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Conserved domains on  [gi|2250557577|ref|XP_009353567|]
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probable inactive ATP-dependent zinc metalloprotease FTSHI 2, chloroplastic [Pyrus x bretschneideri]

Protein Classification

ATP-dependent metallopeptidase FtsH/Yme1/Tma family protein( domain architecture ID 1000290)

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

Gene Ontology:  GO:0016020
PubMed:  31988523|29097521|22498346|19656850|16966379|10788805

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
HflB super family cl33892
ATP-dependent Zn proteases [Posttranslational modification, protein turnover, chaperones];
388-846 1.07e-149

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


The actual alignment was detected with superfamily member COG0465:

Pssm-ID: 440233 [Multi-domain]  Cd Length: 583  Bit Score: 453.34  E-value: 1.07e-149
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2250557577 388 AMQFMKSGARVrrahnkrlpqYLERGVDVKFTDVAGLGKIRLELEEIVKFFTHGEMYRRRGVKIPGGILLCGPPGVGKTL 467
Cdd:COG0465   121 AMSFGKSKAKL----------YDEDKPKVTFDDVAGVDEAKEELQEIVDFLKDPEKFTRLGAKIPKGVLLVGPPGTGKTL 190

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2250557577 468 LAKAVAGEAGVNFFSISASQFVEIYVGVGASRVRALYQEARENAPSVVFIDELDAVGRERGliKGSGG--QERDATLNQL 545
Cdd:COG0465   191 LAKAVAGEAGVPFFSISGSDFVEMFVGVGASRVRDLFEQAKKNAPCIIFIDEIDAVGRQRG--AGLGGghDEREQTLNQL 268

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2250557577 546 LVCLDGFEGRGEVITIASTNRPDILDPALVRPGRFDRKIFIPKPGLIGRIEILKVHARKKPMAEDVDYMAIASMTDGMVG 625
Cdd:COG0465   269 LVEMDGFEGNEGVIVIAATNRPDVLDPALLRPGRFDRQVVVDLPDVKGREAILKVHARKKPLAPDVDLEVIARRTPGFSG 348

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2250557577 626 AELANIIEVAAINMMRDGRTEITTDDLLQA-----AQMEERGM-LDRKERsldtwKQVAINEAAMAVVAVNFPDLRNIEF 699
Cdd:COG0465   349 ADLANLVNEAALLAARRNKKAVTMEDFEEAidrviAGPERKSRvISEKEK-----KITAYHEAGHALVAALLPGADPVHK 423

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2250557577 700 VTIAPRaGRELGYVRMKmdPIKFReGMLTRQSLLDHITVQLAPRAADELWFGEdqLSTIwaetADN--------ARSAAR 771
Cdd:COG0465   424 VTIIPR-GRALGYTMQL--PEEDR-YLYTKEELLDRIAVLLGGRAAEELVFGE--VTTG----ASNdleratkiARAMVT 493

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2250557577 772 TYvlgGLSEK----------HHGLSNFWVADRLN-------DLDVEALQIVNMCYERAKEILQKNRTLMDAVVDELVQKK 834
Cdd:COG0465   494 EY---GMSEKlgpvaygeseGEVFLGRDIGQSRNyseetarEIDEEVRRIIDEAYERAKEILTENRDKLDALAEALLEKE 570

                         490
                  ....*....|..
gi 2250557577 835 SLTKQEFFSLVE 846
Cdd:COG0465   571 TLDGEELEEILA 582
 
Name Accession Description Interval E-value
HflB COG0465
ATP-dependent Zn proteases [Posttranslational modification, protein turnover, chaperones];
388-846 1.07e-149

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


Pssm-ID: 440233 [Multi-domain]  Cd Length: 583  Bit Score: 453.34  E-value: 1.07e-149
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2250557577 388 AMQFMKSGARVrrahnkrlpqYLERGVDVKFTDVAGLGKIRLELEEIVKFFTHGEMYRRRGVKIPGGILLCGPPGVGKTL 467
Cdd:COG0465   121 AMSFGKSKAKL----------YDEDKPKVTFDDVAGVDEAKEELQEIVDFLKDPEKFTRLGAKIPKGVLLVGPPGTGKTL 190

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2250557577 468 LAKAVAGEAGVNFFSISASQFVEIYVGVGASRVRALYQEARENAPSVVFIDELDAVGRERGliKGSGG--QERDATLNQL 545
Cdd:COG0465   191 LAKAVAGEAGVPFFSISGSDFVEMFVGVGASRVRDLFEQAKKNAPCIIFIDEIDAVGRQRG--AGLGGghDEREQTLNQL 268

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2250557577 546 LVCLDGFEGRGEVITIASTNRPDILDPALVRPGRFDRKIFIPKPGLIGRIEILKVHARKKPMAEDVDYMAIASMTDGMVG 625
Cdd:COG0465   269 LVEMDGFEGNEGVIVIAATNRPDVLDPALLRPGRFDRQVVVDLPDVKGREAILKVHARKKPLAPDVDLEVIARRTPGFSG 348

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2250557577 626 AELANIIEVAAINMMRDGRTEITTDDLLQA-----AQMEERGM-LDRKERsldtwKQVAINEAAMAVVAVNFPDLRNIEF 699
Cdd:COG0465   349 ADLANLVNEAALLAARRNKKAVTMEDFEEAidrviAGPERKSRvISEKEK-----KITAYHEAGHALVAALLPGADPVHK 423

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2250557577 700 VTIAPRaGRELGYVRMKmdPIKFReGMLTRQSLLDHITVQLAPRAADELWFGEdqLSTIwaetADN--------ARSAAR 771
Cdd:COG0465   424 VTIIPR-GRALGYTMQL--PEEDR-YLYTKEELLDRIAVLLGGRAAEELVFGE--VTTG----ASNdleratkiARAMVT 493

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2250557577 772 TYvlgGLSEK----------HHGLSNFWVADRLN-------DLDVEALQIVNMCYERAKEILQKNRTLMDAVVDELVQKK 834
Cdd:COG0465   494 EY---GMSEKlgpvaygeseGEVFLGRDIGQSRNyseetarEIDEEVRRIIDEAYERAKEILTENRDKLDALAEALLEKE 570

                         490
                  ....*....|..
gi 2250557577 835 SLTKQEFFSLVE 846
Cdd:COG0465   571 TLDGEELEEILA 582
FtsH_fam TIGR01241
ATP-dependent metalloprotease FtsH; HflB(FtsH) is a pleiotropic protein required for correct ...
 386-846 1.61e-139

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: 424.01  E-value: 1.61e-139
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2250557577 386 KMAMQFMKSGARVrrahnkrlpqYLERGVDVKFTDVAGLGKIRLELEEIVKFFTHGEMYRRRGVKIPGGILLCGPPGVGK 465
Cdd:TIGR01241  32 GRAFSFGKSKAKL----------LNEEKPKVTFKDVAGIDEAKEELMEIVDFLKNPSKFTKLGAKIPKGVLLVGPPGTGK 101

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2250557577 466 TLLAKAVAGEAGVNFFSISASQFVEIYVGVGASRVRALYQEARENAPSVVFIDELDAVGRERGLIKGSGGQERDATLNQL 545
Cdd:TIGR01241 102 TLLAKAVAGEAGVPFFSISGSDFVEMFVGVGASRVRDLFEQAKKNAPCIIFIDEIDAVGRQRGAGLGGGNDEREQTLNQL 181

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2250557577 546 LVCLDGFEGRGEVITIASTNRPDILDPALVRPGRFDRKIFIPKPGLIGRIEILKVHARKKPMAEDVDYMAIASMTDGMVG 625
Cdd:TIGR01241 182 LVEMDGFGTNTGVIVIAATNRPDVLDPALLRPGRFDRQVVVDLPDIKGREEILKVHAKNKKLAPDVDLKAVARRTPGFSG 261

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2250557577 626 AELANIIEVAAINMMRDGRTEITTDDLLQA-----AQMEERGMLDRKERSldtwKQVAINEAAMAVVAVNFPDLRNIEFV 700
Cdd:TIGR01241 262 ADLANLLNEAALLAARKNKTEITMNDIEEAidrviAGPEKKSRVISEKEK----KLVAYHEAGHALVGLLLKDADPVHKV 337

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2250557577 701 TIAPRaGRELGYVRMKmdPIKFReGMLTRQSLLDHITVQLAPRAADELWFGEdqLSTIWAETADNARSAARTYVLG-GLS 779
Cdd:TIGR01241 338 TIIPR-GQALGYTQFL--PEEDK-YLYTKSQLLAQIAVLLGGRAAEEIIFGE--VTTGASNDIKQATNIARAMVTEwGMS 411

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2250557577 780 EK-----------------HHGLSNFWVADRLNDLDVEALQIVNMCYERAKEILQKNRTLMDAVVDELVQKKSLTKQEFF 842
Cdd:TIGR01241 412 DKlgpvaygsdggdvflgrGFAKAKEYSEETAREIDEEVKRIIEEAYKRAKQILTENRDELELLAKALLEKETITREEIK 491


                  ....
gi 2250557577 843 SLVE 846
Cdd:TIGR01241 492 ELLA 495
ftsH CHL00176
cell division protein; Validated
 388-855 4.43e-120

cell division protein; Validated


Pssm-ID: 214386 [Multi-domain]  Cd Length: 638  Bit Score: 378.24  E-value: 4.43e-120
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2250557577 388 AMQFMKSGARVRRAHNKrlpqylergvDVKFTDVAGLGKIRLELEEIVKFFTHGEMYRRRGVKIPGGILLCGPPGVGKTL 467
Cdd:CHL00176  162 LMNFGKSKARFQMEADT----------GITFRDIAGIEEAKEEFEEVVSFLKKPERFTAVGAKIPKGVLLVGPPGTGKTL 231

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2250557577 468 LAKAVAGEAGVNFFSISASQFVEIYVGVGASRVRALYQEARENAPSVVFIDELDAVGRERGLIKGSGGQERDATLNQLLV 547
Cdd:CHL00176  232 LAKAIAGEAEVPFFSISGSEFVEMFVGVGAARVRDLFKKAKENSPCIVFIDEIDAVGRQRGAGIGGGNDEREQTLNQLLT 311

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2250557577 548 CLDGFEGRGEVITIASTNRPDILDPALVRPGRFDRKIFIPKPGLIGRIEILKVHARKKPMAEDVDYMAIASMTDGMVGAE 627
Cdd:CHL00176  312 EMDGFKGNKGVIVIAATNRVDILDAALLRPGRFDRQITVSLPDREGRLDILKVHARNKKLSPDVSLELIARRTPGFSGAD 391

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2250557577 628 LANIIEVAAINMMRDGRTEITTDDLLQA-----AQMEERGMLDRKERSLdtwkqVAINEAAMAVVAVNFPDLRNIEFVTI 702
Cdd:CHL00176  392 LANLLNEAAILTARRKKATITMKEIDTAidrviAGLEGTPLEDSKNKRL-----IAYHEVGHAIVGTLLPNHDPVQKVTL 466

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2250557577 703 APRAG-RELGYVRMKMDPIKfregmLTRQSLLDHITVQLAPRAADELWFGEDQLSTIWAETADNARSAARTYV------- 774
Cdd:CHL00176  467 IPRGQaKGLTWFTPEEDQSL-----VSRSQILARIVGALGGRAAEEVVFGSTEVTTGASNDLQQVTNLARQMVtrfgmss 541

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2250557577 775 LGGLSEKHHGLSNFWVADRL-----------NDLDVEALQIVNMCYERAKEILQKNRTLMDAVVDELVQKKSLTKQEFFS 843
Cdd:CHL00176  542 IGPISLESNNSTDPFLGRFMqrnseyseeiaDKIDMEVRSILHTCYQYAYQILKDNRVLIDLLVELLLQKETIDGDEFRE 621

                         490
                  ....*....|..
gi 2250557577 844 LVELHGTLKPMP 855
Cdd:CHL00176  622 IVNSYTILPPKK 633
RecA-like_FtsH cd19501
ATP-dependent zinc metalloprotease FtsH; FtsH ATPase is a processive, ATP-dependent zinc ...
 416-586 2.22e-87

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: 275.27  E-value: 2.22e-87
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2250557577 416 VKFTDVAGLGKIRLELEEIVKFFTHGEMYRRRGVKIPGGILLCGPPGVGKTLLAKAVAGEAGVNFFSISASQFVEIYVGV 495
Cdd:cd19501     1 VTFKDVAGCEEAKEELKEVVEFLKNPEKFTKLGAKIPKGVLLVGPPGTGKTLLAKAVAGEAGVPFFSISGSDFVEMFVGV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2250557577 496 GASRVRALYQEARENAPSVVFIDELDAVGRERGLIKGSGGQERDATLNQLLVCLDGFEGRGEVITIASTNRPDILDPALV 575
Cdd:cd19501    81 GASRVRDLFEQAKKNAPCIVFIDEIDAVGRKRGAGLGGGHDEREQTLNQLLVEMDGFESNTGVIVIAATNRPDVLDPALL 160

                         170
                  ....*....|.
gi 2250557577 576 RPGRFDRKIFI 586
Cdd:cd19501   161 RPGRFDRQVYV 171
AAA pfam00004
ATPase family associated with various cellular activities (AAA); AAA family proteins often ...
 455-587 2.79e-50

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: 172.78  E-value: 2.79e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2250557577 455 ILLCGPPGVGKTLLAKAVAGEAGVNFFSISASQFVEIYVGVGASRVRALYQEARENAPSVVFIDELDAVGRERGlikGSG 534
Cdd:pfam00004   1 LLLYGPPGTGKTTLAKAVAKELGAPFIEISGSELVSKYVGESEKRLRELFEAAKKLAPCVIFIDEIDALAGSRG---SGG 77

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 2250557577 535 GQERDATLNQLLVCLDGFEGR-GEVITIASTNRPDILDPALVrpGRFDRKIFIP 587
Cdd:pfam00004  78 DSESRRVVNQLLTELDGFTSSnSKVIVIAATNRPDKLDPALL--GRFDRIIEFP 129
AAA smart00382
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ...
 452-589 3.62e-17

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: 79.34  E-value: 3.62e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2250557577  452 PGGILLCGPPGVGKTLLAKAVAGEAGVN---FFSISASQFVEI--------------YVGVGASRVRALYQEARENAPSV 514
Cdd:smart00382   2 GEVILIVGPPGSGKTTLARALARELGPPgggVIYIDGEDILEEvldqllliivggkkASGSGELRLRLALALARKLKPDV 81

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2250557577  515 VFIDELDAVGRERglikgsggQERDATLNQLLVCLDGFEGRGEVITIASTNRPDILDPALVRPgRFDRKIFIPKP 589
Cdd:smart00382  82 LILDEITSLLDAE--------QEALLLLLEELRLLLLLKSEKNLTVILTTNDEKDLGPALLRR-RFDRRIVLLLI 147
 
Name Accession Description Interval E-value
HflB COG0465
ATP-dependent Zn proteases [Posttranslational modification, protein turnover, chaperones];
388-846 1.07e-149

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


Pssm-ID: 440233 [Multi-domain]  Cd Length: 583  Bit Score: 453.34  E-value: 1.07e-149
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2250557577 388 AMQFMKSGARVrrahnkrlpqYLERGVDVKFTDVAGLGKIRLELEEIVKFFTHGEMYRRRGVKIPGGILLCGPPGVGKTL 467
Cdd:COG0465   121 AMSFGKSKAKL----------YDEDKPKVTFDDVAGVDEAKEELQEIVDFLKDPEKFTRLGAKIPKGVLLVGPPGTGKTL 190

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2250557577 468 LAKAVAGEAGVNFFSISASQFVEIYVGVGASRVRALYQEARENAPSVVFIDELDAVGRERGliKGSGG--QERDATLNQL 545
Cdd:COG0465   191 LAKAVAGEAGVPFFSISGSDFVEMFVGVGASRVRDLFEQAKKNAPCIIFIDEIDAVGRQRG--AGLGGghDEREQTLNQL 268

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2250557577 546 LVCLDGFEGRGEVITIASTNRPDILDPALVRPGRFDRKIFIPKPGLIGRIEILKVHARKKPMAEDVDYMAIASMTDGMVG 625
Cdd:COG0465   269 LVEMDGFEGNEGVIVIAATNRPDVLDPALLRPGRFDRQVVVDLPDVKGREAILKVHARKKPLAPDVDLEVIARRTPGFSG 348

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2250557577 626 AELANIIEVAAINMMRDGRTEITTDDLLQA-----AQMEERGM-LDRKERsldtwKQVAINEAAMAVVAVNFPDLRNIEF 699
Cdd:COG0465   349 ADLANLVNEAALLAARRNKKAVTMEDFEEAidrviAGPERKSRvISEKEK-----KITAYHEAGHALVAALLPGADPVHK 423

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2250557577 700 VTIAPRaGRELGYVRMKmdPIKFReGMLTRQSLLDHITVQLAPRAADELWFGEdqLSTIwaetADN--------ARSAAR 771
Cdd:COG0465   424 VTIIPR-GRALGYTMQL--PEEDR-YLYTKEELLDRIAVLLGGRAAEELVFGE--VTTG----ASNdleratkiARAMVT 493

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2250557577 772 TYvlgGLSEK----------HHGLSNFWVADRLN-------DLDVEALQIVNMCYERAKEILQKNRTLMDAVVDELVQKK 834
Cdd:COG0465   494 EY---GMSEKlgpvaygeseGEVFLGRDIGQSRNyseetarEIDEEVRRIIDEAYERAKEILTENRDKLDALAEALLEKE 570

                         490
                  ....*....|..
gi 2250557577 835 SLTKQEFFSLVE 846
Cdd:COG0465   571 TLDGEELEEILA 582
FtsH_fam TIGR01241
ATP-dependent metalloprotease FtsH; HflB(FtsH) is a pleiotropic protein required for correct ...
 386-846 1.61e-139

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: 424.01  E-value: 1.61e-139
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2250557577 386 KMAMQFMKSGARVrrahnkrlpqYLERGVDVKFTDVAGLGKIRLELEEIVKFFTHGEMYRRRGVKIPGGILLCGPPGVGK 465
Cdd:TIGR01241  32 GRAFSFGKSKAKL----------LNEEKPKVTFKDVAGIDEAKEELMEIVDFLKNPSKFTKLGAKIPKGVLLVGPPGTGK 101

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2250557577 466 TLLAKAVAGEAGVNFFSISASQFVEIYVGVGASRVRALYQEARENAPSVVFIDELDAVGRERGLIKGSGGQERDATLNQL 545
Cdd:TIGR01241 102 TLLAKAVAGEAGVPFFSISGSDFVEMFVGVGASRVRDLFEQAKKNAPCIIFIDEIDAVGRQRGAGLGGGNDEREQTLNQL 181

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2250557577 546 LVCLDGFEGRGEVITIASTNRPDILDPALVRPGRFDRKIFIPKPGLIGRIEILKVHARKKPMAEDVDYMAIASMTDGMVG 625
Cdd:TIGR01241 182 LVEMDGFGTNTGVIVIAATNRPDVLDPALLRPGRFDRQVVVDLPDIKGREEILKVHAKNKKLAPDVDLKAVARRTPGFSG 261

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2250557577 626 AELANIIEVAAINMMRDGRTEITTDDLLQA-----AQMEERGMLDRKERSldtwKQVAINEAAMAVVAVNFPDLRNIEFV 700
Cdd:TIGR01241 262 ADLANLLNEAALLAARKNKTEITMNDIEEAidrviAGPEKKSRVISEKEK----KLVAYHEAGHALVGLLLKDADPVHKV 337

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2250557577 701 TIAPRaGRELGYVRMKmdPIKFReGMLTRQSLLDHITVQLAPRAADELWFGEdqLSTIWAETADNARSAARTYVLG-GLS 779
Cdd:TIGR01241 338 TIIPR-GQALGYTQFL--PEEDK-YLYTKSQLLAQIAVLLGGRAAEEIIFGE--VTTGASNDIKQATNIARAMVTEwGMS 411

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2250557577 780 EK-----------------HHGLSNFWVADRLNDLDVEALQIVNMCYERAKEILQKNRTLMDAVVDELVQKKSLTKQEFF 842
Cdd:TIGR01241 412 DKlgpvaygsdggdvflgrGFAKAKEYSEETAREIDEEVKRIIEEAYKRAKQILTENRDELELLAKALLEKETITREEIK 491


                  ....
gi 2250557577 843 SLVE 846
Cdd:TIGR01241 492 ELLA 495
ftsH CHL00176
cell division protein; Validated
 388-855 4.43e-120

cell division protein; Validated


Pssm-ID: 214386 [Multi-domain]  Cd Length: 638  Bit Score: 378.24  E-value: 4.43e-120
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2250557577 388 AMQFMKSGARVRRAHNKrlpqylergvDVKFTDVAGLGKIRLELEEIVKFFTHGEMYRRRGVKIPGGILLCGPPGVGKTL 467
Cdd:CHL00176  162 LMNFGKSKARFQMEADT----------GITFRDIAGIEEAKEEFEEVVSFLKKPERFTAVGAKIPKGVLLVGPPGTGKTL 231

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2250557577 468 LAKAVAGEAGVNFFSISASQFVEIYVGVGASRVRALYQEARENAPSVVFIDELDAVGRERGLIKGSGGQERDATLNQLLV 547
Cdd:CHL00176  232 LAKAIAGEAEVPFFSISGSEFVEMFVGVGAARVRDLFKKAKENSPCIVFIDEIDAVGRQRGAGIGGGNDEREQTLNQLLT 311

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2250557577 548 CLDGFEGRGEVITIASTNRPDILDPALVRPGRFDRKIFIPKPGLIGRIEILKVHARKKPMAEDVDYMAIASMTDGMVGAE 627
Cdd:CHL00176  312 EMDGFKGNKGVIVIAATNRVDILDAALLRPGRFDRQITVSLPDREGRLDILKVHARNKKLSPDVSLELIARRTPGFSGAD 391

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2250557577 628 LANIIEVAAINMMRDGRTEITTDDLLQA-----AQMEERGMLDRKERSLdtwkqVAINEAAMAVVAVNFPDLRNIEFVTI 702
Cdd:CHL00176  392 LANLLNEAAILTARRKKATITMKEIDTAidrviAGLEGTPLEDSKNKRL-----IAYHEVGHAIVGTLLPNHDPVQKVTL 466

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2250557577 703 APRAG-RELGYVRMKMDPIKfregmLTRQSLLDHITVQLAPRAADELWFGEDQLSTIWAETADNARSAARTYV------- 774
Cdd:CHL00176  467 IPRGQaKGLTWFTPEEDQSL-----VSRSQILARIVGALGGRAAEEVVFGSTEVTTGASNDLQQVTNLARQMVtrfgmss 541

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2250557577 775 LGGLSEKHHGLSNFWVADRL-----------NDLDVEALQIVNMCYERAKEILQKNRTLMDAVVDELVQKKSLTKQEFFS 843
Cdd:CHL00176  542 IGPISLESNNSTDPFLGRFMqrnseyseeiaDKIDMEVRSILHTCYQYAYQILKDNRVLIDLLVELLLQKETIDGDEFRE 621

                         490
                  ....*....|..
gi 2250557577 844 LVELHGTLKPMP 855
Cdd:CHL00176  622 IVNSYTILPPKK 633
RPT1 COG1222
ATP-dependent 26S proteasome regulatory subunit [Posttranslational modification, protein ...
 405-655 8.27e-101

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


Pssm-ID: 440835 [Multi-domain]  Cd Length: 326  Bit Score: 316.95  E-value: 8.27e-101
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2250557577 405 RLPQYLERGVDVKFTDVAGLGKIRLELEE-IVKFFTHGEMYRRRGVKIPGGILLCGPPGVGKTLLAKAVAGEAGVNFFSI 483
Cdd:COG1222    64 RGTAVPAESPDVTFDDIGGLDEQIEEIREaVELPLKNPELFRKYGIEPPKGVLLYGPPGTGKTLLAKAVAGELGAPFIRV 143

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2250557577 484 SASQFVEIYVGVGASRVRALYQEARENAPSVVFIDELDAVGRERGLIKGSGGQERdaTLNQLLVCLDGFEGRGEVITIAS 563
Cdd:COG1222   144 RGSELVSKYIGEGARNVREVFELAREKAPSIIFIDEIDAIAARRTDDGTSGEVQR--TVNQLLAELDGFESRGDVLIIAA 221

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2250557577 564 TNRPDILDPALVRPGRFDRKIFIPKPGLIGRIEILKVHARKKPMAEDVDYMAIASMTDGMVGAELANIIEVAAINMMRDG 643
Cdd:COG1222   222 TNRPDLLDPALLRPGRFDRVIEVPLPDEEAREEILKIHLRDMPLADDVDLDKLAKLTEGFSGADLKAIVTEAGMFAIREG 301

                         250
                  ....*....|..
gi 2250557577 644 RTEITTDDLLQA 655
Cdd:COG1222   302 RDTVTMEDLEKA 313
hflB PRK10733
ATP-dependent zinc metalloprotease FtsH;
386-836 9.67e-95

ATP-dependent zinc metalloprotease FtsH;


Pssm-ID: 182683 [Multi-domain]  Cd Length: 644  Bit Score: 311.58  E-value: 9.67e-95
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2250557577 386 KMAMQFMKSGARVrrahnkrlpqYLERGVDVKFTDVAGLGKIRLELEEIVKFFTHGEMYRRRGVKIPGGILLCGPPGVGK 465
Cdd:PRK10733  129 KGAMSFGKSKARM----------LTEDQIKTTFADVAGCDEAKEEVAELVEYLREPSRFQKLGGKIPKGVLMVGPPGTGK 198

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2250557577 466 TLLAKAVAGEAGVNFFSISASQFVEIYVGVGASRVRALYQEARENAPSVVFIDELDAVGRERGLIKGSGGQERDATLNQL 545
Cdd:PRK10733  199 TLLAKAIAGEAKVPFFTISGSDFVEMFVGVGASRVRDMFEQAKKAAPCIIFIDEIDAVGRQRGAGLGGGHDEREQTLNQM 278

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2250557577 546 LVCLDGFEGRGEVITIASTNRPDILDPALVRPGRFDRKIFIPKPGLIGRIEILKVHARKKPMAEDVDYMAIASMTDGMVG 625
Cdd:PRK10733  279 LVEMDGFEGNEGIIVIAATNRPDVLDPALLRPGRFDRQVVVGLPDVRGREQILKVHMRRVPLAPDIDAAIIARGTPGFSG 358

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2250557577 626 AELANIIEVAAINMMRDGRTEITtddLLQAAQMEERGMLDRKERSL----DTWKQVAINEAAMAVVAVNFPDLRNIEFVT 701
Cdd:PRK10733  359 ADLANLVNEAALFAARGNKRVVS---MVEFEKAKDKIMMGAERRSMvmteAQKESTAYHEAGHAIIGRLVPEHDPVHKVT 435

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2250557577 702 IAPRaGRELG--YVRMKMDPIKfregmLTRQSLLDHITVQLAPRAADELWFGEDQLSTIWAETADNARSAARTYVLG-GL 778
Cdd:PRK10733  436 IIPR-GRALGvtFFLPEGDAIS-----ASRQKLESQISTLYGGRLAEEIIYGPEHVSTGASNDIKVATNLARNMVTQwGF 509

                         410       420       430       440       450       460       470
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2250557577 779 SEKHHGL------------SNFWVADRLND-----LDVEALQIVNMCYERAKEILQKNRTLMDAVVDELVQKKSL 836
Cdd:PRK10733  510 SEKLGPLlyaeeegevflgRSVAKAKHMSDetariIDQEVKALIERNYNRARQLLTDNMDILHAMKDALMKYETI 584
RecA-like_FtsH cd19501
ATP-dependent zinc metalloprotease FtsH; FtsH ATPase is a processive, ATP-dependent zinc ...
 416-586 2.22e-87

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: 275.27  E-value: 2.22e-87
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2250557577 416 VKFTDVAGLGKIRLELEEIVKFFTHGEMYRRRGVKIPGGILLCGPPGVGKTLLAKAVAGEAGVNFFSISASQFVEIYVGV 495
Cdd:cd19501     1 VTFKDVAGCEEAKEELKEVVEFLKNPEKFTKLGAKIPKGVLLVGPPGTGKTLLAKAVAGEAGVPFFSISGSDFVEMFVGV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2250557577 496 GASRVRALYQEARENAPSVVFIDELDAVGRERGLIKGSGGQERDATLNQLLVCLDGFEGRGEVITIASTNRPDILDPALV 575
Cdd:cd19501    81 GASRVRDLFEQAKKNAPCIVFIDEIDAVGRKRGAGLGGGHDEREQTLNQLLVEMDGFESNTGVIVIAATNRPDVLDPALL 160

                         170
                  ....*....|.
gi 2250557577 576 RPGRFDRKIFI 586
Cdd:cd19501   161 RPGRFDRQVYV 171
PRK03992 PRK03992
proteasome-activating nucleotidase; Provisional
 415-655 1.14e-86

proteasome-activating nucleotidase; Provisional


Pssm-ID: 179699 [Multi-domain]  Cd Length: 389  Bit Score: 281.72  E-value: 1.14e-86
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2250557577 415 DVKFTDVAGLGKIRLELEEIVKF-FTHGEMYRRRGVKIPGGILLCGPPGVGKTLLAKAVAGEAGVNFFSISASQFVEIYV 493
Cdd:PRK03992  127 NVTYEDIGGLEEQIREVREAVELpLKKPELFEEVGIEPPKGVLLYGPPGTGKTLLAKAVAHETNATFIRVVGSELVQKFI 206

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2250557577 494 GVGASRVRALYQEARENAPSVVFIDELDAVGRERGLIKGSGGQERDATLNQLLVCLDGFEGRGEVITIASTNRPDILDPA 573
Cdd:PRK03992  207 GEGARLVRELFELAREKAPSIIFIDEIDAIAAKRTDSGTSGDREVQRTLMQLLAEMDGFDPRGNVKIIAATNRIDILDPA 286

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2250557577 574 LVRPGRFDRKIFIPKPGLIGRIEILKVHARKKPMAEDVDYMAIASMTDGMVGAELANIIEVAAINMMRDGRTEITTDDLL 653
Cdd:PRK03992  287 ILRPGRFDRIIEVPLPDEEGRLEILKIHTRKMNLADDVDLEELAELTEGASGADLKAICTEAGMFAIRDDRTEVTMEDFL 366


                  ..
gi 2250557577 654 QA 655
Cdd:PRK03992  367 KA 368
26Sp45 TIGR01242
26S proteasome subunit P45 family; Many proteins may score above the trusted cutoff because an ...
 415-655 6.16e-78

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


Pssm-ID: 130309 [Multi-domain]  Cd Length: 364  Bit Score: 257.42  E-value: 6.16e-78
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2250557577 415 DVKFTDVAGLGKIRLELEEIVKF-FTHGEMYRRRGVKIPGGILLCGPPGVGKTLLAKAVAGEAGVNFFSISASQFVEIYV 493
Cdd:TIGR01242 118 NVSYEDIGGLEEQIREIREAVELpLKHPELFEEVGIEPPKGVLLYGPPGTGKTLLAKAVAHETNATFIRVVGSELVRKYI 197

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2250557577 494 GVGASRVRALYQEARENAPSVVFIDELDAVGRERGLIKGSGGQERDATLNQLLVCLDGFEGRGEVITIASTNRPDILDPA 573
Cdd:TIGR01242 198 GEGARLVREIFELAKEKAPSIIFIDEIDAIAAKRTDSGTSGDREVQRTLMQLLAELDGFDPRGNVKVIAATNRPDILDPA 277

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2250557577 574 LVRPGRFDRKIFIPKPGLIGRIEILKVHARKKPMAEDVDYMAIASMTDGMVGAELANIIEVAAINMMRDGRTEITTDDLL 653
Cdd:TIGR01242 278 LLRPGRFDRIIEVPLPDFEGRLEILKIHTRKMKLAEDVDLEAIAKMTEGASGADLKAICTEAGMFAIREERDYVTMDDFI 357


                  ..
gi 2250557577 654 QA 655
Cdd:TIGR01242 358 KA 359
SpoVK COG0464
AAA+-type ATPase, SpoVK/Ycf46/Vps4 family [Cell wall/membrane/envelope biogenesis, Cell cycle ...
 340-663 8.70e-72

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: 242.12  E-value: 8.70e-72
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2250557577 340 EDRLKIEKAEAEERKKMRELEREMEGIEGDEEDEIEPGKGEQNPYLKMAMQFMKSGARVRRAHNKRLPQYLERGVDVKFT 419
Cdd:COG0464    78 LLALLAALLSALELLLLGELLLLLLLLLLLLLLLLDLERALLELLRESAEALALAAPLVTYEDIGGLEEELLELREAILD 157

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2250557577 420 DVAGLGKIRLELEEIVKFFTHG-EMYRRRGVKIPGGILLCGPPGVGKTLLAKAVAGEAGVNFFSISASQFVEIYVGVGAS 498
Cdd:COG0464   158 DLGGLEEVKEELRELVALPLKRpELREEYGLPPPRGLLLYGPPGTGKTLLARALAGELGLPLIEVDLSDLVSKYVGETEK 237

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2250557577 499 RVRALYQEARENAPSVVFIDELDAVGRERGLIKGSGGQErdaTLNQLLVCLDGFegRGEVITIASTNRPDILDPALVRpg 578
Cdd:COG0464   238 NLREVFDKARGLAPCVLFIDEADALAGKRGEVGDGVGRR---VVNTLLTEMEEL--RSDVVVIAATNRPDLLDPALLR-- 310

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2250557577 579 RFDRKIFIPKPGLIGRIEILKVHARKKPMAEDVDYMAIASMTDGMVGAELANIIEVAAINMMRDGRTEITTDDLLQAAQM 658
Cdd:COG0464   311 RFDEIIFFPLPDAEERLEIFRIHLRKRPLDEDVDLEELAEATEGLSGADIRNVVRRAALQALRLGREPVTTEDLLEALER 390


                  ....*
gi 2250557577 659 EERGM 663
Cdd:COG0464   391 EDIFL 395
CDC48 TIGR01243
AAA family ATPase, CDC48 subfamily; This subfamily of the AAA family ATPases includes two ...
 411-641 3.90e-59

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: 215.54  E-value: 3.90e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2250557577 411 ERGV-DVKFTDVAGLGKIRLELEEIVKF-FTHGEMYRRRGVKIPGGILLCGPPGVGKTLLAKAVAGEAGVNFFSISASQF 488
Cdd:TIGR01243 169 ERKVpKVTYEDIGGLKEAKEKIREMVELpMKHPELFEHLGIEPPKGVLLYGPPGTGKTLLAKAVANEAGAYFISINGPEI 248

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2250557577 489 VEIYVGVGASRVRALYQEARENAPSVVFIDELDAVGRERGLIKGsggQERDATLNQLLVCLDGFEGRGEVITIASTNRPD 568
Cdd:TIGR01243 249 MSKYYGESEERLREIFKEAEENAPSIIFIDEIDAIAPKREEVTG---EVEKRVVAQLLTLMDGLKGRGRVIVIGATNRPD 325

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2250557577 569 ILDPALVRPGRFDRKIFIPKPGLIGRIEILKVHARKKPMAEDVDYMAIASMTDGMVGAELANIIEVAAINMMR 641
Cdd:TIGR01243 326 ALDPALRRPGRFDREIVIRVPDKRARKEILKVHTRNMPLAEDVDLDKLAEVTHGFVGADLAALAKEAAMAALR 398
CDC48 TIGR01243
AAA family ATPase, CDC48 subfamily; This subfamily of the AAA family ATPases includes two ...
 415-642 4.65e-58

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: 212.46  E-value: 4.65e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2250557577 415 DVKFTDVAGLGKIRLELEEIVKF-FTHGEMYRRRGVKIPGGILLCGPPGVGKTLLAKAVAGEAGVNFFSISASQFVEIYV 493
Cdd:TIGR01243 449 NVRWSDIGGLEEVKQELREAVEWpLKHPEIFEKMGIRPPKGVLLFGPPGTGKTLLAKAVATESGANFIAVRGPEILSKWV 528

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2250557577 494 GVGASRVRALYQEARENAPSVVFIDELDAVGRERGLIKGSGGQERdaTLNQLLVCLDGFEGRGEVITIASTNRPDILDPA 573
Cdd:TIGR01243 529 GESEKAIREIFRKARQAAPAIIFFDEIDAIAPARGARFDTSVTDR--IVNQLLTEMDGIQELSNVVVIAATNRPDILDPA 606

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2250557577 574 LVRPGRFDRKIFIPKPGLIGRIEILKVHARKKPMAEDVDYMAIASMTDGMVGAELANIIEVAAINMMRD 642
Cdd:TIGR01243 607 LLRPGRFDRLILVPPPDEEARKEIFKIHTRSMPLAEDVDLEELAEMTEGYTGADIEAVCREAAMAALRE 675
RecA-like_protease cd19481
proteases similar to RecA; RecA-like NTPases. This family includes the NTP binding domain of ...
 427-586 8.19e-57

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


Pssm-ID: 410889 [Multi-domain]  Cd Length: 158  Bit Score: 192.11  E-value: 8.19e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2250557577 427 IRLELEEIVKFFTHGEMYRRRGVKIPGGILLCGPPGVGKTLLAKAVAGEAGVNFFSISASQFVEIYVGVGASRVRALYQE 506
Cdd:cd19481     1 LKASLREAVEAPRRGSRLRRYGLGLPKGILLYGPPGTGKTLLAKALAGELGLPLIVVKLSSLLSKYVGESEKNLRKIFER 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2250557577 507 ARENAPSVVFIDELDAVGRERGLIKGSGgqERDATLNQLLVCLDGFEGRGEVITIASTNRPDILDPALVRPGRFDRKIFI 586
Cdd:cd19481    81 ARRLAPCILFIDEIDAIGRKRDSSGESG--ELRRVLNQLLTELDGVNSRSKVLVIAATNRPDLLDPALLRPGRFDEVIEF 158
COG1223 COG1223
Predicted ATPase, AAA+ superfamily [General function prediction only];
418-669 8.63e-57

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


Pssm-ID: 440836 [Multi-domain]  Cd Length: 246  Bit Score: 195.49  E-value: 8.63e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2250557577 418 FTDVAGLGKIRLELEEIVKFFTHGEMYRRRGVKIPGGILLCGPPGVGKTLLAKAVAGEAGVNFFSISASQFVEIYVGVGA 497
Cdd:COG1223     1 LDDVVGQEEAKKKLKLIIKELRRRENLRKFGLWPPRKILFYGPPGTGKTMLAEALAGELKLPLLTVRLDSLIGSYLGETA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2250557577 498 SRVRALYQEAREnAPSVVFIDELDAVGRERGLIKGSGgqERDATLNQLLVCLDGFegRGEVITIASTNRPDILDPALVRp 577
Cdd:COG1223    81 RNLRKLFDFARR-APCVIFFDEFDAIAKDRGDQNDVG--EVKRVVNALLQELDGL--PSGSVVIAATNHPELLDSALWR- 154

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2250557577 578 gRFDRKIFIPKPGLIGRIEILKVHARKKPMAEDVDYMAIASMTDGMVGAELANIIEVAAINMMRDGRTEITTDDLLQAAQ 657
Cdd:COG1223   155 -RFDEVIEFPLPDKEERKEILELNLKKFPLPFELDLKKLAKKLEGLSGADIEKVLKTALKKAILEDREKVTKEDLEEALK 233

                         250
                  ....*....|...
gi 2250557577 658 ME-ERGMLDRKER 669
Cdd:COG1223   234 QRkERKKEPKKEG 246
RecA-like_PAN_like cd19502
proteasome activating nucleotidase PAN and related proteasome subunits; This subfamily ...
 418-584 4.58e-56

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: 190.63  E-value: 4.58e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2250557577 418 FTDVAGLGKIRLELEEIVKF-FTHGEMYRRRGVKIPGGILLCGPPGVGKTLLAKAVAGEAGVNFFSISASQFVEIYVGVG 496
Cdd:cd19502     2 YEDIGGLDEQIREIREVVELpLKHPELFEELGIEPPKGVLLYGPPGTGKTLLAKAVANHTDATFIRVVGSELVQKYIGEG 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2250557577 497 ASRVRALYQEARENAPSVVFIDELDAVGRERGLIKGSGGQERDATLNQLLVCLDGFEGRGEVITIASTNRPDILDPALVR 576
Cdd:cd19502    82 ARLVRELFEMAREKAPSIIFIDEIDAIGAKRFDSGTGGDREVQRTMLELLNQLDGFDPRGNIKVIMATNRPDILDPALLR 161


                  ....*...
gi 2250557577 577 PGRFDRKI 584
Cdd:cd19502   162 PGRFDRKI 169
PTZ00361 PTZ00361
26 proteosome regulatory subunit 4-like protein; Provisional
 418-655 7.50e-55

26 proteosome regulatory subunit 4-like protein; Provisional


Pssm-ID: 185575 [Multi-domain]  Cd Length: 438  Bit Score: 196.53  E-value: 7.50e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2250557577 418 FTDVAGLGKIRLELEEIVKF-FTHGEMYRRRGVKIPGGILLCGPPGVGKTLLAKAVAGEAGVNFFSISASQFVEIYVGVG 496
Cdd:PTZ00361  182 YADIGGLEQQIQEIKEAVELpLTHPELYDDIGIKPPKGVILYGPPGTGKTLLAKAVANETSATFLRVVGSELIQKYLGDG 261

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2250557577 497 ASRVRALYQEARENAPSVVFIDELDAVGRERGLIKGSGGQERDATLNQLLVCLDGFEGRGEVITIASTNRPDILDPALVR 576
Cdd:PTZ00361  262 PKLVRELFRVAEENAPSIVFIDEIDAIGTKRYDATSGGEKEIQRTMLELLNQLDGFDSRGDVKVIMATNRIESLDPALIR 341

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2250557577 577 PGRFDRKIFIPKPGLIGRIEILKVHARKKPMAEDVDYMAIASMTDGMVGAELANIIEVAAINMMRDGRTEITTDDLLQA 655
Cdd:PTZ00361  342 PGRIDRKIEFPNPDEKTKRRIFEIHTSKMTLAEDVDLEEFIMAKDELSGADIKAICTEAGLLALRERRMKVTQADFRKA 420
RecA-like_CDC48_r2-like cd19511
second of two ATPase domains of CDC48/p97, PEX1 and -6, VAT and NVL, and similar ATPase ...
 427-586 2.00e-54

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


Pssm-ID: 410919 [Multi-domain]  Cd Length: 159  Bit Score: 185.56  E-value: 2.00e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2250557577 427 IRLELEEIVKF-FTHGEMYRRRGVKIPGGILLCGPPGVGKTLLAKAVAGEAGVNFFSISASQFVEIYVGVGASRVRALYQ 505
Cdd:cd19511     1 VKRELKEAVEWpLKHPDAFKRLGIRPPKGVLLYGPPGCGKTLLAKALASEAGLNFISVKGPELFSKYVGESERAVREIFQ 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2250557577 506 EARENAPSVVFIDELDAVGRERGLIKGSGGQERdaTLNQLLVCLDGFEGRGEVITIASTNRPDILDPALVRPGRFDRKIF 585
Cdd:cd19511    81 KARQAAPCIIFFDEIDSLAPRRGQSDSSGVTDR--VVSQLLTELDGIESLKGVVVIAATNRPDMIDPALLRPGRLDKLIY 158


                  .
gi 2250557577 586 I 586
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 ...
 420-586 7.01e-54

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


Pssm-ID: 410911 [Multi-domain]  Cd Length: 165  Bit Score: 184.42  E-value: 7.01e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2250557577 420 DVAGLGKIRLELEEIVKF-FTHGEMYRRRGVKIPGGILLCGPPGVGKTLLAKAVAGEAGVNFFSISASQFVEIYVGVGAS 498
Cdd:cd19503     1 DIGGLDEQIASLKELIELpLKYPELFRALGLKPPRGVLLHGPPGTGKTLLARAVANEAGANFLSISGPSIVSKYLGESEK 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2250557577 499 RVRALYQEARENAPSVVFIDELDAVGRERGliKGSGGQERDAtLNQLLVCLDGFEGRGEVITIASTNRPDILDPALVRPG 578
Cdd:cd19503    81 NLREIFEEARSHAPSIIFIDEIDALAPKRE--EDQREVERRV-VAQLLTLMDGMSSRGKVVVIAATNRPDAIDPALRRPG 157


                  ....*...
gi 2250557577 579 RFDRKIFI 586
Cdd:cd19503   158 RFDREVEI 165
AAA pfam00004
ATPase family associated with various cellular activities (AAA); AAA family proteins often ...
 455-587 2.79e-50

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: 172.78  E-value: 2.79e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2250557577 455 ILLCGPPGVGKTLLAKAVAGEAGVNFFSISASQFVEIYVGVGASRVRALYQEARENAPSVVFIDELDAVGRERGlikGSG 534
Cdd:pfam00004   1 LLLYGPPGTGKTTLAKAVAKELGAPFIEISGSELVSKYVGESEKRLRELFEAAKKLAPCVIFIDEIDALAGSRG---SGG 77

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 2250557577 535 GQERDATLNQLLVCLDGFEGR-GEVITIASTNRPDILDPALVrpGRFDRKIFIP 587
Cdd:pfam00004  78 DSESRRVVNQLLTELDGFTSSnSKVIVIAATNRPDKLDPALL--GRFDRIIEFP 129
RecA-like_VCP_r2 cd19529
second of two ATPase domains of Valosin-containing protein-like ATPase (VAT) and similar ...
 430-586 8.81e-50

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: 172.68  E-value: 8.81e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2250557577 430 ELEEIVKF-FTHGEMYRRRGVKIPGGILLCGPPGVGKTLLAKAVAGEAGVNFFSISASQFVEIYVGVGASRVRALYQEAR 508
Cdd:cd19529     4 ELKEAVEWpLLKPEVFKRLGIRPPKGILLYGPPGTGKTLLAKAVATESNANFISVKGPELLSKWVGESEKAIREIFRKAR 83

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2250557577 509 ENAPSVVFIDELDAVGRERGLIKGSGGQERdaTLNQLLVCLDGFEGRGEVITIASTNRPDILDPALVRPGRFDRKIFI 586
Cdd:cd19529    84 QVAPCVIFFDEIDSIAPRRGTTGDSGVTER--VVNQLLTELDGLEEMNGVVVIAATNRPDIIDPALLRAGRFDRLIYI 159
PTZ00454 PTZ00454
26S protease regulatory subunit 6B-like protein; Provisional
 415-655 1.73e-49

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


Pssm-ID: 240423 [Multi-domain]  Cd Length: 398  Bit Score: 179.96  E-value: 1.73e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2250557577 415 DVKFTDVAGLGKIRLELEEIVKF-FTHGEMYRRRGVKIPGGILLCGPPGVGKTLLAKAVAGEAGVNFFSISASQFVEIYV 493
Cdd:PTZ00454  141 DVTYSDIGGLDIQKQEIREAVELpLTCPELYEQIGIDPPRGVLLYGPPGTGKTMLAKAVAHHTTATFIRVVGSEFVQKYL 220

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2250557577 494 GVGASRVRALYQEARENAPSVVFIDELDAVGRERGLIKGSGGQERDATLNQLLVCLDGFEGRGEVITIASTNRPDILDPA 573
Cdd:PTZ00454  221 GEGPRMVRDVFRLARENAPSIIFIDEVDSIATKRFDAQTGADREVQRILLELLNQMDGFDQTTNVKVIMATNRADTLDPA 300

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2250557577 574 LVRPGRFDRKIFIPKPGLIGRIEILKVHARKKPMAEDVDYMAIASMTDGMVGAELANIIEVAAINMMRDGRTEITTDDLL 653
Cdd:PTZ00454  301 LLRPGRLDRKIEFPLPDRRQKRLIFQTITSKMNLSEEVDLEDFVSRPEKISAADIAAICQEAGMQAVRKNRYVILPKDFE 380


                  ..
gi 2250557577 654 QA 655
Cdd:PTZ00454  381 KG 382
RecA-like_NVL_r2-like cd19530
second of two ATPase domains of NVL (nuclear VCP-like protein) and similar ATPase domains; NVL ...
 424-586 8.64e-48

second of two ATPase domains of NVL (nuclear VCP-like protein) and similar ATPase domains; NVL exists in two forms with N-terminal extensions of different lengths in mammalian cells. NVL has two alternatively spliced isoforms, a short form, NVL1, and a long form, NVL2. NVL2, the major species, is mainly present in the nucleolus, whereas NVL1 is nucleoplasmic. Each has an N-terminal domain, followed by two tandem ATPase domains; this subfamily includes the first of the two ATPase domains. NVL2 is involved in the biogenesis of the 60S ribosome subunit by associating specifically with ribosome protein L5 and modulating the function of DOB1. NVL2 is also required for telomerase assembly and the regulation of telomerase activity, and is involved in pre-rRNA processing. The role of NVL1 is unclear. This RecA-like_NVL_r1-like subfamily belongs to the RecA-like NTPase family which includes the NTP binding domain of F1 and V1 H(+)ATPases, DnaB and related helicases as well as bacterial RecA and related eukaryotic and archaeal recombinases. The RecA-like NTPase family also includes bacterial conjugation proteins and related DNA transfer proteins involved in type II and type IV secretion.


Pssm-ID: 410938 [Multi-domain]  Cd Length: 161  Bit Score: 167.28  E-value: 8.64e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2250557577 424 LGKIRLELE-EIVKFFTHGEMYRRRGVKIPGGILLCGPPGVGKTLLAKAVAGEAGVNFFSISASQFVEIYVGVGASRVRA 502
Cdd:cd19530     1 LDHVREELTmSILRPIKRPDIYKALGIDLPTGVLLYGPPGCGKTLLAKAVANESGANFISVKGPELLNKYVGESERAVRQ 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2250557577 503 LYQEARENAPSVVFIDELDAVGRERGlIKGSGGQERdaTLNQLLVCLDGFEGRGEVITIASTNRPDILDPALVRPGRFDR 582
Cdd:cd19530    81 VFQRARASAPCVIFFDEVDALVPKRG-DGGSWASER--VVNQLLTEMDGLEERSNVFVIAATNRPDIIDPAMLRPGRLDK 157


                  ....
gi 2250557577 583 KIFI 586
Cdd:cd19530   158 TLYV 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 ...
 420-587 5.34e-47

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: 165.30  E-value: 5.34e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2250557577 420 DVAGLGKIRLELEEIVKF-FTHGEMYRRRGVKIPGGILLCGPPGVGKTLLAKAVAGEAGVNFFSISASQFVEIYVGVGAS 498
Cdd:cd19519     1 DIGGCRKQLAQIREMVELpLRHPELFKAIGIKPPRGILLYGPPGTGKTLIARAVANETGAFFFLINGPEIMSKLAGESES 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2250557577 499 RVRALYQEARENAPSVVFIDELDAVGRERGliKGSGGQERdATLNQLLVCLDGFEGRGEVITIASTNRPDILDPALVRPG 578
Cdd:cd19519    81 NLRKAFEEAEKNAPAIIFIDEIDAIAPKRE--KTHGEVER-RIVSQLLTLMDGLKQRAHVIVMAATNRPNSIDPALRRFG 157


                  ....*....
gi 2250557577 579 RFDRKIFIP 587
Cdd:cd19519   158 RFDREIDIG 166
RecA-like_CDC48_r2-like cd19528
second of two ATPase domains of CDC48 and similar ATPase domains; CDC48 in yeast and p97 or ...
 427-586 3.07e-45

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: 159.98  E-value: 3.07e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2250557577 427 IRLELEEIVKF-FTHGEMYRRRGVKIPGGILLCGPPGVGKTLLAKAVAGEAGVNFFSISASQFVEIYVGVGASRVRALYQ 505
Cdd:cd19528     1 VKRELQELVQYpVEHPDKFLKFGMTPSKGVLFYGPPGCGKTLLAKAIANECQANFISVKGPELLTMWFGESEANVRDIFD 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2250557577 506 EARENAPSVVFIDELDAVGRERGLIKGSGGQERDATLNQLLVCLDGFEGRGEVITIASTNRPDILDPALVRPGRFDRKIF 585
Cdd:cd19528    81 KARAAAPCVLFFDELDSIAKARGGNIGDAGGAADRVINQILTEMDGMNTKKNVFIIGATNRPDIIDPAILRPGRLDQLIY 160


                  .
gi 2250557577 586 I 586
Cdd:cd19528   161 I 161
RecA-like_NVL_r1-like cd19518
first of two ATPase domains of NVL (nuclear VCP-like protein) and similar ATPase domains; NVL ...
 420-584 5.07e-43

first of two ATPase domains of NVL (nuclear VCP-like protein) and similar ATPase domains; NVL exists in two forms with N-terminal extensions of different lengths in mammalian cells. NVL has two alternatively spliced isoforms, a short form, NVL1, and a long form, NVL2. NVL2, the major species, is mainly present in the nucleolus, whereas NVL1 is nucleoplasmic. Each has an N-terminal domain, followed by two tandem ATPase domains; this subfamily includes the first of the two ATPase domains. NVL2 is involved in the biogenesis of the 60S ribosome subunit by associating specifically with ribosome protein L5 and modulating the function of DOB1. NVL2 is also required for telomerase assembly and the regulation of telomerase activity, and is involved in pre-rRNA processing. The role of NVL1 is unclear. This RecA-like_NVL_r1-like subfamily belongs to the RecA-like NTPase family which includes the NTP binding domain of F1 and V1 H(+)ATPases, DnaB and related helicases as well as bacterial RecA and related eukaryotic and archaeal recombinases. The RecA-like NTPase family also includes bacterial conjugation proteins and related DNA transfer proteins involved in type II and type IV secretion.


Pssm-ID: 410926 [Multi-domain]  Cd Length: 169  Bit Score: 154.10  E-value: 5.07e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2250557577 420 DVAGLGKIRLELEEIVKF-FTHGEMYRRRGVKIPGGILLCGPPGVGKTLLAKAVAGEAGVNFFSISASQFVEIYVGVGAS 498
Cdd:cd19518     1 DIGGMDSTLKELCELLIHpILPPEYFQHLGVEPPRGVLLHGPPGCGKTMLANAIAGELKVPFLKISATEIVSGVSGESEE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2250557577 499 RVRALYQEARENAPSVVFIDELDAVGRERglikgsGGQERDA---TLNQLLVCLD--GFEGR--GEVITIASTNRPDILD 571
Cdd:cd19518    81 KIRELFDQAISNAPCIVFIDEIDAITPKR------ESAQREMerrIVSQLLTCMDelNNEKTagGPVLVIGATNRPDSLD 154

                         170
                  ....*....|...
gi 2250557577 572 PALVRPGRFDRKI 584
Cdd:cd19518   155 PALRRAGRFDREI 167
RecA-like_PEX6_r2 cd19527
second of two ATPase domains of Peroxisomal biogenesis factor 6 (PEX6); PEX6(also known as ...
 448-586 2.87e-39

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: 143.04  E-value: 2.87e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2250557577 448 GVKIPGGILLCGPPGVGKTLLAKAVAGEAGVNFFSISASQFVEIYVGVGASRVRALYQEARENAPSVVFIDELDAVGRER 527
Cdd:cd19527    22 GLRKRSGILLYGPPGTGKTLLAKAIATECSLNFLSVKGPELINMYIGESEANVREVFQKARDAKPCVIFFDELDSLAPSR 101

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 2250557577 528 GLIKGSGGQeRDATLNQLLVCLDGFEGRGE-VITIASTNRPDILDPALVRPGRFDRKIFI 586
Cdd:cd19527   102 GNSGDSGGV-MDRVVSQLLAELDGMSSSGQdVFVIGATNRPDLLDPALLRPGRFDKLLYL 160
RecA-like_PEX1_r2 cd19526
second of two ATPase domains of Peroxisomal biogenesis factor 1 (PEX1); PEX1(also known as ...
 431-585 1.41e-36

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: 135.25  E-value: 1.41e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2250557577 431 LEEIVKFFT-HGEMYRRRGVKIPGGILLCGPPGVGKTLLAKAVAGEAGVNFFSISASQFVEIYVGVGASRVRALYQEARE 509
Cdd:cd19526     5 LEETIEWPSkYPKIFASSPLRLRSGILLYGPPGCGKTLLASAIASECGLNFISVKGPELLNKYIGASEQNVRDLFSRAQS 84

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2250557577 510 NAPSVVFIDELDAVGRERGliKGSGGQErDATLNQLLVCLDGFEGRGEVITIASTNRPDILDPALVRPGRFDRKIF 585
Cdd:cd19526    85 AKPCILFFDEFDSIAPKRG--HDSTGVT-DRVVNQLLTQLDGVEGLDGVYVLAATSRPDLIDPALLRPGRLDKLVY 157
RecA-like_VPS4-like cd19509
ATPase domain of VPS4, ATAD1, K, KTNA1, Spastin, FIGL-1 and similar ATPase domains; This ...
 421-586 2.95e-35

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: 131.71  E-value: 2.95e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2250557577 421 VAGLGKIRLELEEIV-------KFFTHGEmyrrrgvKIPGGILLCGPPGVGKTLLAKAVAGEAGVNFFSISASQFVEIYV 493
Cdd:cd19509     1 IAGLDDAKEALKEAVilpslrpDLFPGLR-------GPPRGILLYGPPGTGKTLLARAVASESGSTFFSISASSLVSKWV 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2250557577 494 GVGASRVRALYQEARENAPSVVFIDELDAVGRERglikGSGGQERDATL-NQLLVCLDGFEGRGE--VITIASTNRPDIL 570
Cdd:cd19509    74 GESEKIVRALFALARELQPSIIFIDEIDSLLSER----GSGEHEASRRVkTEFLVQMDGVLNKPEdrVLVLGATNRPWEL 149

                         170
                  ....*....|....*.
gi 2250557577 571 DPALVRpgRFDRKIFI 586
Cdd:cd19509   150 DEAFLR--RFEKRIYI 163
RecA-like_Yta7-like cd19517
ATPase domain of Saccharomyces cerevisiae Yta7 and similar ATPase domains; Saccharomyces ...
 420-585 2.61e-34

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


Pssm-ID: 410925 [Multi-domain]  Cd Length: 170  Bit Score: 129.17  E-value: 2.61e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2250557577 420 DVAGLGKIRLELEEIVKF-FTHGEMYRRRGVKIPGGILLCGPPGVGKTLLAKAVAGEAG-----VNFFSISASQFVEIYV 493
Cdd:cd19517     1 DIGGLSHYINQLKEMVFFpLLYPEVFAKFKITPPRGVLFHGPPGTGKTLMARALAAECSkggqkVSFFMRKGADCLSKWV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2250557577 494 GVGASRVRALYQEARENAPSVVFIDELDAVGRERglikgSGGQER--DATLNQLLVCLDGFEGRGEVITIASTNRPDILD 571
Cdd:cd19517    81 GEAERQLRLLFEEAYRMQPSIIFFDEIDGLAPVR-----SSKQEQihASIVSTLLALMDGLDNRGQVVVIGATNRPDALD 155

                         170
                  ....*....|....
gi 2250557577 572 PALVRPGRFDRKIF 585
Cdd:cd19517   156 PALRRPGRFDREFY 169
RecA-like_VPS4 cd19521
ATPase domain of vacuolar protein sorting-associated protein 4; Vacuolar protein ...
 415-586 1.06e-29

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: 115.73  E-value: 1.06e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2250557577 415 DVKFTDVAGLGKIRLELEEIV-------KFFTHGemyrRRGVKipgGILLCGPPGVGKTLLAKAVAGEAGVNFFSISASQ 487
Cdd:cd19521     3 NVKWEDVAGLEGAKEALKEAVilpvkfpHLFTGN----RKPWS---GILLYGPPGTGKSYLAKAVATEANSTFFSVSSSD 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2250557577 488 FVEIYVGVGASRVRALYQEARENAPSVVFIDELDAVGRERglikgsGGQERDATL---NQLLVCLDGFEGRGE-VITIAS 563
Cdd:cd19521    76 LVSKWMGESEKLVKQLFAMARENKPSIIFIDEVDSLCGTR------GEGESEASRrikTELLVQMNGVGNDSQgVLVLGA 149

                         170       180
                  ....*....|....*....|...
gi 2250557577 564 TNRPDILDPALVRpgRFDRKIFI 586
Cdd:cd19521   150 TNIPWQLDSAIRR--RFEKRIYI 170
RecA-like_spastin cd19524
ATPase domain of spastin; Spastin is an ATP-dependent microtubule-severing protein involved in ...
 420-586 1.83e-29

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: 114.95  E-value: 1.83e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2250557577 420 DVAGLGKIRLELEEIV-------KFFThgemyrrrGVKIPG-GILLCGPPGVGKTLLAKAVAGEAGVNFFSISASQFVEI 491
Cdd:cd19524     1 DIAGQDLAKQALQEMVilpslrpELFT--------GLRAPArGLLLFGPPGNGKTMLAKAVAAESNATFFNISAASLTSK 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2250557577 492 YVGVGASRVRALYQEARENAPSVVFIDELDAVGRERglikgsGGQERDATL---NQLLVCLDGFEGRGE--VITIASTNR 566
Cdd:cd19524    73 YVGEGEKLVRALFAVARELQPSIIFIDEVDSLLSER------SEGEHEASRrlkTEFLIEFDGVQSNGDdrVLVMGATNR 146

                         170       180
                  ....*....|....*....|
gi 2250557577 567 PDILDPALVRpgRFDRKIFI 586
Cdd:cd19524   147 PQELDDAVLR--RFTKRVYV 164
RecA-like_KTNA1 cd19522
Katanin p60 ATPase-containing subunit A1; Katanin p60 ATPase-containing subunit A1 (KTNA1) is ...
 420-586 1.36e-28

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: 112.77  E-value: 1.36e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2250557577 420 DVAGLGKIRLELEEIV-------KFFthgemyrrRGVKIP-GGILLCGPPGVGKTLLAKAVAGEAGVNFFSISASQFVEI 491
Cdd:cd19522     1 DIADLEEAKKLLEEAVvlpmwmpEFF--------KGIRRPwKGVLMVGPPGTGKTLLAKAVATECGTTFFNVSSSTLTSK 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2250557577 492 YVGVGASRVRALYQEARENAPSVVFIDELDAVGRERGlikgsGGQERDATL---NQLLVCLDGFEGRGE-------VITI 561
Cdd:cd19522    73 YRGESEKLVRLLFEMARFYAPTTIFIDEIDSICSRRG-----TSEEHEASRrvkSELLVQMDGVGGASEnddpskmVMVL 147

                         170       180
                  ....*....|....*....|....*
gi 2250557577 562 ASTNRPDILDPALVRpgRFDRKIFI 586
Cdd:cd19522   148 AATNFPWDIDEALRR--RLEKRIYI 170
RecA-like_ATAD1 cd19520
ATPase domain of ATPase family AAA domain-containing protein 1 and similar ATPase domains; ...
 420-580 5.58e-28

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: 110.98  E-value: 5.58e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2250557577 420 DVAGLGKIRLELEEIVKF-FTHGEMYRRRGV-KIPGGILLCGPPGVGKTLLAKAVAGEAGVNFFSISASQFVEIYVGVGA 497
Cdd:cd19520     1 DIGGLDEVITELKELVILpLQRPELFDNSRLlQPPKGVLLYGPPGCGKTMLAKATAKEAGARFINLQVSSLTDKWYGESQ 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2250557577 498 SRVRALYQEARENAPSVVFIDELDAVGRERglikGSGGQERDATL-NQLLVCLDGF--EGRGEVITIASTNRPDILDPAL 574
Cdd:cd19520    81 KLVAAVFSLASKLQPSIIFIDEIDSFLRQR----SSTDHEATAMMkAEFMSLWDGLstDGNCRVIVMGATNRPQDLDEAI 156


                  ....*...
gi 2250557577 575 VR--PGRF 580
Cdd:cd19520   157 LRrmPKRF 164
RecA-like_Figl-1 cd19525
ATPase domain of Fidgetin-Like 1 (FIGL-1); FIGL-1 may participate in DNA repair in the nucleus; ...
 408-586 6.11e-28

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: 111.62  E-value: 6.11e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2250557577 408 QYLERGVDVKFTDVAGLGKIRLELEEIVKF-FTHGEMYRrrGVKIP-GGILLCGPPGVGKTLLAKAVAGEAGVNFFSISA 485
Cdd:cd19525    11 EIMDHGPPINWADIAGLEFAKKTIKEIVVWpMLRPDIFT--GLRGPpKGILLFGPPGTGKTLIGKCIASQSGATFFSISA 88

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2250557577 486 SQFVEIYVGVGASRVRALYQEARENAPSVVFIDELDAVGRERglikGSGGQERDATL-NQLLVCLDGFEGRGE--VITIA 562
Cdd:cd19525    89 SSLTSKWVGEGEKMVRALFSVARCKQPAVIFIDEIDSLLSQR----GEGEHESSRRIkTEFLVQLDGATTSSEdrILVVG 164

                         170       180
                  ....*....|....*....|....
gi 2250557577 563 STNRPDILDPALVRpgRFDRKIFI 586
Cdd:cd19525   165 ATNRPQEIDEAARR--RLVKRLYI 186
AAA cd00009
The AAA+ (ATPases Associated with a wide variety of cellular Activities) superfamily ...
 452-588 1.62e-25

The AAA+ (ATPases Associated with a wide variety of cellular Activities) superfamily represents an ancient group of ATPases belonging to the ASCE (for additional strand, catalytic E) division of the P-loop NTPase fold. The ASCE division also includes ABC, RecA-like, VirD4-like, PilT-like, and SF1/2 helicases. Members of the AAA+ ATPases function as molecular chaperons, ATPase subunits of proteases, helicases, or nucleic-acid stimulated ATPases. The AAA+ proteins contain several distinct features in addition to the conserved alpha-beta-alpha core domain structure and the Walker A and B motifs of the P-loop NTPases.


Pssm-ID: 99707 [Multi-domain]  Cd Length: 151  Bit Score: 103.38  E-value: 1.62e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2250557577 452 PGGILLCGPPGVGKTLLAKAVAGEA---GVNFFSISASQFVEIYVGVGASRVRALYQE---ARENAPSVVFIDELDAVGR 525
Cdd:cd00009    19 PKNLLLYGPPGTGKTTLARAIANELfrpGAPFLYLNASDLLEGLVVAELFGHFLVRLLfelAEKAKPGVLFIDEIDSLSR 98

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2250557577 526 ErglikgsggqERDATLNQLLVCLDGFEGRGEVITIASTNRPDILDPALVRPGRFDRKIFIPK 588
Cdd:cd00009    99 G----------AQNALLRVLETLNDLRIDRENVRVIGATNRPLLGDLDRALYDRLDIRIVIPL 151
RecA-like_BCS1 cd19510
Mitochondrial chaperone BCS1; Mitochondrial chaperone BCS1 is necessary for the assembly of ...
 431-586 1.03e-24

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: 100.89  E-value: 1.03e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2250557577 431 LEEIVKFFTHGEMYRRRGVKIPGGILLCGPPGVGKTLLAKAVAGEAGVNFFSISASQfveiyVGVGASRVRALYQEAREN 510
Cdd:cd19510     2 IDDLKDFIKNEDWYNDRGIPYRRGYLLYGPPGTGKSSFIAALAGELDYDICDLNLSE-----VVLTDDRLNHLLNTAPKQ 76

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2250557577 511 apSVVFIDELDA--VGRERGLIKGSGGQERDA-TLNQLLVCLDGFEGRGEVITIASTNRPDILDPALVRPGRFDRKIFI 586
Cdd:cd19510    77 --SIILLEDIDAafESREHNKKNPSAYGGLSRvTFSGLLNALDGVASSEERIVFMTTNHIERLDPALIRPGRVDMKIYM 153
RecA-like_NSF-SEC18_r1-like cd19504
first of two ATPase domains of NSF and SEC18, and similar ATPase domains; ...
 442-586 6.15e-24

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: 99.49  E-value: 6.15e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2250557577 442 EMYRRRGVKIPGGILLCGPPGVGKTLLAKAV-----AGEAGVnffsISASQFVEIYVGVGASRVRALYQEARENAPS--- 513
Cdd:cd19504    25 EIVEQLGCKHVKGILLYGPPGTGKTLMARQIgkmlnAREPKI----VNGPEILNKYVGESEANIRKLFADAEEEQRRlga 100

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2250557577 514 -----VVFIDELDAVGRERGLIKGSGGQErDATLNQLLVCLDGFEGRGEVITIASTNRPDILDPALVRPGRFDRKIFI 586
Cdd:cd19504   101 nsglhIIIFDEIDAICKQRGSMAGSTGVH-DTVVNQLLSKIDGVEQLNNILVIGMTNRKDLIDEALLRPGRLEVQMEI 177
RecA-like_fidgetin cd19523
ATPase domain of fidgetin; Fidgetin (FIGN) is a ATP-dependent microtubule severing protein. ...
 420-586 6.76e-20

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: 87.63  E-value: 6.76e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2250557577 420 DVAGLGKIRLEL-EEIVKFFTHGEMYRRRgVKIPGGILLCGPPGVGKTLLAKAVAGEAGVNFFSISASQFVEIYVGVGAS 498
Cdd:cd19523     1 DIAGLGALKAAIkEEVLWPLLRPDAFSGL-LRLPRSILLFGPRGTGKTLLGRCLASQLGATFLRLRGSTLVAKWAGEGEK 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2250557577 499 RVRALYQEARENAPSVVFIDELDAVGRERGLIKGSGGQERdatlNQLLVCLDGFEGRGE--VITIASTNRPDILDPALVR 576
Cdd:cd19523    80 ILQASFLAARCRQPSVLFISDLDALLSSQDDEASPVGRLQ----VELLAQLDGVLGSGEdgVLVVCTTSKPEEIDESLRR 155

                         170
                  ....*....|
gi 2250557577 577 pgRFDRKIFI 586
Cdd:cd19523   156 --YFSKRLLV 163
ycf46 CHL00195
Ycf46; Provisional
 414-657 1.10e-18

Ycf46; Provisional


Pssm-ID: 177094 [Multi-domain]  Cd Length: 489  Bit Score: 90.08  E-value: 1.10e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2250557577 414 VDVKFTDVAGLGKIRLELEEIVKFFThgEMYRRRGVKIPGGILLCGPPGVGKTLLAKAVAGEAGVNFFSISASQFVEIYV 493
Cdd:CHL00195  223 VNEKISDIGGLDNLKDWLKKRSTSFS--KQASNYGLPTPRGLLLVGIQGTGKSLTAKAIANDWQLPLLRLDVGKLFGGIV 300

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2250557577 494 GVGASRVRALYQEARENAPSVVFIDELDAVgrerglIKGSGGQERDATLNQLLVCLDGF--EGRGEVITIASTNRPDILD 571
Cdd:CHL00195  301 GESESRMRQMIRIAEALSPCILWIDEIDKA------FSNSESKGDSGTTNRVLATFITWlsEKKSPVFVVATANNIDLLP 374

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2250557577 572 PALVRPGRFDRKIFIPKPGLIGRIEILKVHARK-KPMA-EDVDYMAIASMTDGMVGAElaniIEVAAINMMR---DGRTE 646
Cdd:CHL00195  375 LEILRKGRFDEIFFLDLPSLEEREKIFKIHLQKfRPKSwKKYDIKKLSKLSNKFSGAE----IEQSIIEAMYiafYEKRE 450

                         250
                  ....*....|.
gi 2250557577 647 ITTDDLLQAAQ 657
Cdd:CHL00195  451 FTTDDILLALK 461
AAA smart00382
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ...
 452-589 3.62e-17

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: 79.34  E-value: 3.62e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2250557577  452 PGGILLCGPPGVGKTLLAKAVAGEAGVN---FFSISASQFVEI--------------YVGVGASRVRALYQEARENAPSV 514
Cdd:smart00382   2 GEVILIVGPPGSGKTTLARALARELGPPgggVIYIDGEDILEEvldqllliivggkkASGSGELRLRLALALARKLKPDV 81

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2250557577  515 VFIDELDAVGRERglikgsggQERDATLNQLLVCLDGFEGRGEVITIASTNRPDILDPALVRPgRFDRKIFIPKP 589
Cdd:smart00382  82 LILDEITSLLDAE--------QEALLLLLEELRLLLLLKSEKNLTVILTTNDEKDLGPALLRR-RFDRRIVLLLI 147
RecA-like_Ycf46-like cd19507
ATPase domain of Ycf46 and similar ATPase domains; Ycf46 may play a role in the regulation of ...
 420-586 4.77e-16

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: 76.25  E-value: 4.77e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2250557577 420 DVAGLGKIRLELEEIVKFFThgEMYRRRGVKIPGGILLCGPPGVGKTLLAKAVAGEAGVNFFSISASQFVEIYVGVGASR 499
Cdd:cd19507     1 DVGGLDNLKDWLKKRKAAFS--KQASAYGLPTPKGLLLVGIQGTGKSLTAKAIAGVWQLPLLRLDMGRLFGGLVGESESR 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2250557577 500 VRALYQEARENAPSVVFIDELD-AVGRERGliKGSGGQERdATLNQLLVCLDgfEGRGEVITIASTNRPDILDPALVRPG 578
Cdd:cd19507    79 LRQMIQTAEAIAPCVLWIDEIEkGFSNADS--KGDSGTSS-RVLGTFLTWLQ--EKKKPVFVVATANNVQSLPPELLRKG 153


                  ....*...
gi 2250557577 579 RFDRKIFI 586
Cdd:cd19507   154 RFDEIFFV 161
Peptidase_M41 pfam01434
Peptidase family M41;
663-844 8.78e-14

Peptidase family M41;


Pssm-ID: 460210 [Multi-domain]  Cd Length: 190  Bit Score: 70.71  E-value: 8.78e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2250557577 663 MLDRKERSLdtwkqVAINEAAMAVVAVNFPDLRNIEFVTIAPRaGRELGYVRM--KMDPikfreGMLTRQSLLDHITVQL 740
Cdd:pfam01434   2 VISEEEKKI-----VAYHEAGHALVGLLLPGADPVHKVTIIPR-GQALGYTQFlpEEDK-----LLYTKEQLLARIAVLL 70

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2250557577 741 APRAADELWFGEdqLSTIWAETADNARSAARTYVLG-GLSEKHhGLSNFWVADRLNDL------------------DVEA 801
Cdd:pfam01434  71 GGRAAEELIFGE--VTTGASNDLEKATKIARQMVTEfGMSDKL-GPVSLEESDGNVFLgrgmgkrkpyseetadiiDEEV 147

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 2250557577 802 LQIVNMCYERAKEILQKNRTLMDAVVDELVQKKSLTKQEFFSL 844
Cdd:pfam01434 148 KRLLEEAYERAKEILTEHRDELEALAEALLEKETLDAEEIREL 190
AAA_lid_3 pfam17862
AAA+ lid domain; This entry represents the alpha helical AAA+ lid domain that is found to the ...
 610-654 1.70e-09

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


Pssm-ID: 465537 [Multi-domain]  Cd Length: 45  Bit Score: 54.08  E-value: 1.70e-09
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 2250557577 610 DVDYMAIASMTDGMVGAELANIIEVAAINMMRDGRTEITTDDLLQ 654
Cdd:pfam17862   1 DVDLEELAERTEGFSGADLEALCREAALAALRRGLEAVTQEDLEE 45
RarA COG2256
Replication-associated recombination protein RarA (DNA-dependent ATPase) [Replication, ...
 455-519 1.76e-08

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


Pssm-ID: 441857 [Multi-domain]  Cd Length: 439  Bit Score: 57.76  E-value: 1.76e-08
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2250557577 455 ILLCGPPGVGKTLLAKAVAGEAGVNFFSISAsqfveiyVGVGASRVRALYQEARENA----PSVVFIDE 519
Cdd:COG2256    52 MILWGPPGTGKTTLARLIANATDAEFVALSA-------VTSGVKDIREVIEEARERRaygrRTILFVDE 113
RecA-like_Pch2-like cd19508
ATPase domain of Pachytene checkpoint 2 (Pch2) and similar ATPase domains; Pch2 (known as ...
 455-586 2.52e-08

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: 55.15  E-value: 2.52e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2250557577 455 ILLCGPPGVGKTLLAKAVAGEAGVNF-FSISASQFVEI--------YVGVGASRVRALYQEARE-----NAPSVVFIDEL 520
Cdd:cd19508    55 VLLHGPPGTGKTSLCKALAQKLSIRLsSRYRYGQLIEInshslfskWFSESGKLVTKMFQKIQEliddkDALVFVLIDEV 134

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2250557577 521 DAVGRERGLIKgSGGQERDA--TLNQLLVCLDGFEGRGEVITIASTNRPDILDPALVrpGRFDRKIFI 586
Cdd:cd19508   135 ESLAAARSASS-SGTEPSDAirVVNAVLTQIDRIKRYHNNVILLTSNLLEKIDVAFV--DRADIKQYI 199
PRK13342 PRK13342
recombination factor protein RarA; Reviewed
 455-519 4.23e-08

recombination factor protein RarA; Reviewed


Pssm-ID: 237355 [Multi-domain]  Cd Length: 413  Bit Score: 56.63  E-value: 4.23e-08
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2250557577 455 ILLCGPPGVGKTLLAKAVAGEAGVNFFSISAsqfveIYVGVgaSRVRALYQEARENAPS----VVFIDE 519
Cdd:PRK13342   39 MILWGPPGTGKTTLARIIAGATDAPFEALSA-----VTSGV--KDLREVIEEARQRRSAgrrtILFIDE 100
RecA-like_HslU cd19498
ATP-dependent protease ATPase subunit HslU; HslU is a component of the ATP-dependent protease ...
 444-539 1.41e-07

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: 52.38  E-value: 1.41e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2250557577 444 YRRRGVK-------IPGGILLCGPPGVGKTLLAKAVAGEAGVNFFSISASQFVEI-YVGvgasrvRALYQEARENAPSVV 515
Cdd:cd19498    31 WRRMQLPeelrdevTPKNILMIGPTGVGKTEIARRLAKLAGAPFIKVEATKFTEVgYVG------RDVESIIRDLVEGIV 104

                          90       100
                  ....*....|....*....|....*...
gi 2250557577 516 FIDELDAVGReRGLIKGSG----GQERD 539
Cdd:cd19498   105 FIDEIDKIAK-RGGSSGPDvsreGVQRD 131
RecA-like_Ycf2 cd19505
ATPase domain of plant YCF2; Ycf2 is a chloroplast ATPase which has an essential function; ...
 454-586 2.63e-07

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: 51.22  E-value: 2.63e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2250557577 454 GILLCGPPGVGKTLLAKAVAGEAGVNFFSISASQFV--------------EIYVGVGASRVRALYQEARENAPSVVFID- 518
Cdd:cd19505    14 GILLIGSIETGRSYLIKSLAANSYVPLIRISLNKLLynkpdfgnddwidgMLILKESLHRLNLQFELAKAMSPCIIWIPn 93

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2250557577 519 --ELDaVGRERGLIKGSggqeRDATLNQLLVCL-DGFEGRG--EVITIASTNRPDILDPALVRPGRFDRKIFI 586
Cdd:cd19505    94 ihELN-VNRSTQNLEED----PKLLLGLLLNYLsRDFEKSStrNILVIASTHIPQKVDPALIAPNRLDTCINI 161
RecA-like_Lon cd19500
lon protease homolog 2 peroxisomal; Lon protease (also known as Lon peptidase) is an ...
 420-525 2.74e-07

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: 51.41  E-value: 2.74e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2250557577 420 DVAGLGKIRlelEEIVKFFThgemYRRRGVKIPGGIL-LCGPPGVGKTLLAKAVAGEAGVNFFSIS---ASQFVEI---- 491
Cdd:cd19500    11 DHYGLEDVK---ERILEYLA----VRKLKGSMKGPILcLVGPPGVGKTSLGKSIARALGRKFVRISlggVRDEAEIrghr 83

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 2250557577 492 --YVGVGASRVRALYQEARENAPsVVFIDELDAVGR 525
Cdd:cd19500    84 rtYVGAMPGRIIQALKKAGTNNP-VFLLDEIDKIGS 118
RecA-like_ATAD3-like cd19512
ATPase domains of ATPase AAA-domain protein 3A (ATAD3A), -3B, and -3C, and similar ATPase ...
 455-574 6.17e-07

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: 49.83  E-value: 6.17e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2250557577 455 ILLCGPPGVGKTLLAKAVAGEAGVNFFSISASQFVEIyvgvGASRVRALYQ----EARENAPSVVFIDELDAVGRERGLI 530
Cdd:cd19512    25 ILFYGPPGTGKTLFAKKLALHSGMDYAIMTGGDVAPM----GREGVTAIHKvfdwANTSRRGLLLFVDEADAFLRKRSTE 100

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 2250557577 531 KGSggQERDATLNQLLVcLDGFEGRGEVITIAStNRPDILDPAL 574
Cdd:cd19512   101 KIS--EDLRAALNAFLY-RTGEQSNKFMLVLAS-NQPEQFDWAI 140
RecA-like_superfamily cd01120
RecA-like_NTPases; RecA-like NTPases. This superfamily includes the NTP binding domain of F1 ...
 455-592 7.26e-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: 7.26e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2250557577 455 ILLCGPPGVGKTLLAKAVAGEA---GVNFFSISasqFVEIYvgvgasrVRALYQEARENAPSVVFIDELDAVGRErglik 531
Cdd:cd01120     1 ILITGPPGSGKTTLLLQFAEQAllsDEPVIFIS---FLDTI-------LEAIEDLIEEKKLDIIIIDSLSSLARA----- 65

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2250557577 532 gSGGQERDATLNQLLVCLDGFeGRGEVITIASTNRPDILDpalvrpGRFDRKIFIPKPGLI 592
Cdd:cd01120    66 -SQGDRSSELLEDLAKLLRAA-RNTGITVIATIHSDKFDI------DRGGSSNDERLLKSL 118
AAA_5 pfam07728
AAA domain (dynein-related subfamily); This Pfam entry includes some of the AAA proteins not ...
 454-580 4.54e-06

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


Pssm-ID: 400191 [Multi-domain]  Cd Length: 135  Bit Score: 46.90  E-value: 4.54e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2250557577 454 GILLCGPPGVGKTLLAKAVAgEA--GVNFFSI------SASQFVEIYV--GVGASRV-RALYQEAREnaPSVVFIDELDA 522
Cdd:pfam07728   1 GVLLVGPPGTGKTELAERLA-AAlsNRPVFYVqltrdtTEEDLFGRRNidPGGASWVdGPLVRAARE--GEIAVLDEINR 77

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2250557577 523 VGR-----------ERGLIKGSGGQERDATLNQLLVcldgfegrgevitIASTNRPDI----LDPALVRpgRF 580
Cdd:pfam07728  78 ANPdvlnsllslldERRLLLPDGGELVKAAPDGFRL-------------IATMNPLDRglneLSPALRS--RF 135
RecA-like_IQCA1 cd19506
ATPase domain of IQ and AAA domain-containing protein 1 (IQCA1); IQCA1 (also known as dynein ...
 455-519 1.07e-05

ATPase domain of IQ and AAA domain-containing protein 1 (IQCA1); IQCA1 (also known as dynein regulatory complex subunit 11, DRC11 and IQCA) is an ATPase subunit of the nexin-dynein regulatory complex (N-DRC). The 9 + 2 axoneme of most motile cilia and flagella consists of nine outer doublet microtubules arranged in a ring surrounding a central pair of two singlet microtubules. The N-DRC complex maintains alignment between outer doublet microtubules and limits microtubule sliding in motile axonemes. 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: 410914 [Multi-domain]  Cd Length: 160  Bit Score: 46.37  E-value: 1.07e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2250557577 455 ILLCGPPGVGKTLLAKAVAGEAGVNFFSISASQFVEIYVGVGASR--VRALYQEARENAPSVVFIDE 519
Cdd:cd19506    29 LLLAGPSGVGKKMLVHAICTETGANLFNLSPSNIAGKYPGKNGLQmmLHLVLKVARQLQPSVIWIGD 95
AAA_2 pfam07724
AAA domain (Cdc48 subfamily); This Pfam entry includes some of the AAA proteins not detected ...
 455-521 1.13e-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: 46.42  E-value: 1.13e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2250557577 455 ILLCGPPGVGKTLLAKAVAGEAGV---NFFSISASQFVE-------I-----YVGVGASRVraLYQEARENAPSVVFIDE 519
Cdd:pfam07724   6 FLFLGPTGVGKTELAKALAELLFGderALIRIDMSEYMEehsvsrlIgappgYVGYEEGGQ--LTEAVRRKPYSIVLIDE 83


                  ..
gi 2250557577 520 LD 521
Cdd:pfam07724  84 IE 85
T7SS_EccA TIGR03922
type VII secretion AAA-ATPase EccA; This model represents the AAA family ATPase, EccA, of the ...
 390-584 7.93e-05

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


Pssm-ID: 188437 [Multi-domain]  Cd Length: 557  Bit Score: 46.38  E-value: 7.93e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2250557577 390 QFMKSGARVRRAHnkrlpqYLERGvDVKFTDVAGLGKIRLELEEIvKFFTHGEMYR-RRGVKIPGG---ILLCGPPGVGK 465
Cdd:TIGR03922 254 EFVDPAAAERKAK------LLAEA-EAELAEQIGLERVKRQVAAL-KSSTAMALARaERGLPVAQTsnhMLFAGPPGTGK 325

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2250557577 466 TLLAKAVAGE-AGV------NFFSISASQFVEIYVGVGASRVRALYQEAREnapSVVFIDELDAvgrergLIKGSGGQER 538
Cdd:TIGR03922 326 TTIARVVAKIyCGLgvlrkpLVREVSRADLIGQYIGESEAKTNEIIDSALG---GVLFLDEAYT------LVETGYGQKD 396

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 2250557577 539 D---ATLNQLLVCLDGfeGRGEVITIASTNRPDIlDPAL-VRPG---RFDRKI 584
Cdd:TIGR03922 397 PfglEAIDTLLARMEN--DRDRLVVIGAGYRKDL-DKFLeVNEGlrsRFTRVI 446
RecA-like_ClpB_Hsp104-like cd19499
Chaperone protein ClpB/Hsp104 subfamily; Bacterial Caseinolytic peptidase B (ClpB) and ...
 452-521 1.50e-04

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


Pssm-ID: 410907 [Multi-domain]  Cd Length: 178  Bit Score: 43.32  E-value: 1.50e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2250557577 452 PGGILLCGPPGVGKTLLAKAVAGE---AGVNFFSISASQFVE------------IYVGVGASRVraLYQEARENAPSVVF 516
Cdd:cd19499    41 IGSFLFLGPTGVGKTELAKALAELlfgDEDNLIRIDMSEYMEkhsvsrligappGYVGYTEGGQ--LTEAVRRKPYSVVL 118


                  ....*
gi 2250557577 517 IDELD 521
Cdd:cd19499   119 LDEIE 123
RuvB_N pfam05496
Holliday junction DNA helicase RuvB P-loop domain; The RuvB protein makes up part of the ...
 455-485 1.72e-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: 42.87  E-value: 1.72e-04
                          10        20        30
                  ....*....|....*....|....*....|.
gi 2250557577 455 ILLCGPPGVGKTLLAKAVAGEAGVNFFSISA 485
Cdd:pfam05496  36 VLLYGPPGLGKTTLANIIANEMGVNIRITSG 66
ruvB PRK00080
Holliday junction branch migration DNA helicase RuvB;
455-519 2.62e-04

Holliday junction branch migration DNA helicase RuvB;


Pssm-ID: 234619 [Multi-domain]  Cd Length: 328  Bit Score: 43.97  E-value: 2.62e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2250557577 455 ILLCGPPGVGKTLLAKAVAGEAGVNFFSISASQFVEiyvgvgASRVRALYQEARENapSVVFIDE 519
Cdd:PRK00080   54 VLLYGPPGLGKTTLANIIANEMGVNIRITSGPALEK------PGDLAAILTNLEEG--DVLFIDE 110
PRK04195 PRK04195
replication factor C large subunit; Provisional
 417-521 3.18e-04

replication factor C large subunit; Provisional


Pssm-ID: 235250 [Multi-domain]  Cd Length: 482  Bit Score: 44.14  E-value: 3.18e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2250557577 417 KFTDVAGLGKIRLELEEIVKFFTHGEMYRrrgvkipgGILLCGPPGVGKTLLAKAVAGEAGVNFFSISASQF-----VEI 491
Cdd:PRK04195   12 TLSDVVGNEKAKEQLREWIESWLKGKPKK--------ALLLYGPPGVGKTSLAHALANDYGWEVIELNASDQrtadvIER 83

                          90       100       110
                  ....*....|....*....|....*....|
gi 2250557577 492 YVGvGASRVRALYQEARenapSVVFIDELD 521
Cdd:PRK04195   84 VAG-EAATSGSLFGARR----KLILLDEVD 108
RuvB COG2255
Holliday junction resolvasome RuvABC, ATP-dependent DNA helicase subunit RuvB [Replication, ...
 455-485 4.88e-04

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


Pssm-ID: 441856 [Multi-domain]  Cd Length: 337  Bit Score: 43.15  E-value: 4.88e-04
                          10        20        30
                  ....*....|....*....|....*....|.
gi 2250557577 455 ILLCGPPGVGKTLLAKAVAGEAGVNFFSISA 485
Cdd:COG2255    57 VLLYGPPGLGKTTLAHIIANEMGVNIRITSG 87
ruvB TIGR00635
Holliday junction DNA helicase, RuvB subunit; All proteins in this family for which functions ...
 455-525 5.56e-04

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: 43.06  E-value: 5.56e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2250557577 455 ILLCGPPGVGKTLLAKAVAGEAGVNFFSISASQFVEiyvgvgASRVRALYQEARENapSVVFIDELDAVGR 525
Cdd:TIGR00635  33 LLLYGPPGLGKTTLAHIIANEMGVNLKITSGPALEK------PGDLAAILTNLEEG--DVLFIDEIHRLSP 95
TIP49 COG1224
DNA helicase TIP49, TBP-interacting protein [Transcription];
454-492 6.06e-04

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


Pssm-ID: 440837 [Multi-domain]  Cd Length: 452  Bit Score: 43.42  E-value: 6.06e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 2250557577 454 GILLCGPPGVGKTLLAKAVAGEAG--VNFFSISASqfvEIY 492
Cdd:COG1224    66 GILIVGPPGTGKTALAVAIARELGedTPFVAISGS---EIY 103
TIP49 pfam06068
TIP49 P-loop domain; This family consists of the C-terminal region of several eukaryotic and ...
 450-492 9.21e-04

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: 42.30  E-value: 9.21e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 2250557577 450 KIPG-GILLCGPPGVGKTLLAKAVAGEAG--VNFFSISASqfvEIY 492
Cdd:pfam06068  47 KIAGrAVLIAGPPGTGKTALAIAISKELGedTPFTSISGS---EVY 89
RecA-like_ClpX cd19497
ATP-dependent Clp protease ATP-binding subunit ClpX; ClpX is a component of the ATP-dependent ...
 440-525 1.18e-03

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


Pssm-ID: 410905 [Multi-domain]  Cd Length: 251  Bit Score: 41.43  E-value: 1.18e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2250557577 440 HGEMYRRRGVKIP-GGILLCGPPGVGKTLLAKAVAGEAGVNFFSISASQFVEI-YVG--VGASRVRaLYQEARENAPS-- 513
Cdd:cd19497    37 NNLKQKDDDVELEkSNILLIGPTGSGKTLLAQTLAKILDVPFAIADATTLTEAgYVGedVENILLK-LLQAADYDVERaq 115

                          90
                  ....*....|....
gi 2250557577 514 --VVFIDELDAVGR 525
Cdd:cd19497   116 rgIVYIDEIDKIAR 129
44 PHA02544
clamp loader, small subunit; Provisional
 450-524 1.52e-03

clamp loader, small subunit; Provisional


Pssm-ID: 222866 [Multi-domain]  Cd Length: 316  Bit Score: 41.51  E-value: 1.52e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2250557577 450 KIPGGILLCGPPGVGKTLLAKAVAGEAGVNFFSISAS----QFVEIYVGVGASRVralyqeARENAPSVVFIDELDAVG 524
Cdd:PHA02544   41 RIPNMLLHSPSPGTGKTTVAKALCNEVGAEVLFVNGSdcriDFVRNRLTRFASTV------SLTGGGKVIIIDEFDRLG 113
Kti12 COG4088
tRNA uridine 5-carbamoylmethylation protein Kti12 (Killer toxin insensitivity protein) ...
 455-509 2.01e-03

tRNA uridine 5-carbamoylmethylation protein Kti12 (Killer toxin insensitivity protein) [Translation, ribosomal structure and biogenesis, Defense mechanisms];


Pssm-ID: 443264 [Multi-domain]  Cd Length: 179  Bit Score: 40.10  E-value: 2.01e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 2250557577 455 ILLCGPPGVGKTLLAKAVAGE---AGVNFFSISASQFVEIYVGVGA--SRVRALYQEARE 509
Cdd:COG4088     7 LILTGPPGSGKTTFAKALAQRlyaEGIAVALLHSDDFRRFLVNESFpkETYEEVVEDVRT 66
PRK13341 PRK13341
AAA family ATPase;
453-519 3.62e-03

AAA family ATPase;


Pssm-ID: 237354 [Multi-domain]  Cd Length: 725  Bit Score: 41.19  E-value: 3.62e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2250557577 453 GGILLCGPPGVGKTLLAKAVAGEAGVNFFSISAsqfveiyVGVGASRVRALYQEARE-----NAPSVVFIDE 519
Cdd:PRK13341   53 GSLILYGPPGVGKTTLARIIANHTRAHFSSLNA-------VLAGVKDLRAEVDRAKErlerhGKRTILFIDE 117
MoxR COG0714
MoxR-like ATPase [General function prediction only]; MoxR-like ATPase is part of the Pathway ...
 455-488 3.68e-03

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: 40.15  E-value: 3.68e-03
                          10        20        30
                  ....*....|....*....|....*....|....
gi 2250557577 455 ILLCGPPGVGKTLLAKAVAGEAGVNFFSIsasQF 488
Cdd:COG0714    34 LLLEGVPGVGKTTLAKALARALGLPFIRI---QF 64
PRK11388 PRK11388
DNA-binding transcriptional regulator DhaR; Provisional
 424-475 7.30e-03

DNA-binding transcriptional regulator DhaR; Provisional


Pssm-ID: 183114 [Multi-domain]  Cd Length: 638  Bit Score: 40.05  E-value: 7.30e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 2250557577 424 LGKIRLELEEIVKffTHGEMYR-----RRGVKIPGGILLCGPPGVGKTLLAKAVAGE 475
Cdd:PRK11388  317 LGKVSHTFDHMPQ--DSPQMRRlihfgRQAAKSSFPVLLCGEEGVGKALLAQAIHNE 371
 
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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