGREAILKVHARKKPLAPDVDLEVIARRTPGFSGADLANLVNEAALLAARRNKKAVTMEDFEEAIDRVIAGPERKSR 391
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1088032500 410 AISDKEKKITAYHEAGHALVTASLKDADPVQKVSIVSRGRAGGYTLKLPLEEQRLKTKSQFLADLAVMLGGYVSEKLVFG 489
Cdd:COG0465   392 VISEKEKKITAYHEAGHALVAALLPGADPVHKVTIIPRGRALGYTMQLPEEDRYLYTKEELLDRIAVLLGGRAAEELVFG 471
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1088032500 490 DVSTGASNDLEGASELSRNLVVKYGMSEALGPMTFGKSEEMVFLGREIATGKDYSEETASKIDAETRGFIERAHQAAARI 569
Cdd:COG0465   472 EVTTGASNDLERATKIARAMVTEYGMSEKLGPVAYGESEGEVFLGRDIGQSRNYSEETAREIDEEVRRIIDEAYERAKEI 551
                         570       580       590
                  ....*....|....*....|....*....|..
gi 1088032500 570 LKTHRRALDAIAKTLIEKETLEHEDFYALLKG 601
Cdd:COG0465   552 LTENRDKLDALAEALLEKETLDGEELEEILAG 583
FtsH_fam TIGR01241
ATP-dependent metalloprotease FtsH; HflB(FtsH) is a pleiotropic protein required for correct ...
106-600 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: 751.04  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1088032500 106 FWASILIPTLVPLLIIGGIFFFMFRQAKSGVNQAFTFGRANLRLSGGEKDRATFKDVAGLKEAKQELEEVVDFLKNPKKF 185
Cdd:TIGR01241   1 SLLGFLFSLLPPILLLVGVWFFFRRQMQGGGGRAFSFGKSKAKLLNEEKPKVTFKDVAGIDEAKEELMEIVDFLKNPSKF 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1088032500 186 LDIGARIPRGVLLMGAPGTGKTLLARAVAGEAGVPFFHISASEFVEMFVGVGASRTRDAFQTAKRAAPSILFIDEIDAVG 265
Cdd:TIGR01241  81 TKLGAKIPKGVLLVGPPGTGKTLLAKAVAGEAGVPFFSISGSDFVEMFVGVGASRVRDLFEQAKKNAPCIIFIDEIDAVG 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1088032500 266 RERGAGLGGGHDEREQTLNQILVEMDGFDRDTKVIVLAATNRPDILDSALLRPGRFDRRVVLDLPDINDREAILAIHARG 345
Cdd:TIGR01241 161 RQRGAGLGGGNDEREQTLNQLLVEMDGFGTNTGVIVIAATNRPDVLDPALLRPGRFDRQVVVDLPDIKGREEILKVHAKN 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1088032500 346 KKLDASVDMRRIAVRTPGFSGADLANLVNEAAISSARKNKKMVGQEELLDSIEKVLLGPERKGRAISDKEKKITAYHEAG 425
Cdd:TIGR01241 241 KKLAPDVDLKAVARRTPGFSGADLANLLNEAALLAARKNKTEITMNDIEEAIDRVIAGPEKKSRVISEKEKKLVAYHEAG 320
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1088032500 426 HALVTASLKDADPVQKVSIVSRGRAGGYTLKLPLEEQRLKTKSQFLADLAVMLGGYVSEKLVFGDVSTGASNDLEGASEL 505
Cdd:TIGR01241 321 HALVGLLLKDADPVHKVTIIPRGQALGYTQFLPEEDKYLYTKSQLLAQIAVLLGGRAAEEIIFGEVTTGASNDIKQATNI 400
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1088032500 506 SRNLVVKYGMSEALGPMTFGKSEEMVFLGREIATGKDYSEETASKIDAETRGFIERAHQAAARILKTHRRALDAIAKTLI 585
Cdd:TIGR01241 401 ARAMVTEWGMSDKLGPVAYGSDGGDVFLGRGFAKAKEYSEETAREIDEEVKRIIEEAYKRAKQILTENRDELELLAKALL 480
                         490
                  ....*....|....*
gi 1088032500 586 EKETLEHEDFYALLK 600
Cdd:TIGR01241 481 EKETITREEIKELLA 495
ftsH CHL00176
cell division protein; Validated
98-602 0e+00

cell division protein; Validated


Pssm-ID: 214386 [Multi-domain]  Cd Length: 638  Bit Score: 583.55  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1088032500  98 VKEESGLRFWASILiptLVPLLIIGGIFFFMFR--QAKSGVNQAF-TFGRANLRLSGGEKDRATFKDVAGLKEAKQELEE 174
Cdd:CHL00176  121 PVLKSNIVTILSNL---LLPLILIGVLWFFFQRssNFKGGPGQNLmNFGKSKARFQMEADTGITFRDIAGIEEAKEEFEE 197
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1088032500 175 VVDFLKNPKKFLDIGARIPRGVLLMGAPGTGKTLLARAVAGEAGVPFFHISASEFVEMFVGVGASRTRDAFQTAKRAAPS 254
Cdd:CHL00176  198 VVSFLKKPERFTAVGAKIPKGVLLVGPPGTGKTLLAKAIAGEAEVPFFSISGSEFVEMFVGVGAARVRDLFKKAKENSPC 277
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1088032500 255 ILFIDEIDAVGRERGAGLGGGHDEREQTLNQILVEMDGFDRDTKVIVLAATNRPDILDSALLRPGRFDRRVVLDLPDIND 334
Cdd:CHL00176  278 IVFIDEIDAVGRQRGAGIGGGNDEREQTLNQLLTEMDGFKGNKGVIVIAATNRVDILDAALLRPGRFDRQITVSLPDREG 357
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1088032500 335 REAILAIHARGKKLDASVDMRRIAVRTPGFSGADLANLVNEAAISSARKNKKMVGQEELLDSIEKVLLGPErkGRAISD- 413
Cdd:CHL00176  358 RLDILKVHARNKKLSPDVSLELIARRTPGFSGADLANLLNEAAILTARRKKATITMKEIDTAIDRVIAGLE--GTPLEDs 435
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1088032500 414 KEKKITAYHEAGHALVTASLKDADPVQKVSIVSRGRAGGYTLKLPLEEQRLKTKSQFLADLAVMLGGYVSEKLVFGD--V 491
Cdd:CHL00176  436 KNKRLIAYHEVGHAIVGTLLPNHDPVQKVTLIPRGQAKGLTWFTPEEDQSLVSRSQILARIVGALGGRAAEEVVFGSteV 515
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1088032500 492 STGASNDLEGASELSRNLVVKYGMSeALGPMTF-GKSEEMVFLGREIATGKDYSEETASKIDAETRGFIERAHQAAARIL 570
Cdd:CHL00176  516 TTGASNDLQQVTNLARQMVTRFGMS-SIGPISLeSNNSTDPFLGRFMQRNSEYSEEIADKIDMEVRSILHTCYQYAYQIL 594
                         490       500       510
                  ....*....|....*....|....*....|..
gi 1088032500 571 KTHRRALDAIAKTLIEKETLEHEDFYALLKGF 602
Cdd:CHL00176  595 KDNRVLIDLLVELLLQKETIDGDEFREIVNSY 626
hflB PRK10733
ATP-dependent zinc metalloprotease FtsH;
41-591 0e+00

ATP-dependent zinc metalloprotease FtsH;


Pssm-ID: 182683 [Multi-domain]  Cd Length: 644  Bit Score: 531.15  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1088032500  41 KVSAGEVAKIVIAGDDLEVTLKDGTTASA------KKEAEAGLSETFKNYGvsqealaatsvEVKEESGLrfWASILIPT 114
Cdd:PRK10733   40 EVNQDQVREARINGREINVTKKDSNRYTTyipvndPKLLDNLLTKNVKVVG-----------EPPEEPSL--LASIFISW 106
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1088032500 115 LVPLLIIGGIFFFMFRQAKSGVNQAFTFGRANLRLSGGEKDRATFKDVAGLKEAKQELEEVVDFLKNPKKFLDIGARIPR 194
Cdd:PRK10733  107 FPMLLLIGVWIFFMRQMQGGGGKGAMSFGKSKARMLTEDQIKTTFADVAGCDEAKEEVAELVEYLREPSRFQKLGGKIPK 186
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1088032500 195 GVLLMGAPGTGKTLLARAVAGEAGVPFFHISASEFVEMFVGVGASRTRDAFQTAKRAAPSILFIDEIDAVGRERGAGLGG 274
Cdd:PRK10733  187 GVLMVGPPGTGKTLLAKAIAGEAKVPFFTISGSDFVEMFVGVGASRVRDMFEQAKKAAPCIIFIDEIDAVGRQRGAGLGG 266
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1088032500 275 GHDEREQTLNQILVEMDGFDRDTKVIVLAATNRPDILDSALLRPGRFDRRVVLDLPDINDREAILAIHARGKKLDASVDM 354
Cdd:PRK10733  267 GHDEREQTLNQMLVEMDGFEGNEGIIVIAATNRPDVLDPALLRPGRFDRQVVVGLPDVRGREQILKVHMRRVPLAPDIDA 346
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1088032500 355 RRIAVRTPGFSGADLANLVNEAAISSARKNKKMVGQEELLDSIEKVLLGPERKGRAISDKEKKITAYHEAGHALVTASLK 434
Cdd:PRK10733  347 AIIARGTPGFSGADLANLVNEAALFAARGNKRVVSMVEFEKAKDKIMMGAERRSMVMTEAQKESTAYHEAGHAIIGRLVP 426
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1088032500 435 DADPVQKVSIVSRGRAGGYTLKLPLEEQRLKTKSQFLADLAVMLGGYVSEKLVFG--DVSTGASNDLEGASELSRNLVVK 512
Cdd:PRK10733  427 EHDPVHKVTIIPRGRALGVTFFLPEGDAISASRQKLESQISTLYGGRLAEEIIYGpeHVSTGASNDIKVATNLARNMVTQ 506
                         490       500       510       520       530       540       550
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1088032500 513 YGMSEALGPMTFGKSEEMVFLGREIATGKDYSEETASKIDAETRGFIERAHQAAARILKTHRRALDAIAKTLIEKETLE 591
Cdd:PRK10733  507 WGFSEKLGPLLYAEEEGEVFLGRSVAKAKHMSDETARIIDQEVKALIERNYNRARQLLTDNMDILHAMKDALMKYETID 585
RecA-like_FtsH cd19501
ATP-dependent zinc metalloprotease FtsH; FtsH ATPase is a processive, ATP-dependent zinc ...
158-326 2.25e-113

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: 335.74  E-value: 2.25e-113
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1088032500 158 TFKDVAGLKEAKQELEEVVDFLKNPKKFLDIGARIPRGVLLMGAPGTGKTLLARAVAGEAGVPFFHISASEFVEMFVGVG 237
Cdd:cd19501     2 TFKDVAGCEEAKEELKEVVEFLKNPEKFTKLGAKIPKGVLLVGPPGTGKTLLAKAVAGEAGVPFFSISGSDFVEMFVGVG 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1088032500 238 ASRTRDAFQTAKRAAPSILFIDEIDAVGRERGAGLGGGHDEREQTLNQILVEMDGFDRDTKVIVLAATNRPDILDSALLR 317
Cdd:cd19501    82 ASRVRDLFEQAKKNAPCIVFIDEIDAVGRKRGAGLGGGHDEREQTLNQLLVEMDGFESNTGVIVIAATNRPDVLDPALLR 161

                  ....*....
gi 1088032500 318 PGRFDRRVV 326
Cdd:cd19501   162 PGRFDRQVY 170
RPT1 COG1222
ATP-dependent 26S proteasome regulatory subunit [Posttranslational modification, protein ...
141-409 1.04e-102

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


Pssm-ID: 440835 [Multi-domain]  Cd Length: 326  Bit Score: 314.25  E-value: 1.04e-102
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1088032500 141 TFGRANLRLSGGEKDRATFKDVAGLKEAKQELEEVV-DFLKNPKKFLDIGARIPRGVLLMGAPGTGKTLLARAVAGEAGV 219
Cdd:COG1222    59 RLGTPRGTAVPAESPDVTFDDIGGLDEQIEEIREAVeLPLKNPELFRKYGIEPPKGVLLYGPPGTGKTLLAKAVAGELGA 138
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1088032500 220 PFFHISASEFVEMFVGVGASRTRDAFQTAKRAAPSILFIDEIDAVGRERGAGlgGGHDEREQTLNQILVEMDGFDRDTKV 299
Cdd:COG1222   139 PFIRVRGSELVSKYIGEGARNVREVFELAREKAPSIIFIDEIDAIAARRTDD--GTSGEVQRTVNQLLAELDGFESRGDV 216
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1088032500 300 IVLAATNRPDILDSALLRPGRFDRRVVLDLPDINDREAILAIHARGKKLDASVDMRRIAVRTPGFSGADLANLVNEAAIS 379
Cdd:COG1222   217 LIIAATNRPDLLDPALLRPGRFDRVIEVPLPDEEAREEILKIHLRDMPLADDVDLDKLAKLTEGFSGADLKAIVTEAGMF 296
                         250       260       270
                  ....*....|....*....|....*....|
gi 1088032500 380 SARKNKKMVGQEELLDSIEKVLLGPERKGR 409
Cdd:COG1222   297 AIREGRDTVTMEDLEKAIEKVKKKTETATN 326
PRK03992 PRK03992
proteasome-activating nucleotidase; Provisional
153-407 6.28e-90

proteasome-activating nucleotidase; Provisional


Pssm-ID: 179699 [Multi-domain]  Cd Length: 389  Bit Score: 283.26  E-value: 6.28e-90
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1088032500 153 EKDRATFKDVAGLKEAKQELEEVVDF-LKNPKKFLDIGARIPRGVLLMGAPGTGKTLLARAVAGEAGVPFFHISASEFVE 231
Cdd:PRK03992  124 ESPNVTYEDIGGLEEQIREVREAVELpLKKPELFEEVGIEPPKGVLLYGPPGTGKTLLAKAVAHETNATFIRVVGSELVQ 203
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1088032500 232 MFVGVGASRTRDAFQTAKRAAPSILFIDEIDAVGRERGAGLGGGHDEREQTLNQILVEMDGFDRDTKVIVLAATNRPDIL 311
Cdd:PRK03992  204 KFIGEGARLVRELFELAREKAPSIIFIDEIDAIAAKRTDSGTSGDREVQRTLMQLLAEMDGFDPRGNVKIIAATNRIDIL 283
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1088032500 312 DSALLRPGRFDRRVVLDLPDINDREAILAIHARGKKLDASVDMRRIAVRTPGFSGADLANLVNEAAISSARKNKKMVGQE 391
Cdd:PRK03992  284 DPAILRPGRFDRIIEVPLPDEEGRLEILKIHTRKMNLADDVDLEELAELTEGASGADLKAICTEAGMFAIRDDRTEVTME 363
                         250
                  ....*....|....*.
gi 1088032500 392 ELLDSIEKVLLGPERK 407
Cdd:PRK03992  364 DFLKAIEKVMGKEEKD 379
Peptidase_M41 pfam01434
Peptidase family M41;
409-598 3.14e-81

Peptidase family M41;


Pssm-ID: 460210 [Multi-domain]  Cd Length: 190  Bit Score: 253.68  E-value: 3.14e-81
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1088032500 409 RAISDKEKKITAYHEAGHALVTASLKDADPVQKVSIVSRGRAGGYTLKLPLEEQRLKTKSQFLADLAVMLGGYVSEKLVF 488
Cdd:pfam01434   1 RVISEEEKKIVAYHEAGHALVGLLLPGADPVHKVTIIPRGQALGYTQFLPEEDKLLYTKEQLLARIAVLLGGRAAEELIF 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1088032500 489 GDVSTGASNDLEGASELSRNLVVKYGMSEALGPMTFGKSEEMVFLGREIATGKDYSEETASKIDAETRGFIERAHQAAAR 568
Cdd:pfam01434  81 GEVTTGASNDLEKATKIARQMVTEFGMSDKLGPVSLEESDGNVFLGRGMGKRKPYSEETADIIDEEVKRLLEEAYERAKE 160
                         170       180       190
                  ....*....|....*....|....*....|
gi 1088032500 569 ILKTHRRALDAIAKTLIEKETLEHEDFYAL 598
Cdd:pfam01434 161 ILTEHRDELEALAEALLEKETLDAEEIREL 190
26Sp45 TIGR01242
26S proteasome subunit P45 family; Many proteins may score above the trusted cutoff because an ...
153-401 2.57e-78

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: 252.41  E-value: 2.57e-78
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1088032500 153 EKDRATFKDVAGLKEAKQELEEVVDF-LKNPKKFLDIGARIPRGVLLMGAPGTGKTLLARAVAGEAGVPFFHISASEFVE 231
Cdd:TIGR01242 115 ERPNVSYEDIGGLEEQIREIREAVELpLKHPELFEEVGIEPPKGVLLYGPPGTGKTLLAKAVAHETNATFIRVVGSELVR 194
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1088032500 232 MFVGVGASRTRDAFQTAKRAAPSILFIDEIDAVGRERGAGLGGGHDEREQTLNQILVEMDGFDRDTKVIVLAATNRPDIL 311
Cdd:TIGR01242 195 KYIGEGARLVREIFELAKEKAPSIIFIDEIDAIAAKRTDSGTSGDREVQRTLMQLLAELDGFDPRGNVKVIAATNRPDIL 274
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1088032500 312 DSALLRPGRFDRRVVLDLPDINDREAILAIHARGKKLDASVDMRRIAVRTPGFSGADLANLVNEAAISSARKNKKMVGQE 391
Cdd:TIGR01242 275 DPALLRPGRFDRIIEVPLPDFEGRLEILKIHTRKMKLAEDVDLEAIAKMTEGASGADLKAICTEAGMFAIREERDYVTMD 354
                         250
                  ....*....|
gi 1088032500 392 ELLDSIEKVL 401
Cdd:TIGR01242 355 DFIKAVEKVL 364
SpoVK COG0464
AAA+-type ATPase, SpoVK/Ycf46/Vps4 family [Cell wall/membrane/envelope biogenesis, Cell cycle ...
9-400 1.42e-74

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: 243.66  E-value: 1.42e-74
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1088032500   9 TVAVLLAFALLFSFLVENVASSPSLTLNDLARKVSAGEVAKIVIAGDDLEVTLKDGTTASAKKEAEAGLSETFKNYGVSQ 88
Cdd:COG0464     6 ALAVALALALLLLDDAALRLLLLLLLALAAALLLLLLLLLLLLLALLLVELLLLLLSGALAALLLLALLLLALLALLAAL 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1088032500  89 EALAATSVEVKEESGLRFWASILIPTLVPLLIIGGIFFFMFRQAKSGVNQAFTFGRANLRLSGGEKDRATFKDVAGLKEA 168
Cdd:COG0464    86 LSALELLLLGELLLLLLLLLLLLLLLLDLERALLELLRESAEALALAAPLVTYEDIGGLEEELLELREAILDDLGGLEEV 165
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1088032500 169 KQELEEVVD-FLKNPKKFLDIGARIPRGVLLMGAPGTGKTLLARAVAGEAGVPFFHISASEFVEMFVGVGASRTRDAFQT 247
Cdd:COG0464   166 KEELRELVAlPLKRPELREEYGLPPPRGLLLYGPPGTGKTLLARALAGELGLPLIEVDLSDLVSKYVGETEKNLREVFDK 245
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1088032500 248 AKRAAPSILFIDEIDAVGRERGaGLGGGHDEREqtLNQILVEMDGFDRDtkVIVLAATNRPDILDSALLRpgRFDRRVVL 327
Cdd:COG0464   246 ARGLAPCVLFIDEADALAGKRG-EVGDGVGRRV--VNTLLTEMEELRSD--VVVIAATNRPDLLDPALLR--RFDEIIFF 318
                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1088032500 328 DLPDINDREAILAIHARGKKLDASVDMRRIAVRTPGFSGADLANLVNEAAISSARKNKKMVGQEELLDSIEKV 400
Cdd:COG0464   319 PLPDAEERLEIFRIHLRKRPLDEDVDLEELAEATEGLSGADIRNVVRRAALQALRLGREPVTTEDLLEALERE 391
CDC48 TIGR01243
AAA family ATPase, CDC48 subfamily; This subfamily of the AAA family ATPases includes two ...
159-418 8.36e-64

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: 223.63  E-value: 8.36e-64
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1088032500 159 FKDVAGLKEAKQELEEVVDF-LKNPKKFLDIGARIPRGVLLMGAPGTGKTLLARAVAGEAGVPFFHISASEFVEMFVGVG 237
Cdd:TIGR01243 452 WSDIGGLEEVKQELREAVEWpLKHPEIFEKMGIRPPKGVLLFGPPGTGKTLLAKAVATESGANFIAVRGPEILSKWVGES 531
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1088032500 238 ASRTRDAFQTAKRAAPSILFIDEIDAVGRERGAGLGGGHDEReqTLNQILVEMDGFDRDTKVIVLAATNRPDILDSALLR 317
Cdd:TIGR01243 532 EKAIREIFRKARQAAPAIIFFDEIDAIAPARGARFDTSVTDR--IVNQLLTEMDGIQELSNVVVIAATNRPDILDPALLR 609
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1088032500 318 PGRFDRRVVLDLPDINDREAILAIHARGKKLDASVDMRRIAVRTPGFSGADLANLVNEAAISSARKNKKMVGQEELLDSI 397
Cdd:TIGR01243 610 PGRFDRLILVPPPDEEARKEIFKIHTRSMPLAEDVDLEELAEMTEGYTGADIEAVCREAAMAALRESIGSPAKEKLEVGE 689
                         250       260
                  ....*....|....*....|.
gi 1088032500 398 EKVLLGPERKGRAISDKEKKI 418
Cdd:TIGR01243 690 EEFLKDLKVEMRHFLEALKKV 710
RecA-like_PAN_like cd19502
proteasome activating nucleotidase PAN and related proteasome subunits; This subfamily ...
158-325 1.46e-63

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: 206.80  E-value: 1.46e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1088032500 158 TFKDVAGLKEAKQELEEVVDF-LKNPKKFLDIGARIPRGVLLMGAPGTGKTLLARAVAGEAGVPFFHISASEFVEMFVGV 236
Cdd:cd19502     1 TYEDIGGLDEQIREIREVVELpLKHPELFEELGIEPPKGVLLYGPPGTGKTLLAKAVANHTDATFIRVVGSELVQKYIGE 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1088032500 237 GASRTRDAFQTAKRAAPSILFIDEIDAVGRERGAGLGGGHDEREQTLNQILVEMDGFDRDTKVIVLAATNRPDILDSALL 316
Cdd:cd19502    81 GARLVRELFEMAREKAPSIIFIDEIDAIGAKRFDSGTGGDREVQRTMLELLNQLDGFDPRGNIKVIMATNRPDILDPALL 160

                  ....*....
gi 1088032500 317 RPGRFDRRV 325
Cdd:cd19502   161 RPGRFDRKI 169
RecA-like_protease cd19481
proteases similar to RecA; RecA-like NTPases. This family includes the NTP binding domain of ...
168-325 1.49e-57

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: 190.57  E-value: 1.49e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1088032500 168 AKQELEEVVDFLKNPKKFLDIGARIPRGVLLMGAPGTGKTLLARAVAGEAGVPFFHISASEFVEMFVGVGASRTRDAFQT 247
Cdd:cd19481     1 LKASLREAVEAPRRGSRLRRYGLGLPKGILLYGPPGTGKTLLAKALAGELGLPLIVVKLSSLLSKYVGESEKNLRKIFER 80
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1088032500 248 AKRAAPSILFIDEIDAVGRERGAglGGGHDEREQTLNQILVEMDGFDRDTKVIVLAATNRPDILDSALLRPGRFDRRV 325
Cdd:cd19481    81 ARRLAPCILFIDEIDAIGRKRDS--SGESGELRRVLNQLLTELDGVNSRSKVLVIAATNRPDLLDPALLRPGRFDEVI 156
PTZ00454 PTZ00454
26S protease regulatory subunit 6B-like protein; Provisional
149-393 3.38e-57

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


Pssm-ID: 240423 [Multi-domain]  Cd Length: 398  Bit Score: 197.68  E-value: 3.38e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1088032500 149 LSGGEKDRATFKDVAGLKEAKQELEEVVDF-LKNPKKFLDIGARIPRGVLLMGAPGTGKTLLARAVAGEAGVPFFHISAS 227
Cdd:PTZ00454  134 LQMSEKPDVTYSDIGGLDIQKQEIREAVELpLTCPELYEQIGIDPPRGVLLYGPPGTGKTMLAKAVAHHTTATFIRVVGS 213
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1088032500 228 EFVEMFVGVGASRTRDAFQTAKRAAPSILFIDEIDAVGRERGAGLGGGHDEREQTLNQILVEMDGFDRDTKVIVLAATNR 307
Cdd:PTZ00454  214 EFVQKYLGEGPRMVRDVFRLARENAPSIIFIDEVDSIATKRFDAQTGADREVQRILLELLNQMDGFDQTTNVKVIMATNR 293
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1088032500 308 PDILDSALLRPGRFDRRVVLDLPDINDREAILAIHARGKKLDASVDMRRIAVRTPGFSGADLANLVNEAAISSARKNKKM 387
Cdd:PTZ00454  294 ADTLDPALLRPGRLDRKIEFPLPDRRQKRLIFQTITSKMNLSEEVDLEDFVSRPEKISAADIAAICQEAGMQAVRKNRYV 373

                  ....*.
gi 1088032500 388 VGQEEL 393
Cdd:PTZ00454  374 ILPKDF 379
COG1223 COG1223
Predicted ATPase, AAA+ superfamily [General function prediction only];
159-417 3.68e-56

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


Pssm-ID: 440836 [Multi-domain]  Cd Length: 246  Bit Score: 190.09  E-value: 3.68e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1088032500 159 FKDVAGLKEAKQELEEVVDFLKNPKKFLDIGARIPRGVLLMGAPGTGKTLLARAVAGEAGVPFFHISASEFVEMFVGVGA 238
Cdd:COG1223     1 LDDVVGQEEAKKKLKLIIKELRRRENLRKFGLWPPRKILFYGPPGTGKTMLAEALAGELKLPLLTVRLDSLIGSYLGETA 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1088032500 239 SRTRDAFQTAKRaAPSILFIDEIDAVGRERGAglGGGHDEREQTLNQILVEMDGFDRDtkVIVLAATNRPDILDSALLRp 318
Cdd:COG1223    81 RNLRKLFDFARR-APCVIFFDEFDAIAKDRGD--QNDVGEVKRVVNALLQELDGLPSG--SVVIAATNHPELLDSALWR- 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1088032500 319 gRFDRRVVLDLPDINDREAILAIHARGKKLDASVDMRRIAVRTPGFSGADLANLVNEAAISSARKNKKMVGQEELLDSIE 398
Cdd:COG1223   155 -RFDEVIEFPLPDKEERKEILELNLKKFPLPFELDLKKLAKKLEGLSGADIEKVLKTALKKAILEDREKVTKEDLEEALK 233
                         250
                  ....*....|....*....
gi 1088032500 399 kvllgpERKGRAISDKEKK 417
Cdd:COG1223   234 ------QRKERKKEPKKEG 246
PTZ00361 PTZ00361
26 proteosome regulatory subunit 4-like protein; Provisional
158-401 5.97e-56

26 proteosome regulatory subunit 4-like protein; Provisional


Pssm-ID: 185575 [Multi-domain]  Cd Length: 438  Bit Score: 195.37  E-value: 5.97e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1088032500 158 TFKDVAGLKEAKQELEEVVDF-LKNPKKFLDIGARIPRGVLLMGAPGTGKTLLARAVAGEAGVPFFHISASEFVEMFVGV 236
Cdd:PTZ00361  181 SYADIGGLEQQIQEIKEAVELpLTHPELYDDIGIKPPKGVILYGPPGTGKTLLAKAVANETSATFLRVVGSELIQKYLGD 260
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1088032500 237 GASRTRDAFQTAKRAAPSILFIDEIDAVGRERGAGLGGGHDEREQTLNQILVEMDGFDRDTKVIVLAATNRPDILDSALL 316
Cdd:PTZ00361  261 GPKLVRELFRVAEENAPSIVFIDEIDAIGTKRYDATSGGEKEIQRTMLELLNQLDGFDSRGDVKVIMATNRIESLDPALI 340
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1088032500 317 RPGRFDRRVVLDLPDINDREAILAIHARGKKLDASVDMRRIAVRTPGFSGADLANLVNEAAISSARKNKKMVGQEELLDS 396
Cdd:PTZ00361  341 RPGRIDRKIEFPNPDEKTKRRIFEIHTSKMTLAEDVDLEEFIMAKDELSGADIKAICTEAGLLALRERRMKVTQADFRKA 420

                  ....*
gi 1088032500 397 IEKVL 401
Cdd:PTZ00361  421 KEKVL 425
CDC48 TIGR01243
AAA family ATPase, CDC48 subfamily; This subfamily of the AAA family ATPases includes two ...
158-383 1.12e-55

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: 200.90  E-value: 1.12e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1088032500 158 TFKDVAGLKEAKQELEEVVDF-LKNPKKFLDIGARIPRGVLLMGAPGTGKTLLARAVAGEAGVPFFHISASEFVEMFVGV 236
Cdd:TIGR01243 176 TYEDIGGLKEAKEKIREMVELpMKHPELFEHLGIEPPKGVLLYGPPGTGKTLLAKAVANEAGAYFISINGPEIMSKYYGE 255
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1088032500 237 GASRTRDAFQTAKRAAPSILFIDEIDAVGRERGAGLGgghDEREQTLNQILVEMDGFDRDTKVIVLAATNRPDILDSALL 316
Cdd:TIGR01243 256 SEERLREIFKEAEENAPSIIFIDEIDAIAPKREEVTG---EVEKRVVAQLLTLMDGLKGRGRVIVIGATNRPDALDPALR 332
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1088032500 317 RPGRFDRRVVLDLPDINDREAILAIHARGKKLDASVDMRRIAVRTPGFSGADLANLVNEAAISSARK 383
Cdd:TIGR01243 333 RPGRFDREIVIRVPDKRARKEILKVHTRNMPLAEDVDLDKLAEVTHGFVGADLAALAKEAAMAALRR 399
RecA-like_CDC48_r2-like cd19511
second of two ATPase domains of CDC48/p97, PEX1 and -6, VAT and NVL, and similar ATPase ...
168-325 1.63e-54

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: 182.48  E-value: 1.63e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1088032500 168 AKQELEEVVDF-LKNPKKFLDIGARIPRGVLLMGAPGTGKTLLARAVAGEAGVPFFHISASEFVEMFVGVGASRTRDAFQ 246
Cdd:cd19511     1 VKRELKEAVEWpLKHPDAFKRLGIRPPKGVLLYGPPGCGKTLLAKALASEAGLNFISVKGPELFSKYVGESERAVREIFQ 80
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1088032500 247 TAKRAAPSILFIDEIDAVGRERGAGLGGGHDEReqTLNQILVEMDGFDRDTKVIVLAATNRPDILDSALLRPGRFDRRV 325
Cdd:cd19511    81 KARQAAPCIIFFDEIDSLAPRRGQSDSSGVTDR--VVSQLLTELDGIESLKGVVVIAATNRPDMIDPALLRPGRLDKLI 157
RecA-like_CDC48_NLV2_r1-like cd19503
first of two ATPase domains of CDC48 and NLV2, and similar ATPase domains; CDC48 in yeast and ...
161-327 3.96e-54

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: 181.72  E-value: 3.96e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1088032500 161 DVAGLKEAKQELEEVVDF-LKNPKKFLDIGARIPRGVLLMGAPGTGKTLLARAVAGEAGVPFFHISASEFVEMFVGVGAS 239
Cdd:cd19503     1 DIGGLDEQIASLKELIELpLKYPELFRALGLKPPRGVLLHGPPGTGKTLLARAVANEAGANFLSISGPSIVSKYLGESEK 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1088032500 240 RTRDAFQTAKRAAPSILFIDEIDAVGRERGAglggGHDEREQTL-NQILVEMDGFDRDTKVIVLAATNRPDILDSALLRP 318
Cdd:cd19503    81 NLREIFEEARSHAPSIIFIDEIDALAPKREE----DQREVERRVvAQLLTLMDGMSSRGKVVVIAATNRPDAIDPALRRP 156

                  ....*....
gi 1088032500 319 GRFDRRVVL 327
Cdd:cd19503   157 GRFDREVEI 165
RecA-like_CDC48_r2-like cd19528
second of two ATPase domains of CDC48 and similar ATPase domains; CDC48 in yeast and p97 or ...
169-325 7.69e-49

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: 167.30  E-value: 7.69e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1088032500 169 KQELEEVVDF-LKNPKKFLDIGARIPRGVLLMGAPGTGKTLLARAVAGEAGVPFFHISASEFVEMFVGVGASRTRDAFQT 247
Cdd:cd19528     2 KRELQELVQYpVEHPDKFLKFGMTPSKGVLFYGPPGCGKTLLAKAIANECQANFISVKGPELLTMWFGESEANVRDIFDK 81
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1088032500 248 AKRAAPSILFIDEIDAVGRERGAGLGGGHDEREQTLNQILVEMDGFDRDTKVIVLAATNRPDILDSALLRPGRFDRRV 325
Cdd:cd19528    82 ARAAAPCVLFFDELDSIAKARGGNIGDAGGAADRVINQILTEMDGMNTKKNVFIIGATNRPDIIDPAILRPGRLDQLI 159
RecA-like_VCP_r2 cd19529
second of two ATPase domains of Valosin-containing protein-like ATPase (VAT) and similar ...
168-325 1.05e-48

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: 166.90  E-value: 1.05e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1088032500 168 AKQELEEVVDF-LKNPKKFLDIGARIPRGVLLMGAPGTGKTLLARAVAGEAGVPFFHISASEFVEMFVGVGASRTRDAFQ 246
Cdd:cd19529     1 VKQELKEAVEWpLLKPEVFKRLGIRPPKGILLYGPPGTGKTLLAKAVATESNANFISVKGPELLSKWVGESEKAIREIFR 80
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1088032500 247 TAKRAAPSILFIDEIDAVGRERGAGLGGGHDEReqTLNQILVEMDGFDRDTKVIVLAATNRPDILDSALLRPGRFDRRV 325
Cdd:cd19529    81 KARQVAPCVIFFDEIDSIAPRRGTTGDSGVTER--VVNQLLTELDGLEEMNGVVVIAATNRPDIIDPALLRAGRFDRLI 157
AAA pfam00004
ATPase family associated with various cellular activities (AAA); AAA family proteins often ...
196-329 2.69e-48

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: 164.69  E-value: 2.69e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1088032500 196 VLLMGAPGTGKTLLARAVAGEAGVPFFHISASEFVEMFVGVGASRTRDAFQTAKRAAPSILFIDEIDAVGRERGaglGGG 275
Cdd:pfam00004   1 LLLYGPPGTGKTTLAKAVAKELGAPFIEISGSELVSKYVGESEKRLRELFEAAKKLAPCVIFIDEIDALAGSRG---SGG 77
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1088032500 276 HDEREQTLNQILVEMDGFDRDT-KVIVLAATNRPDILDSALLrpGRFDRRVVLDL 329
Cdd:pfam00004  78 DSESRRVVNQLLTELDGFTSSNsKVIVIAATNRPDKLDPALL--GRFDRIIEFPL 130
RecA-like_CDC48_r1-like cd19519
first of two ATPase domains of CDC48 and similar ATPase domains; CDC48 in yeast and p97 or VCP ...
161-327 2.86e-45

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: 157.98  E-value: 2.86e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1088032500 161 DVAGLKEAKQELEEVVDF-LKNPKKFLDIGARIPRGVLLMGAPGTGKTLLARAVAGEAGVPFFHISASEFVEMFVGVGAS 239
Cdd:cd19519     1 DIGGCRKQLAQIREMVELpLRHPELFKAIGIKPPRGILLYGPPGTGKTLIARAVANETGAFFFLINGPEIMSKLAGESES 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1088032500 240 RTRDAFQTAKRAAPSILFIDEIDAVGRERGAglggGHDEREQTL-NQILVEMDGFDRDTKVIVLAATNRPDILDSALLRP 318
Cdd:cd19519    81 NLRKAFEEAEKNAPAIIFIDEIDAIAPKREK----THGEVERRIvSQLLTLMDGLKQRAHVIVMAATNRPNSIDPALRRF 156

                  ....*....
gi 1088032500 319 GRFDRRVVL 327
Cdd:cd19519   157 GRFDREIDI 165
RecA-like_NVL_r2-like cd19530
second of two ATPase domains of NVL (nuclear VCP-like protein) and similar ATPase domains; NVL ...
165-323 2.77e-43

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: 152.26  E-value: 2.77e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1088032500 165 LKEAKQELE-EVVDFLKNPKKFLDIGARIPRGVLLMGAPGTGKTLLARAVAGEAGVPFFHISASEFVEMFVGVGASRTRD 243
Cdd:cd19530     1 LDHVREELTmSILRPIKRPDIYKALGIDLPTGVLLYGPPGCGKTLLAKAVANESGANFISVKGPELLNKYVGESERAVRQ 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1088032500 244 AFQTAKRAAPSILFIDEIDAVGRERGAGLGGGhdeREQTLNQILVEMDGFDRDTKVIVLAATNRPDILDSALLRPGRFDR 323
Cdd:cd19530    81 VFQRARASAPCVIFFDEVDALVPKRGDGGSWA---SERVVNQLLTEMDGLEERSNVFVIAATNRPDIIDPAMLRPGRLDK 157
RecA-like_NVL_r1-like cd19518
first of two ATPase domains of NVL (nuclear VCP-like protein) and similar ATPase domains; NVL ...
161-327 3.06e-43

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: 152.56  E-value: 3.06e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1088032500 161 DVAGLKEAKQELEEVVDFLKNPKK-FLDIGARIPRGVLLMGAPGTGKTLLARAVAGEAGVPFFHISASEFVEMFVGVGAS 239
Cdd:cd19518     1 DIGGMDSTLKELCELLIHPILPPEyFQHLGVEPPRGVLLHGPPGCGKTMLANAIAGELKVPFLKISATEIVSGVSGESEE 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1088032500 240 RTRDAFQTAKRAAPSILFIDEIDAVGRERGaglGGGHDEREQTLNQILVEMDGFD---RDTK-VIVLAATNRPDILDSAL 315
Cdd:cd19518    81 KIRELFDQAISNAPCIVFIDEIDAITPKRE---SAQREMERRIVSQLLTCMDELNnekTAGGpVLVIGATNRPDSLDPAL 157
                         170
                  ....*....|..
gi 1088032500 316 LRPGRFDRRVVL 327
Cdd:cd19518   158 RRAGRFDREICL 169
RecA-like_PEX1_r2 cd19526
second of two ATPase domains of Peroxisomal biogenesis factor 1 (PEX1); PEX1(also known as ...
168-325 5.36e-39

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: 140.64  E-value: 5.36e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1088032500 168 AKQELEEVVDF-LKNPKKFLDIGARIPRGVLLMGAPGTGKTLLARAVAGEAGVPFFHISASEFVEMFVGVGASRTRDAFQ 246
Cdd:cd19526     1 VKKALEETIEWpSKYPKIFASSPLRLRSGILLYGPPGCGKTLLASAIASECGLNFISVKGPELLNKYIGASEQNVRDLFS 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1088032500 247 TAKRAAPSILFIDEIDAVGRERgaglggGHDER---EQTLNQILVEMDGFDRDTKVIVLAATNRPDILDSALLRPGRFDR 323
Cdd:cd19526    81 RAQSAKPCILFFDEFDSIAPKR------GHDSTgvtDRVVNQLLTQLDGVEGLDGVYVLAATSRPDLIDPALLRPGRLDK 154

                  ..
gi 1088032500 324 RV 325
Cdd:cd19526   155 LV 156
RecA-like_VPS4-like cd19509
ATPase domain of VPS4, ATAD1, K, KTNA1, Spastin, FIGL-1 and similar ATPase domains; This ...
162-325 4.12e-37

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: 135.56  E-value: 4.12e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1088032500 162 VAGLKEAKQELEEVVDFlknPKKFLDI---GARIPRGVLLMGAPGTGKTLLARAVAGEAGVPFFHISASEFVEMFVGVGA 238
Cdd:cd19509     1 IAGLDDAKEALKEAVIL---PSLRPDLfpgLRGPPRGILLYGPPGTGKTLLARAVASESGSTFFSISASSLVSKWVGESE 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1088032500 239 SRTRDAFQTAKRAAPSILFIDEIDAVGRERGAglgGGHDEREQTLNQILVEMDGF--DRDTKVIVLAATNRPDILDSALL 316
Cdd:cd19509    78 KIVRALFALARELQPSIIFIDEIDSLLSERGS---GEHEASRRVKTEFLVQMDGVlnKPEDRVLVLGATNRPWELDEAFL 154

                  ....*....
gi 1088032500 317 RpgRFDRRV 325
Cdd:cd19509   155 R--RFEKRI 161
RecA-like_PEX6_r2 cd19527
second of two ATPase domains of Peroxisomal biogenesis factor 6 (PEX6); PEX6(also known as ...
169-327 6.61e-35

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: 129.56  E-value: 6.61e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1088032500 169 KQELEEVVDF-LKNPKKFLDiGARIPRGVLLMGAPGTGKTLLARAVAGEAGVPFFHISASEFVEMFVGVGASRTRDAFQT 247
Cdd:cd19527     2 KKEILDTIQLpLEHPELFSS-GLRKRSGILLYGPPGTGKTLLAKAIATECSLNFLSVKGPELINMYIGESEANVREVFQK 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1088032500 248 AKRAAPSILFIDEIDAVGRERGA-GLGGGHDEReqTLNQILVEMDGF-DRDTKVIVLAATNRPDILDSALLRPGRFDRRV 325
Cdd:cd19527    81 ARDAKPCVIFFDELDSLAPSRGNsGDSGGVMDR--VVSQLLAELDGMsSSGQDVFVIGATNRPDLLDPALLRPGRFDKLL 158

                  ..
gi 1088032500 326 VL 327
Cdd:cd19527   159 YL 160
RecA-like_VPS4 cd19521
ATPase domain of vacuolar protein sorting-associated protein 4; Vacuolar protein ...
154-325 1.39e-34

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: 128.83  E-value: 1.39e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1088032500 154 KDRATFKDVAGLKEAKQELEEVVDF-LKNPKKFldIGARIP-RGVLLMGAPGTGKTLLARAVAGEAGVPFFHISASEFVE 231
Cdd:cd19521     1 KPNVKWEDVAGLEGAKEALKEAVILpVKFPHLF--TGNRKPwSGILLYGPPGTGKSYLAKAVATEANSTFFSVSSSDLVS 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1088032500 232 MFVGVGASRTRDAFQTAKRAAPSILFIDEIDAVGRERGAglgGGHDEREQTLNQILVEMDGFDRDT-KVIVLAATNRPDI 310
Cdd:cd19521    79 KWMGESEKLVKQLFAMARENKPSIIFIDEVDSLCGTRGE---GESEASRRIKTELLVQMNGVGNDSqGVLVLGATNIPWQ 155
                         170
                  ....*....|....*
gi 1088032500 311 LDSALLRpgRFDRRV 325
Cdd:cd19521   156 LDSAIRR--RFEKRI 168
RecA-like_spastin cd19524
ATPase domain of spastin; Spastin is an ATP-dependent microtubule-severing protein involved in ...
161-325 3.60e-33

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


Pssm-ID: 410932 [Multi-domain]  Cd Length: 164  Bit Score: 124.58  E-value: 3.60e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1088032500 161 DVAGLKEAKQELEEVVdFLKNPKKFLDIGARIP-RGVLLMGAPGTGKTLLARAVAGEAGVPFFHISASEFVEMFVGVGAS 239
Cdd:cd19524     1 DIAGQDLAKQALQEMV-ILPSLRPELFTGLRAPaRGLLLFGPPGNGKTMLAKAVAAESNATFFNISAASLTSKYVGEGEK 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1088032500 240 RTRDAFQTAKRAAPSILFIDEIDAVGRERGAglgGGHDEREQTLNQILVEMDGF--DRDTKVIVLAATNRPDILDSALLR 317
Cdd:cd19524    80 LVRALFAVARELQPSIIFIDEVDSLLSERSE---GEHEASRRLKTEFLIEFDGVqsNGDDRVLVMGATNRPQELDDAVLR 156

                  ....*...
gi 1088032500 318 pgRFDRRV 325
Cdd:cd19524   157 --RFTKRV 162
RecA-like_KTNA1 cd19522
Katanin p60 ATPase-containing subunit A1; Katanin p60 ATPase-containing subunit A1 (KTNA1) is ...
161-325 8.46e-33

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: 123.94  E-value: 8.46e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1088032500 161 DVAGLKEAKQELEEVV-------DFLKnpkkfldiGARIP-RGVLLMGAPGTGKTLLARAVAGEAGVPFFHISASEFVEM 232
Cdd:cd19522     1 DIADLEEAKKLLEEAVvlpmwmpEFFK--------GIRRPwKGVLMVGPPGTGKTLLAKAVATECGTTFFNVSSSTLTSK 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1088032500 233 FVGVGASRTRDAFQTAKRAAPSILFIDEIDAVGRERGAglGGGHDEREQTLNQILVEMDGF-------DRDTKVIVLAAT 305
Cdd:cd19522    73 YRGESEKLVRLLFEMARFYAPTTIFIDEIDSICSRRGT--SEEHEASRRVKSELLVQMDGVggasendDPSKMVMVLAAT 150
                         170       180
                  ....*....|....*....|
gi 1088032500 306 NRPDILDSALLRpgRFDRRV 325
Cdd:cd19522   151 NFPWDIDEALRR--RLEKRI 168
RecA-like_Figl-1 cd19525
ATPase domain of Fidgetin-Like 1 (FIGL-1); FIGL-1 may participate in DNA repair in the nucleus; ...
159-325 1.72e-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: 123.56  E-value: 1.72e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1088032500 159 FKDVAGLKEAKQELEEVVDF-LKNPKKFLDIGARiPRGVLLMGAPGTGKTLLARAVAGEAGVPFFHISASEFVEMFVGVG 237
Cdd:cd19525    21 WADIAGLEFAKKTIKEIVVWpMLRPDIFTGLRGP-PKGILLFGPPGTGKTLIGKCIASQSGATFFSISASSLTSKWVGEG 99
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1088032500 238 ASRTRDAFQTAKRAAPSILFIDEIDAVGRERGAglgGGHDEREQTLNQILVEMDGFDR--DTKVIVLAATNRPDILDSAL 315
Cdd:cd19525   100 EKMVRALFSVARCKQPAVIFIDEIDSLLSQRGE---GEHESSRRIKTEFLVQLDGATTssEDRILVVGATNRPQEIDEAA 176
                         170
                  ....*....|
gi 1088032500 316 LRpgRFDRRV 325
Cdd:cd19525   177 RR--RLVKRL 184
RecA-like_Yta7-like cd19517
ATPase domain of Saccharomyces cerevisiae Yta7 and similar ATPase domains; Saccharomyces ...
161-323 2.14e-32

ATPase domain of Saccharomyces cerevisiae Yta7 and similar ATPase domains; Saccharomyces cerevisiae Yta7 is a chromatin-associated AAA-ATPase involved in regulation of chromatin dynamics. Its human ortholog ANCCA/ATAD2 transcriptionally activates pathways of malignancy in a broad range of cancers. The RecA-like_Yta7 subfamily belongs to the RecA-like NTPase family which includes the NTP binding domain of F1 and V1 H(+)ATPases, DnaB and related helicases as well as bacterial RecA and related eukaryotic and archaeal recombinases. The RecA-like NTPase family also includes bacterial conjugation proteins and related DNA transfer proteins involved in type II and type IV secretion.


Pssm-ID: 410925 [Multi-domain]  Cd Length: 170  Bit Score: 122.62  E-value: 2.14e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1088032500 161 DVAGLKEAKQELEEVVDF-LKNPKKFLDIGARIPRGVLLMGAPGTGKTLLARAVAGEAG-----VPFFHISASEFVEMFV 234
Cdd:cd19517     1 DIGGLSHYINQLKEMVFFpLLYPEVFAKFKITPPRGVLFHGPPGTGKTLMARALAAECSkggqkVSFFMRKGADCLSKWV 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1088032500 235 GVGASRTRDAFQTAKRAAPSILFIDEIDAVGRERGAglggghdEREQTLNQI----LVEMDGFDRDTKVIVLAATNRPDI 310
Cdd:cd19517    81 GEAERQLRLLFEEAYRMQPSIIFFDEIDGLAPVRSS-------KQEQIHASIvstlLALMDGLDNRGQVVVIGATNRPDA 153
                         170
                  ....*....|...
gi 1088032500 311 LDSALLRPGRFDR 323
Cdd:cd19517   154 LDPALRRPGRFDR 166
RecA-like_ATAD1 cd19520
ATPase domain of ATPase family AAA domain-containing protein 1 and similar ATPase domains; ...
161-321 6.70e-31

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: 118.30  E-value: 6.70e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1088032500 161 DVAGLKEAKQELEEVVDF-LKNPKKFLDIG-ARIPRGVLLMGAPGTGKTLLARAVAGEAGVPFFHISASEFVEMFVGVGA 238
Cdd:cd19520     1 DIGGLDEVITELKELVILpLQRPELFDNSRlLQPPKGVLLYGPPGCGKTMLAKATAKEAGARFINLQVSSLTDKWYGESQ 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1088032500 239 SRTRDAFQTAKRAAPSILFIDEIDAVGRERGAglgGGHDEREQTLNQILVEMDGFDRD--TKVIVLAATNRPDILDSALL 316
Cdd:cd19520    81 KLVAAVFSLASKLQPSIIFIDEIDSFLRQRSS---TDHEATAMMKAEFMSLWDGLSTDgnCRVIVMGATNRPQDLDEAIL 157

                  ....*..
gi 1088032500 317 R--PGRF 321
Cdd:cd19520   158 RrmPKRF 164
ycf46 CHL00195
Ycf46; Provisional
158-376 8.18e-25

Ycf46; Provisional


Pssm-ID: 177094 [Multi-domain]  Cd Length: 489  Bit Score: 108.18  E-value: 8.18e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1088032500 158 TFKDVAGLKEAKQELEEVVDFLKnpKKFLDIGARIPRGVLLMGAPGTGKTLLARAVAGEAGVPFFHISASEFVEMFVGVG 237
Cdd:CHL00195  226 KISDIGGLDNLKDWLKKRSTSFS--KQASNYGLPTPRGLLLVGIQGTGKSLTAKAIANDWQLPLLRLDVGKLFGGIVGES 303
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1088032500 238 ASRTRDAFQTAKRAAPSILFIDEID-AVGRERGAGLGGghdereqTLNQILVEMDGF--DRDTKVIVLAATNRPDILDSA 314
Cdd:CHL00195  304 ESRMRQMIRIAEALSPCILWIDEIDkAFSNSESKGDSG-------TTNRVLATFITWlsEKKSPVFVVATANNIDLLPLE 376
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1088032500 315 LLRPGRFDRRVVLDLPDINDREAILAIHARGKKLDA--SVDMRRIAVRTPGFSGADLANLVNEA 376
Cdd:CHL00195  377 ILRKGRFDEIFFLDLPSLEEREKIFKIHLQKFRPKSwkKYDIKKLSKLSNKFSGAEIEQSIIEA 440
AAA cd00009
The AAA+ (ATPases Associated with a wide variety of cellular Activities) superfamily ...
191-329 5.36e-24

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: 98.37  E-value: 5.36e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1088032500 191 RIPRGVLLMGAPGTGKTLLARAVAGEA---GVPFFHISASEFVEMFVG---VGASRTRDAFQTAKRAAPSILFIDEIDAV 264
Cdd:cd00009    17 PPPKNLLLYGPPGTGKTTLARAIANELfrpGAPFLYLNASDLLEGLVVaelFGHFLVRLLFELAEKAKPGVLFIDEIDSL 96
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1088032500 265 GRErgaglggghdEREQTLNQILVEMDGFDRDTKVIVLAATNRPDILDSALLRPGRFDRRVVLDL 329
Cdd:cd00009    97 SRG----------AQNALLRVLETLNDLRIDRENVRVIGATNRPLLGDLDRALYDRLDIRIVIPL 151
RecA-like_Ycf46-like cd19507
ATPase domain of Ycf46 and similar ATPase domains; Ycf46 may play a role in the regulation of ...
161-323 2.06e-23

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: 97.05  E-value: 2.06e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1088032500 161 DVAGLKEAKqeleevvDFLKNPKKFLDIGAR-----IPRGVLLMGAPGTGKTLLARAVAGEAGVPFFHISASEFVEMFVG 235
Cdd:cd19507     1 DVGGLDNLK-------DWLKKRKAAFSKQASayglpTPKGLLLVGIQGTGKSLTAKAIAGVWQLPLLRLDMGRLFGGLVG 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1088032500 236 VGASRTRDAFQTAKRAAPSILFIDEID-AVGrerGAGLGGGHDEREQTLNQILVEMDgfDRDTKVIVLAATNRPDILDSA 314
Cdd:cd19507    74 ESESRLRQMIQTAEAIAPCVLWIDEIEkGFS---NADSKGDSGTSSRVLGTFLTWLQ--EKKKPVFVVATANNVQSLPPE 148

                  ....*....
gi 1088032500 315 LLRPGRFDR 323
Cdd:cd19507   149 LLRKGRFDE 157
RecA-like_NSF-SEC18_r1-like cd19504
first of two ATPase domains of NSF and SEC18, and similar ATPase domains; ...
194-325 4.04e-23

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: 96.79  E-value: 4.04e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1088032500 194 RGVLLMGAPGTGKTLLARAV-----AGEAGVpffhISASEFVEMFVGVGASRTRDAFQTAKR--------AAPSILFIDE 260
Cdd:cd19504    36 KGILLYGPPGTGKTLMARQIgkmlnAREPKI----VNGPEILNKYVGESEANIRKLFADAEEeqrrlganSGLHIIIFDE 111
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1088032500 261 IDAVGRERGAGlGGGHDEREQTLNQILVEMDGFDRDTKVIVLAATNRPDILDSALLRPGRFDRRV 325
Cdd:cd19504   112 IDAICKQRGSM-AGSTGVHDTVVNQLLSKIDGVEQLNNILVIGMTNRKDLIDEALLRPGRLEVQM 175
RecA-like_fidgetin cd19523
ATPase domain of fidgetin; Fidgetin (FIGN) is a ATP-dependent microtubule severing protein. ...
161-327 3.17e-18

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: 82.24  E-value: 3.17e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1088032500 161 DVAGLKEAKQEL-EEVVDFLKNPKKFLDIgARIPRGVLLMGAPGTGKTLLARAVAGEAGVPFFHISASEFVEMFVGVGAS 239
Cdd:cd19523     1 DIAGLGALKAAIkEEVLWPLLRPDAFSGL-LRLPRSILLFGPRGTGKTLLGRCLASQLGATFLRLRGSTLVAKWAGEGEK 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1088032500 240 RTRDAFQTAKRAAPSILFIDEIDAV--GRERGAGLGGghdeREQTlnQILVEMDGF--DRDTKVIVLAATNRPDILDSAL 315
Cdd:cd19523    80 ILQASFLAARCRQPSVLFISDLDALlsSQDDEASPVG----RLQV--ELLAQLDGVlgSGEDGVLVVCTTSKPEEIDESL 153
                         170
                  ....*....|..
gi 1088032500 316 LRpgRFDRRVVL 327
Cdd:cd19523   154 RR--YFSKRLLV 163
RecA-like_BCS1 cd19510
Mitochondrial chaperone BCS1; Mitochondrial chaperone BCS1 is necessary for the assembly of ...
172-325 1.11e-17

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: 80.47  E-value: 1.11e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1088032500 172 LEEVVDFLKNPKKFLDIGARIPRGVLLMGAPGTGKTLLARAVAGEAGVPFFHISASEfvemfVGVGASRTRDAFQTAKRA 251
Cdd:cd19510     2 IDDLKDFIKNEDWYNDRGIPYRRGYLLYGPPGTGKSSFIAALAGELDYDICDLNLSE-----VVLTDDRLNHLLNTAPKQ 76
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1088032500 252 apSILFIDEIDA--VGRER-GAGLGGGHDEREQTLNQILVEMDGFDRDTKVIVLAATNRPDILDSALLRPGRFDRRV 325
Cdd:cd19510    77 --SIILLEDIDAafESREHnKKNPSAYGGLSRVTFSGLLNALDGVASSEERIVFMTTNHIERLDPALIRPGRVDMKI 151
AAA smart00382
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ...
193-331 4.60e-16

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: 75.49  E-value: 4.60e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1088032500  193 PRGVLLMGAPGTGKTLLARAVAGEA---GVPFFHISASEFVE--------------MFVGVGASRTRDAFQTAKRAAPSI 255
Cdd:smart00382   2 GEVILIVGPPGSGKTTLARALARELgppGGGVIYIDGEDILEevldqllliivggkKASGSGELRLRLALALARKLKPDV 81
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1088032500  256 LFIDEIDAVGRERGaglggghdEREQTLNQILVEMDGFDRDTKVIVLAATNRPDILDSALLRPgRFDRRVVLDLPD 331
Cdd:smart00382  82 LILDEITSLLDAEQ--------EALLLLLEELRLLLLLKSEKNLTVILTTNDEKDLGPALLRR-RFDRRIVLLLIL 148
AAA_lid_3 pfam17862
AAA+ lid domain; This entry represents the alpha helical AAA+ lid domain that is found to the ...
351-395 8.04e-10

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: 54.47  E-value: 8.04e-10
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 1088032500 351 SVDMRRIAVRTPGFSGADLANLVNEAAISSARKNKKMVGQEELLD 395
Cdd:pfam17862   1 DVDLEELAERTEGFSGADLEALCREAALAALRRGLEAVTQEDLEE 45
PRK13342 PRK13342
recombination factor protein RarA; Reviewed
172-261 3.66e-09

recombination factor protein RarA; Reviewed


Pssm-ID: 237355 [Multi-domain]  Cd Length: 413  Bit Score: 58.94  E-value: 3.66e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1088032500 172 LEEVV--DFLKNPKKFLD--IGARIPRGVLLMGAPGTGKTLLARAVAGEAGVPFFHISASefvemFVGVgaSRTRDAFQT 247
Cdd:PRK13342   11 LDEVVgqEHLLGPGKPLRrmIEAGRLSSMILWGPPGTGKTTLARIIAGATDAPFEALSAV-----TSGV--KDLREVIEE 83
                          90
                  ....*....|....*...
gi 1088032500 248 AKRAAPS----ILFIDEI 261
Cdd:PRK13342   84 ARQRRSAgrrtILFIDEI 101
RecA-like_ATAD3-like cd19512
ATPase domains of ATPase AAA-domain protein 3A (ATAD3A), -3B, and -3C, and similar ATPase ...
194-315 4.12e-09

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: 55.61  E-value: 4.12e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1088032500 194 RGVLLMGAPGTGKTLLARAVAGEAGVPFFHISASEFVEMFV-GVGA-SRTRDAFQTAKRAApsILFIDEIDAVGRERgAG 271
Cdd:cd19512    23 RNILFYGPPGTGKTLFAKKLALHSGMDYAIMTGGDVAPMGReGVTAiHKVFDWANTSRRGL--LLFVDEADAFLRKR-ST 99
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 1088032500 272 LGGGHDEReQTLNQILVEMDgfDRDTKVIVLAATNRPDILDSAL 315
Cdd:cd19512   100 EKISEDLR-AALNAFLYRTG--EQSNKFMLVLASNQPEQFDWAI 140
RarA COG2256
Replication-associated recombination protein RarA (DNA-dependent ATPase) [Replication, ...
170-261 4.96e-09

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


Pssm-ID: 441857 [Multi-domain]  Cd Length: 439  Bit Score: 58.91  E-value: 4.96e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1088032500 170 QELEEVV--DFLKNPKKFLD--IGARIPRGVLLMGAPGTGKTLLARAVAGEAGVPFFHISAsefvemfVGVGASRTRDAF 245
Cdd:COG2256    22 RTLDEVVgqEHLLGPGKPLRraIEAGRLSSMILWGPPGTGKTTLARLIANATDAEFVALSA-------VTSGVKDIREVI 94
                          90       100
                  ....*....|....*....|
gi 1088032500 246 QTAKRAA----PSILFIDEI 261
Cdd:COG2256    95 EEARERRaygrRTILFVDEI 114
PRK04195 PRK04195
replication factor C large subunit; Provisional
153-262 7.22e-09

replication factor C large subunit; Provisional


Pssm-ID: 235250 [Multi-domain]  Cd Length: 482  Bit Score: 58.39  E-value: 7.22e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1088032500 153 EKDR-ATFKDVAGLKEAKQELEEVVD-FLKNPKKfldigaripRGVLLMGAPGTGKTLLARAVAGEAGVPFFHISASEF- 229
Cdd:PRK04195    6 EKYRpKTLSDVVGNEKAKEQLREWIEsWLKGKPK---------KALLLYGPPGVGKTSLAHALANDYGWEVIELNASDQr 76
                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 1088032500 230 ----VEMFVGvGASRTRDAFQTAKRaapsILFIDEID 262
Cdd:PRK04195   77 tadvIERVAG-EAATSGSLFGARRK----LILLDEVD 108
RecA-like_Ycf2 cd19505
ATPase domain of plant YCF2; Ycf2 is a chloroplast ATPase which has an essential function; ...
186-323 1.17e-08

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: 54.69  E-value: 1.17e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1088032500 186 LDIGARIPRGVLLMGAPGTGKTLLARAVAGEAGVPFFHISASEFV--------------EMFVGVGASRTRDAFQTAKRA 251
Cdd:cd19505     5 LRLGLSPSKGILLIGSIETGRSYLIKSLAANSYVPLIRISLNKLLynkpdfgnddwidgMLILKESLHRLNLQFELAKAM 84
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1088032500 252 APSILFIDEIDAVGRERgagLGGGHDEREQTLNQILVEM--DGFDRDTK--VIVLAATNRPDILDSALLRPGRFDR 323
Cdd:cd19505    85 SPCIIWIPNIHELNVNR---STQNLEEDPKLLLGLLLNYlsRDFEKSSTrnILVIASTHIPQKVDPALIAPNRLDT 157
RecA-like_HslU cd19498
ATP-dependent protease ATPase subunit HslU; HslU is a component of the ATP-dependent protease ...
192-298 2.03e-08

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: 54.31  E-value: 2.03e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1088032500 192 IPRGVLLMGAPGTGKTLLARAVAGEAGVPFFHISASEFVEM-FVGvgasrtRDAFQTAKRAAPSILFIDEIDAVGRERGa 270
Cdd:cd19498    45 TPKNILMIGPTGVGKTEIARRLAKLAGAPFIKVEATKFTEVgYVG------RDVESIIRDLVEGIVFIDEIDKIAKRGG- 117
                          90       100
                  ....*....|....*....|....*....
gi 1088032500 271 glGGGHD-EREQTLNQILVEMDGFDRDTK 298
Cdd:cd19498   118 --SSGPDvSREGVQRDLLPIVEGSTVSTK 144
TIP49 COG1224
DNA helicase TIP49, TBP-interacting protein [Transcription];
194-229 4.38e-06

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


Pssm-ID: 440837 [Multi-domain]  Cd Length: 452  Bit Score: 49.58  E-value: 4.38e-06
                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 1088032500 194 RGVLLMGAPGTGKTLLARAVAGEAG--VPFFHISASEF 229
Cdd:COG1224    65 KGILIVGPPGTGKTALAVAIARELGedTPFVAISGSEI 102
AAA_5 pfam07728
AAA domain (dynein-related subfamily); This Pfam entry includes some of the AAA proteins not ...
195-321 5.82e-06

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: 46.13  E-value: 5.82e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1088032500 195 GVLLMGAPGTGKTLLARAVAgEA--GVPFFHI------SASEFV-EMFVGVGASRTRDafQTAKRAA--PSILFIDEIDA 263
Cdd:pfam07728   1 GVLLVGPPGTGKTELAERLA-AAlsNRPVFYVqltrdtTEEDLFgRRNIDPGGASWVD--GPLVRAAreGEIAVLDEINR 77
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1088032500 264 VGRERGAGLGGGHDEREQTLN----QILVEMDGFdrdtkvIVLAATNRPDI----LDSALLRpgRF 321
Cdd:pfam07728  78 ANPDVLNSLLSLLDERRLLLPdggeLVKAAPDGF------RLIATMNPLDRglneLSPALRS--RF 135
TIP49 pfam06068
TIP49 P-loop domain; This family consists of the C-terminal region of several eukaryotic and ...
194-229 1.25e-05

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


Pssm-ID: 399217 [Multi-domain]  Cd Length: 347  Bit Score: 47.69  E-value: 1.25e-05
                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 1088032500 194 RGVLLMGAPGTGKTLLARAVAGEAG--VPFFHISASEF 229
Cdd:pfam06068  51 RAVLIAGPPGTGKTALAIAISKELGedTPFTSISGSEV 88
T7SS_EccA TIGR03922
type VII secretion AAA-ATPase EccA; This model represents the AAA family ATPase, EccA, of the ...
164-325 1.98e-05

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: 47.53  E-value: 1.98e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1088032500 164 GLKEAKQELEEVVDFLKNPKKFLDIGARIP---RGVLLMGAPGTGKTLLARAVAGE-AGVPFF------HISASEFVEMF 233
Cdd:TIGR03922 280 GLERVKRQVAALKSSTAMALARAERGLPVAqtsNHMLFAGPPGTGKTTIARVVAKIyCGLGVLrkplvrEVSRADLIGQY 359
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1088032500 234 VGVGASRTRdafQTAKRAAPSILFIDEIDAVGRERGaglGGGHDEREQTLNQILVEMDGfDRDTKVIVLAATNrpDILDS 313
Cdd:TIGR03922 360 IGESEAKTN---EIIDSALGGVLFLDEAYTLVETGY---GQKDPFGLEAIDTLLARMEN-DRDRLVVIGAGYR--KDLDK 430
                         170
                  ....*....|....*..
gi 1088032500 314 AL-----LRpGRFDRRV 325
Cdd:TIGR03922 431 FLevnegLR-SRFTRVI 446
RecA-like_Lon cd19500
lon protease homolog 2 peroxisomal; Lon protease (also known as Lon peptidase) is an ...
160-266 2.69e-05

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


Pssm-ID: 410908 [Multi-domain]  Cd Length: 182  Bit Score: 45.24  E-value: 2.69e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1088032500 160 KDVAGLKEAKqelEEVVDFLKNPKKFLDIGARIprgVLLMGAPGTGKTLLARAVAGEAGVPFFHIS---ASEFVEM---- 232
Cdd:cd19500    10 ADHYGLEDVK---ERILEYLAVRKLKGSMKGPI---LCLVGPPGVGKTSLGKSIARALGRKFVRISlggVRDEAEIrghr 83
                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 1088032500 233 --FVGVGASRTRDAFQTAKRAAPSILfIDEIDAVGR 266
Cdd:cd19500    84 rtYVGAMPGRIIQALKKAGTNNPVFL-LDEIDKIGS 118
MoxR COG0714
MoxR-like ATPase [General function prediction only]; MoxR-like ATPase is part of the Pathway ...
196-345 1.45e-04

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: 44.00  E-value: 1.45e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1088032500 196 VLLMGAPGTGKTLLARAVAGEAGVPFFHIsasEF-----------VEMFVgvgaSRTRDaFQTAKRAAP-SILFIDEIDa 263
Cdd:COG0714    34 LLLEGVPGVGKTTLAKALARALGLPFIRI---QFtpdllpsdilgTYIYD----QQTGE-FEFRPGPLFaNVLLADEIN- 104
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1088032500 264 vgreRGaglggghdeREQTLN---------QILVEMDGFDRDTKVIVLAATNRPDI-----LDSALLRpgRFDRRVVLDL 329
Cdd:COG0714   105 ----RA---------PPKTQSalleameerQVTIPGGTYKLPEPFLVIATQNPIEQegtypLPEAQLD--RFLLKLYIGY 169
                         170
                  ....*....|....*.
gi 1088032500 330 PDINDREAILAIHARG 345
Cdd:COG0714   170 PDAEEEREILRRHTGR 185
44 PHA02544
clamp loader, small subunit; Provisional
183-265 2.16e-04

clamp loader, small subunit; Provisional


Pssm-ID: 222866 [Multi-domain]  Cd Length: 316  Bit Score: 43.83  E-value: 2.16e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1088032500 183 KKFLDIGaRIPRGVLLMGAPGTGKTLLARAVAGEAGVPFFHISASEfvemfVGVGASRTR-DAFQTAK--RAAPSILFID 259
Cdd:PHA02544   34 KSIVKKG-RIPNMLLHSPSPGTGKTTVAKALCNEVGAEVLFVNGSD-----CRIDFVRNRlTRFASTVslTGGGKVIIID 107

                  ....*.
gi 1088032500 260 EIDAVG 265
Cdd:PHA02544  108 EFDRLG 113
RecA-like_ClpX cd19497
ATP-dependent Clp protease ATP-binding subunit ClpX; ClpX is a component of the ATP-dependent ...
196-266 2.26e-04

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: 43.36  E-value: 2.26e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1088032500 196 VLLMGAPGTGKTLLARAVAGEAGVPFFHISASEFVEM-FVG-----VGASRTRDAFQTAKRAAPSILFIDEIDAVGR 266
Cdd:cd19497    53 ILLIGPTGSGKTLLAQTLAKILDVPFAIADATTLTEAgYVGedvenILLKLLQAADYDVERAQRGIVYIDEIDKIAR 129
AAA_2 pfam07724
AAA domain (Cdc48 subfamily); This Pfam entry includes some of the AAA proteins not detected ...
196-262 4.54e-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: 4.54e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1088032500 196 VLLMGAPGTGKTLLARAVAGEAGV---PFFHISASEFVE-----MFVG-----VGASRTRDAFQTAKRAAPSILFIDEID 262
Cdd:pfam07724   6 FLFLGPTGVGKTELAKALAELLFGderALIRIDMSEYMEehsvsRLIGappgyVGYEEGGQLTEAVRRKPYSIVLIDEIE 85
RuvB_N pfam05496
Holliday junction DNA helicase RuvB P-loop domain; The RuvB protein makes up part of the ...
158-261 5.67e-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: 40.95  E-value: 5.67e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1088032500 158 TFKDVAGLKEAKQELEEVVDFLKNPKKFLDigariprGVLLMGAPGTGKTLLARAVAGEAGVPfFHISASEFVEmfvgvg 237
Cdd:pfam05496   5 TLDEYIGQEKVKENLKIFIEAAKQRGEALD-------HVLLYGPPGLGKTTLANIIANEMGVN-IRITSGPAIE------ 70
                          90       100
                  ....*....|....*....|....*.
gi 1088032500 238 asRTRD--AFQTAKRAApSILFIDEI 261
Cdd:pfam05496  71 --RPGDlaAILTNLEPG-DVLFIDEI 93
RecA-like_superfamily cd01120
RecA-like_NTPases; RecA-like NTPases. This superfamily includes the NTP binding domain of F1 ...
196-312 2.03e-03

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: 38.25  E-value: 2.03e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1088032500 196 VLLMGAPGTGKTLLARAVAGEAGVPFFHISASEFVEMFVgvgasrtRDAFQTAKRAAPSILFIDEIDAVGRERGAglggg 275
Cdd:cd01120     1 ILITGPPGSGKTTLLLQFAEQALLSDEPVIFISFLDTIL-------EAIEDLIEEKKLDIIIIDSLSSLARASQG----- 68
                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 1088032500 276 hDEREQTLNQILVEMDGFdRDTKVIVLAATNRPDILD 312
Cdd:cd01120    69 -DRSSELLEDLAKLLRAA-RNTGITVIATIHSDKFDI 103
PRK11361 PRK11361
acetoacetate metabolism transcriptional regulator AtoC;
156-357 2.12e-03

acetoacetate metabolism transcriptional regulator AtoC;


Pssm-ID: 183099 [Multi-domain]  Cd Length: 457  Bit Score: 40.99  E-value: 2.12e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1088032500 156 RATFKDVAGLKEAKQELEEVVDFLKNPKKFLDI---GARIPRG---VLLMGAPGTGKTLLARAV---AGEAGVPFFHISA 226
Cdd:PRK11361  123 QSMKKEIRHLHQALSTSWQWGHILTNSPAMMDIckdTAKIALSqasVLISGESGTGKELIARAIhynSRRAKGPFIKVNC 202
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1088032500 227 ---------SEFV----EMFVGvGASRTRDAFQTAKRAApsiLFIDEIDAVGRERGAGLGGGHDEREqtlnqilvemdgF 293
Cdd:PRK11361  203 aalpeslleSELFghekGAFTG-AQTLRQGLFERANEGT---LLLDEIGEMPLVLQAKLLRILQERE------------F 266
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1088032500 294 DR-------DTKVIVLAATNRpDIldSALLRPGRFDRR-------VVLDLPDINDRE---AILAIHARGK-KLDASVDMR 355
Cdd:PRK11361  267 ERigghqtiKVDIRIIAATNR-DL--QAMVKEGTFREDlfyrlnvIHLILPPLRDRRediSLLANHFLQKfSSENQRDII 343

                  ..
gi 1088032500 356 RI 357
Cdd:PRK11361  344 DI 345
GntK COG3265
Gluconate kinase [Carbohydrate transport and metabolism]; Gluconate kinase is part of the ...
193-223 4.26e-03

Gluconate kinase [Carbohydrate transport and metabolism]; Gluconate kinase is part of the Pathway/BioSystem: Non-phosphorylated Entner-Doudoroff pathway


Pssm-ID: 442496 [Multi-domain]  Cd Length: 164  Bit Score: 38.19  E-value: 4.26e-03
                          10        20        30
                  ....*....|....*....|....*....|.
gi 1088032500 193 PRGVLLMGAPGTGKTLLARAVAGEAGVPFFH 223
Cdd:COG3265     1 PMVIVVMGVSGSGKSTVGQALAERLGWPFID 31
DnaC COG1484
DNA replication protein DnaC [Replication, recombination and repair];
194-261 7.64e-03

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


Pssm-ID: 441093 [Multi-domain]  Cd Length: 242  Bit Score: 38.61  E-value: 7.64e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1088032500 194 RGVLLMGAPGTGKTLLARAVAGEA---GVPFFHISASEFVEMFvgVGASRTRDAFQTAKR-AAPSILFIDEI 261
Cdd:COG1484   100 ENLILLGPPGTGKTHLAIALGHEAcraGYRVRFTTAPDLVNEL--KEARADGRLERLLKRlAKVDLLILDEL 169
NACHT COG5635
Predicted NTPase, NACHT family domain [Signal transduction mechanisms];
180-362 9.04e-03

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


Pssm-ID: 444362 [Multi-domain]  Cd Length: 935  Bit Score: 39.02  E-value: 9.04e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1088032500 180 KNPKKFLDIGARIPRGVLLMGAPGTGKTLLARAVA---------GEAGVPFF--------HISASEFVEMFVGVGASRTR 242
Cdd:COG5635   167 IESLKRLELLEAKKKRLLILGEPGSGKTTLLRYLAlelaeryldAEDPIPILielrdlaeEASLEDLLAEALEKRGGEPE 246
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1088032500 243 DAFQTAKRAAPSILFIDEIDAVGRErgaglggghDEREQTLNQILVEMDGFDRdTKVIVlaaTNRPDILDSALLRpgRFD 322
Cdd:COG5635   247 DALERLLRNGRLLLLLDGLDEVPDE---------ADRDEVLNQLRRFLERYPK-ARVII---TSRPEGYDSSELE--GFE 311
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 1088032500 323 RRVVLDLpDINDREAIL-----AIHARG----KKLDASVDMRRIAvRTP 362
Cdd:COG5635   312 VLELAPL-SDEQIEEFLkkwfeATERKAerllEALEENPELRELA-RNP 358
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH