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Conserved domains on  [gi|489185780|ref|WP_003095200|]
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MULTISPECIES: ATP-dependent zinc metalloprotease FtsH [Pseudomonas]

Protein Classification

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

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

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
HflB COG0465
ATP-dependent Zn proteases [Posttranslational modification, protein turnover, chaperones];
11-598 0e+00

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


:

Pssm-ID: 440233 [Multi-domain]  Cd Length: 583  Bit Score: 1084.68  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489185780  11 IAAVLVTVMNNFSSP-SEPQTLNYSDFIQQVKDGKVERVTVDGYVITGKRSDGD--TFKTIRPaiQDNGLIGDLVNNNVV 87
Cdd:COG0465    1 IALLLVLLFNLFSSSsSSVKEISYSEFLQLVEAGKVKSVTIQGDRITGTLKDGTktRFTTYRV--NDPELVDLLEEKGVE 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489185780  88 VEGKQPEQQSIWTQLLVASFPILVIIAVFMFFMRQMQGGGGGrggPMSFGKSKARLLSEDQVKTTFADVAGCDEAKEEVS 167
Cdd:COG0465   79 VTAKPPEESSWLLSLLISLLPILLLIGLWIFFMRRMQGGGGG---AMSFGKSKAKLYDEDKPKVTFDDVAGVDEAKEELQ 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489185780 168 ELVEFLRDPGKFQRLGGRIPRGVLMVGPPGTGKTLLAKAIAGEAKVPFFTISGSDFVEMFVGVGASRVRDMFDQAKKHAP 247
Cdd:COG0465  156 EIVDFLKDPEKFTRLGAKIPKGVLLVGPPGTGKTLLAKAVAGEAGVPFFSISGSDFVEMFVGVGASRVRDLFEQAKKNAP 235
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489185780 248 CIIFIDEIDAVGRHRGAGLGGGHDEREQTLNQLLVEMDGFEMNDGIIVIAATNRPDVLDPALLRPGRFDRQVVVGLPDIR 327
Cdd:COG0465  236 CIIFIDEIDAVGRQRGAGLGGGHDEREQTLNQLLVEMDGFEGNEGVIVIAATNRPDVLDPALLRPGRFDRQVVVDLPDVK 315
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489185780 328 GREQILKVHMRKVPLGDHVDPAVIARGTPGFSGADLANLVNEASLFAARSNKRIVDMREFELAKDKIMMGAERKTMVMSE 407
Cdd:COG0465  316 GREAILKVHARKKPLAPDVDLEVIARRTPGFSGADLANLVNEAALLAARRNKKAVTMEDFEEAIDRVIAGPERKSRVISE 395
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489185780 408 KEKRNTAYHEAGHAIVGRLVPEHDPVYKVSIIPRGRALGVTMFLPEEDRYSLSKRALESQICSLFGGRIAEEMTlgFEGV 487
Cdd:COG0465  396 KEKKITAYHEAGHALVAALLPGADPVHKVTIIPRGRALGYTMQLPEEDRYLYTKEELLDRIAVLLGGRAAEELV--FGEV 473
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489185780 488 TTGASNDIMRATQLARNMVTKWGLSEKLGPLMYAEEEGEVFLGRSaGSQHANVSGETAKMIDQEVRRIIDDCYGTAKRLL 567
Cdd:COG0465  474 TTGASNDLERATKIARAMVTEYGMSEKLGPVAYGESEGEVFLGRD-IGQSRNYSEETAREIDEEVRRIIDEAYERAKEIL 552
                        570       580       590
                 ....*....|....*....|....*....|.
gi 489185780 568 DENRDKLEMMADALMKYETIDSDQIDDIMAG 598
Cdd:COG0465  553 TENRDKLDALAEALLEKETLDGEELEEILAG 583
 
Name Accession Description Interval E-value
HflB COG0465
ATP-dependent Zn proteases [Posttranslational modification, protein turnover, chaperones];
11-598 0e+00

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


Pssm-ID: 440233 [Multi-domain]  Cd Length: 583  Bit Score: 1084.68  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489185780  11 IAAVLVTVMNNFSSP-SEPQTLNYSDFIQQVKDGKVERVTVDGYVITGKRSDGD--TFKTIRPaiQDNGLIGDLVNNNVV 87
Cdd:COG0465    1 IALLLVLLFNLFSSSsSSVKEISYSEFLQLVEAGKVKSVTIQGDRITGTLKDGTktRFTTYRV--NDPELVDLLEEKGVE 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489185780  88 VEGKQPEQQSIWTQLLVASFPILVIIAVFMFFMRQMQGGGGGrggPMSFGKSKARLLSEDQVKTTFADVAGCDEAKEEVS 167
Cdd:COG0465   79 VTAKPPEESSWLLSLLISLLPILLLIGLWIFFMRRMQGGGGG---AMSFGKSKAKLYDEDKPKVTFDDVAGVDEAKEELQ 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489185780 168 ELVEFLRDPGKFQRLGGRIPRGVLMVGPPGTGKTLLAKAIAGEAKVPFFTISGSDFVEMFVGVGASRVRDMFDQAKKHAP 247
Cdd:COG0465  156 EIVDFLKDPEKFTRLGAKIPKGVLLVGPPGTGKTLLAKAVAGEAGVPFFSISGSDFVEMFVGVGASRVRDLFEQAKKNAP 235
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489185780 248 CIIFIDEIDAVGRHRGAGLGGGHDEREQTLNQLLVEMDGFEMNDGIIVIAATNRPDVLDPALLRPGRFDRQVVVGLPDIR 327
Cdd:COG0465  236 CIIFIDEIDAVGRQRGAGLGGGHDEREQTLNQLLVEMDGFEGNEGVIVIAATNRPDVLDPALLRPGRFDRQVVVDLPDVK 315
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489185780 328 GREQILKVHMRKVPLGDHVDPAVIARGTPGFSGADLANLVNEASLFAARSNKRIVDMREFELAKDKIMMGAERKTMVMSE 407
Cdd:COG0465  316 GREAILKVHARKKPLAPDVDLEVIARRTPGFSGADLANLVNEAALLAARRNKKAVTMEDFEEAIDRVIAGPERKSRVISE 395
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489185780 408 KEKRNTAYHEAGHAIVGRLVPEHDPVYKVSIIPRGRALGVTMFLPEEDRYSLSKRALESQICSLFGGRIAEEMTlgFEGV 487
Cdd:COG0465  396 KEKKITAYHEAGHALVAALLPGADPVHKVTIIPRGRALGYTMQLPEEDRYLYTKEELLDRIAVLLGGRAAEELV--FGEV 473
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489185780 488 TTGASNDIMRATQLARNMVTKWGLSEKLGPLMYAEEEGEVFLGRSaGSQHANVSGETAKMIDQEVRRIIDDCYGTAKRLL 567
Cdd:COG0465  474 TTGASNDLERATKIARAMVTEYGMSEKLGPVAYGESEGEVFLGRD-IGQSRNYSEETAREIDEEVRRIIDEAYERAKEIL 552
                        570       580       590
                 ....*....|....*....|....*....|.
gi 489185780 568 DENRDKLEMMADALMKYETIDSDQIDDIMAG 598
Cdd:COG0465  553 TENRDKLDALAEALLEKETLDGEELEEILAG 583
hflB PRK10733
ATP-dependent zinc metalloprotease FtsH;
1-639 0e+00

ATP-dependent zinc metalloprotease FtsH;


Pssm-ID: 182683 [Multi-domain]  Cd Length: 644  Bit Score: 903.25  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489185780   1 MAKNLILWLIIAAVLVTVMNNFS-SPSEPQTLNYSDFIQQVKDGKVERVTVDGYVITGKRSDGDTFKTIRPaIQDNGLIG 79
Cdd:PRK10733   1 MAKNLILWLVIAVVLMSVFQSFGpSESNGRKVDYSTFLQEVNQDQVREARINGREINVTKKDSNRYTTYIP-VNDPKLLD 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489185780  80 DLVNNNVVVEGKQPEQQSIWTQLLVASFPILVIIAVFMFFMRQMQGGGGGRGgpMSFGKSKARLLSEDQVKTTFADVAGC 159
Cdd:PRK10733  80 NLLTKNVKVVGEPPEEPSLLASIFISWFPMLLLIGVWIFFMRQMQGGGGKGA--MSFGKSKARMLTEDQIKTTFADVAGC 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489185780 160 DEAKEEVSELVEFLRDPGKFQRLGGRIPRGVLMVGPPGTGKTLLAKAIAGEAKVPFFTISGSDFVEMFVGVGASRVRDMF 239
Cdd:PRK10733 158 DEAKEEVAELVEYLREPSRFQKLGGKIPKGVLMVGPPGTGKTLLAKAIAGEAKVPFFTISGSDFVEMFVGVGASRVRDMF 237
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489185780 240 DQAKKHAPCIIFIDEIDAVGRHRGAGLGGGHDEREQTLNQLLVEMDGFEMNDGIIVIAATNRPDVLDPALLRPGRFDRQV 319
Cdd:PRK10733 238 EQAKKAAPCIIFIDEIDAVGRQRGAGLGGGHDEREQTLNQMLVEMDGFEGNEGIIVIAATNRPDVLDPALLRPGRFDRQV 317
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489185780 320 VVGLPDIRGREQILKVHMRKVPLGDHVDPAVIARGTPGFSGADLANLVNEASLFAARSNKRIVDMREFELAKDKIMMGAE 399
Cdd:PRK10733 318 VVGLPDVRGREQILKVHMRRVPLAPDIDAAIIARGTPGFSGADLANLVNEAALFAARGNKRVVSMVEFEKAKDKIMMGAE 397
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489185780 400 RKTMVMSEKEKRNTAYHEAGHAIVGRLVPEHDPVYKVSIIPRGRALGVTMFLPEEDRYSLSKRALESQICSLFGGRIAEE 479
Cdd:PRK10733 398 RRSMVMTEAQKESTAYHEAGHAIIGRLVPEHDPVHKVTIIPRGRALGVTFFLPEGDAISASRQKLESQISTLYGGRLAEE 477
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489185780 480 MTLGFEGVTTGASNDIMRATQLARNMVTKWGLSEKLGPLMYAEEEGEVFLGRS-AGSQHanVSGETAKMIDQEVRRIIDD 558
Cdd:PRK10733 478 IIYGPEHVSTGASNDIKVATNLARNMVTQWGFSEKLGPLLYAEEEGEVFLGRSvAKAKH--MSDETARIIDQEVKALIER 555
                        570       580       590       600       610       620       630       640
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489185780 559 CYGTAKRLLDENRDKLEMMADALMKYETIDSDQIDDIMAGRVPREPRDWQGGSGT----GTPPANLEESGRRENTPPIGG 634
Cdd:PRK10733 556 NYNRARQLLTDNMDILHAMKDALMKYETIDAPQIDDLMARRDVRPPAGWEEPGASnnsdDNGTPKAPRPVDEPRTPNPGN 635

                 ....*
gi 489185780 635 PAGEH 639
Cdd:PRK10733 636 TMSEQ 640
FtsH_fam TIGR01241
ATP-dependent metalloprotease FtsH; HflB(FtsH) is a pleiotropic protein required for correct ...
97-597 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: 846.57  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489185780   97 SIWTQLLVASFPILVIIAVFMFFMRQMQGGGGGRggpMSFGKSKARLLSEDQVKTTFADVAGCDEAKEEVSELVEFLRDP 176
Cdd:TIGR01241   1 SLLGFLFSLLPPILLLVGVWFFFRRQMQGGGGRA---FSFGKSKAKLLNEEKPKVTFKDVAGIDEAKEELMEIVDFLKNP 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489185780  177 GKFQRLGGRIPRGVLMVGPPGTGKTLLAKAIAGEAKVPFFTISGSDFVEMFVGVGASRVRDMFDQAKKHAPCIIFIDEID 256
Cdd:TIGR01241  78 SKFTKLGAKIPKGVLLVGPPGTGKTLLAKAVAGEAGVPFFSISGSDFVEMFVGVGASRVRDLFEQAKKNAPCIIFIDEID 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489185780  257 AVGRHRGAGLGGGHDEREQTLNQLLVEMDGFEMNDGIIVIAATNRPDVLDPALLRPGRFDRQVVVGLPDIRGREQILKVH 336
Cdd:TIGR01241 158 AVGRQRGAGLGGGNDEREQTLNQLLVEMDGFGTNTGVIVIAATNRPDVLDPALLRPGRFDRQVVVDLPDIKGREEILKVH 237
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489185780  337 MRKVPLGDHVDPAVIARGTPGFSGADLANLVNEASLFAARSNKRIVDMREFELAKDKIMMGAERKTMVMSEKEKRNTAYH 416
Cdd:TIGR01241 238 AKNKKLAPDVDLKAVARRTPGFSGADLANLLNEAALLAARKNKTEITMNDIEEAIDRVIAGPEKKSRVISEKEKKLVAYH 317
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489185780  417 EAGHAIVGRLVPEHDPVYKVSIIPRGRALGVTMFLPEEDRYSLSKRALESQICSLFGGRIAEEMTLGfeGVTTGASNDIM 496
Cdd:TIGR01241 318 EAGHALVGLLLKDADPVHKVTIIPRGQALGYTQFLPEEDKYLYTKSQLLAQIAVLLGGRAAEEIIFG--EVTTGASNDIK 395
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489185780  497 RATQLARNMVTKWGLSEKLGPLMYAEEEGEVFLGRSAGSQHaNVSGETAKMIDQEVRRIIDDCYGTAKRLLDENRDKLEM 576
Cdd:TIGR01241 396 QATNIARAMVTEWGMSDKLGPVAYGSDGGDVFLGRGFAKAK-EYSEETAREIDEEVKRIIEEAYKRAKQILTENRDELEL 474
                         490       500
                  ....*....|....*....|.
gi 489185780  577 MADALMKYETIDSDQIDDIMA 597
Cdd:TIGR01241 475 LAKALLEKETITREEIKELLA 495
RecA-like_FtsH cd19501
ATP-dependent zinc metalloprotease FtsH; FtsH ATPase is a processive, ATP-dependent zinc ...
151-321 4.90e-128

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: 374.26  E-value: 4.90e-128
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489185780 151 TTFADVAGCDEAKEEVSELVEFLRDPGKFQRLGGRIPRGVLMVGPPGTGKTLLAKAIAGEAKVPFFTISGSDFVEMFVGV 230
Cdd:cd19501    1 VTFKDVAGCEEAKEELKEVVEFLKNPEKFTKLGAKIPKGVLLVGPPGTGKTLLAKAVAGEAGVPFFSISGSDFVEMFVGV 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489185780 231 GASRVRDMFDQAKKHAPCIIFIDEIDAVGRHRGAGLGGGHDEREQTLNQLLVEMDGFEMNDGIIVIAATNRPDVLDPALL 310
Cdd:cd19501   81 GASRVRDLFEQAKKNAPCIVFIDEIDAVGRKRGAGLGGGHDEREQTLNQLLVEMDGFESNTGVIVIAATNRPDVLDPALL 160
                        170
                 ....*....|.
gi 489185780 311 RPGRFDRQVVV 321
Cdd:cd19501  161 RPGRFDRQVYV 171
Peptidase_M41 pfam01434
Peptidase family M41;
403-595 3.00e-93

Peptidase family M41;


Pssm-ID: 460210 [Multi-domain]  Cd Length: 190  Bit Score: 285.65  E-value: 3.00e-93
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489185780  403 MVMSEKEKRNTAYHEAGHAIVGRLVPEHDPVYKVSIIPRGRALGVTMFLPEEDRYSLSKRALESQICSLFGGRIAEEmtL 482
Cdd:pfam01434   1 RVISEEEKKIVAYHEAGHALVGLLLPGADPVHKVTIIPRGQALGYTQFLPEEDKLLYTKEQLLARIAVLLGGRAAEE--L 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489185780  483 GFEGVTTGASNDIMRATQLARNMVTKWGLSEKLGPLMYAEEEGEVFLGRSAGSQhANVSGETAKMIDQEVRRIIDDCYGT 562
Cdd:pfam01434  79 IFGEVTTGASNDLEKATKIARQMVTEFGMSDKLGPVSLEESDGNVFLGRGMGKR-KPYSEETADIIDEEVKRLLEEAYER 157
                         170       180       190
                  ....*....|....*....|....*....|...
gi 489185780  563 AKRLLDENRDKLEMMADALMKYETIDSDQIDDI 595
Cdd:pfam01434 158 AKEILTEHRDELEALAEALLEKETLDAEEIREL 190
AAA smart00382
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ...
187-325 3.95e-21

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: 90.13  E-value: 3.95e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489185780   187 PRGVLMVGPPGTGKTLLAKAIAGEAKVP---FFTISGSDFVE--------------MFVGVGASRVRDMFDQAKKHAPCI 249
Cdd:smart00382   2 GEVILIVGPPGSGKTTLARALARELGPPgggVIYIDGEDILEevldqllliivggkKASGSGELRLRLALALARKLKPDV 81
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 489185780   250 IFIDEIDAVGRHRGaglggghdEREQTLNQLLVEMDGFEMNDGIIVIAATNRPDVLDPALLRPgRFDRQVVVGLPD 325
Cdd:smart00382  82 LILDEITSLLDAEQ--------EALLLLLEELRLLLLLKSEKNLTVILTTNDEKDLGPALLRR-RFDRRIVLLLIL 148
IS21_help_AAA NF038214
IS21-like element helper ATPase IstB; This protein family model resembles PF01695, but was ...
190-225 1.51e-03

IS21-like element helper ATPase IstB; This protein family model resembles PF01695, but was built to hit full-length AAA+ ATPases of IS21 family IS (insertion sequence) elements.


Pssm-ID: 439516  Cd Length: 232  Bit Score: 40.53  E-value: 1.51e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|.
gi 489185780 190 VLMVGPPGTGKTLLAKAIAGEA-----KVPFFTIsgSDFVE 225
Cdd:NF038214  93 VLLLGPPGTGKTHLAIALGYAAcrqgyRVRFTTA--ADLVE 131
 
Name Accession Description Interval E-value
HflB COG0465
ATP-dependent Zn proteases [Posttranslational modification, protein turnover, chaperones];
11-598 0e+00

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


Pssm-ID: 440233 [Multi-domain]  Cd Length: 583  Bit Score: 1084.68  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489185780  11 IAAVLVTVMNNFSSP-SEPQTLNYSDFIQQVKDGKVERVTVDGYVITGKRSDGD--TFKTIRPaiQDNGLIGDLVNNNVV 87
Cdd:COG0465    1 IALLLVLLFNLFSSSsSSVKEISYSEFLQLVEAGKVKSVTIQGDRITGTLKDGTktRFTTYRV--NDPELVDLLEEKGVE 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489185780  88 VEGKQPEQQSIWTQLLVASFPILVIIAVFMFFMRQMQGGGGGrggPMSFGKSKARLLSEDQVKTTFADVAGCDEAKEEVS 167
Cdd:COG0465   79 VTAKPPEESSWLLSLLISLLPILLLIGLWIFFMRRMQGGGGG---AMSFGKSKAKLYDEDKPKVTFDDVAGVDEAKEELQ 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489185780 168 ELVEFLRDPGKFQRLGGRIPRGVLMVGPPGTGKTLLAKAIAGEAKVPFFTISGSDFVEMFVGVGASRVRDMFDQAKKHAP 247
Cdd:COG0465  156 EIVDFLKDPEKFTRLGAKIPKGVLLVGPPGTGKTLLAKAVAGEAGVPFFSISGSDFVEMFVGVGASRVRDLFEQAKKNAP 235
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489185780 248 CIIFIDEIDAVGRHRGAGLGGGHDEREQTLNQLLVEMDGFEMNDGIIVIAATNRPDVLDPALLRPGRFDRQVVVGLPDIR 327
Cdd:COG0465  236 CIIFIDEIDAVGRQRGAGLGGGHDEREQTLNQLLVEMDGFEGNEGVIVIAATNRPDVLDPALLRPGRFDRQVVVDLPDVK 315
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489185780 328 GREQILKVHMRKVPLGDHVDPAVIARGTPGFSGADLANLVNEASLFAARSNKRIVDMREFELAKDKIMMGAERKTMVMSE 407
Cdd:COG0465  316 GREAILKVHARKKPLAPDVDLEVIARRTPGFSGADLANLVNEAALLAARRNKKAVTMEDFEEAIDRVIAGPERKSRVISE 395
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489185780 408 KEKRNTAYHEAGHAIVGRLVPEHDPVYKVSIIPRGRALGVTMFLPEEDRYSLSKRALESQICSLFGGRIAEEMTlgFEGV 487
Cdd:COG0465  396 KEKKITAYHEAGHALVAALLPGADPVHKVTIIPRGRALGYTMQLPEEDRYLYTKEELLDRIAVLLGGRAAEELV--FGEV 473
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489185780 488 TTGASNDIMRATQLARNMVTKWGLSEKLGPLMYAEEEGEVFLGRSaGSQHANVSGETAKMIDQEVRRIIDDCYGTAKRLL 567
Cdd:COG0465  474 TTGASNDLERATKIARAMVTEYGMSEKLGPVAYGESEGEVFLGRD-IGQSRNYSEETAREIDEEVRRIIDEAYERAKEIL 552
                        570       580       590
                 ....*....|....*....|....*....|.
gi 489185780 568 DENRDKLEMMADALMKYETIDSDQIDDIMAG 598
Cdd:COG0465  553 TENRDKLDALAEALLEKETLDGEELEEILAG 583
hflB PRK10733
ATP-dependent zinc metalloprotease FtsH;
1-639 0e+00

ATP-dependent zinc metalloprotease FtsH;


Pssm-ID: 182683 [Multi-domain]  Cd Length: 644  Bit Score: 903.25  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489185780   1 MAKNLILWLIIAAVLVTVMNNFS-SPSEPQTLNYSDFIQQVKDGKVERVTVDGYVITGKRSDGDTFKTIRPaIQDNGLIG 79
Cdd:PRK10733   1 MAKNLILWLVIAVVLMSVFQSFGpSESNGRKVDYSTFLQEVNQDQVREARINGREINVTKKDSNRYTTYIP-VNDPKLLD 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489185780  80 DLVNNNVVVEGKQPEQQSIWTQLLVASFPILVIIAVFMFFMRQMQGGGGGRGgpMSFGKSKARLLSEDQVKTTFADVAGC 159
Cdd:PRK10733  80 NLLTKNVKVVGEPPEEPSLLASIFISWFPMLLLIGVWIFFMRQMQGGGGKGA--MSFGKSKARMLTEDQIKTTFADVAGC 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489185780 160 DEAKEEVSELVEFLRDPGKFQRLGGRIPRGVLMVGPPGTGKTLLAKAIAGEAKVPFFTISGSDFVEMFVGVGASRVRDMF 239
Cdd:PRK10733 158 DEAKEEVAELVEYLREPSRFQKLGGKIPKGVLMVGPPGTGKTLLAKAIAGEAKVPFFTISGSDFVEMFVGVGASRVRDMF 237
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489185780 240 DQAKKHAPCIIFIDEIDAVGRHRGAGLGGGHDEREQTLNQLLVEMDGFEMNDGIIVIAATNRPDVLDPALLRPGRFDRQV 319
Cdd:PRK10733 238 EQAKKAAPCIIFIDEIDAVGRQRGAGLGGGHDEREQTLNQMLVEMDGFEGNEGIIVIAATNRPDVLDPALLRPGRFDRQV 317
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489185780 320 VVGLPDIRGREQILKVHMRKVPLGDHVDPAVIARGTPGFSGADLANLVNEASLFAARSNKRIVDMREFELAKDKIMMGAE 399
Cdd:PRK10733 318 VVGLPDVRGREQILKVHMRRVPLAPDIDAAIIARGTPGFSGADLANLVNEAALFAARGNKRVVSMVEFEKAKDKIMMGAE 397
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489185780 400 RKTMVMSEKEKRNTAYHEAGHAIVGRLVPEHDPVYKVSIIPRGRALGVTMFLPEEDRYSLSKRALESQICSLFGGRIAEE 479
Cdd:PRK10733 398 RRSMVMTEAQKESTAYHEAGHAIIGRLVPEHDPVHKVTIIPRGRALGVTFFLPEGDAISASRQKLESQISTLYGGRLAEE 477
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489185780 480 MTLGFEGVTTGASNDIMRATQLARNMVTKWGLSEKLGPLMYAEEEGEVFLGRS-AGSQHanVSGETAKMIDQEVRRIIDD 558
Cdd:PRK10733 478 IIYGPEHVSTGASNDIKVATNLARNMVTQWGFSEKLGPLLYAEEEGEVFLGRSvAKAKH--MSDETARIIDQEVKALIER 555
                        570       580       590       600       610       620       630       640
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489185780 559 CYGTAKRLLDENRDKLEMMADALMKYETIDSDQIDDIMAGRVPREPRDWQGGSGT----GTPPANLEESGRRENTPPIGG 634
Cdd:PRK10733 556 NYNRARQLLTDNMDILHAMKDALMKYETIDAPQIDDLMARRDVRPPAGWEEPGASnnsdDNGTPKAPRPVDEPRTPNPGN 635

                 ....*
gi 489185780 635 PAGEH 639
Cdd:PRK10733 636 TMSEQ 640
FtsH_fam TIGR01241
ATP-dependent metalloprotease FtsH; HflB(FtsH) is a pleiotropic protein required for correct ...
97-597 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: 846.57  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489185780   97 SIWTQLLVASFPILVIIAVFMFFMRQMQGGGGGRggpMSFGKSKARLLSEDQVKTTFADVAGCDEAKEEVSELVEFLRDP 176
Cdd:TIGR01241   1 SLLGFLFSLLPPILLLVGVWFFFRRQMQGGGGRA---FSFGKSKAKLLNEEKPKVTFKDVAGIDEAKEELMEIVDFLKNP 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489185780  177 GKFQRLGGRIPRGVLMVGPPGTGKTLLAKAIAGEAKVPFFTISGSDFVEMFVGVGASRVRDMFDQAKKHAPCIIFIDEID 256
Cdd:TIGR01241  78 SKFTKLGAKIPKGVLLVGPPGTGKTLLAKAVAGEAGVPFFSISGSDFVEMFVGVGASRVRDLFEQAKKNAPCIIFIDEID 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489185780  257 AVGRHRGAGLGGGHDEREQTLNQLLVEMDGFEMNDGIIVIAATNRPDVLDPALLRPGRFDRQVVVGLPDIRGREQILKVH 336
Cdd:TIGR01241 158 AVGRQRGAGLGGGNDEREQTLNQLLVEMDGFGTNTGVIVIAATNRPDVLDPALLRPGRFDRQVVVDLPDIKGREEILKVH 237
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489185780  337 MRKVPLGDHVDPAVIARGTPGFSGADLANLVNEASLFAARSNKRIVDMREFELAKDKIMMGAERKTMVMSEKEKRNTAYH 416
Cdd:TIGR01241 238 AKNKKLAPDVDLKAVARRTPGFSGADLANLLNEAALLAARKNKTEITMNDIEEAIDRVIAGPEKKSRVISEKEKKLVAYH 317
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489185780  417 EAGHAIVGRLVPEHDPVYKVSIIPRGRALGVTMFLPEEDRYSLSKRALESQICSLFGGRIAEEMTLGfeGVTTGASNDIM 496
Cdd:TIGR01241 318 EAGHALVGLLLKDADPVHKVTIIPRGQALGYTQFLPEEDKYLYTKSQLLAQIAVLLGGRAAEEIIFG--EVTTGASNDIK 395
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489185780  497 RATQLARNMVTKWGLSEKLGPLMYAEEEGEVFLGRSAGSQHaNVSGETAKMIDQEVRRIIDDCYGTAKRLLDENRDKLEM 576
Cdd:TIGR01241 396 QATNIARAMVTEWGMSDKLGPVAYGSDGGDVFLGRGFAKAK-EYSEETAREIDEEVKRIIEEAYKRAKQILTENRDELEL 474
                         490       500
                  ....*....|....*....|.
gi 489185780  577 MADALMKYETIDSDQIDDIMA 597
Cdd:TIGR01241 475 LAKALLEKETITREEIKELLA 495
ftsH CHL00176
cell division protein; Validated
7-597 0e+00

cell division protein; Validated


Pssm-ID: 214386 [Multi-domain]  Cd Length: 638  Bit Score: 639.40  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489185780   7 LWLIIAAVLVTVMNNFSSPSEP-QTLNYSDFIQQVKDGKVERVTVDGYVITG--KRSD-----------------GDTFK 66
Cdd:CHL00176  13 LPLIVEKFTVWDVFYYSSVEDGlKSPNNPDVVQNKASSRMTYGRFLEYLDMGwiKKVDlydngrtaiveasspelGNRPQ 92
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489185780  67 TIRPAI--QDNGLIGDLVNNNVVVEGKQPEQQS-IWTQLLVASFPILVIIAVFMFFMRQMQGGGGGRGGPMSFGKSKARL 143
Cdd:CHL00176  93 RIRVELpvGASELIQKLKEANIDFDAHPPVLKSnIVTILSNLLLPLILIGVLWFFFQRSSNFKGGPGQNLMNFGKSKARF 172
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489185780 144 LSEDQVKTTFADVAGCDEAKEEVSELVEFLRDPGKFQRLGGRIPRGVLMVGPPGTGKTLLAKAIAGEAKVPFFTISGSDF 223
Cdd:CHL00176 173 QMEADTGITFRDIAGIEEAKEEFEEVVSFLKKPERFTAVGAKIPKGVLLVGPPGTGKTLLAKAIAGEAEVPFFSISGSEF 252
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489185780 224 VEMFVGVGASRVRDMFDQAKKHAPCIIFIDEIDAVGRHRGAGLGGGHDEREQTLNQLLVEMDGFEMNDGIIVIAATNRPD 303
Cdd:CHL00176 253 VEMFVGVGAARVRDLFKKAKENSPCIVFIDEIDAVGRQRGAGIGGGNDEREQTLNQLLTEMDGFKGNKGVIVIAATNRVD 332
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489185780 304 VLDPALLRPGRFDRQVVVGLPDIRGREQILKVHMRKVPLGDHVDPAVIARGTPGFSGADLANLVNEASLFAARSNKRIVD 383
Cdd:CHL00176 333 ILDAALLRPGRFDRQITVSLPDREGRLDILKVHARNKKLSPDVSLELIARRTPGFSGADLANLLNEAAILTARRKKATIT 412
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489185780 384 MREFELAKDKIMMGAERKTMVMSeKEKRNTAYHEAGHAIVGRLVPEHDPVYKVSIIPRGRALGVTMFLPEEDRYSLSKRA 463
Cdd:CHL00176 413 MKEIDTAIDRVIAGLEGTPLEDS-KNKRLIAYHEVGHAIVGTLLPNHDPVQKVTLIPRGQAKGLTWFTPEEDQSLVSRSQ 491
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489185780 464 LESQICSLFGGRIAEEMTLGFEGVTTGASNDIMRATQLARNMVTKWGLSeKLGPL-MYAEEEGEVFLGRSAGSQHaNVSG 542
Cdd:CHL00176 492 ILARIVGALGGRAAEEVVFGSTEVTTGASNDLQQVTNLARQMVTRFGMS-SIGPIsLESNNSTDPFLGRFMQRNS-EYSE 569
                        570       580       590       600       610
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 489185780 543 ETAKMIDQEVRRIIDDCYGTAKRLLDENRDKLEMMADALMKYETIDSDQIDDIMA 597
Cdd:CHL00176 570 EIADKIDMEVRSILHTCYQYAYQILKDNRVLIDLLVELLLQKETIDGDEFREIVN 624
RecA-like_FtsH cd19501
ATP-dependent zinc metalloprotease FtsH; FtsH ATPase is a processive, ATP-dependent zinc ...
151-321 4.90e-128

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: 374.26  E-value: 4.90e-128
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489185780 151 TTFADVAGCDEAKEEVSELVEFLRDPGKFQRLGGRIPRGVLMVGPPGTGKTLLAKAIAGEAKVPFFTISGSDFVEMFVGV 230
Cdd:cd19501    1 VTFKDVAGCEEAKEELKEVVEFLKNPEKFTKLGAKIPKGVLLVGPPGTGKTLLAKAVAGEAGVPFFSISGSDFVEMFVGV 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489185780 231 GASRVRDMFDQAKKHAPCIIFIDEIDAVGRHRGAGLGGGHDEREQTLNQLLVEMDGFEMNDGIIVIAATNRPDVLDPALL 310
Cdd:cd19501   81 GASRVRDLFEQAKKNAPCIVFIDEIDAVGRKRGAGLGGGHDEREQTLNQLLVEMDGFESNTGVIVIAATNRPDVLDPALL 160
                        170
                 ....*....|.
gi 489185780 311 RPGRFDRQVVV 321
Cdd:cd19501  161 RPGRFDRQVYV 171
RPT1 COG1222
ATP-dependent 26S proteasome regulatory subunit [Posttranslational modification, protein ...
145-403 1.66e-114

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


Pssm-ID: 440835 [Multi-domain]  Cd Length: 326  Bit Score: 345.45  E-value: 1.66e-114
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489185780 145 SEDQVKTTFADVAGCDEAKEEVSELVE-FLRDPGKFQRLGGRIPRGVLMVGPPGTGKTLLAKAIAGEAKVPFFTISGSDF 223
Cdd:COG1222   69 PAESPDVTFDDIGGLDEQIEEIREAVElPLKNPELFRKYGIEPPKGVLLYGPPGTGKTLLAKAVAGELGAPFIRVRGSEL 148
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489185780 224 VEMFVGVGASRVRDMFDQAKKHAPCIIFIDEIDAVGRHRGAGlgGGHDEREQTLNQLLVEMDGFEMNDGIIVIAATNRPD 303
Cdd:COG1222  149 VSKYIGEGARNVREVFELAREKAPSIIFIDEIDAIAARRTDD--GTSGEVQRTVNQLLAELDGFESRGDVLIIAATNRPD 226
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489185780 304 VLDPALLRPGRFDRQVVVGLPDIRGREQILKVHMRKVPLGDHVDPAVIARGTPGFSGADLANLVNEASLFAARSNKRIVD 383
Cdd:COG1222  227 LLDPALLRPGRFDRVIEVPLPDEEAREEILKIHLRDMPLADDVDLDKLAKLTEGFSGADLKAIVTEAGMFAIREGRDTVT 306
                        250       260
                 ....*....|....*....|
gi 489185780 384 MREFELAKDKIMMGAERKTM 403
Cdd:COG1222  307 MEDLEKAIEKVKKKTETATN 326
PRK03992 PRK03992
proteasome-activating nucleotidase; Provisional
146-407 2.90e-99

proteasome-activating nucleotidase; Provisional


Pssm-ID: 179699 [Multi-domain]  Cd Length: 389  Bit Score: 308.68  E-value: 2.90e-99
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489185780 146 EDQVKTTFADVAGCDEAKEEVSELVEF-LRDPGKFQRLGGRIPRGVLMVGPPGTGKTLLAKAIAGEAKVPFFTISGSDFV 224
Cdd:PRK03992 123 IESPNVTYEDIGGLEEQIREVREAVELpLKKPELFEEVGIEPPKGVLLYGPPGTGKTLLAKAVAHETNATFIRVVGSELV 202
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489185780 225 EMFVGVGASRVRDMFDQAKKHAPCIIFIDEIDAVGRHRGAGLGGGHDEREQTLNQLLVEMDGFEMNDGIIVIAATNRPDV 304
Cdd:PRK03992 203 QKFIGEGARLVRELFELAREKAPSIIFIDEIDAIAAKRTDSGTSGDREVQRTLMQLLAEMDGFDPRGNVKIIAATNRIDI 282
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489185780 305 LDPALLRPGRFDRQVVVGLPDIRGREQILKVHMRKVPLGDHVDPAVIARGTPGFSGADLANLVNEASLFAARSNKRIVDM 384
Cdd:PRK03992 283 LDPAILRPGRFDRIIEVPLPDEEGRLEILKIHTRKMNLADDVDLEELAELTEGASGADLKAICTEAGMFAIRDDRTEVTM 362
                        250       260
                 ....*....|....*....|...
gi 489185780 385 REFELAKDKIMMGAERKTMVMSE 407
Cdd:PRK03992 363 EDFLKAIEKVMGKEEKDSMEEPG 385
Peptidase_M41 pfam01434
Peptidase family M41;
403-595 3.00e-93

Peptidase family M41;


Pssm-ID: 460210 [Multi-domain]  Cd Length: 190  Bit Score: 285.65  E-value: 3.00e-93
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489185780  403 MVMSEKEKRNTAYHEAGHAIVGRLVPEHDPVYKVSIIPRGRALGVTMFLPEEDRYSLSKRALESQICSLFGGRIAEEmtL 482
Cdd:pfam01434   1 RVISEEEKKIVAYHEAGHALVGLLLPGADPVHKVTIIPRGQALGYTQFLPEEDKLLYTKEQLLARIAVLLGGRAAEE--L 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489185780  483 GFEGVTTGASNDIMRATQLARNMVTKWGLSEKLGPLMYAEEEGEVFLGRSAGSQhANVSGETAKMIDQEVRRIIDDCYGT 562
Cdd:pfam01434  79 IFGEVTTGASNDLEKATKIARQMVTEFGMSDKLGPVSLEESDGNVFLGRGMGKR-KPYSEETADIIDEEVKRLLEEAYER 157
                         170       180       190
                  ....*....|....*....|....*....|...
gi 489185780  563 AKRLLDENRDKLEMMADALMKYETIDSDQIDDI 595
Cdd:pfam01434 158 AKEILTEHRDELEALAEALLEKETLDAEEIREL 190
26Sp45 TIGR01242
26S proteasome subunit P45 family; Many proteins may score above the trusted cutoff because an ...
146-395 1.20e-83

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: 267.05  E-value: 1.20e-83
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489185780  146 EDQVKTTFADVAGCDEAKEEVSELVEF-LRDPGKFQRLGGRIPRGVLMVGPPGTGKTLLAKAIAGEAKVPFFTISGSDFV 224
Cdd:TIGR01242 114 EERPNVSYEDIGGLEEQIREIREAVELpLKHPELFEEVGIEPPKGVLLYGPPGTGKTLLAKAVAHETNATFIRVVGSELV 193
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489185780  225 EMFVGVGASRVRDMFDQAKKHAPCIIFIDEIDAVGRHRGAGLGGGHDEREQTLNQLLVEMDGFEMNDGIIVIAATNRPDV 304
Cdd:TIGR01242 194 RKYIGEGARLVREIFELAKEKAPSIIFIDEIDAIAAKRTDSGTSGDREVQRTLMQLLAELDGFDPRGNVKVIAATNRPDI 273
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489185780  305 LDPALLRPGRFDRQVVVGLPDIRGREQILKVHMRKVPLGDHVDPAVIARGTPGFSGADLANLVNEASLFAARSNKRIVDM 384
Cdd:TIGR01242 274 LDPALLRPGRFDRIIEVPLPDFEGRLEILKIHTRKMKLAEDVDLEAIAKMTEGASGADLKAICTEAGMFAIREERDYVTM 353
                         250
                  ....*....|.
gi 489185780  385 REFELAKDKIM 395
Cdd:TIGR01242 354 DDFIKAVEKVL 364
SpoVK COG0464
AAA+-type ATPase, SpoVK/Ycf46/Vps4 family [Cell wall/membrane/envelope biogenesis, Cell cycle ...
153-400 7.68e-81

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: 261.00  E-value: 7.68e-81
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489185780 153 FADVAGCDEAKEEVSELVE-FLRDPGKFQRLGGRIPRGVLMVGPPGTGKTLLAKAIAGEAKVPFFTISGSDFVEMFVGVG 231
Cdd:COG0464  156 LDDLGGLEEVKEELRELVAlPLKRPELREEYGLPPPRGLLLYGPPGTGKTLLARALAGELGLPLIEVDLSDLVSKYVGET 235
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489185780 232 ASRVRDMFDQAKKHAPCIIFIDEIDAVGRHRGaGLGGGHDEREqtLNQLLVEMDGFEmnDGIIVIAATNRPDVLDPALLR 311
Cdd:COG0464  236 EKNLREVFDKARGLAPCVLFIDEADALAGKRG-EVGDGVGRRV--VNTLLTEMEELR--SDVVVIAATNRPDLLDPALLR 310
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489185780 312 pgRFDRQVVVGLPDIRGREQILKVHMRKVPLGDHVDPAVIARGTPGFSGADLANLVNEASLFAARSNKRIVDMREFELAK 391
Cdd:COG0464  311 --RFDEIIFFPLPDAEERLEIFRIHLRKRPLDEDVDLEELAEATEGLSGADIRNVVRRAALQALRLGREPVTTEDLLEAL 388

                 ....*....
gi 489185780 392 DKIMMGAER 400
Cdd:COG0464  389 EREDIFLKR 397
CDC48 TIGR01243
AAA family ATPase, CDC48 subfamily; This subfamily of the AAA family ATPases includes two ...
155-408 5.08e-70

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: 241.35  E-value: 5.08e-70
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489185780  155 DVAGCDEAKEEVSELVEF-LRDPGKFQRLGGRIPRGVLMVGPPGTGKTLLAKAIAGEAKVPFFTISGSDFVEMFVGVGAS 233
Cdd:TIGR01243 454 DIGGLEEVKQELREAVEWpLKHPEIFEKMGIRPPKGVLLFGPPGTGKTLLAKAVATESGANFIAVRGPEILSKWVGESEK 533
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489185780  234 RVRDMFDQAKKHAPCIIFIDEIDAVGRHRGAGLGGGHDEReqTLNQLLVEMDGFEMNDGIIVIAATNRPDVLDPALLRPG 313
Cdd:TIGR01243 534 AIREIFRKARQAAPAIIFFDEIDAIAPARGARFDTSVTDR--IVNQLLTEMDGIQELSNVVVIAATNRPDILDPALLRPG 611
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489185780  314 RFDRQVVVGLPDIRGREQILKVHMRKVPLGDHVDPAVIARGTPGFSGADLANLVNEASLFAAR----------------- 376
Cdd:TIGR01243 612 RFDRLILVPPPDEEARKEIFKIHTRSMPLAEDVDLEELAEMTEGYTGADIEAVCREAAMAALResigspakeklevgeee 691
                         250       260       270
                  ....*....|....*....|....*....|...
gi 489185780  377 -SNKRIVDMREFELAKDKIMMGAERKTMVMSEK 408
Cdd:TIGR01243 692 fLKDLKVEMRHFLEALKKVKPSVSKEDMLRYER 724
RecA-like_PAN_like cd19502
proteasome activating nucleotidase PAN and related proteasome subunits; This subfamily ...
152-319 3.59e-67

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


Pssm-ID: 410910 [Multi-domain]  Cd Length: 171  Bit Score: 216.82  E-value: 3.59e-67
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489185780 152 TFADVAGCDEAKEEVSELVEF-LRDPGKFQRLGGRIPRGVLMVGPPGTGKTLLAKAIAGEAKVPFFTISGSDFVEMFVGV 230
Cdd:cd19502    1 TYEDIGGLDEQIREIREVVELpLKHPELFEELGIEPPKGVLLYGPPGTGKTLLAKAVANHTDATFIRVVGSELVQKYIGE 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489185780 231 GASRVRDMFDQAKKHAPCIIFIDEIDAVGRHRGAGLGGGHDEREQTLNQLLVEMDGFEMNDGIIVIAATNRPDVLDPALL 310
Cdd:cd19502   81 GARLVRELFEMAREKAPSIIFIDEIDAIGAKRFDSGTGGDREVQRTMLELLNQLDGFDPRGNIKVIMATNRPDILDPALL 160

                 ....*....
gi 489185780 311 RPGRFDRQV 319
Cdd:cd19502  161 RPGRFDRKI 169
RecA-like_protease cd19481
proteases similar to RecA; RecA-like NTPases. This family includes the NTP binding domain of ...
162-319 1.80e-66

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: 214.45  E-value: 1.80e-66
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489185780 162 AKEEVSELVEFLRDPGKFQRLGGRIPRGVLMVGPPGTGKTLLAKAIAGEAKVPFFTISGSDFVEMFVGVGASRVRDMFDQ 241
Cdd:cd19481    1 LKASLREAVEAPRRGSRLRRYGLGLPKGILLYGPPGTGKTLLAKALAGELGLPLIVVKLSSLLSKYVGESEKNLRKIFER 80
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 489185780 242 AKKHAPCIIFIDEIDAVGRHRGAglGGGHDEREQTLNQLLVEMDGFEMNDGIIVIAATNRPDVLDPALLRPGRFDRQV 319
Cdd:cd19481   81 ARRLAPCILFIDEIDAIGRKRDS--SGESGELRRVLNQLLTELDGVNSRSKVLVIAATNRPDLLDPALLRPGRFDEVI 156
COG1223 COG1223
Predicted ATPase, AAA+ superfamily [General function prediction only];
153-411 1.39e-64

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


Pssm-ID: 440836 [Multi-domain]  Cd Length: 246  Bit Score: 212.82  E-value: 1.39e-64
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489185780 153 FADVAGCDEAKEEVSELVEFLRDPGKFQRLGGRIPRGVLMVGPPGTGKTLLAKAIAGEAKVPFFTISGSDFVEMFVGVGA 232
Cdd:COG1223    1 LDDVVGQEEAKKKLKLIIKELRRRENLRKFGLWPPRKILFYGPPGTGKTMLAEALAGELKLPLLTVRLDSLIGSYLGETA 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489185780 233 SRVRDMFDQAKKhAPCIIFIDEIDAVGRHRGAglGGGHDEREQTLNQLLVEMDGfeMNDGIIVIAATNRPDVLDPALLRp 312
Cdd:COG1223   81 RNLRKLFDFARR-APCVIFFDEFDAIAKDRGD--QNDVGEVKRVVNALLQELDG--LPSGSVVIAATNHPELLDSALWR- 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489185780 313 gRFDRQVVVGLPDIRGREQILKVHMRKVPLGDHVDPAVIARGTPGFSGADLANLVNEAslfaarSNKRIVDMREFELAKD 392
Cdd:COG1223  155 -RFDEVIEFPLPDKEERKEILELNLKKFPLPFELDLKKLAKKLEGLSGADIEKVLKTA------LKKAILEDREKVTKED 227
                        250
                 ....*....|....*....
gi 489185780 393 KIMMGAERKTMVMSEKEKR 411
Cdd:COG1223  228 LEEALKQRKERKKEPKKEG 246
CDC48 TIGR01243
AAA family ATPase, CDC48 subfamily; This subfamily of the AAA family ATPases includes two ...
150-376 1.32e-63

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


Pssm-ID: 273521 [Multi-domain]  Cd Length: 733  Bit Score: 223.63  E-value: 1.32e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489185780  150 KTTFADVAGCDEAKEEVSELVEF-LRDPGKFQRLGGRIPRGVLMVGPPGTGKTLLAKAIAGEAKVPFFTISGSDFVEMFV 228
Cdd:TIGR01243 174 KVTYEDIGGLKEAKEKIREMVELpMKHPELFEHLGIEPPKGVLLYGPPGTGKTLLAKAVANEAGAYFISINGPEIMSKYY 253
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489185780  229 GVGASRVRDMFDQAKKHAPCIIFIDEIDAVGRHRGAGLGgghDEREQTLNQLLVEMDGFEMNDGIIVIAATNRPDVLDPA 308
Cdd:TIGR01243 254 GESEERLREIFKEAEENAPSIIFIDEIDAIAPKREEVTG---EVEKRVVAQLLTLMDGLKGRGRVIVIGATNRPDALDPA 330
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 489185780  309 LLRPGRFDRQVVVGLPDIRGREQILKVHMRKVPLGDHVDPAVIARGTPGFSGADLANLVNEASLFAAR 376
Cdd:TIGR01243 331 LRRPGRFDREIVIRVPDKRARKEILKVHTRNMPLAEDVDLDKLAEVTHGFVGADLAALAKEAAMAALR 398
PTZ00454 PTZ00454
26S protease regulatory subunit 6B-like protein; Provisional
143-390 9.63e-63

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


Pssm-ID: 240423 [Multi-domain]  Cd Length: 398  Bit Score: 213.09  E-value: 9.63e-63
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489185780 143 LLSEDQVKTTFADVAGCDEAKEEVSELVEF-LRDPGKFQRLGGRIPRGVLMVGPPGTGKTLLAKAIAGEAKVPFFTISGS 221
Cdd:PTZ00454 134 LQMSEKPDVTYSDIGGLDIQKQEIREAVELpLTCPELYEQIGIDPPRGVLLYGPPGTGKTMLAKAVAHHTTATFIRVVGS 213
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489185780 222 DFVEMFVGVGASRVRDMFDQAKKHAPCIIFIDEIDAVGRHRGAGLGGGHDEREQTLNQLLVEMDGFEMNDGIIVIAATNR 301
Cdd:PTZ00454 214 EFVQKYLGEGPRMVRDVFRLARENAPSIIFIDEVDSIATKRFDAQTGADREVQRILLELLNQMDGFDQTTNVKVIMATNR 293
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489185780 302 PDVLDPALLRPGRFDRQVVVGLPDIRGREQILKVHMRKVPLGDHVDPAVIARGTPGFSGADLANLVNEASLFAARSNKRI 381
Cdd:PTZ00454 294 ADTLDPALLRPGRLDRKIEFPLPDRRQKRLIFQTITSKMNLSEEVDLEDFVSRPEKISAADIAAICQEAGMQAVRKNRYV 373

                 ....*....
gi 489185780 382 VDMREFELA 390
Cdd:PTZ00454 374 ILPKDFEKG 382
RecA-like_CDC48_r2-like cd19511
second of two ATPase domains of CDC48/p97, PEX1 and -6, VAT and NVL, and similar ATPase ...
162-321 5.75e-62

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


Pssm-ID: 410919 [Multi-domain]  Cd Length: 159  Bit Score: 202.90  E-value: 5.75e-62
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489185780 162 AKEEVSELVEF-LRDPGKFQRLGGRIPRGVLMVGPPGTGKTLLAKAIAGEAKVPFFTISGSDFVEMFVGVGASRVRDMFD 240
Cdd:cd19511    1 VKRELKEAVEWpLKHPDAFKRLGIRPPKGVLLYGPPGCGKTLLAKALASEAGLNFISVKGPELFSKYVGESERAVREIFQ 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489185780 241 QAKKHAPCIIFIDEIDAVGRHRGAGLGGGHDEReqTLNQLLVEMDGFEMNDGIIVIAATNRPDVLDPALLRPGRFDRQVV 320
Cdd:cd19511   81 KARQAAPCIIFFDEIDSLAPRRGQSDSSGVTDR--VVSQLLTELDGIESLKGVVVIAATNRPDMIDPALLRPGRLDKLIY 158

                 .
gi 489185780 321 V 321
Cdd:cd19511  159 V 159
RecA-like_CDC48_NLV2_r1-like cd19503
first of two ATPase domains of CDC48 and NLV2, and similar ATPase domains; CDC48 in yeast and ...
155-321 1.91e-58

first of two ATPase domains of CDC48 and NLV2, and similar ATPase domains; CDC48 in yeast and p97 or VCP metazoans is an ATP-dependent molecular chaperone which plays an essential role in many cellular processes, by segregating polyubiquitinated proteins from complexes or membranes. Cdc48/p97 consists of an N-terminal domain and two ATPase domains; this subfamily represents the first of the two ATPase domains. This subfamily also includes the first of the two ATPase domains of NVL (nuclear VCP-like protein) 2, an isoform of NVL mainly present in the nucleolus, which is involved in ribosome biogenesis, in telomerase assembly and the regulation of telomerase activity, and in pre-rRNA processing. This subfamily belongs to the RecA-like NTPase family which includes the NTP binding domain of F1 and V1 H(+)ATPases, DnaB and related helicases as well as bacterial RecA and related eukaryotic and archaeal recombinases. The RecA-like NTPase family also includes bacterial conjugation proteins and related DNA transfer proteins involved in type II and type IV secretion.


Pssm-ID: 410911 [Multi-domain]  Cd Length: 165  Bit Score: 193.66  E-value: 1.91e-58
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489185780 155 DVAGCDEAKEEVSELVEF-LRDPGKFQRLGGRIPRGVLMVGPPGTGKTLLAKAIAGEAKVPFFTISGSDFVEMFVGVGAS 233
Cdd:cd19503    1 DIGGLDEQIASLKELIELpLKYPELFRALGLKPPRGVLLHGPPGTGKTLLARAVANEAGANFLSISGPSIVSKYLGESEK 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489185780 234 RVRDMFDQAKKHAPCIIFIDEIDAVGRHRGAglggGHDEREQTL-NQLLVEMDGFEMNDGIIVIAATNRPDVLDPALLRP 312
Cdd:cd19503   81 NLREIFEEARSHAPSIIFIDEIDALAPKREE----DQREVERRVvAQLLTLMDGMSSRGKVVVIAATNRPDAIDPALRRP 156

                 ....*....
gi 489185780 313 GRFDRQVVV 321
Cdd:cd19503  157 GRFDREVEI 165
PTZ00361 PTZ00361
26 proteosome regulatory subunit 4-like protein; Provisional
152-395 3.12e-58

26 proteosome regulatory subunit 4-like protein; Provisional


Pssm-ID: 185575 [Multi-domain]  Cd Length: 438  Bit Score: 202.31  E-value: 3.12e-58
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489185780 152 TFADVAGCDEAKEEVSELVEF-LRDPGKFQRLGGRIPRGVLMVGPPGTGKTLLAKAIAGEAKVPFFTISGSDFVEMFVGV 230
Cdd:PTZ00361 181 SYADIGGLEQQIQEIKEAVELpLTHPELYDDIGIKPPKGVILYGPPGTGKTLLAKAVANETSATFLRVVGSELIQKYLGD 260
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489185780 231 GASRVRDMFDQAKKHAPCIIFIDEIDAVGRHRGAGLGGGHDEREQTLNQLLVEMDGFEMNDGIIVIAATNRPDVLDPALL 310
Cdd:PTZ00361 261 GPKLVRELFRVAEENAPSIVFIDEIDAIGTKRYDATSGGEKEIQRTMLELLNQLDGFDSRGDVKVIMATNRIESLDPALI 340
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489185780 311 RPGRFDRQVVVGLPDIRGREQILKVHMRKVPLGDHVDPAVIARGTPGFSGADLANLVNEASLFAARSNKRIVDMREFELA 390
Cdd:PTZ00361 341 RPGRIDRKIEFPNPDEKTKRRIFEIHTSKMTLAEDVDLEEFIMAKDELSGADIKAICTEAGLLALRERRMKVTQADFRKA 420

                 ....*
gi 489185780 391 KDKIM 395
Cdd:PTZ00361 421 KEKVL 425
AAA pfam00004
ATPase family associated with various cellular activities (AAA); AAA family proteins often ...
190-323 4.76e-56

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: 185.87  E-value: 4.76e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489185780  190 VLMVGPPGTGKTLLAKAIAGEAKVPFFTISGSDFVEMFVGVGASRVRDMFDQAKKHAPCIIFIDEIDAVGRHRGaglGGG 269
Cdd:pfam00004   1 LLLYGPPGTGKTTLAKAVAKELGAPFIEISGSELVSKYVGESEKRLRELFEAAKKLAPCVIFIDEIDALAGSRG---SGG 77
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 489185780  270 HDEREQTLNQLLVEMDGFE-MNDGIIVIAATNRPDVLDPALLrpGRFDRQVVVGL 323
Cdd:pfam00004  78 DSESRRVVNQLLTELDGFTsSNSKVIVIAATNRPDKLDPALL--GRFDRIIEFPL 130
RecA-like_VCP_r2 cd19529
second of two ATPase domains of Valosin-containing protein-like ATPase (VAT) and similar ...
162-321 2.96e-55

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


Pssm-ID: 410937 [Multi-domain]  Cd Length: 159  Bit Score: 185.01  E-value: 2.96e-55
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489185780 162 AKEEVSELVEF-LRDPGKFQRLGGRIPRGVLMVGPPGTGKTLLAKAIAGEAKVPFFTISGSDFVEMFVGVGASRVRDMFD 240
Cdd:cd19529    1 VKQELKEAVEWpLLKPEVFKRLGIRPPKGILLYGPPGTGKTLLAKAVATESNANFISVKGPELLSKWVGESEKAIREIFR 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489185780 241 QAKKHAPCIIFIDEIDAVGRHRGAGLGGGHDEReqTLNQLLVEMDGFEMNDGIIVIAATNRPDVLDPALLRPGRFDRQVV 320
Cdd:cd19529   81 KARQVAPCVIFFDEIDSIAPRRGTTGDSGVTER--VVNQLLTELDGLEEMNGVVVIAATNRPDIIDPALLRAGRFDRLIY 158

                 .
gi 489185780 321 V 321
Cdd:cd19529  159 I 159
RecA-like_CDC48_r2-like cd19528
second of two ATPase domains of CDC48 and similar ATPase domains; CDC48 in yeast and p97 or ...
163-321 5.82e-55

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: 184.25  E-value: 5.82e-55
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489185780 163 KEEVSELVEF-LRDPGKFQRLGGRIPRGVLMVGPPGTGKTLLAKAIAGEAKVPFFTISGSDFVEMFVGVGASRVRDMFDQ 241
Cdd:cd19528    2 KRELQELVQYpVEHPDKFLKFGMTPSKGVLFYGPPGCGKTLLAKAIANECQANFISVKGPELLTMWFGESEANVRDIFDK 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489185780 242 AKKHAPCIIFIDEIDAVGRHRGAGLGGGHDEREQTLNQLLVEMDGFEMNDGIIVIAATNRPDVLDPALLRPGRFDRQVVV 321
Cdd:cd19528   82 ARAAAPCVLFFDELDSIAKARGGNIGDAGGAADRVINQILTEMDGMNTKKNVFIIGATNRPDIIDPAILRPGRLDQLIYI 161
RecA-like_CDC48_r1-like cd19519
first of two ATPase domains of CDC48 and similar ATPase domains; CDC48 in yeast and p97 or VCP ...
155-322 9.09e-52

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: 176.09  E-value: 9.09e-52
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489185780 155 DVAGCDEAKEEVSELVEF-LRDPGKFQRLGGRIPRGVLMVGPPGTGKTLLAKAIAGEAKVPFFTISGSDFVEMFVGVGAS 233
Cdd:cd19519    1 DIGGCRKQLAQIREMVELpLRHPELFKAIGIKPPRGILLYGPPGTGKTLIARAVANETGAFFFLINGPEIMSKLAGESES 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489185780 234 RVRDMFDQAKKHAPCIIFIDEIDAVGRHRGAglggGHDEREQTL-NQLLVEMDGFEMNDGIIVIAATNRPDVLDPALLRP 312
Cdd:cd19519   81 NLRKAFEEAEKNAPAIIFIDEIDAIAPKREK----THGEVERRIvSQLLTLMDGLKQRAHVIVMAATNRPNSIDPALRRF 156
                        170
                 ....*....|
gi 489185780 313 GRFDRQVVVG 322
Cdd:cd19519  157 GRFDREIDIG 166
RecA-like_NVL_r1-like cd19518
first of two ATPase domains of NVL (nuclear VCP-like protein) and similar ATPase domains; NVL ...
155-319 2.37e-48

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: 166.81  E-value: 2.37e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489185780 155 DVAGCDEAKEEVSELVEFLRDPGK-FQRLGGRIPRGVLMVGPPGTGKTLLAKAIAGEAKVPFFTISGSDFVEMFVGVGAS 233
Cdd:cd19518    1 DIGGMDSTLKELCELLIHPILPPEyFQHLGVEPPRGVLLHGPPGCGKTMLANAIAGELKVPFLKISATEIVSGVSGESEE 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489185780 234 RVRDMFDQAKKHAPCIIFIDEIDAVGRHRGaglGGGHDEREQTLNQLLVEMDGFEMND----GIIVIAATNRPDVLDPAL 309
Cdd:cd19518   81 KIRELFDQAISNAPCIVFIDEIDAITPKRE---SAQREMERRIVSQLLTCMDELNNEKtaggPVLVIGATNRPDSLDPAL 157
                        170
                 ....*....|
gi 489185780 310 LRPGRFDRQV 319
Cdd:cd19518  158 RRAGRFDREI 167
RecA-like_NVL_r2-like cd19530
second of two ATPase domains of NVL (nuclear VCP-like protein) and similar ATPase domains; NVL ...
173-321 1.88e-47

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: 164.20  E-value: 1.88e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489185780 173 LRDPGKFQRLGGRIPRGVLMVGPPGTGKTLLAKAIAGEAKVPFFTISGSDFVEMFVGVGASRVRDMFDQAKKHAPCIIFI 252
Cdd:cd19530   16 IKRPDIYKALGIDLPTGVLLYGPPGCGKTLLAKAVANESGANFISVKGPELLNKYVGESERAVRQVFQRARASAPCVIFF 95
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 489185780 253 DEIDAVGRHRGAGLGGGhdeREQTLNQLLVEMDGFEMNDGIIVIAATNRPDVLDPALLRPGRFDRQVVV 321
Cdd:cd19530   96 DEVDALVPKRGDGGSWA---SERVVNQLLTEMDGLEERSNVFVIAATNRPDIIDPAMLRPGRLDKTLYV 161
RecA-like_PEX1_r2 cd19526
second of two ATPase domains of Peroxisomal biogenesis factor 1 (PEX1); PEX1(also known as ...
162-319 2.12e-42

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: 150.27  E-value: 2.12e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489185780 162 AKEEVSELVEF-LRDPGKFQRLGGRIPRGVLMVGPPGTGKTLLAKAIAGEAKVPFFTISGSDFVEMFVGVGASRVRDMFD 240
Cdd:cd19526    1 VKKALEETIEWpSKYPKIFASSPLRLRSGILLYGPPGCGKTLLASAIASECGLNFISVKGPELLNKYIGASEQNVRDLFS 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489185780 241 QAKKHAPCIIFIDEIDAVGRHRgaglggGHDER---EQTLNQLLVEMDGFEMNDGIIVIAATNRPDVLDPALLRPGRFDR 317
Cdd:cd19526   81 RAQSAKPCILFFDEFDSIAPKR------GHDSTgvtDRVVNQLLTQLDGVEGLDGVYVLAATSRPDLIDPALLRPGRLDK 154

                 ..
gi 489185780 318 QV 319
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 ...
156-321 4.22e-40

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: 144.03  E-value: 4.22e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489185780 156 VAGCDEAKEEVSELV--EFLRdPGKFqRLGGRIPRGVLMVGPPGTGKTLLAKAIAGEAKVPFFTISGSDFVEMFVGVGAS 233
Cdd:cd19509    1 IAGLDDAKEALKEAVilPSLR-PDLF-PGLRGPPRGILLYGPPGTGKTLLARAVASESGSTFFSISASSLVSKWVGESEK 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489185780 234 RVRDMFDQAKKHAPCIIFIDEIDAVGRHRGAglgGGHDEREQTLNQLLVEMDGFE--MNDGIIVIAATNRPDVLDPALLR 311
Cdd:cd19509   79 IVRALFALARELQPSIIFIDEIDSLLSERGS---GEHEASRRVKTEFLVQMDGVLnkPEDRVLVLGATNRPWELDEAFLR 155
                        170
                 ....*....|
gi 489185780 312 pgRFDRQVVV 321
Cdd:cd19509  156 --RFEKRIYI 163
RecA-like_PEX6_r2 cd19527
second of two ATPase domains of Peroxisomal biogenesis factor 6 (PEX6); PEX6(also known as ...
163-321 4.76e-40

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: 143.81  E-value: 4.76e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489185780 163 KEEVSELVEF-LRDPGKFQrLGGRIPRGVLMVGPPGTGKTLLAKAIAGEAKVPFFTISGSDFVEMFVGVGASRVRDMFDQ 241
Cdd:cd19527    2 KKEILDTIQLpLEHPELFS-SGLRKRSGILLYGPPGTGKTLLAKAIATECSLNFLSVKGPELINMYIGESEANVREVFQK 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489185780 242 AKKHAPCIIFIDEIDAVGRHRGA-GLGGGHDEReqTLNQLLVEMDGFE-MNDGIIVIAATNRPDVLDPALLRPGRFDRQV 319
Cdd:cd19527   81 ARDAKPCVIFFDELDSLAPSRGNsGDSGGVMDR--VVSQLLAELDGMSsSGQDVFVIGATNRPDLLDPALLRPGRFDKLL 158

                 ..
gi 489185780 320 VV 321
Cdd:cd19527  159 YL 160
RecA-like_VPS4 cd19521
ATPase domain of vacuolar protein sorting-associated protein 4; Vacuolar protein ...
153-321 2.53e-37

ATPase domain of vacuolar protein sorting-associated protein 4; Vacuolar protein sorting-associated protein 4 (Vps4) is believed to be involved in intracellular protein transport out of a prevacuolar endosomal compartment. This subfamily belongs to the RecA-like NTPase family which includes the NTP binding domain of F1 and V1 H(+)ATPases, DnaB and related helicases as well as bacterial RecA and related eukaryotic and archaeal recombinases. The RecA-like NTPase family also includes bacterial conjugation proteins and related DNA transfer proteins involved in type II and type IV secretion.


Pssm-ID: 410929 [Multi-domain]  Cd Length: 170  Bit Score: 136.53  E-value: 2.53e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489185780 153 FADVAGCDEAKEEVSELVEFlrdPGKFQRL--GGRIP-RGVLMVGPPGTGKTLLAKAIAGEAKVPFFTISGSDFVEMFVG 229
Cdd:cd19521    6 WEDVAGLEGAKEALKEAVIL---PVKFPHLftGNRKPwSGILLYGPPGTGKSYLAKAVATEANSTFFSVSSSDLVSKWMG 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489185780 230 VGASRVRDMFDQAKKHAPCIIFIDEIDAVGRHRGAglgGGHDEREQTLNQLLVEMDGFEMN-DGIIVIAATNRPDVLDPA 308
Cdd:cd19521   83 ESEKLVKQLFAMARENKPSIIFIDEVDSLCGTRGE---GESEASRRIKTELLVQMNGVGNDsQGVLVLGATNIPWQLDSA 159
                        170
                 ....*....|...
gi 489185780 309 LLRpgRFDRQVVV 321
Cdd:cd19521  160 IRR--RFEKRIYI 170
RecA-like_Yta7-like cd19517
ATPase domain of Saccharomyces cerevisiae Yta7 and similar ATPase domains; Saccharomyces ...
155-318 6.33e-37

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: 135.71  E-value: 6.33e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489185780 155 DVAGCDEAKEEVSELVEF-LRDPGKFQRLGGRIPRGVLMVGPPGTGKTLLAKAIA-----GEAKVPFFTISGSDFVEMFV 228
Cdd:cd19517    1 DIGGLSHYINQLKEMVFFpLLYPEVFAKFKITPPRGVLFHGPPGTGKTLMARALAaecskGGQKVSFFMRKGADCLSKWV 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489185780 229 GVGASRVRDMFDQAKKHAPCIIFIDEIDAVGRHRGAglggghdEREQT----LNQLLVEMDGFEMNDGIIVIAATNRPDV 304
Cdd:cd19517   81 GEAERQLRLLFEEAYRMQPSIIFFDEIDGLAPVRSS-------KQEQIhasiVSTLLALMDGLDNRGQVVVIGATNRPDA 153
                        170
                 ....*....|....
gi 489185780 305 LDPALLRPGRFDRQ 318
Cdd:cd19517  154 LDPALRRPGRFDRE 167
RecA-like_KTNA1 cd19522
Katanin p60 ATPase-containing subunit A1; Katanin p60 ATPase-containing subunit A1 (KTNA1) is ...
155-321 6.70e-34

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: 127.02  E-value: 6.70e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489185780 155 DVAGCDEAKEEVSELVEF-LRDPGKFQrlGGRIP-RGVLMVGPPGTGKTLLAKAIAGEAKVPFFTISGSDFVEMFVGVGA 232
Cdd:cd19522    1 DIADLEEAKKLLEEAVVLpMWMPEFFK--GIRRPwKGVLMVGPPGTGKTLLAKAVATECGTTFFNVSSSTLTSKYRGESE 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489185780 233 SRVRDMFDQAKKHAPCIIFIDEIDAVGRHRGAglGGGHDEREQTLNQLLVEMDGF---EMNDG----IIVIAATNRPDVL 305
Cdd:cd19522   79 KLVRLLFEMARFYAPTTIFIDEIDSICSRRGT--SEEHEASRRVKSELLVQMDGVggaSENDDpskmVMVLAATNFPWDI 156
                        170
                 ....*....|....*.
gi 489185780 306 DPALLRpgRFDRQVVV 321
Cdd:cd19522  157 DEALRR--RLEKRIYI 170
RecA-like_ATAD1 cd19520
ATPase domain of ATPase family AAA domain-containing protein 1 and similar ATPase domains; ...
155-315 6.07e-32

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: 121.38  E-value: 6.07e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489185780 155 DVAGCDEAKEEVSELVEF-LRDPGKFQrlGGRI---PRGVLMVGPPGTGKTLLAKAIAGEAKVPFFTISGSDFVEMFVGV 230
Cdd:cd19520    1 DIGGLDEVITELKELVILpLQRPELFD--NSRLlqpPKGVLLYGPPGCGKTMLAKATAKEAGARFINLQVSSLTDKWYGE 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489185780 231 GASRVRDMFDQAKKHAPCIIFIDEIDAVGRHRGAglgGGHDEREQTLNQLLVEMDGFEMNDG--IIVIAATNRPDVLDPA 308
Cdd:cd19520   79 SQKLVAAVFSLASKLQPSIIFIDEIDSFLRQRSS---TDHEATAMMKAEFMSLWDGLSTDGNcrVIVMGATNRPQDLDEA 155

                 ....*....
gi 489185780 309 LLR--PGRF 315
Cdd:cd19520  156 ILRrmPKRF 164
RecA-like_Figl-1 cd19525
ATPase domain of Fidgetin-Like 1 (FIGL-1); FIGL-1 may participate in DNA repair in the nucleus; ...
153-321 1.17e-31

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: 121.25  E-value: 1.17e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489185780 153 FADVAGCDEAKEEVSELV--EFLRdPGKFQRLGGRiPRGVLMVGPPGTGKTLLAKAIAGEAKVPFFTISGSDFVEMFVGV 230
Cdd:cd19525   21 WADIAGLEFAKKTIKEIVvwPMLR-PDIFTGLRGP-PKGILLFGPPGTGKTLIGKCIASQSGATFFSISASSLTSKWVGE 98
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489185780 231 GASRVRDMFDQAKKHAPCIIFIDEIDAVGRHRGAglgGGHDEREQTLNQLLVEMDGFEM--NDGIIVIAATNRPDVLDPA 308
Cdd:cd19525   99 GEKMVRALFSVARCKQPAVIFIDEIDSLLSQRGE---GEHESSRRIKTEFLVQLDGATTssEDRILVVGATNRPQEIDEA 175
                        170
                 ....*....|...
gi 489185780 309 LLRpgRFDRQVVV 321
Cdd:cd19525  176 ARR--RLVKRLYI 186
RecA-like_spastin cd19524
ATPase domain of spastin; Spastin is an ATP-dependent microtubule-severing protein involved in ...
155-321 1.92e-31

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


Pssm-ID: 410932 [Multi-domain]  Cd Length: 164  Bit Score: 119.95  E-value: 1.92e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489185780 155 DVAGCDEAKEEVSELVEFLRD-PGKFQRLGgRIPRGVLMVGPPGTGKTLLAKAIAGEAKVPFFTISGSDFVEMFVGVGAS 233
Cdd:cd19524    1 DIAGQDLAKQALQEMVILPSLrPELFTGLR-APARGLLLFGPPGNGKTMLAKAVAAESNATFFNISAASLTSKYVGEGEK 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489185780 234 RVRDMFDQAKKHAPCIIFIDEIDAVGRHRGAglgGGHDEREQTLNQLLVEMDGFEMN--DGIIVIAATNRPDVLDPALLR 311
Cdd:cd19524   80 LVRALFAVARELQPSIIFIDEVDSLLSERSE---GEHEASRRLKTEFLIEFDGVQSNgdDRVLVMGATNRPQELDDAVLR 156
                        170
                 ....*....|
gi 489185780 312 pgRFDRQVVV 321
Cdd:cd19524  157 --RFTKRVYV 164
AAA cd00009
The AAA+ (ATPases Associated with a wide variety of cellular Activities) superfamily ...
157-323 1.50e-30

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: 116.86  E-value: 1.50e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489185780 157 AGCDEAKEEVSELVEflrdpgkfqrlgGRIPRGVLMVGPPGTGKTLLAKAIAGEA---KVPFFTISGSDFVEMFVG---V 230
Cdd:cd00009    1 VGQEEAIEALREALE------------LPPPKNLLLYGPPGTGKTTLARAIANELfrpGAPFLYLNASDLLEGLVVaelF 68
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489185780 231 GASRVRDMFDQAKKHAPCIIFIDEIDAVGRhrgaglggghDEREQTLNQLLVEMDGFEMNDGIIVIAATNRPDVLDPALL 310
Cdd:cd00009   69 GHFLVRLLFELAEKAKPGVLFIDEIDSLSR----------GAQNALLRVLETLNDLRIDRENVRVIGATNRPLLGDLDRA 138
                        170
                 ....*....|...
gi 489185780 311 RPGRFDRQVVVGL 323
Cdd:cd00009  139 LYDRLDIRIVIPL 151
RecA-like_NSF-SEC18_r1-like cd19504
first of two ATPase domains of NSF and SEC18, and similar ATPase domains; ...
176-319 9.50e-29

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


Pssm-ID: 410912 [Multi-domain]  Cd Length: 177  Bit Score: 112.97  E-value: 9.50e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489185780 176 PGKFQRLGGRIPRGVLMVGPPGTGKTLLAKAI-----AGEAKVpfftISGSDFVEMFVGVGASRVRDMFDQAKKHAPC-- 248
Cdd:cd19504   24 PEIVEQLGCKHVKGILLYGPPGTGKTLMARQIgkmlnAREPKI----VNGPEILNKYVGESEANIRKLFADAEEEQRRlg 99
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 489185780 249 ------IIFIDEIDAVGRHRGAGlGGGHDEREQTLNQLLVEMDGFEMNDGIIVIAATNRPDVLDPALLRPGRFDRQV 319
Cdd:cd19504  100 ansglhIIIFDEIDAICKQRGSM-AGSTGVHDTVVNQLLSKIDGVEQLNNILVIGMTNRKDLIDEALLRPGRLEVQM 175
ycf46 CHL00195
Ycf46; Provisional
138-380 1.66e-27

Ycf46; Provisional


Pssm-ID: 177094 [Multi-domain]  Cd Length: 489  Bit Score: 116.66  E-value: 1.66e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489185780 138 KSKARLLSEDQ------VKTTFADVAGCDEAKEEVSELVEFLRDpgKFQRLGGRIPRGVLMVGPPGTGKTLLAKAIAGEA 211
Cdd:CHL00195 206 EEKKQIISQTEilefysVNEKISDIGGLDNLKDWLKKRSTSFSK--QASNYGLPTPRGLLLVGIQGTGKSLTAKAIANDW 283
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489185780 212 KVPFFTIsgsDFVEMF---VGVGASRVRDMFDQAKKHAPCIIFIDEID-AVGRHRGAGLGGghdereqTLNQLLVEMDGF 287
Cdd:CHL00195 284 QLPLLRL---DVGKLFggiVGESESRMRQMIRIAEALSPCILWIDEIDkAFSNSESKGDSG-------TTNRVLATFITW 353
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489185780 288 --EMNDGIIVIAATNRPDVLDPALLRPGRFDRQVVVGLPDIRGREQILKVHMRKV-PLG-DHVDPAVIARGTPGFSGADL 363
Cdd:CHL00195 354 lsEKKSPVFVVATANNIDLLPLEILRKGRFDEIFFLDLPSLEEREKIFKIHLQKFrPKSwKKYDIKKLSKLSNKFSGAEI 433
                        250
                 ....*....|....*..
gi 489185780 364 ANLVNEAsLFAARSNKR 380
Cdd:CHL00195 434 EQSIIEA-MYIAFYEKR 449
RecA-like_Ycf46-like cd19507
ATPase domain of Ycf46 and similar ATPase domains; Ycf46 may play a role in the regulation of ...
180-317 8.61e-22

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: 92.43  E-value: 8.61e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489185780 180 QRLGGRIPRGVLMVGPPGTGKTLLAKAIAGEAKVPFFTISGSDFVEMFVGVGASRVRDMFDQAKKHAPCIIFIDEID-AV 258
Cdd:cd19507   24 SAYGLPTPKGLLLVGIQGTGKSLTAKAIAGVWQLPLLRLDMGRLFGGLVGESESRLRQMIQTAEAIAPCVLWIDEIEkGF 103
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 489185780 259 GrhrGAGLGGGHDEREQTLNQLLVEMDgfEMNDGIIVIAATNRPDVLDPALLRPGRFDR 317
Cdd:cd19507  104 S---NADSKGDSGTSSRVLGTFLTWLQ--EKKKPVFVVATANNVQSLPPELLRKGRFDE 157
AAA smart00382
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ...
187-325 3.95e-21

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: 90.13  E-value: 3.95e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489185780   187 PRGVLMVGPPGTGKTLLAKAIAGEAKVP---FFTISGSDFVE--------------MFVGVGASRVRDMFDQAKKHAPCI 249
Cdd:smart00382   2 GEVILIVGPPGSGKTTLARALARELGPPgggVIYIDGEDILEevldqllliivggkKASGSGELRLRLALALARKLKPDV 81
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 489185780   250 IFIDEIDAVGRHRGaglggghdEREQTLNQLLVEMDGFEMNDGIIVIAATNRPDVLDPALLRPgRFDRQVVVGLPD 325
Cdd:smart00382  82 LILDEITSLLDAEQ--------EALLLLLEELRLLLLLKSEKNLTVILTTNDEKDLGPALLRR-RFDRRIVLLLIL 148
RecA-like_BCS1 cd19510
Mitochondrial chaperone BCS1; Mitochondrial chaperone BCS1 is necessary for the assembly of ...
166-321 7.91e-20

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: 86.64  E-value: 7.91e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489185780 166 VSELVEFLRDPGKFQRLGgrIP--RGVLMVGPPGTGKTLLAKAIAGEAKVPFFTISGSDfvemfVGVGASRVRDMFDQAK 243
Cdd:cd19510    2 IDDLKDFIKNEDWYNDRG--IPyrRGYLLYGPPGTGKSSFIAALAGELDYDICDLNLSE-----VVLTDDRLNHLLNTAP 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489185780 244 KHApcIIFIDEIDAV---GRHRGAGLGGGHDEREQTLNQLLVEMDGFEMNDGIIVIAATNRPDVLDPALLRPGRFDRQVV 320
Cdd:cd19510   75 KQS--IILLEDIDAAfesREHNKKNPSAYGGLSRVTFSGLLNALDGVASSEERIVFMTTNHIERLDPALIRPGRVDMKIY 152

                 .
gi 489185780 321 V 321
Cdd:cd19510  153 M 153
RecA-like_fidgetin cd19523
ATPase domain of fidgetin; Fidgetin (FIGN) is a ATP-dependent microtubule severing protein. ...
155-321 3.84e-19

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


Pssm-ID: 410931 [Multi-domain]  Cd Length: 163  Bit Score: 84.94  E-value: 3.84e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489185780 155 DVAGCDEAKEEVS-ELVEFLRDPGKFQRLGgRIPRGVLMVGPPGTGKTLLAKAIAGEAKVPFFTISGSDFVEMFVGVGAS 233
Cdd:cd19523    1 DIAGLGALKAAIKeEVLWPLLRPDAFSGLL-RLPRSILLFGPRGTGKTLLGRCLASQLGATFLRLRGSTLVAKWAGEGEK 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489185780 234 RVRDMFDQAKKHAPCIIFIDEIDAV--GRHRGAGLGGghdeREQTlnQLLVEMDGF--EMNDGIIVIAATNRPDVLDPAL 309
Cdd:cd19523   80 ILQASFLAARCRQPSVLFISDLDALlsSQDDEASPVG----RLQV--ELLAQLDGVlgSGEDGVLVVCTTSKPEEIDESL 153
                        170
                 ....*....|..
gi 489185780 310 LRpgRFDRQVVV 321
Cdd:cd19523  154 RR--YFSKRLLV 163
RecA-like_Ycf2 cd19505
ATPase domain of plant YCF2; Ycf2 is a chloroplast ATPase which has an essential function; ...
181-317 2.22e-15

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: 73.95  E-value: 2.22e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489185780 181 RLGGRIPRGVLMVGPPGTGKTLLAKAIAGEAKVPFFTISGSDFV--------------EMFVGVGASRVRDMFDQAKKHA 246
Cdd:cd19505    6 RLGLSPSKGILLIGSIETGRSYLIKSLAANSYVPLIRISLNKLLynkpdfgnddwidgMLILKESLHRLNLQFELAKAMS 85
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 489185780 247 PCIIFIDEIDAVGRHRgagLGGGHDEREQTLNQLLVEM--DGFEMND--GIIVIAATNRPDVLDPALLRPGRFDR 317
Cdd:cd19505   86 PCIIWIPNIHELNVNR---STQNLEEDPKLLLGLLLNYlsRDFEKSStrNILVIASTHIPQKVDPALIAPNRLDT 157
FtsH_ext pfam06480
FtsH Extracellular; This domain is found in the FtsH family of proteins. FtsH is the only ...
5-93 5.81e-15

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


Pssm-ID: 377663 [Multi-domain]  Cd Length: 103  Bit Score: 71.10  E-value: 5.81e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489185780    5 LILWLIIAAVLVTVMNNF--SSPSEPQTLNYSDFIQQVKDGKVERVTVDG------YVITGKRSDGDTFKT------IRP 70
Cdd:pfam06480   1 LLLWLLILLVLLLLFLLFllSSSSSTKEISYSEFLEYLEAGKVKKVVVQDdeilptGVVEGTLKDGSKFTTyfipslPNV 80
                          90       100
                  ....*....|....*....|...
gi 489185780   71 AIQDNGLIGDLVNNNVVVEGKQP 93
Cdd:pfam06480  81 DSLLEKLEDALEEKGVKVSVKPP 103
RecA-like_ATAD3-like cd19512
ATPase domains of ATPase AAA-domain protein 3A (ATAD3A), -3B, and -3C, and similar ATPase ...
188-319 2.41e-13

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: 67.94  E-value: 2.41e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489185780 188 RGVLMVGPPGTGKTLLAKAIAGEAKVPFFTISGSDFVEMFVGvGASRVRDMFDQAKK-HAPCIIFIDEIDAVGRHRgAGL 266
Cdd:cd19512   23 RNILFYGPPGTGKTLFAKKLALHSGMDYAIMTGGDVAPMGRE-GVTAIHKVFDWANTsRRGLLLFVDEADAFLRKR-STE 100
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|...
gi 489185780 267 GGGHDEReQTLNQLLVEMDgfEMNDGIIVIAATNRPDVLDPALlrPGRFDRQV 319
Cdd:cd19512  101 KISEDLR-AALNAFLYRTG--EQSNKFMLVLASNQPEQFDWAI--NDRIDEMV 148
PRK04195 PRK04195
replication factor C large subunit; Provisional
151-268 2.67e-11

replication factor C large subunit; Provisional


Pssm-ID: 235250 [Multi-domain]  Cd Length: 482  Bit Score: 66.10  E-value: 2.67e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489185780 151 TTFADVAGCDEAKEEVSELVE-FLRdpgkfqrlgGRIPRGVLMVGPPGTGKTLLAKAIAGEAKVPFFTISGSDF-----V 224
Cdd:PRK04195  11 KTLSDVVGNEKAKEQLREWIEsWLK---------GKPKKALLLYGPPGVGKTSLAHALANDYGWEVIELNASDQrtadvI 81
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 489185780 225 EMFVGvGASRVRDMFDQAKKhapcIIFIDEIDavGRHRGAGLGG 268
Cdd:PRK04195  82 ERVAG-EAATSGSLFGARRK----LILLDEVD--GIHGNEDRGG 118
PRK13342 PRK13342
recombination factor protein RarA; Reviewed
194-299 7.66e-11

recombination factor protein RarA; Reviewed


Pssm-ID: 237355 [Multi-domain]  Cd Length: 413  Bit Score: 64.34  E-value: 7.66e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489185780 194 GPPGTGKTLLAKAIAGEAKVPFFTISGSDFvemfvgvGASRVRDMFDQAKKHA----PCIIFIDEIdavgrHRgaglggg 269
Cdd:PRK13342  43 GPPGTGKTTLARIIAGATDAPFEALSAVTS-------GVKDLREVIEEARQRRsagrRTILFIDEI-----HR------- 103
                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 489185780 270 hdereqtLN---Q--LL--VEmdgfemnDG-IIVIAAT 299
Cdd:PRK13342 104 -------FNkaqQdaLLphVE-------DGtITLIGAT 127
RarA COG2256
Replication-associated recombination protein RarA (DNA-dependent ATPase) [Replication, ...
194-262 9.44e-11

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


Pssm-ID: 441857 [Multi-domain]  Cd Length: 439  Bit Score: 64.31  E-value: 9.44e-11
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 489185780 194 GPPGTGKTLLAKAIAGEAKVPFFTISGsdfvemfVGVGASRVRDMFDQAKKHA----PCIIFIDEIdavgrHR 262
Cdd:COG2256   56 GPPGTGKTTLARLIANATDAEFVALSA-------VTSGVKDIREVIEEARERRaygrRTILFVDEI-----HR 116
RecA-like_HslU cd19498
ATP-dependent protease ATPase subunit HslU; HslU is a component of the ATP-dependent protease ...
156-315 2.55e-10

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: 60.09  E-value: 2.55e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489185780 156 VAGCDEAKEEVSELvefLRDPGKFQRLGGRI-----PRGVLMVGPPGTGKTLLAKAIAGEAKVPFFTISGSDFVEM-FVG 229
Cdd:cd19498   13 IIGQDEAKRAVAIA---LRNRWRRMQLPEELrdevtPKNILMIGPTGVGKTEIARRLAKLAGAPFIKVEATKFTEVgYVG 89
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489185780 230 VGA-SRVRDMFDQakkhapcIIFIDEIDAVGRHRGaglGGGHD-EREQTLNQLLVEMDGFEMN--------DGIIVIAA- 298
Cdd:cd19498   90 RDVeSIIRDLVEG-------IVFIDEIDKIAKRGG---SSGPDvSREGVQRDLLPIVEGSTVStkygpvktDHILFIAAg 159
                        170       180
                 ....*....|....*....|
gi 489185780 299 ---TNRPDVLDPALlrPGRF 315
Cdd:cd19498  160 afhVAKPSDLIPEL--QGRF 177
AAA_lid_3 pfam17862
AAA+ lid domain; This entry represents the alpha helical AAA+ lid domain that is found to the ...
346-388 4.69e-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: 55.24  E-value: 4.69e-10
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 489185780  346 VDPAVIARGTPGFSGADLANLVNEASLFAARSNKRIVDMREFE 388
Cdd:pfam17862   2 VDLEELAERTEGFSGADLEALCREAALAALRRGLEAVTQEDLE 44
ycf2 CHL00206
Ycf2; Provisional
181-628 1.01e-09

Ycf2; Provisional


Pssm-ID: 214396 [Multi-domain]  Cd Length: 2281  Bit Score: 61.85  E-value: 1.01e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489185780  181 RLGGRIPRGVLMVGPPGTGKTLLAKAIAGEAKVPFFT--------------------ISGSDFVE--------------- 225
Cdd:CHL00206 1624 RLALSPSRGILVIGSIGTGRSYLVKYLATNSYVPFITvflnkfldnkpkgfliddidIDDSDDIDdsddidrdldtellt 1703
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489185780  226 --------MFVGVGASRVRDMFDQAKKHAPCIIFIDEIDAVGRHRGAGLGGG-------HD-EREQTLNqllvemdgfem 289
Cdd:CHL00206 1704 mmnaltmdMMPKIDRFYITLQFELAKAMSPCIIWIPNIHDLNVNESNYLSLGllvnslsRDcERCSTRN----------- 1772
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489185780  290 ndgIIVIAATNRPDVLDPALLRPGRFDRQVVVGLPDIRGREQ-------ILKVHMRKVPLgdHVDpaVIARGTPGFSGAD 362
Cdd:CHL00206 1773 ---ILVIASTHIPQKVDPALIAPNKLNTCIKIRRLLIPQQRKhfftlsyTRGFHLEKKMF--HTN--GFGSITMGSNARD 1845
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489185780  363 LANLVNEASLFAARSNKRIVDMREFELAkdkimmgAERKTMVMSEKEKR----NTAYHEAGHAIVGRLVPEHDPVYKVSI 438
Cdd:CHL00206 1846 LVALTNEALSISITQKKSIIDTNTIRSA-------LHRQTWDLRSQVRSvqdhGILFYQIGRAVAQNVLLSNCPIDPISI 1918
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489185780  439 IPRGRALGvtmflpEEDRY----------SLSKRALESQICSLFGGRIAEEmtlgfegvttgaSNDIMRATQlaRNMVTK 508
Cdd:CHL00206 1919 YMKKKSCK------EGDSYlykwyfelgtSMKKLTILLYLLSCSAGSVAQD------------LWSLPGPDE--KNGITS 1978
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489185780  509 WGLSEKLGPLMYA--EEEGEVFlGRSAG----SQHANvsGETAKMIDQEVRRIIDDCYGTAKRLLDEN--RDKLEMMADA 580
Cdd:CHL00206 1979 YGLVENDSDLVHGllEVEGALV-GSSRTekdcSQFDN--DRVTLLLRPEPRNPLDMMQNGSCSIVDQRflYEKYESEFEE 2055
                         490       500       510       520
                  ....*....|....*....|....*....|....*....|....*...
gi 489185780  581 LMKYETIDSDQIDDIMAGRVPREPRDWqggsgtgTPPANLEESGRREN 628
Cdd:CHL00206 2056 GESEGALDPQQIEEDLFNHIVWAPRIW-------RPWGFLFDCIERPN 2096
AAA_5 pfam07728
AAA domain (dynein-related subfamily); This Pfam entry includes some of the AAA proteins not ...
189-315 1.15e-09

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: 56.92  E-value: 1.15e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489185780  189 GVLMVGPPGTGKTLLAKAIAgEA--KVPFFTISGSDF--VEMFVG------VGASRVrdmfDQAKKHA---PCIIFIDEI 255
Cdd:pfam07728   1 GVLLVGPPGTGKTELAERLA-AAlsNRPVFYVQLTRDttEEDLFGrrnidpGGASWV----DGPLVRAareGEIAVLDEI 75
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 489185780  256 DAvgrhrgaglggGHDEREQTLNQLLVE-----MDGFEM----NDGIIVIAATNRPD----VLDPALLRpgRF 315
Cdd:pfam07728  76 NR-----------ANPDVLNSLLSLLDErrlllPDGGELvkaaPDGFRLIATMNPLDrglnELSPALRS--RF 135
TIP49 COG1224
DNA helicase TIP49, TBP-interacting protein [Transcription];
161-223 3.43e-08

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


Pssm-ID: 440837 [Multi-domain]  Cd Length: 452  Bit Score: 56.13  E-value: 3.43e-08
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 489185780 161 EAKEEVSELVEFLRDpGKFqrlGGRiprGVLMVGPPGTGKTLLAKAIAGE--AKVPFFTISGSDF 223
Cdd:COG1224   45 EAREAAGIVVKMIKE-GKM---AGK---GILIVGPPGTGKTALAVAIARElgEDTPFVAISGSEI 102
TIP49 pfam06068
TIP49 P-loop domain; This family consists of the C-terminal region of several eukaryotic and ...
158-223 3.19e-07

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: 52.70  E-value: 3.19e-07
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 489185780  158 GCDEAKEEVSELVEFLRDpgkfQRLGGRiprGVLMVGPPGTGKTLLAKAIAGE--AKVPFFTISGSDF 223
Cdd:pfam06068  28 GQEKAREAAGVIVEMIKE----GKIAGR---AVLIAGPPGTGKTALAIAISKElgEDTPFTSISGSEV 88
T7SS_EccA TIGR03922
type VII secretion AAA-ATPase EccA; This model represents the AAA family ATPase, EccA, of the ...
140-319 3.80e-07

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: 53.31  E-value: 3.80e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489185780  140 KARLLSEDQVKttFADVAGCDEAKEEVSEL-----VEFLRdpgkfQRLGGRIP---RGVLMVGPPGTGKTLLAKAIA--- 208
Cdd:TIGR03922 264 KAKLLAEAEAE--LAEQIGLERVKRQVAALksstaMALAR-----AERGLPVAqtsNHMLFAGPPGTGKTTIARVVAkiy 336
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489185780  209 ---GEAKVP-FFTISGSDFVEMFVGVGASRVRDMFDQAKKHapcIIFIDEIDA-VGRHRGAglggGHDEREQTLNQLLVE 283
Cdd:TIGR03922 337 cglGVLRKPlVREVSRADLIGQYIGESEAKTNEIIDSALGG---VLFLDEAYTlVETGYGQ----KDPFGLEAIDTLLAR 409
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 489185780  284 MDGFEmnDGIIVIAATNRPDvLDPAL-----LRpGRFDRQV 319
Cdd:TIGR03922 410 MENDR--DRLVVIGAGYRKD-LDKFLevnegLR-SRFTRVI 446
RecA-like_superfamily cd01120
RecA-like_NTPases; RecA-like NTPases. This superfamily includes the NTP binding domain of F1 ...
190-306 5.40e-07

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


Pssm-ID: 410865 [Multi-domain]  Cd Length: 119  Bit Score: 48.65  E-value: 5.40e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489185780 190 VLMVGPPGTGKTLLAKAIAGEAKVPFFTISGSDFVEMFVgvgaSRVRDMfdqAKKHAPCIIFIDEIDAVGRHRGAglggg 269
Cdd:cd01120    1 ILITGPPGSGKTTLLLQFAEQALLSDEPVIFISFLDTIL----EAIEDL---IEEKKLDIIIIDSLSSLARASQG----- 68
                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 489185780 270 hDEREQTLNQLLVEMDGFEmNDGIIVIAATNRPDVLD 306
Cdd:cd01120   69 -DRSSELLEDLAKLLRAAR-NTGITVIATIHSDKFDI 103
RecA-like_Pch2-like cd19508
ATPase domain of Pachytene checkpoint 2 (Pch2) and similar ATPase domains; Pch2 (known as ...
188-309 2.33e-06

ATPase domain of Pachytene checkpoint 2 (Pch2) and similar ATPase domains; Pch2 (known as Thyroid hormone receptor interactor 13 (TRIP13) and 16E1BP) is a key regulator of specific chromosomal events, like the control of G2/prophase processes such as DNA break formation and recombination, checkpoint signaling, and chromosome synapsis. This subfamily belongs to the RecA-like NTPase family which includes the NTP binding domain of F1 and V1 H(+)ATPases, DnaB and related helicases as well as bacterial RecA and related eukaryotic and archaeal recombinases. The RecA-like NTPase family also includes bacterial conjugation proteins and related DNA transfer proteins involved in type II and type IV secretion


Pssm-ID: 410916 [Multi-domain]  Cd Length: 199  Bit Score: 48.60  E-value: 2.33e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489185780 188 RGVLMVGPPGTGKTLLAKAIAGEAKVPF-FTISGSDFVEM--------FVGVGASRVRDMFDQAK---KHAPCIIF--ID 253
Cdd:cd19508   53 RLVLLHGPPGTGKTSLCKALAQKLSIRLsSRYRYGQLIEInshslfskWFSESGKLVTKMFQKIQeliDDKDALVFvlID 132
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 489185780 254 EIDAVGRHRGAGLGGGH-DEREQTLNQLLVEMDGFEMNDGIIVIAATNRPDVLDPAL 309
Cdd:cd19508  133 EVESLAAARSASSSGTEpSDAIRVVNAVLTQIDRIKRYHNNVILLTSNLLEKIDVAF 189
RecA-like_Lon cd19500
lon protease homolog 2 peroxisomal; Lon protease (also known as Lon peptidase) is an ...
154-263 3.47e-06

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


Pssm-ID: 410908 [Multi-domain]  Cd Length: 182  Bit Score: 47.94  E-value: 3.47e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489185780 154 ADVAGCDEAKEEVSELVEFLRDPGKFQrlgGRIprgVLMVGPPGTGKTLLAKAIAGEAKVPFFTIS-G--SDFVEM---- 226
Cdd:cd19500   10 ADHYGLEDVKERILEYLAVRKLKGSMK---GPI---LCLVGPPGVGKTSLGKSIARALGRKFVRISlGgvRDEAEIrghr 83
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 489185780 227 --FVGVGASRVRDMFDQAKKHAPcIIFIDEIDAVGR-HRG 263
Cdd:cd19500   84 rtYVGAMPGRIIQALKKAGTNNP-VFLLDEIDKIGSsFRG 122
CDC6 COG1474
Cdc6-related protein, AAA superfamily ATPase [Replication, recombination and repair];
164-306 5.28e-06

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


Pssm-ID: 441083 [Multi-domain]  Cd Length: 389  Bit Score: 49.08  E-value: 5.28e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489185780 164 EEVSELVEFLRDPgkfqrLGGRIPRGVLMVGPPGTGKTLLAKAIAGEAK-------VPFFTI------------------ 218
Cdd:COG1474   33 EEIEELASALRPA-----LRGERPSNVLIYGPTGTGKTAVAKYVLEELEeeaeergVDVRVVyvncrqastryrvlsril 107
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489185780 219 ----SGSDFVEmfVGVGASRVRDMFDQA--KKHAPCIIFIDEIDAVgrhrgaglggGHDEREQTLNQLLVEMDGFEmNDG 292
Cdd:COG1474  108 eelgSGEDIPS--TGLSTDELFDRLYEAldERDGVLVVVLDEIDYL----------VDDEGDDLLYQLLRANEELE-GAR 174
                        170
                 ....*....|....
gi 489185780 293 IIVIAATNRPDVLD 306
Cdd:COG1474  175 VGVIGISNDLEFLE 188
ruvB PRK00080
Holliday junction branch migration DNA helicase RuvB;
190-262 7.70e-06

Holliday junction branch migration DNA helicase RuvB;


Pssm-ID: 234619 [Multi-domain]  Cd Length: 328  Bit Score: 48.20  E-value: 7.70e-06
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 489185780 190 VLMVGPPGTGKTLLAKAIAGEAKVPFFTISG------SDFVEMFVGVGAsrvRDmfdqakkhapcIIFIDEIdavgrHR 262
Cdd:PRK00080  54 VLLYGPPGLGKTTLANIIANEMGVNIRITSGpalekpGDLAAILTNLEE---GD-----------VLFIDEI-----HR 113
AAA_2 pfam07724
AAA domain (Cdc48 subfamily); This Pfam entry includes some of the AAA proteins not detected ...
190-300 1.02e-05

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: 46.03  E-value: 1.02e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489185780  190 VLMVGPPGTGKTLLAKAIAGE---AKVPFFTISGSDFVE-----MFVG-----VGASRVRDMFDQAKKHAPCIIFIDEID 256
Cdd:pfam07724   6 FLFLGPTGVGKTELAKALAELlfgDERALIRIDMSEYMEehsvsRLIGappgyVGYEEGGQLTEAVRRKPYSIVLIDEIE 85
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 489185780  257 AVgrHRGaglggghdereqTLNQLLVEMDGFEMNDG---------IIVIAATN 300
Cdd:pfam07724  86 KA--HPG------------VQNDLLQILEGGTLTDKqgrtvdfknTLFIMTGN 124
MoxR COG0714
MoxR-like ATPase [General function prediction only]; MoxR-like ATPase is part of the Pathway ...
190-338 2.69e-05

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: 46.31  E-value: 2.69e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489185780 190 VLMVGPPGTGKTLLAKAIAGEAKVPFFTISG------SDfvemFVGVgasrvrDMFDQAK-----KHAP---CIIFIDEI 255
Cdd:COG0714   34 LLLEGVPGVGKTTLAKALARALGLPFIRIQFtpdllpSD----ILGT------YIYDQQTgefefRPGPlfaNVLLADEI 103
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489185780 256 DavgrhRGaglggghdeREQTLNQLL-------VEMDG--FEMNDGIIVIAATNRPDV-----LDPALLRpgRFDRQVVV 321
Cdd:COG0714  104 N-----RA---------PPKTQSALLeameerqVTIPGgtYKLPEPFLVIATQNPIEQegtypLPEAQLD--RFLLKLYI 167
                        170
                 ....*....|....*..
gi 489185780 322 GLPDIRGREQILKVHMR 338
Cdd:COG0714  168 GYPDAEEEREILRRHTG 184
RecA-like_ClpB_Hsp104-like cd19499
Chaperone protein ClpB/Hsp104 subfamily; Bacterial Caseinolytic peptidase B (ClpB) and ...
156-256 3.47e-05

Chaperone protein ClpB/Hsp104 subfamily; Bacterial Caseinolytic peptidase B (ClpB) and eukaryotic Heat shock protein 104 (Hsp104) are ATP-dependent molecular chaperones and essential proteins of the heat-shock response. ClpB/Hsp104 ATPases, in concert with the DnaK/Hsp70 chaperone system, disaggregate and reactivate aggregated proteins. This RecA-like_ClpB_Hsp104_like subfamily belongs to the RecA-like NTPase family which includes the NTP binding domain of F1 and V1 H(+)ATPases, DnaB and related helicases as well as bacterial RecA and related eukaryotic and archaeal recombinases. The RecA-like NTPase family also includes bacterial conjugation proteins and related DNA transfer proteins involved in type II and type IV secretion.


Pssm-ID: 410907 [Multi-domain]  Cd Length: 178  Bit Score: 44.86  E-value: 3.47e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489185780 156 VAGCDEAKEEVSELVEF----LRDPGKfqrlggriPRGVLM-VGPPGTGKTLLAKAIAGE---AKVPFFTISGSDFVEMF 227
Cdd:cd19499   13 VVGQDEAVKAVSDAIRRaragLSDPNR--------PIGSFLfLGPTGVGKTELAKALAELlfgDEDNLIRIDMSEYMEKH 84
                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 489185780 228 VG----------VGASRVRDMFDQAKKHAPCIIFIDEID 256
Cdd:cd19499   85 SVsrligappgyVGYTEGGQLTEAVRRKPYSVVLLDEIE 123
RecA-like_ClpX cd19497
ATP-dependent Clp protease ATP-binding subunit ClpX; ClpX is a component of the ATP-dependent ...
190-260 4.50e-05

ATP-dependent Clp protease ATP-binding subunit ClpX; ClpX is a component of the ATP-dependent protease ClpXP. In ClpXP, ClpX ATPase serves to specifically recognize, unfold, and translocate protein substrates into the chamber of ClpP protease for degradation. This RecA-like_ClpX domain subfamily belongs to the RecA-like NTPase family which includes the NTP binding domain of F1 and V1 H(+)ATPases, DnaB and related helicases as well as bacterial RecA and related eukaryotic and archaeal recombinases. The RecA-like NTPase family also includes bacterial conjugation proteins and related DNA transfer proteins involved in type II and type IV secretion.


Pssm-ID: 410905 [Multi-domain]  Cd Length: 251  Bit Score: 45.28  E-value: 4.50e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489185780 190 VLMVGPPGTGKTLLAKAIAGEAKVPfFTIS-----------GSDfVEMFVG--VGASrvrdMFD--QAKKHapcIIFIDE 254
Cdd:cd19497   53 ILLIGPTGSGKTLLAQTLAKILDVP-FAIAdattlteagyvGED-VENILLklLQAA----DYDveRAQRG---IVYIDE 123

                 ....*.
gi 489185780 255 IDAVGR 260
Cdd:cd19497  124 IDKIAR 129
DnaC COG1484
DNA replication protein DnaC [Replication, recombination and repair];
188-255 5.47e-05

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


Pssm-ID: 441093 [Multi-domain]  Cd Length: 242  Bit Score: 45.16  E-value: 5.47e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 489185780 188 RGVLMVGPPGTGKTLLAKAIAGEA-----KVPFFTIsgSDFV-EMFVGVGASRVRDMFDQAKKhAPCIIfIDEI 255
Cdd:COG1484  100 ENLILLGPPGTGKTHLAIALGHEAcragyRVRFTTA--PDLVnELKEARADGRLERLLKRLAK-VDLLI-LDEL 169
ClpX COG1219
ATP-dependent protease Clp, ATPase subunit ClpX [Posttranslational modification, protein ...
190-260 5.70e-05

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


Pssm-ID: 440832 [Multi-domain]  Cd Length: 409  Bit Score: 45.81  E-value: 5.70e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489185780 190 VLMVGPPGTGKTLLAKAIAGEAKVPfFTIS-----------GSDfVEMFVgvgasrVR-----DmFD--QAKKHapcIIF 251
Cdd:COG1219  112 ILLIGPTGSGKTLLAQTLARILDVP-FAIAdattlteagyvGED-VENIL------LKllqaaD-YDveKAERG---IIY 179

                 ....*....
gi 489185780 252 IDEIDAVGR 260
Cdd:COG1219  180 IDEIDKIAR 188
44 PHA02544
clamp loader, small subunit; Provisional
184-259 6.66e-05

clamp loader, small subunit; Provisional


Pssm-ID: 222866 [Multi-domain]  Cd Length: 316  Bit Score: 45.37  E-value: 6.66e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489185780 184 GRIPRGVLMVGPPGTGKTLLAKAIAGEAKVPFFTISGSDfvemfvgvgaSRVRDMFDQAKKHA--------PCIIFIDEI 255
Cdd:PHA02544  40 GRIPNMLLHSPSPGTGKTTVAKALCNEVGAEVLFVNGSD----------CRIDFVRNRLTRFAstvsltggGKVIIIDEF 109

                 ....
gi 489185780 256 DAVG 259
Cdd:PHA02544 110 DRLG 113
clpX PRK05342
ATP-dependent Clp protease ATP-binding subunit ClpX;
190-260 1.31e-04

ATP-dependent Clp protease ATP-binding subunit ClpX;


Pssm-ID: 235422 [Multi-domain]  Cd Length: 412  Bit Score: 44.76  E-value: 1.31e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489185780 190 VLMVGPPGTGKTLLAKAIAGEAKVPfFTIS-----------GSDfVEMFVgvgasrVR-----DmFD--QAKKHapcIIF 251
Cdd:PRK05342 111 ILLIGPTGSGKTLLAQTLARILDVP-FAIAdattlteagyvGED-VENIL------LKllqaaD-YDveKAQRG---IVY 178

                 ....*....
gi 489185780 252 IDEIDAVGR 260
Cdd:PRK05342 179 IDEIDKIAR 187
YifB COG0606
Predicted Mg-chelatase, contains ChlI-like and ATPase domains, YifB family [Posttranslational ...
190-209 1.35e-04

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


Pssm-ID: 440371 [Multi-domain]  Cd Length: 502  Bit Score: 45.03  E-value: 1.35e-04
                         10        20
                 ....*....|....*....|
gi 489185780 190 VLMVGPPGTGKTLLAKAIAG 209
Cdd:COG0606  214 LLMIGPPGSGKTMLARRLPG 233
McrB COG1401
5-methylcytosine-specific restriction endonuclease McrBC, GTP-binding regulatory subunit McrB ...
185-255 1.85e-04

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


Pssm-ID: 441011 [Multi-domain]  Cd Length: 477  Bit Score: 44.38  E-value: 1.85e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489185780 185 RIPRGVLMVGPPGTGKT----LLAKAIAGEAKVPFFTI------SGSDFVEMFVGVGAS---RVRD-MF----DQAKKH- 245
Cdd:COG1401  219 KTKKNVILAGPPGTGKTylarRLAEALGGEDNGRIEFVqfhpswSYEDFLLGYRPSLDEgkyEPTPgIFlrfcLKAEKNp 298
                         90
                 ....*....|.
gi 489185780 246 -APCIIFIDEI 255
Cdd:COG1401  299 dKPYVLIIDEI 309
RuvB_N pfam05496
Holliday junction DNA helicase RuvB P-loop domain; The RuvB protein makes up part of the ...
152-262 2.35e-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: 42.10  E-value: 2.35e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489185780  152 TFADVAGCDEAKEEVSELVEFLRdpgkfQRlgGRIPRGVLMVGPPGTGKTLLAKAIAGEAKVPFFTISG------SDFVE 225
Cdd:pfam05496   5 TLDEYIGQEKVKENLKIFIEAAK-----QR--GEALDHVLLYGPPGLGKTTLANIIANEMGVNIRITSGpaierpGDLAA 77
                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 489185780  226 MFVGVGAsrvRDmfdqakkhapcIIFIDEIdavgrHR 262
Cdd:pfam05496  78 ILTNLEP---GD-----------VLFIDEI-----HR 95
Mg_chelatase pfam01078
Magnesium chelatase, subunit ChlI; Magnesium-chelatase is a three-component enzyme that ...
190-209 4.88e-04

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


Pssm-ID: 426032 [Multi-domain]  Cd Length: 207  Bit Score: 41.75  E-value: 4.88e-04
                          10        20
                  ....*....|....*....|
gi 489185780  190 VLMVGPPGTGKTLLAKAIAG 209
Cdd:pfam01078  25 LLMIGPPGSGKTMLAKRLPG 44
HolB COG0470
DNA polymerase III, delta prime subunit [Replication, recombination and repair];
184-257 7.94e-04

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


Pssm-ID: 440238 [Multi-domain]  Cd Length: 289  Bit Score: 41.88  E-value: 7.94e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489185780 184 GRIPRGVLMVGPPGTGKTLLAKAIA----GEAKVP-----------FFTISGSDFVEMFVGV-----GASRVRDMFDQAK 243
Cdd:COG0470   15 GRLPHALLLHGPPGIGKTTLALALArdllCENPEGgkacgqchsrlMAAGNHPDLLELNPEEksdqiGIDQIRELGEFLS 94
                         90
                 ....*....|....*...
gi 489185780 244 KHAPC----IIFIDEIDA 257
Cdd:COG0470   95 LTPLEggrkVVIIDEADA 112
ABC_ATPase cd00267
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ...
186-321 9.66e-04

ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.


Pssm-ID: 213179 [Multi-domain]  Cd Length: 157  Bit Score: 40.31  E-value: 9.66e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489185780 186 IPRG--VLMVGPPGTGKTLLAKAIAGEAKVP--FFTISGSDFVEMFVGVGASRVRDMFD----QAKK--------HAPCI 249
Cdd:cd00267   22 LKAGeiVALVGPNGSGKSTLLRAIAGLLKPTsgEILIDGKDIAKLPLEELRRRIGYVPQlsggQRQRvalarallLNPDL 101
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 489185780 250 IFIDEIDavgrhrgAGLgggHDEREQTLNQLLVEMdgfeMNDGIIVIAATNRPDVLDPAllrpgrFDRQVVV 321
Cdd:cd00267  102 LLLDEPT-------SGL---DPASRERLLELLREL----AEEGRTVIIVTHDPELAELA------ADRVIVL 153
ruvB TIGR00635
Holliday junction DNA helicase, RuvB subunit; All proteins in this family for which functions ...
190-260 1.26e-03

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


Pssm-ID: 129721 [Multi-domain]  Cd Length: 305  Bit Score: 41.13  E-value: 1.26e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 489185780  190 VLMVGPPGTGKTLLAKAIAGEAKVPFFTISG------SDFVEMFVGVgasrvrdmfdqaKKHApcIIFIDEIDAVGR 260
Cdd:TIGR00635  33 LLLYGPPGLGKTTLAHIIANEMGVNLKITSGpalekpGDLAAILTNL------------EEGD--VLFIDEIHRLSP 95
IS21_help_AAA NF038214
IS21-like element helper ATPase IstB; This protein family model resembles PF01695, but was ...
190-225 1.51e-03

IS21-like element helper ATPase IstB; This protein family model resembles PF01695, but was built to hit full-length AAA+ ATPases of IS21 family IS (insertion sequence) elements.


Pssm-ID: 439516  Cd Length: 232  Bit Score: 40.53  E-value: 1.51e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|.
gi 489185780 190 VLMVGPPGTGKTLLAKAIAGEA-----KVPFFTIsgSDFVE 225
Cdd:NF038214  93 VLLLGPPGTGKTHLAIALGYAAcrqgyRVRFTTA--ADLVE 131
RAD55 COG0467
RecA-superfamily ATPase, KaiC/GvpD/RAD55 family [Signal transduction mechanisms];
182-211 1.98e-03

RecA-superfamily ATPase, KaiC/GvpD/RAD55 family [Signal transduction mechanisms];


Pssm-ID: 440235 [Multi-domain]  Cd Length: 221  Bit Score: 40.28  E-value: 1.98e-03
                         10        20        30
                 ....*....|....*....|....*....|..
gi 489185780 182 LGGRIPRG--VLMVGPPGTGKTLLAKAIAGEA 211
Cdd:COG0467   13 LGGGLPRGssTLLSGPPGTGKTTLALQFLAEG 44
DnaX COG2812
DNA polymerase III, gamma/tau subunits [Replication, recombination and repair];
147-208 3.10e-03

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


Pssm-ID: 442061 [Multi-domain]  Cd Length: 340  Bit Score: 40.17  E-value: 3.10e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 489185780 147 DQVKTTFADVAGCDEAKEEVSELVEflrdpgkfqrlGGRIPRGVLMVGPPGTGKTLLAKAIA 208
Cdd:COG2812    3 YQVPQTFDDVVGQEHVVRTLKNALA-----------SGRLAHAYLFTGPRGVGKTTLARILA 53
TIGR02928 TIGR02928
orc1/cdc6 family replication initiation protein; Members of this protein family are found ...
164-261 3.16e-03

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


Pssm-ID: 274354 [Multi-domain]  Cd Length: 365  Bit Score: 40.31  E-value: 3.16e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489185780  164 EEVSELVEFLRDPgkfqrLGGRIPRGVLMVGPPGTGKTLLAK-------AIAGEAKVPFFTI---------SGSDFVEMF 227
Cdd:TIGR02928  22 EQIEELAKALRPI-----LRGSRPSNVFIYGKTGTGKTAVTKyvmkeleEAAEDRDVRVVTVyvncqildtLYQVLVELA 96
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 489185780  228 ------------VGVGASRV-RDMFDQAKKHAPCIIFI-DEIDAVGRH 261
Cdd:TIGR02928  97 nqlrgsgeevptTGLSTSEVfRRLYKELNERGDSLIIVlDEIDYLVGD 144
RuvB COG2255
Holliday junction resolvasome RuvABC, ATP-dependent DNA helicase subunit RuvB [Replication, ...
190-220 5.97e-03

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


Pssm-ID: 441856 [Multi-domain]  Cd Length: 337  Bit Score: 39.29  E-value: 5.97e-03
                         10        20        30
                 ....*....|....*....|....*....|.
gi 489185780 190 VLMVGPPGTGKTLLAKAIAGEAKVPFFTISG 220
Cdd:COG2255   57 VLLYGPPGLGKTTLAHIIANEMGVNIRITSG 87
rfc PRK00440
replication factor C small subunit; Reviewed
152-257 7.65e-03

replication factor C small subunit; Reviewed


Pssm-ID: 234763 [Multi-domain]  Cd Length: 319  Bit Score: 38.70  E-value: 7.65e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489185780 152 TFADVAGCDEAKEEVSELVEflrdpgkfqrlGGRIPRgVLMVGPPGTGKTLLAKAIAGEakvpfftISGSDFVEMFVGVG 231
Cdd:PRK00440  15 TLDEIVGQEEIVERLKSYVK-----------EKNMPH-LLFAGPPGTGKTTAALALARE-------LYGEDWRENFLELN 75
                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 489185780 232 AS--R----VRDMFDQAKKHAPC------IIFIDEIDA 257
Cdd:PRK00440  76 ASdeRgidvIRNKIKEFARTAPVggapfkIIFLDEADN 113
PRK13341 PRK13341
AAA family ATPase;
194-262 9.40e-03

AAA family ATPase;


Pssm-ID: 237354 [Multi-domain]  Cd Length: 725  Bit Score: 39.27  E-value: 9.40e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 489185780 194 GPPGTGKTLLAKAIAGEAKVPFFTISGsdfvemfVGVGASRVRDMFDQAK----KHAP-CIIFIDEIdavgrHR 262
Cdd:PRK13341  59 GPPGVGKTTLARIIANHTRAHFSSLNA-------VLAGVKDLRAEVDRAKerleRHGKrTILFIDEV-----HR 120
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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