NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|259445303|emb|CBF59607|]
View 

unnamed protein product [Schizosaccharomyces pombe]

Protein Classification

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

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

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

Name Accession Description Interval E-value
HflB COG0465
ATP-dependent Zn proteases [Posttranslational modification, protein turnover, chaperones];
257-699 0e+00

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


:

Pssm-ID: 440233 [Multi-domain]  Cd Length: 583  Bit Score: 682.53  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259445303 257 MEERAINVRFSDVQGVDEAKEELEEIVDFLRDPTHFTRLGGKLPRGVLLTGPPGTGKTMLARAVAGEANVPFFFMSGSQF 336
Cdd:COG0465  132 YDEDKPKVTFDDVAGVDEAKEELQEIVDFLKDPEKFTRLGAKIPKGVLLVGPPGTGKTLLAKAVAGEAGVPFFSISGSDF 211
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259445303 337 DEMYVGVGAKRVRELFAAARKQAPSIIFIDELDAIGQKRNA--------RDaahmrQTLNQLLVDLDGFSKNEDlahpVV 408
Cdd:COG0465  212 VEMFVGVGASRVRDLFEQAKKNAPCIIFIDEIDAVGRQRGAglggghdeRE-----QTLNQLLVEMDGFEGNEG----VI 282
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259445303 409 FIGATNFPESLDPALTRPGRFDRHIHVPLPDVRGRLAILLQHTRHVPLGKDVDLSIIARGTSGFAGADLANLINQAAVYA 488
Cdd:COG0465  283 VIAATNRPDVLDPALLRPGRFDRQVVVDLPDVKGREAILKVHARKKPLAPDVDLEVIARRTPGFSGADLANLVNEAALLA 362
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259445303 489 SKNLSTAVSMRDLEWSKDRILMGAERKSAFITPENKLMTAYHEGGHALVALFTKNAMRPYKATIMPRGSSLGMTISLPDM 568
Cdd:COG0465  363 ARRNKKAVTMEDFEEAIDRVIAGPERKSRVISEKEKKITAYHEAGHALVAALLPGADPVHKVTIIPRGRALGYTMQLPEE 442
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259445303 569 DKDSWTREEYLAMLDVTMGGRAAEELLYGkdKITSGAHNDIDKATQVARRMVTEFGMSDRIGPVSLEAEMD--------- 639
Cdd:COG0465  443 DRYLYTKEELLDRIAVLLGGRAAEELVFG--EVTTGASNDLERATKIARAMVTEYGMSEKLGPVAYGESEGevflgrdig 520
                        410       420       430       440       450       460
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 259445303 640 ---NLSPATRALVESEIKSLLEASYERSLSLLKSHKKELDALATALVDYEFLTAEEMNRVVKG 699
Cdd:COG0465  521 qsrNYSEETAREIDEEVRRIIDEAYERAKEILTENRDKLDALAEALLEKETLDGEELEEILAG 583
 
Name Accession Description Interval E-value
HflB COG0465
ATP-dependent Zn proteases [Posttranslational modification, protein turnover, chaperones];
257-699 0e+00

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


Pssm-ID: 440233 [Multi-domain]  Cd Length: 583  Bit Score: 682.53  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259445303 257 MEERAINVRFSDVQGVDEAKEELEEIVDFLRDPTHFTRLGGKLPRGVLLTGPPGTGKTMLARAVAGEANVPFFFMSGSQF 336
Cdd:COG0465  132 YDEDKPKVTFDDVAGVDEAKEELQEIVDFLKDPEKFTRLGAKIPKGVLLVGPPGTGKTLLAKAVAGEAGVPFFSISGSDF 211
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259445303 337 DEMYVGVGAKRVRELFAAARKQAPSIIFIDELDAIGQKRNA--------RDaahmrQTLNQLLVDLDGFSKNEDlahpVV 408
Cdd:COG0465  212 VEMFVGVGASRVRDLFEQAKKNAPCIIFIDEIDAVGRQRGAglggghdeRE-----QTLNQLLVEMDGFEGNEG----VI 282
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259445303 409 FIGATNFPESLDPALTRPGRFDRHIHVPLPDVRGRLAILLQHTRHVPLGKDVDLSIIARGTSGFAGADLANLINQAAVYA 488
Cdd:COG0465  283 VIAATNRPDVLDPALLRPGRFDRQVVVDLPDVKGREAILKVHARKKPLAPDVDLEVIARRTPGFSGADLANLVNEAALLA 362
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259445303 489 SKNLSTAVSMRDLEWSKDRILMGAERKSAFITPENKLMTAYHEGGHALVALFTKNAMRPYKATIMPRGSSLGMTISLPDM 568
Cdd:COG0465  363 ARRNKKAVTMEDFEEAIDRVIAGPERKSRVISEKEKKITAYHEAGHALVAALLPGADPVHKVTIIPRGRALGYTMQLPEE 442
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259445303 569 DKDSWTREEYLAMLDVTMGGRAAEELLYGkdKITSGAHNDIDKATQVARRMVTEFGMSDRIGPVSLEAEMD--------- 639
Cdd:COG0465  443 DRYLYTKEELLDRIAVLLGGRAAEELVFG--EVTTGASNDLERATKIARAMVTEYGMSEKLGPVAYGESEGevflgrdig 520
                        410       420       430       440       450       460
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 259445303 640 ---NLSPATRALVESEIKSLLEASYERSLSLLKSHKKELDALATALVDYEFLTAEEMNRVVKG 699
Cdd:COG0465  521 qsrNYSEETAREIDEEVRRIIDEAYERAKEILTENRDKLDALAEALLEKETLDGEELEEILAG 583
FtsH_fam TIGR01241
ATP-dependent metalloprotease FtsH; HflB(FtsH) is a pleiotropic protein required for correct ...
258-698 0e+00

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


Pssm-ID: 273520 [Multi-domain]  Cd Length: 495  Bit Score: 601.97  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259445303  258 EERAINVRFSDVQGVDEAKEELEEIVDFLRDPTHFTRLGGKLPRGVLLTGPPGTGKTMLARAVAGEANVPFFFMSGSQFD 337
Cdd:TIGR01241  46 NEEKPKVTFKDVAGIDEAKEELMEIVDFLKNPSKFTKLGAKIPKGVLLVGPPGTGKTLLAKAVAGEAGVPFFSISGSDFV 125
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259445303  338 EMYVGVGAKRVRELFAAARKQAPSIIFIDELDAIGQKRNA--------RDaahmrQTLNQLLVDLDGFSKNEDlahpVVF 409
Cdd:TIGR01241 126 EMFVGVGASRVRDLFEQAKKNAPCIIFIDEIDAVGRQRGAglgggndeRE-----QTLNQLLVEMDGFGTNTG----VIV 196
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259445303  410 IGATNFPESLDPALTRPGRFDRHIHVPLPDVRGRLAILLQHTRHVPLGKDVDLSIIARGTSGFAGADLANLINQAAVYAS 489
Cdd:TIGR01241 197 IAATNRPDVLDPALLRPGRFDRQVVVDLPDIKGREEILKVHAKNKKLAPDVDLKAVARRTPGFSGADLANLLNEAALLAA 276
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259445303  490 KNLSTAVSMRDLEWSKDRILMGAERKSAFITPENKLMTAYHEGGHALVALFTKNAMRPYKATIMPRGSSLGMTISLPDMD 569
Cdd:TIGR01241 277 RKNKTEITMNDIEEAIDRVIAGPEKKSRVISEKEKKLVAYHEAGHALVGLLLKDADPVHKVTIIPRGQALGYTQFLPEED 356
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259445303  570 KDSWTREEYLAMLDVTMGGRAAEELLYGkdKITSGAHNDIDKATQVARRMVTEFGMSDRIGPVSLEAEMD---------- 639
Cdd:TIGR01241 357 KYLYTKSQLLAQIAVLLGGRAAEEIIFG--EVTTGASNDIKQATNIARAMVTEWGMSDKLGPVAYGSDGGdvflgrgfak 434
                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 259445303  640 --NLSPATRALVESEIKSLLEASYERSLSLLKSHKKELDALATALVDYEFLTAEEMNRVVK 698
Cdd:TIGR01241 435 akEYSEETAREIDEEVKRIIEEAYKRAKQILTENRDELELLAKALLEKETITREEIKELLA 495
hflB PRK10733
ATP-dependent zinc metalloprotease FtsH;
257-695 3.13e-158

ATP-dependent zinc metalloprotease FtsH;


Pssm-ID: 182683 [Multi-domain]  Cd Length: 644  Bit Score: 471.83  E-value: 3.13e-158
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259445303 257 MEERAINVRFSDVQGVDEAKEELEEIVDFLRDPTHFTRLGGKLPRGVLLTGPPGTGKTMLARAVAGEANVPFFFMSGSQF 336
Cdd:PRK10733 142 LTEDQIKTTFADVAGCDEAKEEVAELVEYLREPSRFQKLGGKIPKGVLMVGPPGTGKTLLAKAIAGEAKVPFFTISGSDF 221
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259445303 337 DEMYVGVGAKRVRELFAAARKQAPSIIFIDELDAIGQKRNA-RDAAH--MRQTLNQLLVDLDGFSKNEDlahpVVFIGAT 413
Cdd:PRK10733 222 VEMFVGVGASRVRDMFEQAKKAAPCIIFIDEIDAVGRQRGAgLGGGHdeREQTLNQMLVEMDGFEGNEG----IIVIAAT 297
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259445303 414 NFPESLDPALTRPGRFDRHIHVPLPDVRGRLAILLQHTRHVPLGKDVDLSIIARGTSGFAGADLANLINQAAVYASKNLS 493
Cdd:PRK10733 298 NRPDVLDPALLRPGRFDRQVVVGLPDVRGREQILKVHMRRVPLAPDIDAAIIARGTPGFSGADLANLVNEAALFAARGNK 377
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259445303 494 TAVSMRDLEWSKDRILMGAERKSAFITPENKLMTAYHEGGHALVALFTKNAMRPYKATIMPRGSSLGMTISLPDMDKDSW 573
Cdd:PRK10733 378 RVVSMVEFEKAKDKIMMGAERRSMVMTEAQKESTAYHEAGHAIIGRLVPEHDPVHKVTIIPRGRALGVTFFLPEGDAISA 457
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259445303 574 TREEYLAMLDVTMGGRAAEELLYGKDKITSGAHNDIDKATQVARRMVTEFGMSDRIGPVsLEAEMD-------------N 640
Cdd:PRK10733 458 SRQKLESQISTLYGGRLAEEIIYGPEHVSTGASNDIKVATNLARNMVTQWGFSEKLGPL-LYAEEEgevflgrsvakakH 536
                        410       420       430       440       450
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 259445303 641 LSPATRALVESEIKSLLEASYERSLSLLKSHKKELDALATALVDYEFLTAEE----MNR 695
Cdd:PRK10733 537 MSDETARIIDQEVKALIERNYNRARQLLTDNMDILHAMKDALMKYETIDAPQiddlMAR 595
RecA-like_FtsH cd19501
ATP-dependent zinc metalloprotease FtsH; FtsH ATPase is a processive, ATP-dependent zinc ...
264-435 1.25e-96

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: 295.68  E-value: 1.25e-96
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259445303 264 VRFSDVQGVDEAKEELEEIVDFLRDPTHFTRLGGKLPRGVLLTGPPGTGKTMLARAVAGEANVPFFFMSGSQFDEMYVGV 343
Cdd:cd19501    1 VTFKDVAGCEEAKEELKEVVEFLKNPEKFTKLGAKIPKGVLLVGPPGTGKTLLAKAVAGEAGVPFFSISGSDFVEMFVGV 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259445303 344 GAKRVRELFAAARKQAPSIIFIDELDAIGQKRNA---RDAAHMRQTLNQLLVDLDGFSKNEdlahPVVFIGATNFPESLD 420
Cdd:cd19501   81 GASRVRDLFEQAKKNAPCIVFIDEIDAVGRKRGAglgGGHDEREQTLNQLLVEMDGFESNT----GVIVIAATNRPDVLD 156
                        170
                 ....*....|....*
gi 259445303 421 PALTRPGRFDRHIHV 435
Cdd:cd19501  157 PALLRPGRFDRQVYV 171
Peptidase_M41 pfam01434
Peptidase family M41;
517-696 6.03e-86

Peptidase family M41;


Pssm-ID: 460210 [Multi-domain]  Cd Length: 190  Bit Score: 268.32  E-value: 6.03e-86
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259445303  517 AFITPENKLMTAYHEGGHALVALFTKNAMRPYKATIMPRGSSLGMTISLPDMDKDSWTREEYLAMLDVTMGGRAAEELLY 596
Cdd:pfam01434   1 RVISEEEKKIVAYHEAGHALVGLLLPGADPVHKVTIIPRGQALGYTQFLPEEDKLLYTKEQLLARIAVLLGGRAAEELIF 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259445303  597 GkdKITSGAHNDIDKATQVARRMVTEFGMSDRIGPVSLEAEMDN------------LSPATRALVESEIKSLLEASYERS 664
Cdd:pfam01434  81 G--EVTTGASNDLEKATKIARQMVTEFGMSDKLGPVSLEESDGNvflgrgmgkrkpYSEETADIIDEEVKRLLEEAYERA 158
                         170       180       190
                  ....*....|....*....|....*....|..
gi 259445303  665 LSLLKSHKKELDALATALVDYEFLTAEEMNRV 696
Cdd:pfam01434 159 KEILTEHRDELEALAEALLEKETLDAEEIREL 190
AAA smart00382
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ...
300-439 2.38e-19

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: 85.12  E-value: 2.38e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259445303   300 PRGVLLTGPPGTGKTMLARAVAGEANVP---FFFMSGSQFDE--------------MYVGVGAKRVRELFAAARKQAPSI 362
Cdd:smart00382   2 GEVILIVGPPGSGKTTLARALARELGPPgggVIYIDGEDILEevldqllliivggkKASGSGELRLRLALALARKLKPDV 81
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 259445303   363 IFIDELDAIGQKRNARDAahmrqtlnqLLVDLDGFSKNEDLAHPVVFIGATNFPESLDPALTRPgRFDRHIHVPLPD 439
Cdd:smart00382  82 LILDEITSLLDAEQEALL---------LLLEELRLLLLLKSEKNLTVILTTNDEKDLGPALLRR-RFDRRIVLLLIL 148
 
Name Accession Description Interval E-value
HflB COG0465
ATP-dependent Zn proteases [Posttranslational modification, protein turnover, chaperones];
257-699 0e+00

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


Pssm-ID: 440233 [Multi-domain]  Cd Length: 583  Bit Score: 682.53  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259445303 257 MEERAINVRFSDVQGVDEAKEELEEIVDFLRDPTHFTRLGGKLPRGVLLTGPPGTGKTMLARAVAGEANVPFFFMSGSQF 336
Cdd:COG0465  132 YDEDKPKVTFDDVAGVDEAKEELQEIVDFLKDPEKFTRLGAKIPKGVLLVGPPGTGKTLLAKAVAGEAGVPFFSISGSDF 211
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259445303 337 DEMYVGVGAKRVRELFAAARKQAPSIIFIDELDAIGQKRNA--------RDaahmrQTLNQLLVDLDGFSKNEDlahpVV 408
Cdd:COG0465  212 VEMFVGVGASRVRDLFEQAKKNAPCIIFIDEIDAVGRQRGAglggghdeRE-----QTLNQLLVEMDGFEGNEG----VI 282
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259445303 409 FIGATNFPESLDPALTRPGRFDRHIHVPLPDVRGRLAILLQHTRHVPLGKDVDLSIIARGTSGFAGADLANLINQAAVYA 488
Cdd:COG0465  283 VIAATNRPDVLDPALLRPGRFDRQVVVDLPDVKGREAILKVHARKKPLAPDVDLEVIARRTPGFSGADLANLVNEAALLA 362
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259445303 489 SKNLSTAVSMRDLEWSKDRILMGAERKSAFITPENKLMTAYHEGGHALVALFTKNAMRPYKATIMPRGSSLGMTISLPDM 568
Cdd:COG0465  363 ARRNKKAVTMEDFEEAIDRVIAGPERKSRVISEKEKKITAYHEAGHALVAALLPGADPVHKVTIIPRGRALGYTMQLPEE 442
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259445303 569 DKDSWTREEYLAMLDVTMGGRAAEELLYGkdKITSGAHNDIDKATQVARRMVTEFGMSDRIGPVSLEAEMD--------- 639
Cdd:COG0465  443 DRYLYTKEELLDRIAVLLGGRAAEELVFG--EVTTGASNDLERATKIARAMVTEYGMSEKLGPVAYGESEGevflgrdig 520
                        410       420       430       440       450       460
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 259445303 640 ---NLSPATRALVESEIKSLLEASYERSLSLLKSHKKELDALATALVDYEFLTAEEMNRVVKG 699
Cdd:COG0465  521 qsrNYSEETAREIDEEVRRIIDEAYERAKEILTENRDKLDALAEALLEKETLDGEELEEILAG 583
FtsH_fam TIGR01241
ATP-dependent metalloprotease FtsH; HflB(FtsH) is a pleiotropic protein required for correct ...
258-698 0e+00

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


Pssm-ID: 273520 [Multi-domain]  Cd Length: 495  Bit Score: 601.97  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259445303  258 EERAINVRFSDVQGVDEAKEELEEIVDFLRDPTHFTRLGGKLPRGVLLTGPPGTGKTMLARAVAGEANVPFFFMSGSQFD 337
Cdd:TIGR01241  46 NEEKPKVTFKDVAGIDEAKEELMEIVDFLKNPSKFTKLGAKIPKGVLLVGPPGTGKTLLAKAVAGEAGVPFFSISGSDFV 125
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259445303  338 EMYVGVGAKRVRELFAAARKQAPSIIFIDELDAIGQKRNA--------RDaahmrQTLNQLLVDLDGFSKNEDlahpVVF 409
Cdd:TIGR01241 126 EMFVGVGASRVRDLFEQAKKNAPCIIFIDEIDAVGRQRGAglgggndeRE-----QTLNQLLVEMDGFGTNTG----VIV 196
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259445303  410 IGATNFPESLDPALTRPGRFDRHIHVPLPDVRGRLAILLQHTRHVPLGKDVDLSIIARGTSGFAGADLANLINQAAVYAS 489
Cdd:TIGR01241 197 IAATNRPDVLDPALLRPGRFDRQVVVDLPDIKGREEILKVHAKNKKLAPDVDLKAVARRTPGFSGADLANLLNEAALLAA 276
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259445303  490 KNLSTAVSMRDLEWSKDRILMGAERKSAFITPENKLMTAYHEGGHALVALFTKNAMRPYKATIMPRGSSLGMTISLPDMD 569
Cdd:TIGR01241 277 RKNKTEITMNDIEEAIDRVIAGPEKKSRVISEKEKKLVAYHEAGHALVGLLLKDADPVHKVTIIPRGQALGYTQFLPEED 356
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259445303  570 KDSWTREEYLAMLDVTMGGRAAEELLYGkdKITSGAHNDIDKATQVARRMVTEFGMSDRIGPVSLEAEMD---------- 639
Cdd:TIGR01241 357 KYLYTKSQLLAQIAVLLGGRAAEEIIFG--EVTTGASNDIKQATNIARAMVTEWGMSDKLGPVAYGSDGGdvflgrgfak 434
                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 259445303  640 --NLSPATRALVESEIKSLLEASYERSLSLLKSHKKELDALATALVDYEFLTAEEMNRVVK 698
Cdd:TIGR01241 435 akEYSEETAREIDEEVKRIIEEAYKRAKQILTENRDELELLAKALLEKETITREEIKELLA 495
hflB PRK10733
ATP-dependent zinc metalloprotease FtsH;
257-695 3.13e-158

ATP-dependent zinc metalloprotease FtsH;


Pssm-ID: 182683 [Multi-domain]  Cd Length: 644  Bit Score: 471.83  E-value: 3.13e-158
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259445303 257 MEERAINVRFSDVQGVDEAKEELEEIVDFLRDPTHFTRLGGKLPRGVLLTGPPGTGKTMLARAVAGEANVPFFFMSGSQF 336
Cdd:PRK10733 142 LTEDQIKTTFADVAGCDEAKEEVAELVEYLREPSRFQKLGGKIPKGVLMVGPPGTGKTLLAKAIAGEAKVPFFTISGSDF 221
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259445303 337 DEMYVGVGAKRVRELFAAARKQAPSIIFIDELDAIGQKRNA-RDAAH--MRQTLNQLLVDLDGFSKNEDlahpVVFIGAT 413
Cdd:PRK10733 222 VEMFVGVGASRVRDMFEQAKKAAPCIIFIDEIDAVGRQRGAgLGGGHdeREQTLNQMLVEMDGFEGNEG----IIVIAAT 297
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259445303 414 NFPESLDPALTRPGRFDRHIHVPLPDVRGRLAILLQHTRHVPLGKDVDLSIIARGTSGFAGADLANLINQAAVYASKNLS 493
Cdd:PRK10733 298 NRPDVLDPALLRPGRFDRQVVVGLPDVRGREQILKVHMRRVPLAPDIDAAIIARGTPGFSGADLANLVNEAALFAARGNK 377
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259445303 494 TAVSMRDLEWSKDRILMGAERKSAFITPENKLMTAYHEGGHALVALFTKNAMRPYKATIMPRGSSLGMTISLPDMDKDSW 573
Cdd:PRK10733 378 RVVSMVEFEKAKDKIMMGAERRSMVMTEAQKESTAYHEAGHAIIGRLVPEHDPVHKVTIIPRGRALGVTFFLPEGDAISA 457
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259445303 574 TREEYLAMLDVTMGGRAAEELLYGKDKITSGAHNDIDKATQVARRMVTEFGMSDRIGPVsLEAEMD-------------N 640
Cdd:PRK10733 458 SRQKLESQISTLYGGRLAEEIIYGPEHVSTGASNDIKVATNLARNMVTQWGFSEKLGPL-LYAEEEgevflgrsvakakH 536
                        410       420       430       440       450
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 259445303 641 LSPATRALVESEIKSLLEASYERSLSLLKSHKKELDALATALVDYEFLTAEE----MNR 695
Cdd:PRK10733 537 MSDETARIIDQEVKALIERNYNRARQLLTDNMDILHAMKDALMKYETIDAPQiddlMAR 595
ftsH CHL00176
cell division protein; Validated
264-698 8.75e-149

cell division protein; Validated


Pssm-ID: 214386 [Multi-domain]  Cd Length: 638  Bit Score: 447.19  E-value: 8.75e-149
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259445303 264 VRFSDVQGVDEAKEELEEIVDFLRDPTHFTRLGGKLPRGVLLTGPPGTGKTMLARAVAGEANVPFFFMSGSQFDEMYVGV 343
Cdd:CHL00176 180 ITFRDIAGIEEAKEEFEEVVSFLKKPERFTAVGAKIPKGVLLVGPPGTGKTLLAKAIAGEAEVPFFSISGSEFVEMFVGV 259
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259445303 344 GAKRVRELFAAARKQAPSIIFIDELDAIGQKRNAR---DAAHMRQTLNQLLVDLDGFSKNEDlahpVVFIGATNFPESLD 420
Cdd:CHL00176 260 GAARVRDLFKKAKENSPCIVFIDEIDAVGRQRGAGiggGNDEREQTLNQLLTEMDGFKGNKG----VIVIAATNRVDILD 335
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259445303 421 PALTRPGRFDRHIHVPLPDVRGRLAILLQHTRHVPLGKDVDLSIIARGTSGFAGADLANLINQAAVYASKNLSTAVSMRD 500
Cdd:CHL00176 336 AALLRPGRFDRQITVSLPDREGRLDILKVHARNKKLSPDVSLELIARRTPGFSGADLANLLNEAAILTARRKKATITMKE 415
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259445303 501 LEWSKDRILMGAErKSAFITPENKLMTAYHEGGHALVALFTKNAMRPYKATIMPRGSSLGMTISLPDMDKDSWTREEYLA 580
Cdd:CHL00176 416 IDTAIDRVIAGLE-GTPLEDSKNKRLIAYHEVGHAIVGTLLPNHDPVQKVTLIPRGQAKGLTWFTPEEDQSLVSRSQILA 494
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259445303 581 MLDVTMGGRAAEELLYGKDKITSGAHNDIDKATQVARRMVTEFGMSDrIGPVSLEAE----------MDNLSPATRAL-- 648
Cdd:CHL00176 495 RIVGALGGRAAEEVVFGSTEVTTGASNDLQQVTNLARQMVTRFGMSS-IGPISLESNnstdpflgrfMQRNSEYSEEIad 573
                        410       420       430       440       450
                 ....*....|....*....|....*....|....*....|....*....|.
gi 259445303 649 -VESEIKSLLEASYERSLSLLKSHKKELDALATALVDYEFLTAEEMNRVVK 698
Cdd:CHL00176 574 kIDMEVRSILHTCYQYAYQILKDNRVLIDLLVELLLQKETIDGDEFREIVN 624
RPT1 COG1222
ATP-dependent 26S proteasome regulatory subunit [Posttranslational modification, protein ...
263-517 7.83e-101

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


Pssm-ID: 440835 [Multi-domain]  Cd Length: 326  Bit Score: 312.33  E-value: 7.83e-101
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259445303 263 NVRFSDVQGVDEAKEELEE-IVDFLRDPTHFTRLGGKLPRGVLLTGPPGTGKTMLARAVAGEANVPFFFMSGSQFDEMYV 341
Cdd:COG1222   74 DVTFDDIGGLDEQIEEIREaVELPLKNPELFRKYGIEPPKGVLLYGPPGTGKTLLAKAVAGELGAPFIRVRGSELVSKYI 153
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259445303 342 GVGAKRVRELFAAARKQAPSIIFIDELDAIGQKR-NARDAAHMRQTLNQLLVDLDGFSKNEDlahpVVFIGATNFPESLD 420
Cdd:COG1222  154 GEGARNVREVFELAREKAPSIIFIDEIDAIAARRtDDGTSGEVQRTVNQLLAELDGFESRGD----VLIIAATNRPDLLD 229
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259445303 421 PALTRPGRFDRHIHVPLPDVRGRLAILLQHTRHVPLGKDVDLSIIARGTSGFAGADLANLINQAAVYASKNLSTAVSMRD 500
Cdd:COG1222  230 PALLRPGRFDRVIEVPLPDEEAREEILKIHLRDMPLADDVDLDKLAKLTEGFSGADLKAIVTEAGMFAIREGRDTVTMED 309
                        250
                 ....*....|....*..
gi 259445303 501 LEWSKDRILMGAERKSA 517
Cdd:COG1222  310 LEKAIEKVKKKTETATN 326
RecA-like_FtsH cd19501
ATP-dependent zinc metalloprotease FtsH; FtsH ATPase is a processive, ATP-dependent zinc ...
264-435 1.25e-96

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: 295.68  E-value: 1.25e-96
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259445303 264 VRFSDVQGVDEAKEELEEIVDFLRDPTHFTRLGGKLPRGVLLTGPPGTGKTMLARAVAGEANVPFFFMSGSQFDEMYVGV 343
Cdd:cd19501    1 VTFKDVAGCEEAKEELKEVVEFLKNPEKFTKLGAKIPKGVLLVGPPGTGKTLLAKAVAGEAGVPFFSISGSDFVEMFVGV 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259445303 344 GAKRVRELFAAARKQAPSIIFIDELDAIGQKRNA---RDAAHMRQTLNQLLVDLDGFSKNEdlahPVVFIGATNFPESLD 420
Cdd:cd19501   81 GASRVRDLFEQAKKNAPCIVFIDEIDAVGRKRGAglgGGHDEREQTLNQLLVEMDGFESNT----GVIVIAATNRPDVLD 156
                        170
                 ....*....|....*
gi 259445303 421 PALTRPGRFDRHIHV 435
Cdd:cd19501  157 PALLRPGRFDRQVYV 171
Peptidase_M41 pfam01434
Peptidase family M41;
517-696 6.03e-86

Peptidase family M41;


Pssm-ID: 460210 [Multi-domain]  Cd Length: 190  Bit Score: 268.32  E-value: 6.03e-86
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259445303  517 AFITPENKLMTAYHEGGHALVALFTKNAMRPYKATIMPRGSSLGMTISLPDMDKDSWTREEYLAMLDVTMGGRAAEELLY 596
Cdd:pfam01434   1 RVISEEEKKIVAYHEAGHALVGLLLPGADPVHKVTIIPRGQALGYTQFLPEEDKLLYTKEQLLARIAVLLGGRAAEELIF 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259445303  597 GkdKITSGAHNDIDKATQVARRMVTEFGMSDRIGPVSLEAEMDN------------LSPATRALVESEIKSLLEASYERS 664
Cdd:pfam01434  81 G--EVTTGASNDLEKATKIARQMVTEFGMSDKLGPVSLEESDGNvflgrgmgkrkpYSEETADIIDEEVKRLLEEAYERA 158
                         170       180       190
                  ....*....|....*....|....*....|..
gi 259445303  665 LSLLKSHKKELDALATALVDYEFLTAEEMNRV 696
Cdd:pfam01434 159 KEILTEHRDELEALAEALLEKETLDAEEIREL 190
PRK03992 PRK03992
proteasome-activating nucleotidase; Provisional
257-522 2.93e-85

proteasome-activating nucleotidase; Provisional


Pssm-ID: 179699 [Multi-domain]  Cd Length: 389  Bit Score: 274.02  E-value: 2.93e-85
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259445303 257 ME-ERAINVRFSDVQGVDEAKEELEEIVDF-LRDPTHFTRLGGKLPRGVLLTGPPGTGKTMLARAVAGEANVPFFFMSGS 334
Cdd:PRK03992 120 MEvIESPNVTYEDIGGLEEQIREVREAVELpLKKPELFEEVGIEPPKGVLLYGPPGTGKTLLAKAVAHETNATFIRVVGS 199
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259445303 335 QFDEMYVGVGAKRVRELFAAARKQAPSIIFIDELDAIGQKR----NARDAAHMRqTLNQLLVDLDGFSKNEDlahpVVFI 410
Cdd:PRK03992 200 ELVQKFIGEGARLVRELFELAREKAPSIIFIDEIDAIAAKRtdsgTSGDREVQR-TLMQLLAEMDGFDPRGN----VKII 274
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259445303 411 GATNFPESLDPALTRPGRFDRHIHVPLPDVRGRLAILLQHTRHVPLGKDVDLSIIARGTSGFAGADLANLINQAAVYASK 490
Cdd:PRK03992 275 AATNRIDILDPAILRPGRFDRIIEVPLPDEEGRLEILKIHTRKMNLADDVDLEELAELTEGASGADLKAICTEAGMFAIR 354
                        250       260       270
                 ....*....|....*....|....*....|..
gi 259445303 491 NLSTAVSMRDLEWSKDRIlMGAERKSAFITPE 522
Cdd:PRK03992 355 DDRTEVTMEDFLKAIEKV-MGKEEKDSMEEPG 385
SpoVK COG0464
AAA+-type ATPase, SpoVK/Ycf46/Vps4 family [Cell wall/membrane/envelope biogenesis, Cell cycle ...
259-502 1.29e-76

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: 251.75  E-value: 1.29e-76
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259445303 259 ERAINVRFSDVQGVDEAKEELEEIVD-FLRDPTHFTRLGGKLPRGVLLTGPPGTGKTMLARAVAGEANVPFFFMSGSQFD 337
Cdd:COG0464  149 LELREAILDDLGGLEEVKEELRELVAlPLKRPELREEYGLPPPRGLLLYGPPGTGKTLLARALAGELGLPLIEVDLSDLV 228
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259445303 338 EMYVGVGAKRVRELFAAARKQAPSIIFIDELDAIGQKRNARDAAHMRQTLNQLLVDLDGFSknedlaHPVVFIGATNFPE 417
Cdd:COG0464  229 SKYVGETEKNLREVFDKARGLAPCVLFIDEADALAGKRGEVGDGVGRRVVNTLLTEMEELR------SDVVVIAATNRPD 302
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259445303 418 SLDPALTRpgRFDRHIHVPLPDVRGRLAILLQHTRHVPLGKDVDLSIIARGTSGFAGADLANLINQAAVYASKNLSTAVS 497
Cdd:COG0464  303 LLDPALLR--RFDEIIFFPLPDAEERLEIFRIHLRKRPLDEDVDLEELAEATEGLSGADIRNVVRRAALQALRLGREPVT 380

                 ....*
gi 259445303 498 MRDLE 502
Cdd:COG0464  381 TEDLL 385
26Sp45 TIGR01242
26S proteasome subunit P45 family; Many proteins may score above the trusted cutoff because an ...
252-509 5.50e-76

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: 248.95  E-value: 5.50e-76
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259445303  252 TEQEPM------EERAiNVRFSDVQGVDEAKEELEEIVDF-LRDPTHFTRLGGKLPRGVLLTGPPGTGKTMLARAVAGEA 324
Cdd:TIGR01242 102 TSKDPLvkgmevEERP-NVSYEDIGGLEEQIREIREAVELpLKHPELFEEVGIEPPKGVLLYGPPGTGKTLLAKAVAHET 180
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259445303  325 NVPFFFMSGSQFDEMYVGVGAKRVRELFAAARKQAPSIIFIDELDAIGQKRNARDAAHMRQ---TLNQLLVDLDGFSKNE 401
Cdd:TIGR01242 181 NATFIRVVGSELVRKYIGEGARLVREIFELAKEKAPSIIFIDEIDAIAAKRTDSGTSGDREvqrTLMQLLAELDGFDPRG 260
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259445303  402 DlahpVVFIGATNFPESLDPALTRPGRFDRHIHVPLPDVRGRLAILLQHTRHVPLGKDVDLSIIARGTSGFAGADLANLI 481
Cdd:TIGR01242 261 N----VKVIAATNRPDILDPALLRPGRFDRIIEVPLPDFEGRLEILKIHTRKMKLAEDVDLEAIAKMTEGASGADLKAIC 336
                         250       260
                  ....*....|....*....|....*...
gi 259445303  482 NQAAVYASKNLSTAVSMRDLEWSKDRIL 509
Cdd:TIGR01242 337 TEAGMFAIREERDYVTMDDFIKAVEKVL 364
CDC48 TIGR01243
AAA family ATPase, CDC48 subfamily; This subfamily of the AAA family ATPases includes two ...
263-509 1.46e-66

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: 233.26  E-value: 1.46e-66
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259445303  263 NVRFSDVQGVDEAKEELEEIVDF-LRDPTHFTRLGGKLPRGVLLTGPPGTGKTMLARAVAGEANVPFFFMSGSQFDEMYV 341
Cdd:TIGR01243 449 NVRWSDIGGLEEVKQELREAVEWpLKHPEIFEKMGIRPPKGVLLFGPPGTGKTLLAKAVATESGANFIAVRGPEILSKWV 528
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259445303  342 GVGAKRVRELFAAARKQAPSIIFIDELDAIGQKRNAR-DAAHMRQTLNQLLVDLDGFSKNEDlahpVVFIGATNFPESLD 420
Cdd:TIGR01243 529 GESEKAIREIFRKARQAAPAIIFFDEIDAIAPARGARfDTSVTDRIVNQLLTEMDGIQELSN----VVVIAATNRPDILD 604
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259445303  421 PALTRPGRFDRHIHVPLPDVRGRLAILLQHTRHVPLGKDVDLSIIARGTSGFAGADLANLINQAAVYASKNLSTAVSMRD 500
Cdd:TIGR01243 605 PALLRPGRFDRLILVPPPDEEARKEIFKIHTRSMPLAEDVDLEELAEMTEGYTGADIEAVCREAAMAALRESIGSPAKEK 684

                  ....*....
gi 259445303  501 LEWSKDRIL 509
Cdd:TIGR01243 685 LEVGEEEFL 693
CDC48 TIGR01243
AAA family ATPase, CDC48 subfamily; This subfamily of the AAA family ATPases includes two ...
248-492 3.17e-61

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: 218.62  E-value: 3.17e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259445303  248 MTNTTE----QEPMEER----AINVRFSDVQGVDEAKEELEEIVDF-LRDPTHFTRLGGKLPRGVLLTGPPGTGKTMLAR 318
Cdd:TIGR01243 151 VTEATEveirEKPVREEierkVPKVTYEDIGGLKEAKEKIREMVELpMKHPELFEHLGIEPPKGVLLYGPPGTGKTLLAK 230
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259445303  319 AVAGEANVPFFFMSGSQFDEMYVGVGAKRVRELFAAARKQAPSIIFIDELDAIGQKRNARDAAHMRQTLNQLLVDLDGFS 398
Cdd:TIGR01243 231 AVANEAGAYFISINGPEIMSKYYGESEERLREIFKEAEENAPSIIFIDEIDAIAPKREEVTGEVEKRVVAQLLTLMDGLK 310
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259445303  399 KNEDlahpVVFIGATNFPESLDPALTRPGRFDRHIHVPLPDVRGRLAILLQHTRHVPLGKDVDLSIIARGTSGFAGADLA 478
Cdd:TIGR01243 311 GRGR----VIVIGATNRPDALDPALRRPGRFDREIVIRVPDKRARKEILKVHTRNMPLAEDVDLDKLAEVTHGFVGADLA 386
                         250
                  ....*....|....
gi 259445303  479 NLINQAAVYASKNL 492
Cdd:TIGR01243 387 ALAKEAAMAALRRF 400
RecA-like_protease cd19481
proteases similar to RecA; RecA-like NTPases. This family includes the NTP binding domain of ...
275-435 1.83e-58

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: 194.81  E-value: 1.83e-58
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259445303 275 AKEELEEIVDFLRDPTHFTRLGGKLPRGVLLTGPPGTGKTMLARAVAGEANVPFFFMSGSQFDEMYVGVGAKRVRELFAA 354
Cdd:cd19481    1 LKASLREAVEAPRRGSRLRRYGLGLPKGILLYGPPGTGKTLLAKALAGELGLPLIVVKLSSLLSKYVGESEKNLRKIFER 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259445303 355 ARKQAPSIIFIDELDAIGQKR-NARDAAHMRQTLNQLLVDLDGFSKNEDlahpVVFIGATNFPESLDPALTRPGRFDRHI 433
Cdd:cd19481   81 ARRLAPCILFIDEIDAIGRKRdSSGESGELRRVLNQLLTELDGVNSRSK----VLVIAATNRPDLLDPALLRPGRFDEVI 156

                 ..
gi 259445303 434 HV 435
Cdd:cd19481  157 EF 158
RecA-like_PAN_like cd19502
proteasome activating nucleotidase PAN and related proteasome subunits; This subfamily ...
266-435 1.45e-57

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: 192.94  E-value: 1.45e-57
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259445303 266 FSDVQGVDEAKEELEEIVDF-LRDPTHFTRLGGKLPRGVLLTGPPGTGKTMLARAVAGEANVPFFFMSGSQFDEMYVGVG 344
Cdd:cd19502    2 YEDIGGLDEQIREIREVVELpLKHPELFEELGIEPPKGVLLYGPPGTGKTLLAKAVANHTDATFIRVVGSELVQKYIGEG 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259445303 345 AKRVRELFAAARKQAPSIIFIDELDAIGQKR---NARDAAHMRQTLNQLLVDLDGFskneDLAHPVVFIGATNFPESLDP 421
Cdd:cd19502   82 ARLVRELFEMAREKAPSIIFIDEIDAIGAKRfdsGTGGDREVQRTMLELLNQLDGF----DPRGNIKVIMATNRPDILDP 157
                        170
                 ....*....|....
gi 259445303 422 ALTRPGRFDRHIHV 435
Cdd:cd19502  158 ALLRPGRFDRKIEF 171
RecA-like_CDC48_NLV2_r1-like cd19503
first of two ATPase domains of CDC48 and NLV2, and similar ATPase domains; CDC48 in yeast and ...
268-433 7.55e-56

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: 187.88  E-value: 7.55e-56
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259445303 268 DVQGVDEAKEELEEIVDF-LRDPTHFTRLGGKLPRGVLLTGPPGTGKTMLARAVAGEANVPFFFMSGSQFDEMYVGVGAK 346
Cdd:cd19503    1 DIGGLDEQIASLKELIELpLKYPELFRALGLKPPRGVLLHGPPGTGKTLLARAVANEAGANFLSISGPSIVSKYLGESEK 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259445303 347 RVRELFAAARKQAPSIIFIDELDAIGQKRNARDAAHMRQTLNQLLVDLDGFSKnedlAHPVVFIGATNFPESLDPALTRP 426
Cdd:cd19503   81 NLREIFEEARSHAPSIIFIDEIDALAPKREEDQREVERRVVAQLLTLMDGMSS----RGKVVVIAATNRPDAIDPALRRP 156

                 ....*..
gi 259445303 427 GRFDRHI 433
Cdd:cd19503  157 GRFDREV 163
COG1223 COG1223
Predicted ATPase, AAA+ superfamily [General function prediction only];
266-514 1.14e-55

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


Pssm-ID: 440836 [Multi-domain]  Cd Length: 246  Bit Score: 190.48  E-value: 1.14e-55
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259445303 266 FSDVQGVDEAKEELEEIVDFLRDPTHFTRLGGKLPRGVLLTGPPGTGKTMLARAVAGEANVPFFFMSGSQFDEMYVGVGA 345
Cdd:COG1223    1 LDDVVGQEEAKKKLKLIIKELRRRENLRKFGLWPPRKILFYGPPGTGKTMLAEALAGELKLPLLTVRLDSLIGSYLGETA 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259445303 346 KRVRELFAAARkQAPSIIFIDELDAIG-QKRNARDAAHMRQTLNQLLVDLDGFSKNedlahpVVFIGATNFPESLDPALT 424
Cdd:COG1223   81 RNLRKLFDFAR-RAPCVIFFDEFDAIAkDRGDQNDVGEVKRVVNALLQELDGLPSG------SVVIAATNHPELLDSALW 153
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259445303 425 RpgRFDRHIHVPLPDVRGRLAILLQHTRHVPLGKDVDLSIIARGTSGFAGADLANLINQAAVYASKNLSTAVSMRDLE-- 502
Cdd:COG1223  154 R--RFDEVIEFPLPDKEERKEILELNLKKFPLPFELDLKKLAKKLEGLSGADIEKVLKTALKKAILEDREKVTKEDLEea 231
                        250
                 ....*....|....*
gi 259445303 503 ---WSKDRILMGAER 514
Cdd:COG1223  232 lkqRKERKKEPKKEG 246
PTZ00361 PTZ00361
26 proteosome regulatory subunit 4-like protein; Provisional
189-509 7.94e-55

26 proteosome regulatory subunit 4-like protein; Provisional


Pssm-ID: 185575 [Multi-domain]  Cd Length: 438  Bit Score: 194.22  E-value: 7.94e-55
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259445303 189 IVSSALGTSSKTPVYVVVDEPrftkffrifKFIAGLSVA---SYFVLLGMsIFAETSGLNNIMTntTEQEPMEErainvr 265
Cdd:PTZ00361 120 IVSSSVGPEYYVNILSFVDKE---------QLEPGCSVLlhnKTHSVVGI-LLDEVDPLVSVMK--VDKAPLES------ 181
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259445303 266 FSDVQGVDEAKEELEEIVDF-LRDPTHFTRLGGKLPRGVLLTGPPGTGKTMLARAVAGEANVPFFFMSGSQFDEMYVGVG 344
Cdd:PTZ00361 182 YADIGGLEQQIQEIKEAVELpLTHPELYDDIGIKPPKGVILYGPPGTGKTLLAKAVANETSATFLRVVGSELIQKYLGDG 261
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259445303 345 AKRVRELFAAARKQAPSIIFIDELDAIGQKRNARDAAHMRQ---TLNQLLVDLDGFSKNEDlahpVVFIGATNFPESLDP 421
Cdd:PTZ00361 262 PKLVRELFRVAEENAPSIVFIDEIDAIGTKRYDATSGGEKEiqrTMLELLNQLDGFDSRGD----VKVIMATNRIESLDP 337
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259445303 422 ALTRPGRFDRHIHVPLPDVRGRLAILLQHTRHVPLGKDVDLSIIARGTSGFAGADLANLINQAAVYASKNLSTAVSMRDL 501
Cdd:PTZ00361 338 ALIRPGRIDRKIEFPNPDEKTKRRIFEIHTSKMTLAEDVDLEEFIMAKDELSGADIKAICTEAGLLALRERRMKVTQADF 417

                 ....*...
gi 259445303 502 EWSKDRIL 509
Cdd:PTZ00361 418 RKAKEKVL 425
AAA pfam00004
ATPase family associated with various cellular activities (AAA); AAA family proteins often ...
303-437 2.01e-54

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: 182.79  E-value: 2.01e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259445303  303 VLLTGPPGTGKTMLARAVAGEANVPFFFMSGSQFDEMYVGVGAKRVRELFAAARKQAPSIIFIDELDAIGQKRNARDAAH 382
Cdd:pfam00004   1 LLLYGPPGTGKTTLAKAVAKELGAPFIEISGSELVSKYVGESEKRLRELFEAAKKLAPCVIFIDEIDALAGSRGSGGDSE 80
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 259445303  383 MRQTLNQLLVDLDGFSKNEdlaHPVVFIGATNFPESLDPALtrPGRFDRHIHVPL 437
Cdd:pfam00004  81 SRRVVNQLLTELDGFTSSN---SKVIVIAATNRPDKLDPAL--LGRFDRIIEFPL 130
PTZ00454 PTZ00454
26S protease regulatory subunit 6B-like protein; Provisional
257-502 7.51e-53

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


Pssm-ID: 240423 [Multi-domain]  Cd Length: 398  Bit Score: 187.66  E-value: 7.51e-53
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259445303 257 MEERAiNVRFSDVQGVDEAKEELEEIVDF-LRDPTHFTRLGGKLPRGVLLTGPPGTGKTMLARAVAGEANVPFFFMSGSQ 335
Cdd:PTZ00454 136 MSEKP-DVTYSDIGGLDIQKQEIREAVELpLTCPELYEQIGIDPPRGVLLYGPPGTGKTMLAKAVAHHTTATFIRVVGSE 214
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259445303 336 FDEMYVGVGAKRVRELFAAARKQAPSIIFIDELDAIGQKR-NARDAA--HMRQTLNQLLVDLDGFSKNEDlahpVVFIGA 412
Cdd:PTZ00454 215 FVQKYLGEGPRMVRDVFRLARENAPSIIFIDEVDSIATKRfDAQTGAdrEVQRILLELLNQMDGFDQTTN----VKVIMA 290
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259445303 413 TNFPESLDPALTRPGRFDRHIHVPLPDVRGRLAILLQHTRHVPLGKDVDLSIIARGTSGFAGADLANLINQAAVYASKNL 492
Cdd:PTZ00454 291 TNRADTLDPALLRPGRLDRKIEFPLPDRRQKRLIFQTITSKMNLSEEVDLEDFVSRPEKISAADIAAICQEAGMQAVRKN 370
                        250
                 ....*....|
gi 259445303 493 STAVSMRDLE 502
Cdd:PTZ00454 371 RYVILPKDFE 380
RecA-like_CDC48_r2-like cd19511
second of two ATPase domains of CDC48/p97, PEX1 and -6, VAT and NVL, and similar ATPase ...
275-435 2.77e-51

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: 175.16  E-value: 2.77e-51
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259445303 275 AKEELEEIVDF-LRDPTHFTRLGGKLPRGVLLTGPPGTGKTMLARAVAGEANVPFFFMSGSQFDEMYVGVGAKRVRELFA 353
Cdd:cd19511    1 VKRELKEAVEWpLKHPDAFKRLGIRPPKGVLLYGPPGCGKTLLAKALASEAGLNFISVKGPELFSKYVGESERAVREIFQ 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259445303 354 AARKQAPSIIFIDELDAIGQKRNARDAAH-MRQTLNQLLVDLDGFSKNEDlahpVVFIGATNFPESLDPALTRPGRFDRH 432
Cdd:cd19511   81 KARQAAPCIIFFDEIDSLAPRRGQSDSSGvTDRVVSQLLTELDGIESLKG----VVVIAATNRPDMIDPALLRPGRLDKL 156

                 ...
gi 259445303 433 IHV 435
Cdd:cd19511  157 IYV 159
RecA-like_NVL_r1-like cd19518
first of two ATPase domains of NVL (nuclear VCP-like protein) and similar ATPase domains; NVL ...
268-433 1.19e-49

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


Pssm-ID: 410926 [Multi-domain]  Cd Length: 169  Bit Score: 171.43  E-value: 1.19e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259445303 268 DVQGVDEAKEELEEIVDFL-RDPTHFTRLGGKLPRGVLLTGPPGTGKTMLARAVAGEANVPFFFMSGSQFDEMYVGVGAK 346
Cdd:cd19518    1 DIGGMDSTLKELCELLIHPiLPPEYFQHLGVEPPRGVLLHGPPGCGKTMLANAIAGELKVPFLKISATEIVSGVSGESEE 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259445303 347 RVRELFAAARKQAPSIIFIDELDAIGQKRNARDAAHMRQTLNQLLVDLDGFSKNEDLAHPVVFIGATNFPESLDPALTRP 426
Cdd:cd19518   81 KIRELFDQAISNAPCIVFIDEIDAITPKRESAQREMERRIVSQLLTCMDELNNEKTAGGPVLVIGATNRPDSLDPALRRA 160

                 ....*..
gi 259445303 427 GRFDRHI 433
Cdd:cd19518  161 GRFDREI 167
RecA-like_VCP_r2 cd19529
second of two ATPase domains of Valosin-containing protein-like ATPase (VAT) and similar ...
275-435 4.81e-49

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: 169.21  E-value: 4.81e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259445303 275 AKEELEEIVDF-LRDPTHFTRLGGKLPRGVLLTGPPGTGKTMLARAVAGEANVPFFFMSGSQFDEMYVGVGAKRVRELFA 353
Cdd:cd19529    1 VKQELKEAVEWpLLKPEVFKRLGIRPPKGILLYGPPGTGKTLLAKAVATESNANFISVKGPELLSKWVGESEKAIREIFR 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259445303 354 AARKQAPSIIFIDELDAIGQKRNAR-DAAHMRQTLNQLLVDLDGFSKNEDlahpVVFIGATNFPESLDPALTRPGRFDRH 432
Cdd:cd19529   81 KARQVAPCVIFFDEIDSIAPRRGTTgDSGVTERVVNQLLTELDGLEEMNG----VVVIAATNRPDIIDPALLRAGRFDRL 156

                 ...
gi 259445303 433 IHV 435
Cdd:cd19529  157 IYI 159
RecA-like_CDC48_r1-like cd19519
first of two ATPase domains of CDC48 and similar ATPase domains; CDC48 in yeast and p97 or VCP ...
268-436 1.30e-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: 165.69  E-value: 1.30e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259445303 268 DVQGVDEAKEELEEIVDF-LRDPTHFTRLGGKLPRGVLLTGPPGTGKTMLARAVAGEANVPFFFMSGSQFDEMYVGVGAK 346
Cdd:cd19519    1 DIGGCRKQLAQIREMVELpLRHPELFKAIGIKPPRGILLYGPPGTGKTLIARAVANETGAFFFLINGPEIMSKLAGESES 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259445303 347 RVRELFAAARKQAPSIIFIDELDAIGQKRNARDAAHMRQTLNQLLVDLDGFSKNEDlahpVVFIGATNFPESLDPALTRP 426
Cdd:cd19519   81 NLRKAFEEAEKNAPAIIFIDEIDAIAPKREKTHGEVERRIVSQLLTLMDGLKQRAH----VIVMAATNRPNSIDPALRRF 156
                        170
                 ....*....|
gi 259445303 427 GRFDRHIHVP 436
Cdd:cd19519  157 GRFDREIDIG 166
RecA-like_VPS4-like cd19509
ATPase domain of VPS4, ATAD1, K, KTNA1, Spastin, FIGL-1 and similar ATPase domains; This ...
269-435 4.18e-42

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: 150.20  E-value: 4.18e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259445303 269 VQGVDEAKEELEEIVDFLRDPTHFTRLGGKLPRGVLLTGPPGTGKTMLARAVAGEANVPFFFMSGSQFDEMYVGVGAKRV 348
Cdd:cd19509    1 IAGLDDAKEALKEAVILPSLRPDLFPGLRGPPRGILLYGPPGTGKTLLARAVASESGSTFFSISASSLVSKWVGESEKIV 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259445303 349 RELFAAARKQAPSIIFIDELDAIGQKRNARDAAHMRQTLNQLLVDLDGFSKNEDlaHPVVFIGATNFPESLDPALTRpgR 428
Cdd:cd19509   81 RALFALARELQPSIIFIDEIDSLLSERGSGEHEASRRVKTEFLVQMDGVLNKPE--DRVLVLGATNRPWELDEAFLR--R 156

                 ....*..
gi 259445303 429 FDRHIHV 435
Cdd:cd19509  157 FEKRIYI 163
RecA-like_CDC48_r2-like cd19528
second of two ATPase domains of CDC48 and similar ATPase domains; CDC48 in yeast and p97 or ...
276-435 9.52e-41

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: 146.50  E-value: 9.52e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259445303 276 KEELEEIVDF-LRDPTHFTRLGGKLPRGVLLTGPPGTGKTMLARAVAGEANVPFFFMSGSQFDEMYVGVGAKRVRELFAA 354
Cdd:cd19528    2 KRELQELVQYpVEHPDKFLKFGMTPSKGVLFYGPPGCGKTLLAKAIANECQANFISVKGPELLTMWFGESEANVRDIFDK 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259445303 355 ARKQAPSIIFIDELDAIGQKRN-----ARDAAHmrQTLNQLLVDLDGFSKNEDlahpVVFIGATNFPESLDPALTRPGRF 429
Cdd:cd19528   82 ARAAAPCVLFFDELDSIAKARGgnigdAGGAAD--RVINQILTEMDGMNTKKN----VFIIGATNRPDIIDPAILRPGRL 155

                 ....*.
gi 259445303 430 DRHIHV 435
Cdd:cd19528  156 DQLIYI 161
RecA-like_VPS4 cd19521
ATPase domain of vacuolar protein sorting-associated protein 4; Vacuolar protein ...
263-435 1.86e-39

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: 143.08  E-value: 1.86e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259445303 263 NVRFSDVQGVDEAKEELEEIVDF-LRDPTHFTrlGGKLP-RGVLLTGPPGTGKTMLARAVAGEANVPFFFMSGSQFDEMY 340
Cdd:cd19521    3 NVKWEDVAGLEGAKEALKEAVILpVKFPHLFT--GNRKPwSGILLYGPPGTGKSYLAKAVATEANSTFFSVSSSDLVSKW 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259445303 341 VGVGAKRVRELFAAARKQAPSIIFIDELDAIGQKRNARDAAHMRQTLNQLLVDLDGFSKNEDlahPVVFIGATNFPESLD 420
Cdd:cd19521   81 MGESEKLVKQLFAMARENKPSIIFIDEVDSLCGTRGEGESEASRRIKTELLVQMNGVGNDSQ---GVLVLGATNIPWQLD 157
                        170
                 ....*....|....*
gi 259445303 421 PALTRpgRFDRHIHV 435
Cdd:cd19521  158 SAIRR--RFEKRIYI 170
RecA-like_NVL_r2-like cd19530
second of two ATPase domains of NVL (nuclear VCP-like protein) and similar ATPase domains; NVL ...
272-435 2.74e-39

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: 142.24  E-value: 2.74e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259445303 272 VDEAKEELE-EIVDFLRDPTHFTRLGGKLPRGVLLTGPPGTGKTMLARAVAGEANVPFFFMSGSQFDEMYVGVGAKRVRE 350
Cdd:cd19530    1 LDHVREELTmSILRPIKRPDIYKALGIDLPTGVLLYGPPGCGKTLLAKAVANESGANFISVKGPELLNKYVGESERAVRQ 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259445303 351 LFAAARKQAPSIIFIDELDAIGQKRNARDAAHMRQTLNQLLVDLDGFSKNEDlahpVVFIGATNFPESLDPALTRPGRFD 430
Cdd:cd19530   81 VFQRARASAPCVIFFDEVDALVPKRGDGGSWASERVVNQLLTEMDGLEERSN----VFVIAATNRPDIIDPAMLRPGRLD 156

                 ....*
gi 259445303 431 RHIHV 435
Cdd:cd19530  157 KTLYV 161
RecA-like_Figl-1 cd19525
ATPase domain of Fidgetin-Like 1 (FIGL-1); FIGL-1 may participate in DNA repair in the nucleus; ...
264-435 3.24e-36

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: 134.73  E-value: 3.24e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259445303 264 VRFSDVQGVDEAKEELEEIV--DFLRdPTHFTRLGGKlPRGVLLTGPPGTGKTMLARAVAGEANVPFFFMSGSQFDEMYV 341
Cdd:cd19525   19 INWADIAGLEFAKKTIKEIVvwPMLR-PDIFTGLRGP-PKGILLFGPPGTGKTLIGKCIASQSGATFFSISASSLTSKWV 96
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259445303 342 GVGAKRVRELFAAARKQAPSIIFIDELDAIGQKRNARDAAHMRQTLNQLLVDLDGFSKNEDlaHPVVFIGATNFPESLDP 421
Cdd:cd19525   97 GEGEKMVRALFSVARCKQPAVIFIDEIDSLLSQRGEGEHESSRRIKTEFLVQLDGATTSSE--DRILVVGATNRPQEIDE 174
                        170
                 ....*....|....
gi 259445303 422 ALTRpgRFDRHIHV 435
Cdd:cd19525  175 AARR--RLVKRLYI 186
RecA-like_spastin cd19524
ATPase domain of spastin; Spastin is an ATP-dependent microtubule-severing protein involved in ...
268-435 5.85e-36

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: 133.05  E-value: 5.85e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259445303 268 DVQGVDEAKEELEEIVDFLRD-PTHFTRLGGKlPRGVLLTGPPGTGKTMLARAVAGEANVPFFFMSGSQFDEMYVGVGAK 346
Cdd:cd19524    1 DIAGQDLAKQALQEMVILPSLrPELFTGLRAP-ARGLLLFGPPGNGKTMLAKAVAAESNATFFNISAASLTSKYVGEGEK 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259445303 347 RVRELFAAARKQAPSIIFIDELDAIGQKRNARDAAHMRQTLNQLLVDLDGFSKNEDlaHPVVFIGATNFPESLDPALTRp 426
Cdd:cd19524   80 LVRALFAVARELQPSIIFIDEVDSLLSERSEGEHEASRRLKTEFLIEFDGVQSNGD--DRVLVMGATNRPQELDDAVLR- 156

                 ....*....
gi 259445303 427 gRFDRHIHV 435
Cdd:cd19524  157 -RFTKRVYV 164
RecA-like_PEX6_r2 cd19527
second of two ATPase domains of Peroxisomal biogenesis factor 6 (PEX6); PEX6(also known as ...
276-435 8.57e-36

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: 132.64  E-value: 8.57e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259445303 276 KEELEEIVDFLRDPTHFTRLGGKLPRGVLLTGPPGTGKTMLARAVAGEANVPFFFMSGSQFDEMYVGVGAKRVRELFAAA 355
Cdd:cd19527    2 KKEILDTIQLPLEHPELFSSGLRKRSGILLYGPPGTGKTLLAKAIATECSLNFLSVKGPELINMYIGESEANVREVFQKA 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259445303 356 RKQAPSIIFIDELDAIGQKR-NARDAAH-MRQTLNQLLVDLDGFSKNEDlahPVVFIGATNFPESLDPALTRPGRFDRHI 433
Cdd:cd19527   82 RDAKPCVIFFDELDSLAPSRgNSGDSGGvMDRVVSQLLAELDGMSSSGQ---DVFVIGATNRPDLLDPALLRPGRFDKLL 158

                 ..
gi 259445303 434 HV 435
Cdd:cd19527  159 YL 160
RecA-like_KTNA1 cd19522
Katanin p60 ATPase-containing subunit A1; Katanin p60 ATPase-containing subunit A1 (KTNA1) is ...
268-435 1.97e-34

Katanin p60 ATPase-containing subunit A1; Katanin p60 ATPase-containing subunit A1 (KTNA1) is the catalytic subunit of the Katanin complex which is severs microtubules in an ATP-dependent manner, and is implicated in multiple aspects of microtubule dynamics. In addition to the p60 catalytic ATPase subunit, Katanin contains an accessory subunit (p80 or p80-like). The microtubule-severing activity of the ATPase is essential for female meiotic spindle assembly, and male gamete production; and the katanin complex severing microtubules is under tight regulation during the transition from the meiotic to mitotic stage to allow proper embryogenesis. This subfamily belongs to the RecA-like NTPase family which includes the NTP binding domain of F1 and V1 H(+)ATPases, DnaB and related helicases as well as bacterial RecA and related eukaryotic and archaeal recombinases. The RecA-like NTPase family also includes bacterial conjugation proteins and related DNA transfer proteins involved in type II and type IV secretion.


Pssm-ID: 410930 [Multi-domain]  Cd Length: 170  Bit Score: 128.95  E-value: 1.97e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259445303 268 DVQGVDEAKEELEEIVDF-LRDPTHFTrlGGKLP-RGVLLTGPPGTGKTMLARAVAGEANVPFFFMSGSQFDEMYVGVGA 345
Cdd:cd19522    1 DIADLEEAKKLLEEAVVLpMWMPEFFK--GIRRPwKGVLMVGPPGTGKTLLAKAVATECGTTFFNVSSSTLTSKYRGESE 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259445303 346 KRVRELFAAARKQAPSIIFIDELDAIGQKRNARDAAHM-RQTLNQLLVDLDGFS---KNEDLAHPVVFIGATNFPESLDP 421
Cdd:cd19522   79 KLVRLLFEMARFYAPTTIFIDEIDSICSRRGTSEEHEAsRRVKSELLVQMDGVGgasENDDPSKMVMVLAATNFPWDIDE 158
                        170
                 ....*....|....
gi 259445303 422 ALTRpgRFDRHIHV 435
Cdd:cd19522  159 ALRR--RLEKRIYI 170
RecA-like_PEX1_r2 cd19526
second of two ATPase domains of Peroxisomal biogenesis factor 1 (PEX1); PEX1(also known as ...
275-433 2.42e-33

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: 125.62  E-value: 2.42e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259445303 275 AKEELEEIVDF-LRDPTHFTRLGGKLPRGVLLTGPPGTGKTMLARAVAGEANVPFFFMSGSQFDEMYVGVGAKRVRELFA 353
Cdd:cd19526    1 VKKALEETIEWpSKYPKIFASSPLRLRSGILLYGPPGCGKTLLASAIASECGLNFISVKGPELLNKYIGASEQNVRDLFS 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259445303 354 AARKQAPSIIFIDELDAIGQKRNARDAAHMRQTLNQLLVDLDGFsknEDLaHPVVFIGATNFPESLDPALTRPGRFDRHI 433
Cdd:cd19526   81 RAQSAKPCILFFDEFDSIAPKRGHDSTGVTDRVVNQLLTQLDGV---EGL-DGVYVLAATSRPDLIDPALLRPGRLDKLV 156
RecA-like_Yta7-like cd19517
ATPase domain of Saccharomyces cerevisiae Yta7 and similar ATPase domains; Saccharomyces ...
268-431 2.64e-33

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: 125.70  E-value: 2.64e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259445303 268 DVQGVDEAKEELEEIVDF-LRDPTHFTRLGGKLPRGVLLTGPPGTGKTMLARAVAGEAN-----VPFFFMSGSQFDEMYV 341
Cdd:cd19517    1 DIGGLSHYINQLKEMVFFpLLYPEVFAKFKITPPRGVLFHGPPGTGKTLMARALAAECSkggqkVSFFMRKGADCLSKWV 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259445303 342 GVGAKRVRELFAAARKQAPSIIFIDELDAIGQKRNARDAAHMRQTLNQLLVDLDGFskneDLAHPVVFIGATNFPESLDP 421
Cdd:cd19517   81 GEAERQLRLLFEEAYRMQPSIIFFDEIDGLAPVRSSKQEQIHASIVSTLLALMDGL----DNRGQVVVIGATNRPDALDP 156
                        170
                 ....*....|
gi 259445303 422 ALTRPGRFDR 431
Cdd:cd19517  157 ALRRPGRFDR 166
RecA-like_ATAD1 cd19520
ATPase domain of ATPase family AAA domain-containing protein 1 and similar ATPase domains; ...
268-429 1.04e-31

ATPase domain of ATPase family AAA domain-containing protein 1 and similar ATPase domains; ATPase family AAA domain-containing protein 1 (ATAD1, also known as Thorase) is an ATPase that plays a critical role in regulating the surface expression of alpha-amino-3-hydroxy-5-methyl-4-isoxazolepropionic acid (AMPA) receptors, thereby regulating synaptic plasticity, learning and memory. This subfamily belongs to the RecA-like NTPase family which includes the NTP binding domain of F1 and V1 H(+)ATPases, DnaB and related helicases as well as bacterial RecA and related eukaryotic and archaeal recombinases. The RecA-like NTPase family also includes bacterial conjugation proteins and related DNA transfer proteins involved in type II and type IV secretion.


Pssm-ID: 410928 [Multi-domain]  Cd Length: 166  Bit Score: 120.99  E-value: 1.04e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259445303 268 DVQGVDEAKEELEEIVDF-LRDPTHFTrlGGKL---PRGVLLTGPPGTGKTMLARAVAGEANVPFFFMSGSQFDEMYVGV 343
Cdd:cd19520    1 DIGGLDEVITELKELVILpLQRPELFD--NSRLlqpPKGVLLYGPPGCGKTMLAKATAKEAGARFINLQVSSLTDKWYGE 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259445303 344 GAKRVRELFAAARKQAPSIIFIDELDAIGQKRNARDAAHMRQTLNQLLVDLDGFSKNEDlaHPVVFIGATNFPESLDPAL 423
Cdd:cd19520   79 SQKLVAAVFSLASKLQPSIIFIDEIDSFLRQRSSTDHEATAMMKAEFMSLWDGLSTDGN--CRVIVMGATNRPQDLDEAI 156

                 ....*...
gi 259445303 424 TR--PGRF 429
Cdd:cd19520  157 LRrmPKRF 164
AAA cd00009
The AAA+ (ATPases Associated with a wide variety of cellular Activities) superfamily ...
271-437 2.22e-26

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: 105.31  E-value: 2.22e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259445303 271 GVDEAKEELEEIVDFLRdpthftrlggklPRGVLLTGPPGTGKTMLARAVAGEA---NVPFFFMSGSQFDEMYVG---VG 344
Cdd:cd00009    2 GQEEAIEALREALELPP------------PKNLLLYGPPGTGKTTLARAIANELfrpGAPFLYLNASDLLEGLVVaelFG 69
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259445303 345 AKRVRELFAAARKQAPSIIFIDELDAIGqkrnardaahmRQTLNQLLVDLDGFSKNEDLAHPVVFIGATNFPESLDPALT 424
Cdd:cd00009   70 HFLVRLLFELAEKAKPGVLFIDEIDSLS-----------RGAQNALLRVLETLNDLRIDRENVRVIGATNRPLLGDLDRA 138
                        170
                 ....*....|...
gi 259445303 425 RPGRFDRHIHVPL 437
Cdd:cd00009  139 LYDRLDIRIVIPL 151
RecA-like_BCS1 cd19510
Mitochondrial chaperone BCS1; Mitochondrial chaperone BCS1 is necessary for the assembly of ...
279-435 6.45e-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: 98.58  E-value: 6.45e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259445303 279 LEEIVDFLRDPTHFTRLGGKLPRGVLLTGPPGTGKTMLARAVAGEANVPFFFMSGSQfdemyVGVGAKRVRELFAAARKQ 358
Cdd:cd19510    2 IDDLKDFIKNEDWYNDRGIPYRRGYLLYGPPGTGKSSFIAALAGELDYDICDLNLSE-----VVLTDDRLNHLLNTAPKQ 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259445303 359 apSIIFIDELDAIGQKRNARDAAHM------RQTLNQLLVDLDGFSKNEDLahpvVFIGATNFPESLDPALTRPGRFDRH 432
Cdd:cd19510   77 --SIILLEDIDAAFESREHNKKNPSaygglsRVTFSGLLNALDGVASSEER----IVFMTTNHIERLDPALIRPGRVDMK 150

                 ...
gi 259445303 433 IHV 435
Cdd:cd19510  151 IYM 153
RecA-like_NSF-SEC18_r1-like cd19504
first of two ATPase domains of NSF and SEC18, and similar ATPase domains; ...
289-435 1.56e-22

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: 95.25  E-value: 1.56e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259445303 289 PTHFT-RLGGKLPRGVLLTGPPGTGKTMLARAV-----AGEANVpfffMSGSQFDEMYVGVGAKRVRELFAAA-----RK 357
Cdd:cd19504   23 PPEIVeQLGCKHVKGILLYGPPGTGKTLMARQIgkmlnAREPKI----VNGPEILNKYVGESEANIRKLFADAeeeqrRL 98
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259445303 358 QAPS---IIFIDELDAIGQKRNAR--DAAHMRQTLNQLLVDLDGFskneDLAHPVVFIGATNFPESLDPALTRPGRFDRH 432
Cdd:cd19504   99 GANSglhIIIFDEIDAICKQRGSMagSTGVHDTVVNQLLSKIDGV----EQLNNILVIGMTNRKDLIDEALLRPGRLEVQ 174

                 ...
gi 259445303 433 IHV 435
Cdd:cd19504  175 MEI 177
RecA-like_fidgetin cd19523
ATPase domain of fidgetin; Fidgetin (FIGN) is a ATP-dependent microtubule severing protein. ...
268-435 7.94e-22

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: 92.64  E-value: 7.94e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259445303 268 DVQGVDEAKEELEEIV--DFLRDPTHFTRLggKLPRGVLLTGPPGTGKTMLARAVAGEANVPFFFMSGSQFDEMYVGVGA 345
Cdd:cd19523    1 DIAGLGALKAAIKEEVlwPLLRPDAFSGLL--RLPRSILLFGPRGTGKTLLGRCLASQLGATFLRLRGSTLVAKWAGEGE 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259445303 346 KRVRELFAAARKQAPSIIFIDELDAIGQKRNARDAAHMRQTLnQLLVDLDG-FSKNEDlahPVVFIGATNFPESLDPALT 424
Cdd:cd19523   79 KILQASFLAARCRQPSVLFISDLDALLSSQDDEASPVGRLQV-ELLAQLDGvLGSGED---GVLVVCTTSKPEEIDESLR 154
                        170
                 ....*....|.
gi 259445303 425 RpgRFDRHIHV 435
Cdd:cd19523  155 R--YFSKRLLV 163
AAA smart00382
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ...
300-439 2.38e-19

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: 85.12  E-value: 2.38e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259445303   300 PRGVLLTGPPGTGKTMLARAVAGEANVP---FFFMSGSQFDE--------------MYVGVGAKRVRELFAAARKQAPSI 362
Cdd:smart00382   2 GEVILIVGPPGSGKTTLARALARELGPPgggVIYIDGEDILEevldqllliivggkKASGSGELRLRLALALARKLKPDV 81
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 259445303   363 IFIDELDAIGQKRNARDAahmrqtlnqLLVDLDGFSKNEDLAHPVVFIGATNFPESLDPALTRPgRFDRHIHVPLPD 439
Cdd:smart00382  82 LILDEITSLLDAEQEALL---------LLLEELRLLLLLKSEKNLTVILTTNDEKDLGPALLRR-RFDRRIVLLLIL 148
RecA-like_Ycf46-like cd19507
ATPase domain of Ycf46 and similar ATPase domains; Ycf46 may play a role in the regulation of ...
268-431 1.12e-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: 77.79  E-value: 1.12e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259445303 268 DVQGVDEAKEELEEivdflRDPThFT----RLGGKLPRGVLLTGPPGTGKTMLARAVAGEANVPFFFMSGSQFDEMYVGV 343
Cdd:cd19507    1 DVGGLDNLKDWLKK-----RKAA-FSkqasAYGLPTPKGLLLVGIQGTGKSLTAKAIAGVWQLPLLRLDMGRLFGGLVGE 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259445303 344 GAKRVRELFAAARKQAPSIIFIDELD-AIGQKRNARDAAHMRQTLNQLLVDLDGFSKNedlahpvVFIGAT-NFPESLDP 421
Cdd:cd19507   75 SESRLRQMIQTAEAIAPCVLWIDEIEkGFSNADSKGDSGTSSRVLGTFLTWLQEKKKP-------VFVVATaNNVQSLPP 147
                        170
                 ....*....|
gi 259445303 422 ALTRPGRFDR 431
Cdd:cd19507  148 ELLRKGRFDE 157
ycf46 CHL00195
Ycf46; Provisional
261-488 5.48e-15

Ycf46; Provisional


Pssm-ID: 177094 [Multi-domain]  Cd Length: 489  Bit Score: 78.14  E-value: 5.48e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259445303 261 AINVRFSDVQGVDEAKEELEeivdflRDPTHFTR----LGGKLPRGVLLTGPPGTGKTMLARAVAGEANVPFFFMS-GSQ 335
Cdd:CHL00195 222 SVNEKISDIGGLDNLKDWLK------KRSTSFSKqasnYGLPTPRGLLLVGIQGTGKSLTAKAIANDWQLPLLRLDvGKL 295
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259445303 336 FDEMyVGVGAKRVRELFAAARKQAPSIIFIDELD-AIGQKRNARDAAHMRQTLNQLLVDLDGFSKnedlahPVVFIGATN 414
Cdd:CHL00195 296 FGGI-VGESESRMRQMIRIAEALSPCILWIDEIDkAFSNSESKGDSGTTNRVLATFITWLSEKKS------PVFVVATAN 368
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 259445303 415 FPESLDPALTRPGRFDRHIHVPLPDVRGRLAILLQHTRHV-PLG-KDVDLSIIARGTSGFAGADLANLINQAAVYA 488
Cdd:CHL00195 369 NIDLLPLEILRKGRFDEIFFLDLPSLEEREKIFKIHLQKFrPKSwKKYDIKKLSKLSNKFSGAEIEQSIIEAMYIA 444
RecA-like_ATAD3-like cd19512
ATPase domains of ATPase AAA-domain protein 3A (ATAD3A), -3B, and -3C, and similar ATPase ...
279-434 1.96e-13

ATPase domains of ATPase AAA-domain protein 3A (ATAD3A), -3B, and -3C, and similar ATPase domains; ATPase AAA-domain protein 3 (ATAD3) is a ubiquitously expressed mitochondrial protein involved in mitochondrial dynamics, DNA-nucleoid structural organization, cholesterol transport and steroidogenesis. The ATAD3 gene family in human comprises three paralog genes: ATAD3A, ATAD3B and ATAD3C. This subfamily belongs to the RecA-like NTPase family which includes the NTP binding domain of F1 and V1 H(+)ATPases, DnaB and related helicases as well as bacterial RecA and related eukaryotic and archaeal recombinases. The RecA-like NTPase family also includes bacterial conjugation proteins and related DNA transfer proteins involved in type II and type IV secretion.


Pssm-ID: 410920 [Multi-domain]  Cd Length: 150  Bit Score: 68.32  E-value: 1.96e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259445303 279 LEEIVDFLRDPTHFTRLGGKLPRGVLLTGPPGTGKTMLARAVAGEANVPFFFMSGSQFDEM-YVGVGAkrVRELFAAARK 357
Cdd:cd19512    1 LEARVRDIAIATRNTKKNKGLYRNILFYGPPGTGKTLFAKKLALHSGMDYAIMTGGDVAPMgREGVTA--IHKVFDWANT 78
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 259445303 358 QAPS-IIFIDELDAIGQKRNARDAAH-MRQTLNQLLVdldgfsKNEDLAHPVVFIGATNFPESLDPALTrpGRFDRHIH 434
Cdd:cd19512   79 SRRGlLLFVDEADAFLRKRSTEKISEdLRAALNAFLY------RTGEQSNKFMLVLASNQPEQFDWAIN--DRIDEMVE 149
RecA-like_Ycf2 cd19505
ATPase domain of plant YCF2; Ycf2 is a chloroplast ATPase which has an essential function; ...
294-435 9.25e-13

ATPase domain of plant YCF2; Ycf2 is a chloroplast ATPase which has an essential function; however, its function remains unclear. The gene encoding YCF2 is the largest known plastid gene in angiosperms and has been used to predict phylogenetic relationships. This subfamily belongs to the RecA-like NTPase family which includes the NTP binding domain of F1 and V1 H(+)ATPases, DnaB and related helicases as well as bacterial RecA and related eukaryotic and archaeal recombinases. The RecA-like NTPase family also includes bacterial conjugation proteins and related DNA transfer proteins involved in type II and type IV secretion.


Pssm-ID: 410913 [Multi-domain]  Cd Length: 161  Bit Score: 66.63  E-value: 9.25e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259445303 294 RLGGKLPRGVLLTGPPGTGKTMLARAVAGEANVPFFFMSGSQF--------------DEMYVGVGAKRVRELFAAARKQA 359
Cdd:cd19505    6 RLGLSPSKGILLIGSIETGRSYLIKSLAANSYVPLIRISLNKLlynkpdfgnddwidGMLILKESLHRLNLQFELAKAMS 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259445303 360 PSIIF---IDELDA--IGQKRNARDAAHMRQTLNQLLVDLDGFSKNEdlahpVVFIGATNFPESLDPALTRPGRFDRHIH 434
Cdd:cd19505   86 PCIIWipnIHELNVnrSTQNLEEDPKLLLGLLLNYLSRDFEKSSTRN-----ILVIASTHIPQKVDPALIAPNRLDTCIN 160

                 .
gi 259445303 435 V 435
Cdd:cd19505  161 I 161
PRK04195 PRK04195
replication factor C large subunit; Provisional
265-371 1.85e-10

replication factor C large subunit; Provisional


Pssm-ID: 235250 [Multi-domain]  Cd Length: 482  Bit Score: 63.79  E-value: 1.85e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259445303 265 RFSDVQGVDEAKEELEEIVDflrdpthfTRLGGKLPRGVLLTGPPGTGKTMLARAVAGEANVPFFFMSGSqfD------- 337
Cdd:PRK04195  12 TLSDVVGNEKAKEQLREWIE--------SWLKGKPKKALLLYGPPGVGKTSLAHALANDYGWEVIELNAS--Dqrtadvi 81
                         90       100       110
                 ....*....|....*....|....*....|....
gi 259445303 338 EMYVGVGAKRvRELFAAARKqapsIIFIDELDAI 371
Cdd:PRK04195  82 ERVAGEAATS-GSLFGARRK----LILLDEVDGI 110
RarA COG2256
Replication-associated recombination protein RarA (DNA-dependent ATPase) [Replication, ...
303-367 2.16e-09

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


Pssm-ID: 441857 [Multi-domain]  Cd Length: 439  Bit Score: 60.07  E-value: 2.16e-09
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 259445303 303 VLLTGPPGTGKTMLARAVAGEANVPFFFMSGsqfdemyVGVGAKRVRELFAAARKQA----PSIIFIDE 367
Cdd:COG2256   52 MILWGPPGTGKTTLARLIANATDAEFVALSA-------VTSGVKDIREVIEEARERRaygrRTILFVDE 113
PRK13342 PRK13342
recombination factor protein RarA; Reviewed
303-367 5.24e-09

recombination factor protein RarA; Reviewed


Pssm-ID: 237355 [Multi-domain]  Cd Length: 413  Bit Score: 58.94  E-value: 5.24e-09
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 259445303 303 VLLTGPPGTGKTMLARAVAGEANVPFFFMSGsqfdemyVGVGAKRVRELFAAARKQAPS----IIFIDE 367
Cdd:PRK13342  39 MILWGPPGTGKTTLARIIAGATDAPFEALSA-------VTSGVKDLREVIEEARQRRSAgrrtILFIDE 100
RecA-like_HslU cd19498
ATP-dependent protease ATPase subunit HslU; HslU is a component of the ATP-dependent protease ...
299-429 9.37e-09

ATP-dependent protease ATPase subunit HslU; HslU is a component of the ATP-dependent protease HslVU. In HslVU, HslU ATPase serves to unfold and translocate protein substrate, and the HslV protease degrades the unfolded proteins. This RecA-like_HslU subfamily belongs to the RecA-like NTPase family which includes the NTP binding domain of F1 and V1 H(+)ATPases, DnaB and related helicases as well as bacterial RecA and related eukaryotic and archaeal recombinases. The RecA-like NTPase family also includes bacterial conjugation proteins and related DNA transfer proteins involved in type II and type IV secretion.


Pssm-ID: 410906 [Multi-domain]  Cd Length: 183  Bit Score: 55.46  E-value: 9.37e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259445303 299 LPRGVLLTGPPGTGKTMLARAVAGEANVPFFFMSGSQFDEM-YVGvgakrvRELFAAARKQAPSIIFIDELDAIGQKRNA 377
Cdd:cd19498   45 TPKNILMIGPTGVGKTEIARRLAKLAGAPFIKVEATKFTEVgYVG------RDVESIIRDLVEGIVFIDEIDKIAKRGGS 118
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 259445303 378 RDAAHMRQTLNQ-LLVDLDGFSKNE-----DLAHpVVFIGATNF----PESLDPALTrpGRF 429
Cdd:cd19498  119 SGPDVSREGVQRdLLPIVEGSTVSTkygpvKTDH-ILFIAAGAFhvakPSDLIPELQ--GRF 177
AAA_5 pfam07728
AAA domain (dynein-related subfamily); This Pfam entry includes some of the AAA proteins not ...
302-429 2.26e-08

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


Pssm-ID: 400191 [Multi-domain]  Cd Length: 135  Bit Score: 53.07  E-value: 2.26e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259445303  302 GVLLTGPPGTGKTMLARAVAgEA--NVPFFFMSGSQF---DEM-----YVGVGAKRV-RELFAAARKqaPSIIFIDELDa 370
Cdd:pfam07728   1 GVLLVGPPGTGKTELAERLA-AAlsNRPVFYVQLTRDtteEDLfgrrnIDPGGASWVdGPLVRAARE--GEIAVLDEIN- 76
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 259445303  371 igqkrNARDAAHMrqTLNQLLVD-----LDGFSKNEDLAHPVVFIGATNFP----ESLDPALTRpgRF 429
Cdd:pfam07728  77 -----RANPDVLN--SLLSLLDErrlllPDGGELVKAAPDGFRLIATMNPLdrglNELSPALRS--RF 135
AAA_lid_3 pfam17862
AAA+ lid domain; This entry represents the alpha helical AAA+ lid domain that is found to the ...
459-502 2.37e-08

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: 50.23  E-value: 2.37e-08
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 259445303  459 DVDLSIIARGTSGFAGADLANLINQAAVYASKNLSTAVSMRDLE 502
Cdd:pfam17862   1 DVDLEELAERTEGFSGADLEALCREAALAALRRGLEAVTQEDLE 44
TIP49 pfam06068
TIP49 P-loop domain; This family consists of the C-terminal region of several eukaryotic and ...
271-336 1.01e-07

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


Pssm-ID: 399217 [Multi-domain]  Cd Length: 347  Bit Score: 54.62  E-value: 1.01e-07
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 259445303  271 GVDEAKEELEEIVDFLRDpthfTRLGGklpRGVLLTGPPGTGKTMLARAVAGE--ANVPFFFMSGSQF 336
Cdd:pfam06068  28 GQEKAREAAGVIVEMIKE----GKIAG---RAVLIAGPPGTGKTALAIAISKElgEDTPFTSISGSEV 88
44 PHA02544
clamp loader, small subunit; Provisional
297-423 5.05e-07

clamp loader, small subunit; Provisional


Pssm-ID: 222866 [Multi-domain]  Cd Length: 316  Bit Score: 52.30  E-value: 5.05e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259445303 297 GKLPRGVLLTGPPGTGKTMLARAVAGEANVPFFFMSGSqfdEMYVGVGAKRVRElFAAA--RKQAPSIIFIDELDAIGQK 374
Cdd:PHA02544  40 GRIPNMLLHSPSPGTGKTTVAKALCNEVGAEVLFVNGS---DCRIDFVRNRLTR-FASTvsLTGGGKVIIIDEFDRLGLA 115
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 259445303 375 RNARdaaHMRQTLNQllvdldgFSKNedlahpVVFIGATNFPESLDPAL 423
Cdd:PHA02544 116 DAQR---HLRSFMEA-------YSKN------CSFIITANNKNGIIEPL 148
TIP49 COG1224
DNA helicase TIP49, TBP-interacting protein [Transcription];
271-336 5.23e-07

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


Pssm-ID: 440837 [Multi-domain]  Cd Length: 452  Bit Score: 52.67  E-value: 5.23e-07
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 259445303 271 GVDEAKEELEEIVDFLRDpthfTRLGGklpRGVLLTGPPGTGKTMLARAVAGE--ANVPFFFMSGSQF 336
Cdd:COG1224   42 GQVEAREAAGIVVKMIKE----GKMAG---KGILIVGPPGTGKTALAVAIARElgEDTPFVAISGSEI 102
RecA-like_ClpX cd19497
ATP-dependent Clp protease ATP-binding subunit ClpX; ClpX is a component of the ATP-dependent ...
303-374 9.54e-07

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: 50.68  E-value: 9.54e-07
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 259445303 303 VLLTGPPGTGKTMLARAVAGEANVPFFFMSGSQFDEM-YVG--VGAKRVRELFAA----ARKQApSIIFIDELDAIGQK 374
Cdd:cd19497   53 ILLIGPTGSGKTLLAQTLAKILDVPFAIADATTLTEAgYVGedVENILLKLLQAAdydvERAQR-GIVYIDEIDKIARK 130
RecA-like_Pch2-like cd19508
ATPase domain of Pachytene checkpoint 2 (Pch2) and similar ATPase domains; Pch2 (known as ...
301-424 2.04e-06

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


Pssm-ID: 410916 [Multi-domain]  Cd Length: 199  Bit Score: 48.98  E-value: 2.04e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259445303 301 RGVLLTGPPGTGKTMLARAVAGEANVPF-FFMSGSQFDEM--------YVGVGAKRVRELFA-----AARKQAPSIIFID 366
Cdd:cd19508   53 RLVLLHGPPGTGKTSLCKALAQKLSIRLsSRYRYGQLIEInshslfskWFSESGKLVTKMFQkiqelIDDKDALVFVLID 132
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 259445303 367 ELDAIGQKRNA-------RDAahMRqTLNQLLVDLDGFSKnedlAHPVVFIGATNFPESLDPALT 424
Cdd:cd19508  133 EVESLAAARSAsssgtepSDA--IR-VVNAVLTQIDRIKR----YHNNVILLTSNLLEKIDVAFV 190
RecA-like_IQCA1 cd19506
ATPase domain of IQ and AAA domain-containing protein 1 (IQCA1); IQCA1 (also known as dynein ...
299-420 8.57e-06

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: 8.57e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259445303 299 LPRGVLLTGPPGTGKTMLARAVAGEANVPFFFMSGSQFDEMYVGVGAKR--VRELFAAARKQAPSIIFIDELD-----AI 371
Cdd:cd19506   25 LVKSLLLAGPSGVGKKMLVHAICTETGANLFNLSPSNIAGKYPGKNGLQmmLHLVLKVARQLQPSVIWIGDAEktfykKV 104
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 259445303 372 GQKRNARDAAHMRQTLNQLLVDLdgfsKNEDLahpVVFIGATNFPESLD 420
Cdd:cd19506  105 PKTEKQLDPKRLKKDLPKILKSL----KPEDR---VLIVGTTSRPFEAD 146
CDC6 COG1474
Cdc6-related protein, AAA superfamily ATPase [Replication, recombination and repair];
277-436 1.08e-05

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


Pssm-ID: 441083 [Multi-domain]  Cd Length: 389  Bit Score: 48.31  E-value: 1.08e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259445303 277 EELEEIVDFLRDPTHftrlgGKLPRGVLLTGPPGTGKTMLARAV-------AGEANVPFFF------MSGSQFDEMY--- 340
Cdd:COG1474   33 EEIEELASALRPALR-----GERPSNVLIYGPTGTGKTAVAKYVleeleeeAEERGVDVRVvyvncrQASTRYRVLSril 107
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259445303 341 -----------VGVGAKRVRELFAAA--RKQAPSIIFIDELDAIGQKrnardaaHMRQTLNQLLvDLdgfskNEDLAHP- 406
Cdd:COG1474  108 eelgsgedipsTGLSTDELFDRLYEAldERDGVLVVVLDEIDYLVDD-------EGDDLLYQLL-RA-----NEELEGAr 174
                        170       180       190
                 ....*....|....*....|....*....|....
gi 259445303 407 VVFIGATN---FPESLDPALTRpgRF-DRHIHVP 436
Cdd:COG1474  175 VGVIGISNdleFLENLDPRVKS--SLgEEEIVFP 206
RecA-like_Lon cd19500
lon protease homolog 2 peroxisomal; Lon protease (also known as Lon peptidase) is an ...
271-423 1.20e-05

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


Pssm-ID: 410908 [Multi-domain]  Cd Length: 182  Bit Score: 46.40  E-value: 1.20e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259445303 271 GVDEAKEEleeIVDFLRdpthFTRLGGKLPRGVL-LTGPPGTGKTMLARAVAGEANVPFFFMS-GSQFDE--------MY 340
Cdd:cd19500   14 GLEDVKER---ILEYLA----VRKLKGSMKGPILcLVGPPGVGKTSLGKSIARALGRKFVRISlGGVRDEaeirghrrTY 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259445303 341 VGVGAKRVRELFAAARKQAPsIIFIDELDAIGQKRNARDAAHMRQTL----------NQLLVDLDgFSKnedlahpVVFI 410
Cdd:cd19500   87 VGAMPGRIIQALKKAGTNNP-VFLLDEIDKIGSSFRGDPASALLEVLdpeqnstfsdHYLDVPFD-LSK-------VLFI 157
                        170
                 ....*....|...
gi 259445303 411 GATNFPESLDPAL 423
Cdd:cd19500  158 ATANSLDTIPGPL 170
AAA_16 pfam13191
AAA ATPase domain; This family of domains contain a P-loop motif that is characteriztic of the ...
280-410 1.26e-05

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


Pssm-ID: 433025 [Multi-domain]  Cd Length: 167  Bit Score: 45.96  E-value: 1.26e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259445303  280 EEIVDFLRDptHFTRLGGKLPRGVLLTGPPGTGKTMLARAV---AGEANVPFFFMSGSQFDEMYVGVGAKRVRELFAAAR 356
Cdd:pfam13191   6 EEELEQLLD--ALDRVRSGRPPSVLLTGEAGTGKTTLLRELlraLERDGGYFLRGKCDENLPYSPLLEALTREGLLRQLL 83
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 259445303  357 KQAPSIIF------IDELDAIGQKRNARDAAHMRQTLNQLLVDLdgfsknEDLAHPVVFI 410
Cdd:pfam13191  84 DELESSLLeawraaLLEALAPVPELPGDLAERLLDLLLRLLDLL------ARGERPLVLV 137
AAA_2 pfam07724
AAA domain (Cdc48 subfamily); This Pfam entry includes some of the AAA proteins not detected ...
303-371 6.25e-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: 44.11  E-value: 6.25e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259445303  303 VLLTGPPGTGKTMLARAVA-----GEANVPFFFMS------------GSQfdEMYVGVGAKRVreLFAAARKQAPSIIFI 365
Cdd:pfam07724   6 FLFLGPTGVGKTELAKALAellfgDERALIRIDMSeymeehsvsrliGAP--PGYVGYEEGGQ--LTEAVRRKPYSIVLI 81

                  ....*.
gi 259445303  366 DELDAI 371
Cdd:pfam07724  82 DEIEKA 87
MoxR COG0714
MoxR-like ATPase [General function prediction only]; MoxR-like ATPase is part of the Pathway ...
303-452 6.49e-05

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


Pssm-ID: 440478 [Multi-domain]  Cd Length: 292  Bit Score: 45.54  E-value: 6.49e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259445303 303 VLLTGPPGTGKTMLARAVAGEANVPFFFMsgsQF-----------DEMYV-GVGAKRVRE--LFAaarkqapSIIFIDEL 368
Cdd:COG0714   34 LLLEGVPGVGKTTLAKALARALGLPFIRI---QFtpdllpsdilgTYIYDqQTGEFEFRPgpLFA-------NVLLADEI 103
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259445303 369 DaigqkRnARdaahmRQTLNQLL-------VDLDGfsKNEDLAHPVVFIGATNFPESLDpalTRP------GRFDRHIHV 435
Cdd:COG0714  104 N-----R-AP-----PKTQSALLeameerqVTIPG--GTYKLPEPFLVIATQNPIEQEG---TYPlpeaqlDRFLLKLYI 167
                        170
                 ....*....|....*..
gi 259445303 436 PLPDVRGRLAILLQHTR 452
Cdd:COG0714  168 GYPDAEEEREILRRHTG 184
COG2842 COG2842
Bacteriophage DNA transposition protein, AAA+ family ATPase [Mobilome: prophages, transposons]; ...
298-503 6.91e-05

Bacteriophage DNA transposition protein, AAA+ family ATPase [Mobilome: prophages, transposons];


Pssm-ID: 442090 [Multi-domain]  Cd Length: 254  Bit Score: 44.94  E-value: 6.91e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259445303 298 KLPRGVLLTGPPGTGKTMLARAVAGE-ANVPFF----FMSGSQF-----DEMYVGVGAKRVRELFAAAR---KQAPSIIF 364
Cdd:COG2842   48 ALPGIGVVYGESGVGKTTAAREYANRnPNVIYVtaspSWTSKELleelaEELGIPAPPGTIADLRDRILerlAGTGRLLI 127
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259445303 365 IDEldaigqkrnardAAHMR-QTLNQL--LVDLDGFsknedlahPVVFIGatnfPESLDPALTRPGRFDRHI-------H 434
Cdd:COG2842  128 IDE------------ADHLKpKALEELrdIHDETGV--------GVVLIG----MERLPAKLKRYEQLYSRIgfwvefkP 183
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 259445303 435 VPLPDVRgrlaILLQHTRHVPLgKDVdLSIIARGTSGFAGAdLANLINQAAVYASKNLSTAVSMRDLEW 503
Cdd:COG2842  184 LSLEDVR----ALAEAWGELTD-PDL-LELLHRITRGNLRR-LDRTLRLAARAAKRNGLTKITLDHVRA 245
T7SS_EccA TIGR03922
type VII secretion AAA-ATPase EccA; This model represents the AAA family ATPase, EccA, of the ...
271-436 7.53e-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: 45.99  E-value: 7.53e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259445303  271 GVDEAKEELEEIVDFLRdpTHFTRLGGKLP-----RGVLLTGPPGTGKTMLARAVA------GEANVPFFF-MSGSQFDE 338
Cdd:TIGR03922 280 GLERVKRQVAALKSSTA--MALARAERGLPvaqtsNHMLFAGPPGTGKTTIARVVAkiycglGVLRKPLVReVSRADLIG 357
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259445303  339 MYVGVGAKRVRELFAAArkqAPSIIFIDELDAIGQKRNARDAAHMRQTLNQLLVDLdgfsknEDLAHPVVFIGAtNFPES 418
Cdd:TIGR03922 358 QYIGESEAKTNEIIDSA---LGGVLFLDEAYTLVETGYGQKDPFGLEAIDTLLARM------ENDRDRLVVIGA-GYRKD 427
                         170       180
                  ....*....|....*....|..
gi 259445303  419 LDPAL-TRPG---RFDRHIHVP 436
Cdd:TIGR03922 428 LDKFLeVNEGlrsRFTRVIEFP 449
clpX PRK05342
ATP-dependent Clp protease ATP-binding subunit ClpX;
303-374 1.76e-04

ATP-dependent Clp protease ATP-binding subunit ClpX;


Pssm-ID: 235422 [Multi-domain]  Cd Length: 412  Bit Score: 44.38  E-value: 1.76e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259445303 303 VLLTGPPGTGKTMLARAVAGEANVPFFFMSGSQFDEM-YVG--VGAKRVRELFAA------ARKqapSIIFIDELDAIGQ 373
Cdd:PRK05342 111 ILLIGPTGSGKTLLAQTLARILDVPFAIADATTLTEAgYVGedVENILLKLLQAAdydvekAQR---GIVYIDEIDKIAR 187

                 .
gi 259445303 374 K 374
Cdd:PRK05342 188 K 188
rfc PRK00440
replication factor C small subunit; Reviewed
265-370 2.41e-04

replication factor C small subunit; Reviewed


Pssm-ID: 234763 [Multi-domain]  Cd Length: 319  Bit Score: 43.71  E-value: 2.41e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259445303 265 RFSDVQGVDEAKEELEEIVDflrdpthftrlGGKLPRgVLLTGPPGTGKT----MLARAVAGEA---NvpFFFMSGSqfD 337
Cdd:PRK00440  15 TLDEIVGQEEIVERLKSYVK-----------EKNMPH-LLFAGPPGTGKTtaalALARELYGEDwreN--FLELNAS--D 78
                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 259445303 338 EMYVGVGAKRVRElFAAAR--KQAP-SIIFIDELDA 370
Cdd:PRK00440  79 ERGIDVIRNKIKE-FARTApvGGAPfKIIFLDEADN 113
RepA COG3598
RecA-family ATPase [Replication, recombination and repair];
297-475 3.35e-04

RecA-family ATPase [Replication, recombination and repair];


Pssm-ID: 442817 [Multi-domain]  Cd Length: 313  Bit Score: 43.35  E-value: 3.35e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259445303 297 GKLPRG--VLLTGPPGTGKTMLAR--AVAGEANVPFFFMSGSQFDEMYVG--VGAKRVRELFAAARKQAPSIIFIDE--- 367
Cdd:COG3598    8 GLLPEGgvTLLAGPPGTGKSFLALqlAAAVAAGGPWLGRRVPPGKVLYLAaeDDRGELRRRLKALGADLGLPFADLDgrl 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259445303 368 --LDAIGQKRNARDAAHMRQTLNQ----LLVdLDGFSKnedlahpvVFIGATNFPESLDPALtrpGRFDRHIHvplpdvR 441
Cdd:COG3598   88 rlLSLAGDLDDTDDLEALERAIEEegpdLVV-IDPLAR--------VFGGDENDAEEMRAFL---NPLDRLAE------R 149
                        170       180       190
                 ....*....|....*....|....*....|....*
gi 259445303 442 GRLAILL-QHTRHVPLGKDVDLSiiARGTSGFAGA 475
Cdd:COG3598  150 TGAAVLLvHHTGKGGAGKDSGDR--ARGSSALRGA 182
YifB COG0606
Predicted Mg-chelatase, contains ChlI-like and ATPase domains, YifB family [Posttranslational ...
303-322 3.54e-04

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


Pssm-ID: 440371 [Multi-domain]  Cd Length: 502  Bit Score: 43.88  E-value: 3.54e-04
                         10        20
                 ....*....|....*....|
gi 259445303 303 VLLTGPPGTGKTMLARAVAG 322
Cdd:COG0606  214 LLMIGPPGSGKTMLARRLPG 233
AAA_22 pfam13401
AAA domain;
303-417 4.51e-04

AAA domain;


Pssm-ID: 379165 [Multi-domain]  Cd Length: 129  Bit Score: 40.79  E-value: 4.51e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259445303  303 VLLTGPPGTGKTMLARAVA---GEANVPFFFM------SGSQFDEMYV------GVGAKRVRELFAA-----ARKQAPSI 362
Cdd:pfam13401   8 LVLTGESGTGKTTLLRRLLeqlPEVRDSVVFVdlpsgtSPKDLLRALLralglpLSGRLSKEELLAAlqqllLALAVAVV 87
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 259445303  363 IFIDEldaigqkrnardAAHMRQTLNQLLVDLDGFSKNeDLahPVVFIGATNFPE 417
Cdd:pfam13401  88 LIIDE------------AQHLSLEALEELRDLLNLSSK-LL--QLILVGTPELRE 127
PRK09862 PRK09862
ATP-dependent protease;
254-322 5.32e-04

ATP-dependent protease;


Pssm-ID: 182120 [Multi-domain]  Cd Length: 506  Bit Score: 43.04  E-value: 5.32e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 259445303 254 QEPMEERAINVR----FSDVQGVDEAKEELEeivdflrdpthFTRLGGklpRGVLLTGPPGTGKTMLARAVAG 322
Cdd:PRK09862 174 ERPKPTDAVSRAlqhdLSDVIGQEQGKRGLE-----------ITAAGG---HNLLLIGPPGTGKTMLASRING 232
HolB COG0470
DNA polymerase III, delta prime subunit [Replication, recombination and repair];
297-371 6.23e-04

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


Pssm-ID: 440238 [Multi-domain]  Cd Length: 289  Bit Score: 42.27  E-value: 6.23e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259445303 297 GKLPRGVLLTGPPGTGKTMLARAVA-------------GEANVPFFFMSGSQFDEMYVGVGAKR-------VRELFAAAR 356
Cdd:COG0470   15 GRLPHALLLHGPPGIGKTTLALALArdllcenpeggkaCGQCHSRLMAAGNHPDLLELNPEEKSdqigidqIRELGEFLS 94
                         90
                 ....*....|....*....
gi 259445303 357 KQAPS----IIFIDELDAI 371
Cdd:COG0470   95 LTPLEggrkVVIIDEADAM 113
Mg_chelatase pfam01078
Magnesium chelatase, subunit ChlI; Magnesium-chelatase is a three-component enzyme that ...
266-322 6.40e-04

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


Pssm-ID: 426032 [Multi-domain]  Cd Length: 207  Bit Score: 41.75  E-value: 6.40e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 259445303  266 FSDVQGVDEAKEELEeivdflrdpthFTRLGGklpRGVLLTGPPGTGKTMLARAVAG 322
Cdd:pfam01078   2 LADVKGQEQAKRALE-----------IAAAGG---HNLLMIGPPGSGKTMLAKRLPG 44
RAD55 COG0467
RecA-superfamily ATPase, KaiC/GvpD/RAD55 family [Signal transduction mechanisms];
295-317 7.95e-04

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


Pssm-ID: 440235 [Multi-domain]  Cd Length: 221  Bit Score: 41.44  E-value: 7.95e-04
                         10        20
                 ....*....|....*....|....*
gi 259445303 295 LGGKLPRG--VLLTGPPGTGKTMLA 317
Cdd:COG0467   13 LGGGLPRGssTLLSGPPGTGKTTLA 37
PRK13341 PRK13341
AAA family ATPase;
304-367 8.76e-04

AAA family ATPase;


Pssm-ID: 237354 [Multi-domain]  Cd Length: 725  Bit Score: 42.73  E-value: 8.76e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 259445303 304 LLTGPPGTGKTMLARAVAGEANVPFFFMSGsqfdemyVGVGAKRVRELFAAARKQAP-----SIIFIDE 367
Cdd:PRK13341  56 ILYGPPGVGKTTLARIIANHTRAHFSSLNA-------VLAGVKDLRAEVDRAKERLErhgkrTILFIDE 117
ruvB TIGR00635
Holliday junction DNA helicase, RuvB subunit; All proteins in this family for which functions ...
303-372 8.99e-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: 41.90  E-value: 8.99e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 259445303  303 VLLTGPPGTGKTMLARAVAGEANVPFFFMSGSQFDemyvgvgakRVRELFAA-ARKQAPSIIFIDELDAIG 372
Cdd:TIGR00635  33 LLLYGPPGLGKTTLAHIIANEMGVNLKITSGPALE---------KPGDLAAIlTNLEEGDVLFIDEIHRLS 94
DnaX COG2812
DNA polymerase III, gamma/tau subunits [Replication, recombination and repair];
265-321 1.04e-03

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


Pssm-ID: 442061 [Multi-domain]  Cd Length: 340  Bit Score: 41.72  E-value: 1.04e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 259445303 265 RFSDVQGVDEAKEELEEIVDflrdpthftrlGGKLPRGVLLTGPPGTGKTMLARAVA 321
Cdd:COG2812    8 TFDDVVGQEHVVRTLKNALA-----------SGRLAHAYLFTGPRGVGKTTLARILA 53
RecA-like_ClpB_Hsp104-like cd19499
Chaperone protein ClpB/Hsp104 subfamily; Bacterial Caseinolytic peptidase B (ClpB) and ...
300-369 1.13e-03

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


Pssm-ID: 410907 [Multi-domain]  Cd Length: 178  Bit Score: 40.62  E-value: 1.13e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259445303 300 PRGVLL-TGPPGTGKTMLARAVA-----GEANVPFFFMsgSQFDEMYVG----------VGAKRVRELFAAARKQAPSII 363
Cdd:cd19499   40 PIGSFLfLGPTGVGKTELAKALAellfgDEDNLIRIDM--SEYMEKHSVsrligappgyVGYTEGGQLTEAVRRKPYSVV 117

                 ....*.
gi 259445303 364 FIDELD 369
Cdd:cd19499  118 LLDEIE 123
ruvB PRK00080
Holliday junction branch migration DNA helicase RuvB;
251-333 1.21e-03

Holliday junction branch migration DNA helicase RuvB;


Pssm-ID: 234619 [Multi-domain]  Cd Length: 328  Bit Score: 41.65  E-value: 1.21e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259445303 251 TTEQEPMEERAINV-----RFSDVQGVDEAKEELE----------EIVDflrdptHftrlggklprgVLLTGPPGTGKTM 315
Cdd:PRK00080   4 SPETLEEEEDEIERslrpkSLDEFIGQEKVKENLKifieaakkrgEALD------H-----------VLLYGPPGLGKTT 66
                         90
                 ....*....|....*...
gi 259445303 316 LARAVAGEANVPFFFMSG 333
Cdd:PRK00080  67 LANIIANEMGVNIRITSG 84
ExeA COG3267
Type II secretory pathway ATPase component GspA/ExeA/MshM [Intracellular trafficking, ...
303-394 1.50e-03

Type II secretory pathway ATPase component GspA/ExeA/MshM [Intracellular trafficking, secretion, and vesicular transport, Extracellular structures];


Pssm-ID: 442498 [Multi-domain]  Cd Length: 261  Bit Score: 40.93  E-value: 1.50e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259445303 303 VLLTGPPGTGKTMLARAVAGE--ANVPFFFMSGSQFDemyvgvgakrVRELFAAArkqapsiifideLDAIGQKRNARDA 380
Cdd:COG3267   46 VVLTGEVGTGKTTLLRRLLERlpDDVKVAYIPNPQLS----------PAELLRAI------------ADELGLEPKGASK 103
                         90
                 ....*....|....
gi 259445303 381 AHMRQTLNQLLVDL 394
Cdd:COG3267  104 ADLLRQLQEFLLEL 117
RuvB_N pfam05496
Holliday junction DNA helicase RuvB P-loop domain; The RuvB protein makes up part of the ...
303-333 1.96e-03

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


Pssm-ID: 398900 [Multi-domain]  Cd Length: 159  Bit Score: 39.41  E-value: 1.96e-03
                          10        20        30
                  ....*....|....*....|....*....|.
gi 259445303  303 VLLTGPPGTGKTMLARAVAGEANVPFFFMSG 333
Cdd:pfam05496  36 VLLYGPPGLGKTTLANIIANEMGVNIRITSG 66
KaiC-like cd01124
Circadian Clock Protein KaiC; KaiC is a circadian clock protein, most studied in cyanobacteria. ...
295-394 2.04e-03

Circadian Clock Protein KaiC; KaiC is a circadian clock protein, most studied in cyanobacteria. KaiC, an autokinase, autophosphatase, and ATPase, is part of the core oscillator, composed of three proteins: KaiA, KaiB, and KaiC. The circadian oscillation is regulated via KaiC phosphorylation.


Pssm-ID: 410869 [Multi-domain]  Cd Length: 222  Bit Score: 40.32  E-value: 2.04e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259445303 295 LGGKLPRG--VLLTGPPGTGKTM-----LARAVAGEANVPFFFMS-------------GSQFDEMYVG--------VGAK 346
Cdd:cd01124   12 LGGGIPKGsvTLLTGGPGTGKTLfglqfLYAGAKNGEPGLFFTFEesperllrnaksfGWDFDEMEDEgkliivdaPPTE 91
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 259445303 347 RVRELF--------AAARKQAPSIIFIDELDAIgqKRNARDAAHMRQTLNQLLVDL 394
Cdd:cd01124   92 AGRFSLdellsrilSIIKSFKAKRVVIDSLSGL--RRAKEDQMRARRIVIALLNEL 145
DnaC COG1484
DNA replication protein DnaC [Replication, recombination and repair];
301-368 2.26e-03

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


Pssm-ID: 441093 [Multi-domain]  Cd Length: 242  Bit Score: 40.15  E-value: 2.26e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 259445303 301 RGVLLTGPPGTGKTMLARAVAGEA-----NVPFFFMSgSQFDEMYVGVGAKRVRELFAAARKqaPSIIFIDEL 368
Cdd:COG1484  100 ENLILLGPPGTGKTHLAIALGHEAcragyRVRFTTAP-DLVNELKEARADGRLERLLKRLAK--VDLLILDEL 169
TIGR00368 TIGR00368
Mg chelatase-related protein; The N-terminal end matches very strongly a pfam Mg_chelatase ...
246-322 3.14e-03

Mg chelatase-related protein; The N-terminal end matches very strongly a pfam Mg_chelatase domain. [Unknown function, General]


Pssm-ID: 129465 [Multi-domain]  Cd Length: 499  Bit Score: 40.60  E-value: 3.14e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259445303  246 NIMTNTTEQEPME----ERAINVRFSDVQGVDEAKEELEeivdflrdpthFTRLGGklpRGVLLTGPPGTGKTMLARAVA 321
Cdd:TIGR00368 167 EKLPPRTNTKPKSiinkSYIIDLDLKDIKGQQHAKRALE-----------IAAAGG---HNLLLFGPPGSGKTMLASRLQ 232

                  .
gi 259445303  322 G 322
Cdd:TIGR00368 233 G 233
RuvB COG2255
Holliday junction resolvasome RuvABC, ATP-dependent DNA helicase subunit RuvB [Replication, ...
245-333 3.99e-03

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


Pssm-ID: 441856 [Multi-domain]  Cd Length: 337  Bit Score: 40.06  E-value: 3.99e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259445303 245 NNIMTNTTEQEPMEERAIN-VRFSDVQGVDEAKEELE----------EIVDflrdptHftrlggklprgVLLTGPPGTGK 313
Cdd:COG2255    5 DRLSSSASEEEDALERSLRpKRLDEYIGQEKVKENLKifieaakkrgEALD------H-----------VLLYGPPGLGK 67
                         90       100
                 ....*....|....*....|
gi 259445303 314 TMLARAVAGEANVPFFFMSG 333
Cdd:COG2255   68 TTLAHIIANEMGVNIRITSG 87
ABC_ATPase cd00267
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ...
298-375 5.21e-03

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


Pssm-ID: 213179 [Multi-domain]  Cd Length: 157  Bit Score: 38.38  E-value: 5.21e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259445303 298 KLPRG--VLLTGPPGTGKTMLARAVAGEANVP--FFFMSGSQFDEMYVGVGAKRV----------RELFAAARK--QAPS 361
Cdd:cd00267   21 TLKAGeiVALVGPNGSGKSTLLRAIAGLLKPTsgEILIDGKDIAKLPLEELRRRIgyvpqlsggqRQRVALARAllLNPD 100
                         90
                 ....*....|....*...
gi 259445303 362 IIFIDE----LDAIGQKR 375
Cdd:cd00267  101 LLLLDEptsgLDPASRER 118
Rad51B cd19493
RAD51B recombinase; RAD51B recombinase, a RAD51 paralog, plays an important role in DNA repair ...
295-327 5.64e-03

RAD51B recombinase; RAD51B recombinase, a RAD51 paralog, plays an important role in DNA repair by homologous recombination (HR). HR is an important error-free repair mechanism for chromosomal double-strand break (DSB) which otherwise leads to cell cycle arrest and death. RAD51B, together with the other RAD51 paralogs, RAD51C, RAD51D, XRCC3, and XRCC2, helps recruit RAD51 to the break site.


Pssm-ID: 410901 [Multi-domain]  Cd Length: 222  Bit Score: 38.84  E-value: 5.64e-03
                         10        20        30
                 ....*....|....*....|....*....|....*
gi 259445303 295 LGGKLPRGVL--LTGPPGTGKTMLARAVAGEANVP 327
Cdd:cd19493    4 LAGGLPLGAIteITGASGSGKTQFALTLASSAAMP 38
COG3899 COG3899
Predicted ATPase [General function prediction only];
277-391 8.64e-03

Predicted ATPase [General function prediction only];


Pssm-ID: 443106 [Multi-domain]  Cd Length: 1244  Bit Score: 39.46  E-value: 8.64e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259445303  277 EELEEIVDflrdptHFTRLGGKLPRGVLLTGPPGTGKTMLARAVAGEANV-PFFFMSGsQFDEMYVGVGAKRVRELFAAA 355
Cdd:COG3899   294 AELAALLA------ALERARAGRGELVLVSGEAGIGKSRLVRELARRARArGGRVLRG-KCDQLERGVPYAPLAQALRAL 366
                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 259445303  356 RKQAPSiifiDELDAIGQKRNARDAAHmRQTLNQLL 391
Cdd:COG3899   367 LGQLPE----DELAAWRARLLAALGAN-GRLLADLL 397
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

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