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Conserved domains on  [gi|6323736|ref|NP_013807|]
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m-AAA protease subunit YTA12 [Saccharomyces cerevisiae S288C]

Protein Classification

ATP-dependent metallopeptidase FtsH/Yme1/Tma family protein( domain architecture ID 12070764)

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

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
FtsH_fam TIGR01241
ATP-dependent metalloprotease FtsH; HflB(FtsH) is a pleiotropic protein required for correct ...
290-784 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: 826.54  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323736    290 NWAKAMFQILPTVLMIAGIIWLTRRSAQAAGGsrgGIFGLSRSKAKKFNTEtDVKIKFKDVAGCDEAKEEIMEFVSFLKE 369
Cdd:TIGR01241   1 SLLGFLFSLLPPILLLVGVWFFFRRQMQGGGG---RAFSFGKSKAKLLNEE-KPKVTFKDVAGIDEAKEELMEIVDFLKN 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323736    370 PSRYEKMGAKIPRGAILSGPPGTGKTLLAKATAGEAGVPFYFVSGSEFVEMFVGVGAARVRDLFKTARENAPSIVFIDEI 449
Cdd:TIGR01241  77 PSKFTKLGAKIPKGVLLVGPPGTGKTLLAKAVAGEAGVPFFSISGSDFVEMFVGVGASRVRDLFEQAKKNAPCIIFIDEI 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323736    450 DAIGKARQKGnFSGANDERENTLNQMLVEMDGFTPADHVVVLAGTNRPDILDKALLRPGRFDRHINIDKPELEGRKAIFA 529
Cdd:TIGR01241 157 DAVGRQRGAG-LGGGNDEREQTLNQLLVEMDGFGTNTGVIVIAATNRPDVLDPALLRPGRFDRQVVVDLPDIKGREEILK 235
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323736    530 VHLHHLKLAgEIFDLKnRLAALTPGFSGADIANVCNEAALIAARSDEDAVKLNHFEQAIERVIGGVERKSKLLSPEEKKV 609
Cdd:TIGR01241 236 VHAKNKKLA-PDVDLK-AVARRTPGFSGADLANLLNEAALLAARKNKTEITMNDIEEAIDRVIAGPEKKSRVISEKEKKL 313
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323736    610 VAYHEAGHAVCGWYLKYADPLLKVSIIPRGQgALGYAQYLP-GDIFLLTEQQLKDRMTMSLGGRVSEELHFPSVTSGASD 688
Cdd:TIGR01241 314 VAYHEAGHALVGLLLKDADPVHKVTIIPRGQ-ALGYTQFLPeEDKYLYTKSQLLAQIAVLLGGRAAEEIIFGEVTTGASN 392
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323736    689 DFKKVTSMATAMVTELGMSDKIGWVNYQKRD-------DSDLTKPFSDETGDIIDSEVYRIVQECHDRCTKLLKEKAEDV 761
Cdd:TIGR01241 393 DIKQATNIARAMVTEWGMSDKLGPVAYGSDGgdvflgrGFAKAKEYSEETAREIDEEVKRIIEEAYKRAKQILTENRDEL 472
                         490       500
                  ....*....|....*....|...
gi 6323736    762 EKIAQVLLKKEVLTREDMIDLLG 784
Cdd:TIGR01241 473 ELLAKALLEKETITREEIKELLA 495
FtsH_ext pfam06480
FtsH Extracellular; This domain is found in the FtsH family of proteins. FtsH is the only ...
205-282 2.46e-04

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


:

Pssm-ID: 377663 [Multi-domain]  Cd Length: 103  Bit Score: 41.05  E-value: 2.46e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 6323736    205 EITWQDFREKLlAKGYVAKLIVVNKSMVKVMLNDNGKNQADNYgRNFYYFTIGSIDSFEHKLQKAQDELDIDKDFRIP 282
Cdd:pfam06480  28 EISYSEFLEYL-EAGKVKKVVVQDDEILPTGVVEGTLKDGSKF-TTYFIPSLPNVDSLLEKLEDALEEKGVKVSVKPP 103
 
Name Accession Description Interval E-value
FtsH_fam TIGR01241
ATP-dependent metalloprotease FtsH; HflB(FtsH) is a pleiotropic protein required for correct ...
290-784 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: 826.54  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323736    290 NWAKAMFQILPTVLMIAGIIWLTRRSAQAAGGsrgGIFGLSRSKAKKFNTEtDVKIKFKDVAGCDEAKEEIMEFVSFLKE 369
Cdd:TIGR01241   1 SLLGFLFSLLPPILLLVGVWFFFRRQMQGGGG---RAFSFGKSKAKLLNEE-KPKVTFKDVAGIDEAKEELMEIVDFLKN 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323736    370 PSRYEKMGAKIPRGAILSGPPGTGKTLLAKATAGEAGVPFYFVSGSEFVEMFVGVGAARVRDLFKTARENAPSIVFIDEI 449
Cdd:TIGR01241  77 PSKFTKLGAKIPKGVLLVGPPGTGKTLLAKAVAGEAGVPFFSISGSDFVEMFVGVGASRVRDLFEQAKKNAPCIIFIDEI 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323736    450 DAIGKARQKGnFSGANDERENTLNQMLVEMDGFTPADHVVVLAGTNRPDILDKALLRPGRFDRHINIDKPELEGRKAIFA 529
Cdd:TIGR01241 157 DAVGRQRGAG-LGGGNDEREQTLNQLLVEMDGFGTNTGVIVIAATNRPDVLDPALLRPGRFDRQVVVDLPDIKGREEILK 235
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323736    530 VHLHHLKLAgEIFDLKnRLAALTPGFSGADIANVCNEAALIAARSDEDAVKLNHFEQAIERVIGGVERKSKLLSPEEKKV 609
Cdd:TIGR01241 236 VHAKNKKLA-PDVDLK-AVARRTPGFSGADLANLLNEAALLAARKNKTEITMNDIEEAIDRVIAGPEKKSRVISEKEKKL 313
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323736    610 VAYHEAGHAVCGWYLKYADPLLKVSIIPRGQgALGYAQYLP-GDIFLLTEQQLKDRMTMSLGGRVSEELHFPSVTSGASD 688
Cdd:TIGR01241 314 VAYHEAGHALVGLLLKDADPVHKVTIIPRGQ-ALGYTQFLPeEDKYLYTKSQLLAQIAVLLGGRAAEEIIFGEVTTGASN 392
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323736    689 DFKKVTSMATAMVTELGMSDKIGWVNYQKRD-------DSDLTKPFSDETGDIIDSEVYRIVQECHDRCTKLLKEKAEDV 761
Cdd:TIGR01241 393 DIKQATNIARAMVTEWGMSDKLGPVAYGSDGgdvflgrGFAKAKEYSEETAREIDEEVKRIIEEAYKRAKQILTENRDEL 472
                         490       500
                  ....*....|....*....|...
gi 6323736    762 EKIAQVLLKKEVLTREDMIDLLG 784
Cdd:TIGR01241 473 ELLAKALLEKETITREEIKELLA 495
HflB COG0465
ATP-dependent Zn proteases [Posttranslational modification, protein turnover, chaperones];
202-785 0e+00

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


Pssm-ID: 440233 [Multi-domain]  Cd Length: 583  Bit Score: 807.34  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323736  202 EQSEITWQDFREkLLAKGYVAKlIVVNKSMVKVMLNDNGKNQadnygrnfYYFTIGSIDSFEHKLQKAqdelDIDKDFRI 281
Cdd:COG0465  18 SVKEISYSEFLQ-LVEAGKVKS-VTIQGDRITGTLKDGTKTR--------FTTYRVNDPELVDLLEEK----GVEVTAKP 83
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323736  282 PVlyvQEGNWAKAMFQILPTVLMIAGIIWLTRrsaQAAGGSrGGIFGLSRSKAKKFnTETDVKIKFKDVAGCDEAKEEIM 361
Cdd:COG0465  84 PE---ESSWLLSLLISLLPILLLIGLWIFFMR---RMQGGG-GGAMSFGKSKAKLY-DEDKPKVTFDDVAGVDEAKEELQ 155
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323736  362 EFVSFLKEPSRYEKMGAKIPRGAILSGPPGTGKTLLAKATAGEAGVPFYFVSGSEFVEMFVGVGAARVRDLFKTARENAP 441
Cdd:COG0465 156 EIVDFLKDPEKFTRLGAKIPKGVLLVGPPGTGKTLLAKAVAGEAGVPFFSISGSDFVEMFVGVGASRVRDLFEQAKKNAP 235
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323736  442 SIVFIDEIDAIGKARQKGNfSGANDERENTLNQMLVEMDGFTPADHVVVLAGTNRPDILDKALLRPGRFDRHINIDKPEL 521
Cdd:COG0465 236 CIIFIDEIDAVGRQRGAGL-GGGHDEREQTLNQLLVEMDGFEGNEGVIVIAATNRPDVLDPALLRPGRFDRQVVVDLPDV 314
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323736  522 EGRKAIFAVHLHHLKLAGEIfDLKnRLAALTPGFSGADIANVCNEAALIAARSDEDAVKLNHFEQAIERVIGGVERKSKL 601
Cdd:COG0465 315 KGREAILKVHARKKPLAPDV-DLE-VIARRTPGFSGADLANLVNEAALLAARRNKKAVTMEDFEEAIDRVIAGPERKSRV 392
                       410       420       430       440       450       460       470       480
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323736  602 LSPEEKKVVAYHEAGHAVCGWYLKYADPLLKVSIIPRGqGALGYAQYLP-GDIFLLTEQQLKDRMTMSLGGRVSEELHFP 680
Cdd:COG0465 393 ISEKEKKITAYHEAGHALVAALLPGADPVHKVTIIPRG-RALGYTMQLPeEDRYLYTKEELLDRIAVLLGGRAAEELVFG 471
                       490       500       510       520       530       540       550       560
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323736  681 SVTSGASDDFKKVTSMATAMVTELGMSDKIGWVNYQKRDDSDL-------TKPFSDETGDIIDSEVYRIVQECHDRCTKL 753
Cdd:COG0465 472 EVTTGASNDLERATKIARAMVTEYGMSEKLGPVAYGESEGEVFlgrdigqSRNYSEETAREIDEEVRRIIDEAYERAKEI 551
                       570       580       590
                ....*....|....*....|....*....|..
gi 6323736  754 LKEKAEDVEKIAQVLLKKEVLTREDMIDLLGK 785
Cdd:COG0465 552 LTENRDKLDALAEALLEKETLDGEELEEILAG 583
ftsH CHL00176
cell division protein; Validated
272-793 6.95e-174

cell division protein; Validated


Pssm-ID: 214386 [Multi-domain]  Cd Length: 638  Bit Score: 515.75  E-value: 6.95e-174
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323736   272 ELDIDKDFRIPVLyvQEGNWAKAMFQILPtVLMIAGIIWLTRRSAQAAGGSRGGIFGLSRSKAKkFNTETDVKIKFKDVA 351
Cdd:CHL00176 111 EANIDFDAHPPVL--KSNIVTILSNLLLP-LILIGVLWFFFQRSSNFKGGPGQNLMNFGKSKAR-FQMEADTGITFRDIA 186
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323736   352 GCDEAKEEIMEFVSFLKEPSRYEKMGAKIPRGAILSGPPGTGKTLLAKATAGEAGVPFYFVSGSEFVEMFVGVGAARVRD 431
Cdd:CHL00176 187 GIEEAKEEFEEVVSFLKKPERFTAVGAKIPKGVLLVGPPGTGKTLLAKAIAGEAEVPFFSISGSEFVEMFVGVGAARVRD 266
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323736   432 LFKTARENAPSIVFIDEIDAIGKARQKGnFSGANDERENTLNQMLVEMDGFTPADHVVVLAGTNRPDILDKALLRPGRFD 511
Cdd:CHL00176 267 LFKKAKENSPCIVFIDEIDAVGRQRGAG-IGGGNDEREQTLNQLLTEMDGFKGNKGVIVIAATNRVDILDAALLRPGRFD 345
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323736   512 RHINIDKPELEGRKAIFAVHLHHLKLAGEIfdLKNRLAALTPGFSGADIANVCNEAALIAARSDEDAVKLNHFEQAIERV 591
Cdd:CHL00176 346 RQITVSLPDREGRLDILKVHARNKKLSPDV--SLELIARRTPGFSGADLANLLNEAAILTARRKKATITMKEIDTAIDRV 423
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323736   592 IGGVERKSkLLSPEEKKVVAYHEAGHAVCGWYLKYADPLLKVSIIPRGQgALGYAQYLPG-DIFLLTEQQLKDRMTMSLG 670
Cdd:CHL00176 424 IAGLEGTP-LEDSKNKRLIAYHEVGHAIVGTLLPNHDPVQKVTLIPRGQ-AKGLTWFTPEeDQSLVSRSQILARIVGALG 501
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323736   671 GRVSEELHF--PSVTSGASDDFKKVTSMATAMVTELGMSdKIGWVNYQKRDDSDL--------TKPFSDETGDIIDSEVY 740
Cdd:CHL00176 502 GRAAEEVVFgsTEVTTGASNDLQQVTNLARQMVTRFGMS-SIGPISLESNNSTDPflgrfmqrNSEYSEEIADKIDMEVR 580
                        490       500       510       520       530
                 ....*....|....*....|....*....|....*....|....*....|....
gi 6323736   741 RIVQECHDRCTKLLKEKAEDVEKIAQVLLKKEVLTREDMIDLLGKR-PFPERND 793
Cdd:CHL00176 581 SILHTCYQYAYQILKDNRVLIDLLVELLLQKETIDGDEFREIVNSYtILPPKKT 634
RecA-like_FtsH cd19501
ATP-dependent zinc metalloprotease FtsH; FtsH ATPase is a processive, ATP-dependent zinc ...
345-516 9.02e-114

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: 343.06  E-value: 9.02e-114
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323736  345 IKFKDVAGCDEAKEEIMEFVSFLKEPSRYEKMGAKIPRGAILSGPPGTGKTLLAKATAGEAGVPFYFVSGSEFVEMFVGV 424
Cdd:cd19501   1 VTFKDVAGCEEAKEELKEVVEFLKNPEKFTKLGAKIPKGVLLVGPPGTGKTLLAKAVAGEAGVPFFSISGSDFVEMFVGV 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323736  425 GAARVRDLFKTARENAPSIVFIDEIDAIGKARQKGnFSGANDERENTLNQMLVEMDGFTPADHVVVLAGTNRPDILDKAL 504
Cdd:cd19501  81 GASRVRDLFEQAKKNAPCIVFIDEIDAVGRKRGAG-LGGGHDEREQTLNQLLVEMDGFESNTGVIVIAATNRPDVLDPAL 159
                       170
                ....*....|..
gi 6323736  505 LRPGRFDRHINI 516
Cdd:cd19501 160 LRPGRFDRQVYV 171
Peptidase_M41 pfam01434
Peptidase family M41;
600-782 1.24e-91

Peptidase family M41;


Pssm-ID: 460210 [Multi-domain]  Cd Length: 190  Bit Score: 286.03  E-value: 1.24e-91
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323736    600 KLLSPEEKKVVAYHEAGHAVCGWYLKYADPLLKVSIIPRGQgALGYAQYLP-GDIFLLTEQQLKDRMTMSLGGRVSEELH 678
Cdd:pfam01434   1 RVISEEEKKIVAYHEAGHALVGLLLPGADPVHKVTIIPRGQ-ALGYTQFLPeEDKLLYTKEQLLARIAVLLGGRAAEELI 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323736    679 FPSVTSGASDDFKKVTSMATAMVTELGMSDKIGWVNYQKRD-------DSDLTKPFSDETGDIIDSEVYRIVQECHDRCT 751
Cdd:pfam01434  80 FGEVTTGASNDLEKATKIARQMVTEFGMSDKLGPVSLEESDgnvflgrGMGKRKPYSEETADIIDEEVKRLLEEAYERAK 159
                         170       180       190
                  ....*....|....*....|....*....|.
gi 6323736    752 KLLKEKAEDVEKIAQVLLKKEVLTREDMIDL 782
Cdd:pfam01434 160 EILTEHRDELEALAEALLEKETLDAEEIREL 190
AAA smart00382
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ...
381-520 2.50e-17

ATPases associated with a variety of cellular activities; AAA - ATPases associated with a variety of cellular activities. This profile/alignment only detects a fraction of this vast family. The poorly conserved N-terminal helix is missing from the alignment.


Pssm-ID: 214640 [Multi-domain]  Cd Length: 148  Bit Score: 79.72  E-value: 2.50e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323736     381 PRGAILSGPPGTGKTLLAKATAGEA---GVPFYFVSGSEFVE--------------MFVGVGAARVRDLFKTARENAPSI 443
Cdd:smart00382   2 GEVILIVGPPGSGKTTLARALARELgppGGGVIYIDGEDILEevldqllliivggkKASGSGELRLRLALALARKLKPDV 81
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 6323736     444 VFIDEIDAIGKARQkgnfsgandERENTLNQMLVEMDGFTPADHVVVLAGTNRPDILDKALLRPgRFDRHINIDKPE 520
Cdd:smart00382  82 LILDEITSLLDAEQ---------EALLLLLEELRLLLLLKSEKNLTVILTTNDEKDLGPALLRR-RFDRRIVLLLIL 148
FtsH_ext pfam06480
FtsH Extracellular; This domain is found in the FtsH family of proteins. FtsH is the only ...
205-282 2.46e-04

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


Pssm-ID: 377663 [Multi-domain]  Cd Length: 103  Bit Score: 41.05  E-value: 2.46e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 6323736    205 EITWQDFREKLlAKGYVAKLIVVNKSMVKVMLNDNGKNQADNYgRNFYYFTIGSIDSFEHKLQKAQDELDIDKDFRIP 282
Cdd:pfam06480  28 EISYSEFLEYL-EAGKVKKVVVQDDEILPTGVVEGTLKDGSKF-TTYFIPSLPNVDSLLEKLEDALEEKGVKVSVKPP 103
 
Name Accession Description Interval E-value
FtsH_fam TIGR01241
ATP-dependent metalloprotease FtsH; HflB(FtsH) is a pleiotropic protein required for correct ...
290-784 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: 826.54  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323736    290 NWAKAMFQILPTVLMIAGIIWLTRRSAQAAGGsrgGIFGLSRSKAKKFNTEtDVKIKFKDVAGCDEAKEEIMEFVSFLKE 369
Cdd:TIGR01241   1 SLLGFLFSLLPPILLLVGVWFFFRRQMQGGGG---RAFSFGKSKAKLLNEE-KPKVTFKDVAGIDEAKEELMEIVDFLKN 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323736    370 PSRYEKMGAKIPRGAILSGPPGTGKTLLAKATAGEAGVPFYFVSGSEFVEMFVGVGAARVRDLFKTARENAPSIVFIDEI 449
Cdd:TIGR01241  77 PSKFTKLGAKIPKGVLLVGPPGTGKTLLAKAVAGEAGVPFFSISGSDFVEMFVGVGASRVRDLFEQAKKNAPCIIFIDEI 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323736    450 DAIGKARQKGnFSGANDERENTLNQMLVEMDGFTPADHVVVLAGTNRPDILDKALLRPGRFDRHINIDKPELEGRKAIFA 529
Cdd:TIGR01241 157 DAVGRQRGAG-LGGGNDEREQTLNQLLVEMDGFGTNTGVIVIAATNRPDVLDPALLRPGRFDRQVVVDLPDIKGREEILK 235
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323736    530 VHLHHLKLAgEIFDLKnRLAALTPGFSGADIANVCNEAALIAARSDEDAVKLNHFEQAIERVIGGVERKSKLLSPEEKKV 609
Cdd:TIGR01241 236 VHAKNKKLA-PDVDLK-AVARRTPGFSGADLANLLNEAALLAARKNKTEITMNDIEEAIDRVIAGPEKKSRVISEKEKKL 313
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323736    610 VAYHEAGHAVCGWYLKYADPLLKVSIIPRGQgALGYAQYLP-GDIFLLTEQQLKDRMTMSLGGRVSEELHFPSVTSGASD 688
Cdd:TIGR01241 314 VAYHEAGHALVGLLLKDADPVHKVTIIPRGQ-ALGYTQFLPeEDKYLYTKSQLLAQIAVLLGGRAAEEIIFGEVTTGASN 392
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323736    689 DFKKVTSMATAMVTELGMSDKIGWVNYQKRD-------DSDLTKPFSDETGDIIDSEVYRIVQECHDRCTKLLKEKAEDV 761
Cdd:TIGR01241 393 DIKQATNIARAMVTEWGMSDKLGPVAYGSDGgdvflgrGFAKAKEYSEETAREIDEEVKRIIEEAYKRAKQILTENRDEL 472
                         490       500
                  ....*....|....*....|...
gi 6323736    762 EKIAQVLLKKEVLTREDMIDLLG 784
Cdd:TIGR01241 473 ELLAKALLEKETITREEIKELLA 495
HflB COG0465
ATP-dependent Zn proteases [Posttranslational modification, protein turnover, chaperones];
202-785 0e+00

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


Pssm-ID: 440233 [Multi-domain]  Cd Length: 583  Bit Score: 807.34  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323736  202 EQSEITWQDFREkLLAKGYVAKlIVVNKSMVKVMLNDNGKNQadnygrnfYYFTIGSIDSFEHKLQKAqdelDIDKDFRI 281
Cdd:COG0465  18 SVKEISYSEFLQ-LVEAGKVKS-VTIQGDRITGTLKDGTKTR--------FTTYRVNDPELVDLLEEK----GVEVTAKP 83
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323736  282 PVlyvQEGNWAKAMFQILPTVLMIAGIIWLTRrsaQAAGGSrGGIFGLSRSKAKKFnTETDVKIKFKDVAGCDEAKEEIM 361
Cdd:COG0465  84 PE---ESSWLLSLLISLLPILLLIGLWIFFMR---RMQGGG-GGAMSFGKSKAKLY-DEDKPKVTFDDVAGVDEAKEELQ 155
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323736  362 EFVSFLKEPSRYEKMGAKIPRGAILSGPPGTGKTLLAKATAGEAGVPFYFVSGSEFVEMFVGVGAARVRDLFKTARENAP 441
Cdd:COG0465 156 EIVDFLKDPEKFTRLGAKIPKGVLLVGPPGTGKTLLAKAVAGEAGVPFFSISGSDFVEMFVGVGASRVRDLFEQAKKNAP 235
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323736  442 SIVFIDEIDAIGKARQKGNfSGANDERENTLNQMLVEMDGFTPADHVVVLAGTNRPDILDKALLRPGRFDRHINIDKPEL 521
Cdd:COG0465 236 CIIFIDEIDAVGRQRGAGL-GGGHDEREQTLNQLLVEMDGFEGNEGVIVIAATNRPDVLDPALLRPGRFDRQVVVDLPDV 314
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323736  522 EGRKAIFAVHLHHLKLAGEIfDLKnRLAALTPGFSGADIANVCNEAALIAARSDEDAVKLNHFEQAIERVIGGVERKSKL 601
Cdd:COG0465 315 KGREAILKVHARKKPLAPDV-DLE-VIARRTPGFSGADLANLVNEAALLAARRNKKAVTMEDFEEAIDRVIAGPERKSRV 392
                       410       420       430       440       450       460       470       480
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323736  602 LSPEEKKVVAYHEAGHAVCGWYLKYADPLLKVSIIPRGqGALGYAQYLP-GDIFLLTEQQLKDRMTMSLGGRVSEELHFP 680
Cdd:COG0465 393 ISEKEKKITAYHEAGHALVAALLPGADPVHKVTIIPRG-RALGYTMQLPeEDRYLYTKEELLDRIAVLLGGRAAEELVFG 471
                       490       500       510       520       530       540       550       560
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323736  681 SVTSGASDDFKKVTSMATAMVTELGMSDKIGWVNYQKRDDSDL-------TKPFSDETGDIIDSEVYRIVQECHDRCTKL 753
Cdd:COG0465 472 EVTTGASNDLERATKIARAMVTEYGMSEKLGPVAYGESEGEVFlgrdigqSRNYSEETAREIDEEVRRIIDEAYERAKEI 551
                       570       580       590
                ....*....|....*....|....*....|..
gi 6323736  754 LKEKAEDVEKIAQVLLKKEVLTREDMIDLLGK 785
Cdd:COG0465 552 LTENRDKLDALAEALLEKETLDGEELEEILAG 583
ftsH CHL00176
cell division protein; Validated
272-793 6.95e-174

cell division protein; Validated


Pssm-ID: 214386 [Multi-domain]  Cd Length: 638  Bit Score: 515.75  E-value: 6.95e-174
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323736   272 ELDIDKDFRIPVLyvQEGNWAKAMFQILPtVLMIAGIIWLTRRSAQAAGGSRGGIFGLSRSKAKkFNTETDVKIKFKDVA 351
Cdd:CHL00176 111 EANIDFDAHPPVL--KSNIVTILSNLLLP-LILIGVLWFFFQRSSNFKGGPGQNLMNFGKSKAR-FQMEADTGITFRDIA 186
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323736   352 GCDEAKEEIMEFVSFLKEPSRYEKMGAKIPRGAILSGPPGTGKTLLAKATAGEAGVPFYFVSGSEFVEMFVGVGAARVRD 431
Cdd:CHL00176 187 GIEEAKEEFEEVVSFLKKPERFTAVGAKIPKGVLLVGPPGTGKTLLAKAIAGEAEVPFFSISGSEFVEMFVGVGAARVRD 266
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323736   432 LFKTARENAPSIVFIDEIDAIGKARQKGnFSGANDERENTLNQMLVEMDGFTPADHVVVLAGTNRPDILDKALLRPGRFD 511
Cdd:CHL00176 267 LFKKAKENSPCIVFIDEIDAVGRQRGAG-IGGGNDEREQTLNQLLTEMDGFKGNKGVIVIAATNRVDILDAALLRPGRFD 345
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323736   512 RHINIDKPELEGRKAIFAVHLHHLKLAGEIfdLKNRLAALTPGFSGADIANVCNEAALIAARSDEDAVKLNHFEQAIERV 591
Cdd:CHL00176 346 RQITVSLPDREGRLDILKVHARNKKLSPDV--SLELIARRTPGFSGADLANLLNEAAILTARRKKATITMKEIDTAIDRV 423
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323736   592 IGGVERKSkLLSPEEKKVVAYHEAGHAVCGWYLKYADPLLKVSIIPRGQgALGYAQYLPG-DIFLLTEQQLKDRMTMSLG 670
Cdd:CHL00176 424 IAGLEGTP-LEDSKNKRLIAYHEVGHAIVGTLLPNHDPVQKVTLIPRGQ-AKGLTWFTPEeDQSLVSRSQILARIVGALG 501
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323736   671 GRVSEELHF--PSVTSGASDDFKKVTSMATAMVTELGMSdKIGWVNYQKRDDSDL--------TKPFSDETGDIIDSEVY 740
Cdd:CHL00176 502 GRAAEEVVFgsTEVTTGASNDLQQVTNLARQMVTRFGMS-SIGPISLESNNSTDPflgrfmqrNSEYSEEIADKIDMEVR 580
                        490       500       510       520       530
                 ....*....|....*....|....*....|....*....|....*....|....
gi 6323736   741 RIVQECHDRCTKLLKEKAEDVEKIAQVLLKKEVLTREDMIDLLGKR-PFPERND 793
Cdd:CHL00176 581 SILHTCYQYAYQILKDNRVLIDLLVELLLQKETIDGDEFREIVNSYtILPPKKT 634
hflB PRK10733
ATP-dependent zinc metalloprotease FtsH;
299-786 1.27e-156

ATP-dependent zinc metalloprotease FtsH;


Pssm-ID: 182683 [Multi-domain]  Cd Length: 644  Bit Score: 471.83  E-value: 1.27e-156
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323736   299 LPTVLMIAGIIWLTRrsaQAAGGSRGGIFGLSRSKAKKFnTETDVKIKFKDVAGCDEAKEEIMEFVSFLKEPSRYEKMGA 378
Cdd:PRK10733 107 FPMLLLIGVWIFFMR---QMQGGGGKGAMSFGKSKARML-TEDQIKTTFADVAGCDEAKEEVAELVEYLREPSRFQKLGG 182
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323736   379 KIPRGAILSGPPGTGKTLLAKATAGEAGVPFYFVSGSEFVEMFVGVGAARVRDLFKTARENAPSIVFIDEIDAIGKARQK 458
Cdd:PRK10733 183 KIPKGVLMVGPPGTGKTLLAKAIAGEAKVPFFTISGSDFVEMFVGVGASRVRDMFEQAKKAAPCIIFIDEIDAVGRQRGA 262
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323736   459 GnFSGANDERENTLNQMLVEMDGFTPADHVVVLAGTNRPDILDKALLRPGRFDRHINIDKPELEGRKAIFAVHLHHLKLA 538
Cdd:PRK10733 263 G-LGGGHDEREQTLNQMLVEMDGFEGNEGIIVIAATNRPDVLDPALLRPGRFDRQVVVGLPDVRGREQILKVHMRRVPLA 341
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323736   539 GEIFdlKNRLAALTPGFSGADIANVCNEAALIAARSDEDAVKLNHFEQAIERVIGGVERKSKLLSPEEKKVVAYHEAGHA 618
Cdd:PRK10733 342 PDID--AAIIARGTPGFSGADLANLVNEAALFAARGNKRVVSMVEFEKAKDKIMMGAERRSMVMTEAQKESTAYHEAGHA 419
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323736   619 VCGWYLKYADPLLKVSIIPRGQgALGYAQYLP-GDIFLLTEQQLKDRMTMSLGGRVSEELHF--PSVTSGASDDFKKVTS 695
Cdd:PRK10733 420 IIGRLVPEHDPVHKVTIIPRGR-ALGVTFFLPeGDAISASRQKLESQISTLYGGRLAEEIIYgpEHVSTGASNDIKVATN 498
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323736   696 MATAMVTELGMSDKIGWVNYQKRDDSDL-------TKPFSDETGDIIDSEVYRIVQECHDRCTKLLKEKAEDVEKIAQVL 768
Cdd:PRK10733 499 LARNMVTQWGFSEKLGPLLYAEEEGEVFlgrsvakAKHMSDETARIIDQEVKALIERNYNRARQLLTDNMDILHAMKDAL 578
                        490
                 ....*....|....*...
gi 6323736   769 LKKEVLTREDMIDLLGKR 786
Cdd:PRK10733 579 MKYETIDAPQIDDLMARR 596
RecA-like_FtsH cd19501
ATP-dependent zinc metalloprotease FtsH; FtsH ATPase is a processive, ATP-dependent zinc ...
345-516 9.02e-114

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: 343.06  E-value: 9.02e-114
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323736  345 IKFKDVAGCDEAKEEIMEFVSFLKEPSRYEKMGAKIPRGAILSGPPGTGKTLLAKATAGEAGVPFYFVSGSEFVEMFVGV 424
Cdd:cd19501   1 VTFKDVAGCEEAKEELKEVVEFLKNPEKFTKLGAKIPKGVLLVGPPGTGKTLLAKAVAGEAGVPFFSISGSDFVEMFVGV 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323736  425 GAARVRDLFKTARENAPSIVFIDEIDAIGKARQKGnFSGANDERENTLNQMLVEMDGFTPADHVVVLAGTNRPDILDKAL 504
Cdd:cd19501  81 GASRVRDLFEQAKKNAPCIVFIDEIDAVGRKRGAG-LGGGHDEREQTLNQLLVEMDGFESNTGVIVIAATNRPDVLDPAL 159
                       170
                ....*....|..
gi 6323736  505 LRPGRFDRHINI 516
Cdd:cd19501 160 LRPGRFDRQVYV 171
RPT1 COG1222
ATP-dependent 26S proteasome regulatory subunit [Posttranslational modification, protein ...
290-598 2.48e-106

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


Pssm-ID: 440835 [Multi-domain]  Cd Length: 326  Bit Score: 329.66  E-value: 2.48e-106
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323736  290 NWAKAMFQILPTVLMIAGIIWLTRRSAQAAGGSRGGIFGLSRSKAKKF-NTETDVKIKFKDVAGCDEAKEEIMEFVS-FL 367
Cdd:COG1222  19 DALQERLGVELALLLQPVKALELLEEAPALLLNDANLTQKRLGTPRGTaVPAESPDVTFDDIGGLDEQIEEIREAVElPL 98
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323736  368 KEPSRYEKMGAKIPRGAILSGPPGTGKTLLAKATAGEAGVPFYFVSGSEFVEMFVGVGAARVRDLFKTARENAPSIVFID 447
Cdd:COG1222  99 KNPELFRKYGIEPPKGVLLYGPPGTGKTLLAKAVAGELGAPFIRVRGSELVSKYIGEGARNVREVFELAREKAPSIIFID 178
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323736  448 EIDAIGKARQKGNFSGANDereNTLNQMLVEMDGFTPADHVVVLAGTNRPDILDKALLRPGRFDRHINIDKPELEGRKAI 527
Cdd:COG1222 179 EIDAIAARRTDDGTSGEVQ---RTVNQLLAELDGFESRGDVLIIAATNRPDLLDPALLRPGRFDRVIEVPLPDEEAREEI 255
                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 6323736  528 FAVHLHHLKLAGEIfDLKnRLAALTPGFSGADIANVCNEAALIAARSDEDAVKLNHFEQAIERVIGGVERK 598
Cdd:COG1222 256 LKIHLRDMPLADDV-DLD-KLAKLTEGFSGADLKAIVTEAGMFAIREGRDTVTMEDLEKAIEKVKKKTETA 324
Peptidase_M41 pfam01434
Peptidase family M41;
600-782 1.24e-91

Peptidase family M41;


Pssm-ID: 460210 [Multi-domain]  Cd Length: 190  Bit Score: 286.03  E-value: 1.24e-91
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323736    600 KLLSPEEKKVVAYHEAGHAVCGWYLKYADPLLKVSIIPRGQgALGYAQYLP-GDIFLLTEQQLKDRMTMSLGGRVSEELH 678
Cdd:pfam01434   1 RVISEEEKKIVAYHEAGHALVGLLLPGADPVHKVTIIPRGQ-ALGYTQFLPeEDKLLYTKEQLLARIAVLLGGRAAEELI 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323736    679 FPSVTSGASDDFKKVTSMATAMVTELGMSDKIGWVNYQKRD-------DSDLTKPFSDETGDIIDSEVYRIVQECHDRCT 751
Cdd:pfam01434  80 FGEVTTGASNDLEKATKIARQMVTEFGMSDKLGPVSLEESDgnvflgrGMGKRKPYSEETADIIDEEVKRLLEEAYERAK 159
                         170       180       190
                  ....*....|....*....|....*....|.
gi 6323736    752 KLLKEKAEDVEKIAQVLLKKEVLTREDMIDL 782
Cdd:pfam01434 160 EILTEHRDELEALAEALLEKETLDAEEIREL 190
PRK03992 PRK03992
proteasome-activating nucleotidase; Provisional
344-600 2.87e-90

proteasome-activating nucleotidase; Provisional


Pssm-ID: 179699 [Multi-domain]  Cd Length: 389  Bit Score: 289.81  E-value: 2.87e-90
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323736   344 KIKFKDVAGCDEAKEEIMEFVSF-LKEPSRYEKMGAKIPRGAILSGPPGTGKTLLAKATAGEAGVPFYFVSGSEFVEMFV 422
Cdd:PRK03992 127 NVTYEDIGGLEEQIREVREAVELpLKKPELFEEVGIEPPKGVLLYGPPGTGKTLLAKAVAHETNATFIRVVGSELVQKFI 206
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323736   423 GVGAARVRDLFKTARENAPSIVFIDEIDAIGKARQKGNFSGandERE--NTLNQMLVEMDGFTPADHVVVLAGTNRPDIL 500
Cdd:PRK03992 207 GEGARLVRELFELAREKAPSIIFIDEIDAIAAKRTDSGTSG---DREvqRTLMQLLAEMDGFDPRGNVKIIAATNRIDIL 283
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323736   501 DKALLRPGRFDRHINIDKPELEGRKAIFAVHLHHLKLAGEIfDLKnRLAALTPGFSGADIANVCNEAALIAARSDEDAVK 580
Cdd:PRK03992 284 DPAILRPGRFDRIIEVPLPDEEGRLEILKIHTRKMNLADDV-DLE-ELAELTEGASGADLKAICTEAGMFAIRDDRTEVT 361
                        250       260
                 ....*....|....*....|
gi 6323736   581 LNHFEQAIERVIGGVERKSK 600
Cdd:PRK03992 362 MEDFLKAIEKVMGKEEKDSM 381
26Sp45 TIGR01242
26S proteasome subunit P45 family; Many proteins may score above the trusted cutoff because an ...
334-592 4.31e-78

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


Pssm-ID: 130309 [Multi-domain]  Cd Length: 364  Bit Score: 256.65  E-value: 4.31e-78
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323736    334 AKKFNTETDVKIKFKDVAGCDEAKEEIMEFVSF-LKEPSRYEKMGAKIPRGAILSGPPGTGKTLLAKATAGEAGVPFYFV 412
Cdd:TIGR01242 108 VKGMEVEERPNVSYEDIGGLEEQIREIREAVELpLKHPELFEEVGIEPPKGVLLYGPPGTGKTLLAKAVAHETNATFIRV 187
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323736    413 SGSEFVEMFVGVGAARVRDLFKTARENAPSIVFIDEIDAIGKARQKGNFSGaNDERENTLNQMLVEMDGFTPADHVVVLA 492
Cdd:TIGR01242 188 VGSELVRKYIGEGARLVREIFELAKEKAPSIIFIDEIDAIAAKRTDSGTSG-DREVQRTLMQLLAELDGFDPRGNVKVIA 266
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323736    493 GTNRPDILDKALLRPGRFDRHINIDKPELEGRKAIFAVHLHHLKLAGEIfDLKnRLAALTPGFSGADIANVCNEAALIAA 572
Cdd:TIGR01242 267 ATNRPDILDPALLRPGRFDRIIEVPLPDFEGRLEILKIHTRKMKLAEDV-DLE-AIAKMTEGASGADLKAICTEAGMFAI 344
                         250       260
                  ....*....|....*....|
gi 6323736    573 RSDEDAVKLNHFEQAIERVI 592
Cdd:TIGR01242 345 REERDYVTMDDFIKAVEKVL 364
SpoVK COG0464
AAA+-type ATPase, SpoVK/Ycf46/Vps4 family [Cell wall/membrane/envelope biogenesis, Cell cycle ...
347-591 5.46e-78

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: 257.53  E-value: 5.46e-78
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323736  347 FKDVAGCDEAKEEIMEFVS-FLKEPSRYEKMGAKIPRGAILSGPPGTGKTLLAKATAGEAGVPFYFVSGSEFVEMFVGVG 425
Cdd:COG0464 156 LDDLGGLEEVKEELRELVAlPLKRPELREEYGLPPPRGLLLYGPPGTGKTLLARALAGELGLPLIEVDLSDLVSKYVGET 235
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323736  426 AARVRDLFKTARENAPSIVFIDEIDAIGKARqkgnfSGANDERENT-LNQMLVEMDGFTpaDHVVVLAGTNRPDILDKAL 504
Cdd:COG0464 236 EKNLREVFDKARGLAPCVLFIDEADALAGKR-----GEVGDGVGRRvVNTLLTEMEELR--SDVVVIAATNRPDLLDPAL 308
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323736  505 LRpgRFDRHINIDKPELEGRKAIFAVHLHHLKLAGEiFDLKnRLAALTPGFSGADIANVCNEAALIAARSDEDAVKLNHF 584
Cdd:COG0464 309 LR--RFDEIIFFPLPDAEERLEIFRIHLRKRPLDED-VDLE-ELAEATEGLSGADIRNVVRRAALQALRLGREPVTTEDL 384

                ....*..
gi 6323736  585 EQAIERV 591
Cdd:COG0464 385 LEALERE 391
RecA-like_PAN_like cd19502
proteasome activating nucleotidase PAN and related proteasome subunits; This subfamily ...
347-516 4.53e-65

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: 214.89  E-value: 4.53e-65
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323736  347 FKDVAGCDEAKEEIMEFVSF-LKEPSRYEKMGAKIPRGAILSGPPGTGKTLLAKATAGEAGVPFYFVSGSEFVEMFVGVG 425
Cdd:cd19502   2 YEDIGGLDEQIREIREVVELpLKHPELFEELGIEPPKGVLLYGPPGTGKTLLAKAVANHTDATFIRVVGSELVQKYIGEG 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323736  426 AARVRDLFKTARENAPSIVFIDEIDAIGKARQKGNfSGANDERENTLNQMLVEMDGFTPADHVVVLAGTNRPDILDKALL 505
Cdd:cd19502  82 ARLVRELFEMAREKAPSIIFIDEIDAIGAKRFDSG-TGGDREVQRTMLELLNQLDGFDPRGNIKVIMATNRPDILDPALL 160
                       170
                ....*....|.
gi 6323736  506 RPGRFDRHINI 516
Cdd:cd19502 161 RPGRFDRKIEF 171
CDC48 TIGR01243
AAA family ATPase, CDC48 subfamily; This subfamily of the AAA family ATPases includes two ...
345-591 1.22e-64

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


Pssm-ID: 273521 [Multi-domain]  Cd Length: 733  Bit Score: 230.18  E-value: 1.22e-64
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323736    345 IKFKDVAGCDEAKEEIMEFVSF-LKEPSRYEKMGAKIPRGAILSGPPGTGKTLLAKATAGEAGVPFYFVSGSEFVEMFVG 423
Cdd:TIGR01243 450 VRWSDIGGLEEVKQELREAVEWpLKHPEIFEKMGIRPPKGVLLFGPPGTGKTLLAKAVATESGANFIAVRGPEILSKWVG 529
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323736    424 VGAARVRDLFKTARENAPSIVFIDEIDAIGKARQKGNFSGANDErenTLNQMLVEMDGFTPADHVVVLAGTNRPDILDKA 503
Cdd:TIGR01243 530 ESEKAIREIFRKARQAAPAIIFFDEIDAIAPARGARFDTSVTDR---IVNQLLTEMDGIQELSNVVVIAATNRPDILDPA 606
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323736    504 LLRPGRFDRHINIDKPELEGRKAIFAVHLHHLKLAGEIfDLKnRLAALTPGFSGADIANVCNEAALIAAR---------- 573
Cdd:TIGR01243 607 LLRPGRFDRLILVPPPDEEARKEIFKIHTRSMPLAEDV-DLE-ELAEMTEGYTGADIEAVCREAAMAALResigspakek 684
                         250       260
                  ....*....|....*....|....*.
gi 6323736    574 --------SDEDAVKLNHFEQAIERV 591
Cdd:TIGR01243 685 levgeeefLKDLKVEMRHFLEALKKV 710
RecA-like_protease cd19481
proteases similar to RecA; RecA-like NTPases. This family includes the NTP binding domain of ...
356-516 5.07e-60

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: 200.59  E-value: 5.07e-60
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323736  356 AKEEIMEFVSFLKEPSRYEKMGAKIPRGAILSGPPGTGKTLLAKATAGEAGVPFYFVSGSEFVEMFVGVGAARVRDLFKT 435
Cdd:cd19481   1 LKASLREAVEAPRRGSRLRRYGLGLPKGILLYGPPGTGKTLLAKALAGELGLPLIVVKLSSLLSKYVGESEKNLRKIFER 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323736  436 ARENAPSIVFIDEIDAIGKARQKgnfSGANDERENTLNQMLVEMDGFTPADHVVVLAGTNRPDILDKALLRPGRFDRHIN 515
Cdd:cd19481  81 ARRLAPCILFIDEIDAIGRKRDS---SGESGELRRVLNQLLTELDGVNSRSKVLVIAATNRPDLLDPALLRPGRFDEVIE 157

                .
gi 6323736  516 I 516
Cdd:cd19481 158 F 158
PTZ00454 PTZ00454
26S protease regulatory subunit 6B-like protein; Provisional
345-597 8.71e-60

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


Pssm-ID: 240423 [Multi-domain]  Cd Length: 398  Bit Score: 208.46  E-value: 8.71e-60
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323736   345 IKFKDVAGCDEAKEEIMEFVSF-LKEPSRYEKMGAKIPRGAILSGPPGTGKTLLAKATAGEAGVPFYFVSGSEFVEMFVG 423
Cdd:PTZ00454 142 VTYSDIGGLDIQKQEIREAVELpLTCPELYEQIGIDPPRGVLLYGPPGTGKTMLAKAVAHHTTATFIRVVGSEFVQKYLG 221
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323736   424 VGAARVRDLFKTARENAPSIVFIDEIDAIGKARQKGNfSGANDERENTLNQMLVEMDGFTPADHVVVLAGTNRPDILDKA 503
Cdd:PTZ00454 222 EGPRMVRDVFRLARENAPSIIFIDEVDSIATKRFDAQ-TGADREVQRILLELLNQMDGFDQTTNVKVIMATNRADTLDPA 300
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323736   504 LLRPGRFDRHINIDKPELEGRKAIFAVHLHHLKLAGEIfDLKNrLAALTPGFSGADIANVCNEAALIAARSDEDAVKLNH 583
Cdd:PTZ00454 301 LLRPGRLDRKIEFPLPDRRQKRLIFQTITSKMNLSEEV-DLED-FVSRPEKISAADIAAICQEAGMQAVRKNRYVILPKD 378
                        250
                 ....*....|....
gi 6323736   584 FEQAIERVIGGVER 597
Cdd:PTZ00454 379 FEKGYKTVVRKTDR 392
COG1223 COG1223
Predicted ATPase, AAA+ superfamily [General function prediction only];
347-590 2.52e-59

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


Pssm-ID: 440836 [Multi-domain]  Cd Length: 246  Bit Score: 202.04  E-value: 2.52e-59
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323736  347 FKDVAGCDEAKEEIMEFVSFLKEPSRYEKMGAKIPRGAILSGPPGTGKTLLAKATAGEAGVPFYFVSGSEFVEMFVGVGA 426
Cdd:COG1223   1 LDDVVGQEEAKKKLKLIIKELRRRENLRKFGLWPPRKILFYGPPGTGKTMLAEALAGELKLPLLTVRLDSLIGSYLGETA 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323736  427 ARVRDLFKTAREnAPSIVFIDEIDAIGKARQKGNFSGandERENTLNQMLVEMDGFTpaDHVVVLAGTNRPDILDKALLR 506
Cdd:COG1223  81 RNLRKLFDFARR-APCVIFFDEFDAIAKDRGDQNDVG---EVKRVVNALLQELDGLP--SGSVVIAATNHPELLDSALWR 154
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323736  507 pgRFDRHINIDKPELEGRKAIFAVHLHHLKLAGEiFDLKnRLAALTPGFSGADIANVCNEAALIAARSDEDAVKLNHFEQ 586
Cdd:COG1223 155 --RFDEVIEFPLPDKEERKEILELNLKKFPLPFE-LDLK-KLAKKLEGLSGADIEKVLKTALKKAILEDREKVTKEDLEE 230

                ....
gi 6323736  587 AIER 590
Cdd:COG1223 231 ALKQ 234
RecA-like_CDC48_r2-like cd19511
second of two ATPase domains of CDC48/p97, PEX1 and -6, VAT and NVL, and similar ATPase ...
356-516 8.68e-58

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: 194.42  E-value: 8.68e-58
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323736  356 AKEEIMEFVSF-LKEPSRYEKMGAKIPRGAILSGPPGTGKTLLAKATAGEAGVPFYFVSGSEFVEMFVGVGAARVRDLFK 434
Cdd:cd19511   1 VKRELKEAVEWpLKHPDAFKRLGIRPPKGVLLYGPPGCGKTLLAKALASEAGLNFISVKGPELFSKYVGESERAVREIFQ 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323736  435 TARENAPSIVFIDEIDAIGKARQKGNFSGANDErenTLNQMLVEMDGFTPADHVVVLAGTNRPDILDKALLRPGRFDRHI 514
Cdd:cd19511  81 KARQAAPCIIFFDEIDSLAPRRGQSDSSGVTDR---VVSQLLTELDGIESLKGVVVIAATNRPDMIDPALLRPGRLDKLI 157

                ..
gi 6323736  515 NI 516
Cdd:cd19511 158 YV 159
CDC48 TIGR01243
AAA family ATPase, CDC48 subfamily; This subfamily of the AAA family ATPases includes two ...
331-592 1.06e-57

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: 210.53  E-value: 1.06e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323736    331 RSKAKKFNTETDV-KIKFKDVAGCDEAKEEIMEFVSF-LKEPSRYEKMGAKIPRGAILSGPPGTGKTLLAKATAGEAGVP 408
Cdd:TIGR01243 160 REKPVREEIERKVpKVTYEDIGGLKEAKEKIREMVELpMKHPELFEHLGIEPPKGVLLYGPPGTGKTLLAKAVANEAGAY 239
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323736    409 FYFVSGSEFVEMFVGVGAARVRDLFKTARENAPSIVFIDEIDAIGKARQKgnFSGANDERenTLNQMLVEMDGFTPADHV 488
Cdd:TIGR01243 240 FISINGPEIMSKYYGESEERLREIFKEAEENAPSIIFIDEIDAIAPKREE--VTGEVEKR--VVAQLLTLMDGLKGRGRV 315
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323736    489 VVLAGTNRPDILDKALLRPGRFDRHINIDKPELEGRKAIFAVHLHHLKLAGEIfDLkNRLAALTPGFSGADIANVCNEAA 568
Cdd:TIGR01243 316 IVIGATNRPDALDPALRRPGRFDREIVIRVPDKRARKEILKVHTRNMPLAEDV-DL-DKLAEVTHGFVGADLAALAKEAA 393
                         250       260
                  ....*....|....*....|....
gi 6323736    569 LIAARSDEDAVKLNHFEQAIERVI 592
Cdd:TIGR01243 394 MAALRRFIREGKINFEAEEIPAEV 417
PTZ00361 PTZ00361
26 proteosome regulatory subunit 4-like protein; Provisional
347-592 1.27e-55

26 proteosome regulatory subunit 4-like protein; Provisional


Pssm-ID: 185575 [Multi-domain]  Cd Length: 438  Bit Score: 198.07  E-value: 1.27e-55
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323736   347 FKDVAGCDEAKEEIMEFVSF-LKEPSRYEKMGAKIPRGAILSGPPGTGKTLLAKATAGEAGVPFYFVSGSEFVEMFVGVG 425
Cdd:PTZ00361 182 YADIGGLEQQIQEIKEAVELpLTHPELYDDIGIKPPKGVILYGPPGTGKTLLAKAVANETSATFLRVVGSELIQKYLGDG 261
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323736   426 AARVRDLFKTARENAPSIVFIDEIDAIGKARQKGNfSGANDERENTLNQMLVEMDGFTPADHVVVLAGTNRPDILDKALL 505
Cdd:PTZ00361 262 PKLVRELFRVAEENAPSIVFIDEIDAIGTKRYDAT-SGGEKEIQRTMLELLNQLDGFDSRGDVKVIMATNRIESLDPALI 340
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323736   506 RPGRFDRHINIDKPELEGRKAIFAVHLHHLKLAGEIfDLKNRLAAlTPGFSGADIANVCNEAALIAARSDEDAVKLNHFE 585
Cdd:PTZ00361 341 RPGRIDRKIEFPNPDEKTKRRIFEIHTSKMTLAEDV-DLEEFIMA-KDELSGADIKAICTEAGLLALRERRMKVTQADFR 418

                 ....*..
gi 6323736   586 QAIERVI 592
Cdd:PTZ00361 419 KAKEKVL 425
RecA-like_CDC48_NLV2_r1-like cd19503
first of two ATPase domains of CDC48 and NLV2, and similar ATPase domains; CDC48 in yeast and ...
349-516 1.41e-54

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


Pssm-ID: 410911 [Multi-domain]  Cd Length: 165  Bit Score: 185.96  E-value: 1.41e-54
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323736  349 DVAGCDEAKEEIMEFVSF-LKEPSRYEKMGAKIPRGAILSGPPGTGKTLLAKATAGEAGVPFYFVSGSEFVEMFVGVGAA 427
Cdd:cd19503   1 DIGGLDEQIASLKELIELpLKYPELFRALGLKPPRGVLLHGPPGTGKTLLARAVANEAGANFLSISGPSIVSKYLGESEK 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323736  428 RVRDLFKTARENAPSIVFIDEIDAIGKARQKGnfSGANDERenTLNQMLVEMDGFTPADHVVVLAGTNRPDILDKALLRP 507
Cdd:cd19503  81 NLREIFEEARSHAPSIIFIDEIDALAPKREED--QREVERR--VVAQLLTLMDGMSSRGKVVVIAATNRPDAIDPALRRP 156

                ....*....
gi 6323736  508 GRFDRHINI 516
Cdd:cd19503 157 GRFDREVEI 165
RecA-like_VCP_r2 cd19529
second of two ATPase domains of Valosin-containing protein-like ATPase (VAT) and similar ...
356-516 1.47e-51

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: 177.30  E-value: 1.47e-51
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323736  356 AKEEIMEFVSF-LKEPSRYEKMGAKIPRGAILSGPPGTGKTLLAKATAGEAGVPFYFVSGSEFVEMFVGVGAARVRDLFK 434
Cdd:cd19529   1 VKQELKEAVEWpLLKPEVFKRLGIRPPKGILLYGPPGTGKTLLAKAVATESNANFISVKGPELLSKWVGESEKAIREIFR 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323736  435 TARENAPSIVFIDEIDAIGKARQKGNFSGANderENTLNQMLVEMDGFTPADHVVVLAGTNRPDILDKALLRPGRFDRHI 514
Cdd:cd19529  81 KARQVAPCVIFFDEIDSIAPRRGTTGDSGVT---ERVVNQLLTELDGLEEMNGVVVIAATNRPDIIDPALLRAGRFDRLI 157

                ..
gi 6323736  515 NI 516
Cdd:cd19529 158 YI 159
AAA pfam00004
ATPase family associated with various cellular activities (AAA); AAA family proteins often ...
385-517 2.29e-50

ATPase family associated with various cellular activities (AAA); AAA family proteins often perform chaperone-like functions that assist in the assembly, operation, or disassembly of protein complexes.


Pssm-ID: 459627 [Multi-domain]  Cd Length: 130  Bit Score: 172.78  E-value: 2.29e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323736    385 ILSGPPGTGKTLLAKATAGEAGVPFYFVSGSEFVEMFVGVGAARVRDLFKTARENAPSIVFIDEIDAIGKARqkgnFSGA 464
Cdd:pfam00004   2 LLYGPPGTGKTTLAKAVAKELGAPFIEISGSELVSKYVGESEKRLRELFEAAKKLAPCVIFIDEIDALAGSR----GSGG 77
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 6323736    465 NDERENTLNQMLVEMDGFTPADH-VVVLAGTNRPDILDKALLrpGRFDRHINID 517
Cdd:pfam00004  78 DSESRRVVNQLLTELDGFTSSNSkVIVIAATNRPDKLDPALL--GRFDRIIEFP 129
RecA-like_CDC48_r2-like cd19528
second of two ATPase domains of CDC48 and similar ATPase domains; CDC48 in yeast and p97 or ...
357-516 1.59e-48

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: 168.84  E-value: 1.59e-48
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323736  357 KEEIMEFVSF-LKEPSRYEKMGAKIPRGAILSGPPGTGKTLLAKATAGEAGVPFYFVSGSEFVEMFVGVGAARVRDLFKT 435
Cdd:cd19528   2 KRELQELVQYpVEHPDKFLKFGMTPSKGVLFYGPPGCGKTLLAKAIANECQANFISVKGPELLTMWFGESEANVRDIFDK 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323736  436 ARENAPSIVFIDEIDAIGKARqKGNFSGANDERENTLNQMLVEMDGFTPADHVVVLAGTNRPDILDKALLRPGRFDRHIN 515
Cdd:cd19528  82 ARAAAPCVLFFDELDSIAKAR-GGNIGDAGGAADRVINQILTEMDGMNTKKNVFIIGATNRPDIIDPAILRPGRLDQLIY 160

                .
gi 6323736  516 I 516
Cdd:cd19528 161 I 161
RecA-like_CDC48_r1-like cd19519
first of two ATPase domains of CDC48 and similar ATPase domains; CDC48 in yeast and p97 or VCP ...
349-516 2.79e-48

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: 168.38  E-value: 2.79e-48
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323736  349 DVAGCDEAKEEIMEFVSF-LKEPSRYEKMGAKIPRGAILSGPPGTGKTLLAKATAGEAGVPFYFVSGSEFVEMFVGVGAA 427
Cdd:cd19519   1 DIGGCRKQLAQIREMVELpLRHPELFKAIGIKPPRGILLYGPPGTGKTLIARAVANETGAFFFLINGPEIMSKLAGESES 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323736  428 RVRDLFKTARENAPSIVFIDEIDAIGKARQKgnfsgANDERENTL-NQMLVEMDGFTPADHVVVLAGTNRPDILDKALLR 506
Cdd:cd19519  81 NLRKAFEEAEKNAPAIIFIDEIDAIAPKREK-----THGEVERRIvSQLLTLMDGLKQRAHVIVMAATNRPNSIDPALRR 155
                       170
                ....*....|
gi 6323736  507 PGRFDRHINI 516
Cdd:cd19519 156 FGRFDREIDI 165
RecA-like_NVL_r1-like cd19518
first of two ATPase domains of NVL (nuclear VCP-like protein) and similar ATPase domains; NVL ...
349-516 4.82e-46

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: 162.19  E-value: 4.82e-46
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323736  349 DVAGCDEAKEEIMEFVSFLKEPSR-YEKMGAKIPRGAILSGPPGTGKTLLAKATAGEAGVPFYFVSGSEFVEMFVGVGAA 427
Cdd:cd19518   1 DIGGMDSTLKELCELLIHPILPPEyFQHLGVEPPRGVLLHGPPGCGKTMLANAIAGELKVPFLKISATEIVSGVSGESEE 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323736  428 RVRDLFKTARENAPSIVFIDEIDAIGKARQkgnfsGANDERENTL-NQMLVEMDGF----TPADHVVVLAGTNRPDILDK 502
Cdd:cd19518  81 KIRELFDQAISNAPCIVFIDEIDAITPKRE-----SAQREMERRIvSQLLTCMDELnnekTAGGPVLVIGATNRPDSLDP 155
                       170
                ....*....|....
gi 6323736  503 ALLRPGRFDRHINI 516
Cdd:cd19518 156 ALRRAGRFDREICL 169
RecA-like_NVL_r2-like cd19530
second of two ATPase domains of NVL (nuclear VCP-like protein) and similar ATPase domains; NVL ...
354-512 6.39e-42

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: 150.33  E-value: 6.39e-42
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323736  354 DEAKEEI-MEFVSFLKEPSRYEKMGAKIPRGAILSGPPGTGKTLLAKATAGEAGVPFYFVSGSEFVEMFVGVGAARVRDL 432
Cdd:cd19530   2 DHVREELtMSILRPIKRPDIYKALGIDLPTGVLLYGPPGCGKTLLAKAVANESGANFISVKGPELLNKYVGESERAVRQV 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323736  433 FKTARENAPSIVFIDEIDAIGKARQKGNFSGAnderENTLNQMLVEMDGFTPADHVVVLAGTNRPDILDKALLRPGRFDR 512
Cdd:cd19530  82 FQRARASAPCVIFFDEVDALVPKRGDGGSWAS----ERVVNQLLTEMDGLEERSNVFVIAATNRPDIIDPAMLRPGRLDK 157
RecA-like_PEX1_r2 cd19526
second of two ATPase domains of Peroxisomal biogenesis factor 1 (PEX1); PEX1(also known as ...
355-514 5.16e-38

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: 139.10  E-value: 5.16e-38
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323736  355 EAKEEIMEFVSflKEPSRYEKMGAKIPRGAILSGPPGTGKTLLAKATAGEAGVPFYFVSGSEFVEMFVGVGAARVRDLFK 434
Cdd:cd19526   3 KALEETIEWPS--KYPKIFASSPLRLRSGILLYGPPGCGKTLLASAIASECGLNFISVKGPELLNKYIGASEQNVRDLFS 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323736  435 TARENAPSIVFIDEIDAIGKARQKGNfSGANDErenTLNQMLVEMDGFTPADHVVVLAGTNRPDILDKALLRPGRFDRHI 514
Cdd:cd19526  81 RAQSAKPCILFFDEFDSIAPKRGHDS-TGVTDR---VVNQLLTQLDGVEGLDGVYVLAATSRPDLIDPALLRPGRLDKLV 156
RecA-like_PEX6_r2 cd19527
second of two ATPase domains of Peroxisomal biogenesis factor 6 (PEX6); PEX6(also known as ...
357-512 1.55e-37

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: 138.03  E-value: 1.55e-37
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323736  357 KEEIMEFVSF-LKEPSRYEKmGAKIPRGAILSGPPGTGKTLLAKATAGEAGVPFYFVSGSEFVEMFVGVGAARVRDLFKT 435
Cdd:cd19527   2 KKEILDTIQLpLEHPELFSS-GLRKRSGILLYGPPGTGKTLLAKAIATECSLNFLSVKGPELINMYIGESEANVREVFQK 80
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 6323736  436 ARENAPSIVFIDEIDAIGKARQKGNFSGANDERenTLNQMLVEMDGFTPA-DHVVVLAGTNRPDILDKALLRPGRFDR 512
Cdd:cd19527  81 ARDAKPCVIFFDELDSLAPSRGNSGDSGGVMDR--VVSQLLAELDGMSSSgQDVFVIGATNRPDLLDPALLRPGRFDK 156
RecA-like_VPS4-like cd19509
ATPase domain of VPS4, ATAD1, K, KTNA1, Spastin, FIGL-1 and similar ATPase domains; This ...
350-516 1.17e-36

ATPase domain of VPS4, ATAD1, K, KTNA1, Spastin, FIGL-1 and similar ATPase domains; This subfamily includes the ATPase domains of vacuolar protein sorting-associated protein 4 (VPS4), ATPase family AAA domain-containing protein 1 (ATAD1, also known as Thorase), Katanin p60 ATPase-containing subunit A1 (KTNA1), Spastin, and Fidgetin-Like 1 (FIGL-1). This subfamily belongs to the RecA-like NTPase family which includes the NTP binding domain of F1 and V1 H(+)ATPases, DnaB and related helicases as well as bacterial RecA and related eukaryotic and archaeal recombinases. The RecA-like NTPase family also includes bacterial conjugation proteins and related DNA transfer proteins involved in type II and type IV secretion.


Pssm-ID: 410917 [Multi-domain]  Cd Length: 163  Bit Score: 135.56  E-value: 1.17e-36
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323736  350 VAGCDEAKEEIMEFVSF-LKEPSRYeKMGAKIPRGAILSGPPGTGKTLLAKATAGEAGVPFYFVSGSEFVEMFVGVGAAR 428
Cdd:cd19509   1 IAGLDDAKEALKEAVILpSLRPDLF-PGLRGPPRGILLYGPPGTGKTLLARAVASESGSTFFSISASSLVSKWVGESEKI 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323736  429 VRDLFKTARENAPSIVFIDEIDAIGKARQKGNFSGANDERentlNQMLVEMDGFT--PADHVVVLAGTNRPDILDKALLR 506
Cdd:cd19509  80 VRALFALARELQPSIIFIDEIDSLLSERGSGEHEASRRVK----TEFLVQMDGVLnkPEDRVLVLGATNRPWELDEAFLR 155
                       170
                ....*....|
gi 6323736  507 pgRFDRHINI 516
Cdd:cd19509 156 --RFEKRIYI 163
RecA-like_VPS4 cd19521
ATPase domain of vacuolar protein sorting-associated protein 4; Vacuolar protein ...
344-516 4.61e-34

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


Pssm-ID: 410929 [Multi-domain]  Cd Length: 170  Bit Score: 128.44  E-value: 4.61e-34
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323736  344 KIKFKDVAGCDEAKEEIMEFVSFlkePSRYEKM--GAKIP-RGAILSGPPGTGKTLLAKATAGEAGVPFYFVSGSEFVEM 420
Cdd:cd19521   3 NVKWEDVAGLEGAKEALKEAVIL---PVKFPHLftGNRKPwSGILLYGPPGTGKSYLAKAVATEANSTFFSVSSSDLVSK 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323736  421 FVGVGAARVRDLFKTARENAPSIVFIDEIDAIGKARQKGNfsgaNDERENTLNQMLVEMDGF-TPADHVVVLAGTNRPDI 499
Cdd:cd19521  80 WMGESEKLVKQLFAMARENKPSIIFIDEVDSLCGTRGEGE----SEASRRIKTELLVQMNGVgNDSQGVLVLGATNIPWQ 155
                       170
                ....*....|....*..
gi 6323736  500 LDKALLRpgRFDRHINI 516
Cdd:cd19521 156 LDSAIRR--RFEKRIYI 170
RecA-like_Yta7-like cd19517
ATPase domain of Saccharomyces cerevisiae Yta7 and similar ATPase domains; Saccharomyces ...
349-515 6.82e-32

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


Pssm-ID: 410925 [Multi-domain]  Cd Length: 170  Bit Score: 122.23  E-value: 6.82e-32
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323736  349 DVAGCDEAKEEIMEFVSF-LKEPSRYEKMGAKIPRGAILSGPPGTGKTLLAKATAGEAG-----VPFYFVSGSEFVEMFV 422
Cdd:cd19517   1 DIGGLSHYINQLKEMVFFpLLYPEVFAKFKITPPRGVLFHGPPGTGKTLMARALAAECSkggqkVSFFMRKGADCLSKWV 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323736  423 GVGAARVRDLFKTARENAPSIVFIDEIDAIGKARqkgnfSGANDERENTL-NQMLVEMDGFTPADHVVVLAGTNRPDILD 501
Cdd:cd19517  81 GEAERQLRLLFEEAYRMQPSIIFFDEIDGLAPVR-----SSKQEQIHASIvSTLLALMDGLDNRGQVVVIGATNRPDALD 155
                       170
                ....*....|....
gi 6323736  502 KALLRPGRFDRHIN 515
Cdd:cd19517 156 PALRRPGRFDREFY 169
RecA-like_spastin cd19524
ATPase domain of spastin; Spastin is an ATP-dependent microtubule-severing protein involved in ...
349-514 1.72e-31

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


Pssm-ID: 410932 [Multi-domain]  Cd Length: 164  Bit Score: 120.72  E-value: 1.72e-31
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323736  349 DVAGCDEAKEEIMEFVSF-LKEPSRYEKMGAKiPRGAILSGPPGTGKTLLAKATAGEAGVPFYFVSGSEFVEMFVGVGAA 427
Cdd:cd19524   1 DIAGQDLAKQALQEMVILpSLRPELFTGLRAP-ARGLLLFGPPGNGKTMLAKAVAAESNATFFNISAASLTSKYVGEGEK 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323736  428 RVRDLFKTARENAPSIVFIDEIDAIGKARQkgnfSGANDERENTLNQMLVEMDGFT--PADHVVVLAGTNRPDILDKALL 505
Cdd:cd19524  80 LVRALFAVARELQPSIIFIDEVDSLLSERS----EGEHEASRRLKTEFLIEFDGVQsnGDDRVLVMGATNRPQELDDAVL 155

                ....*....
gi 6323736  506 RpgRFDRHI 514
Cdd:cd19524 156 R--RFTKRV 162
RecA-like_ATAD1 cd19520
ATPase domain of ATPase family AAA domain-containing protein 1 and similar ATPase domains; ...
349-510 2.97e-30

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: 117.14  E-value: 2.97e-30
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323736  349 DVAGCDEAKEEIMEFVSF-LKEPSRYEKMG-AKIPRGAILSGPPGTGKTLLAKATAGEAGVPFYFVSGSEFVEMFVGVGA 426
Cdd:cd19520   1 DIGGLDEVITELKELVILpLQRPELFDNSRlLQPPKGVLLYGPPGCGKTMLAKATAKEAGARFINLQVSSLTDKWYGESQ 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323736  427 ARVRDLFKTARENAPSIVFIDEIDAIGKARQkgnfSGANDERENTLNQMLVEMDGFTPADH--VVVLAGTNRPDILDKAL 504
Cdd:cd19520  81 KLVAAVFSLASKLQPSIIFIDEIDSFLRQRS----STDHEATAMMKAEFMSLWDGLSTDGNcrVIVMGATNRPQDLDEAI 156

                ....*...
gi 6323736  505 LR--PGRF 510
Cdd:cd19520 157 LRrmPKRF 164
RecA-like_Figl-1 cd19525
ATPase domain of Fidgetin-Like 1 (FIGL-1); FIGL-1 may participate in DNA repair in the nucleus; ...
345-516 4.39e-30

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: 117.40  E-value: 4.39e-30
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323736  345 IKFKDVAGCDEAKEEIMEFVSF-LKEPSRYEKMGAKiPRGAILSGPPGTGKTLLAKATAGEAGVPFYFVSGSEFVEMFVG 423
Cdd:cd19525  19 INWADIAGLEFAKKTIKEIVVWpMLRPDIFTGLRGP-PKGILLFGPPGTGKTLIGKCIASQSGATFFSISASSLTSKWVG 97
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323736  424 VGAARVRDLFKTARENAPSIVFIDEIDAIGKARQKGNfsgaNDERENTLNQMLVEMDGFT--PADHVVVLAGTNRPDILD 501
Cdd:cd19525  98 EGEKMVRALFSVARCKQPAVIFIDEIDSLLSQRGEGE----HESSRRIKTEFLVQLDGATtsSEDRILVVGATNRPQEID 173
                       170
                ....*....|....*
gi 6323736  502 KALLRpgRFDRHINI 516
Cdd:cd19525 174 EAARR--RLVKRLYI 186
RecA-like_NSF-SEC18_r1-like cd19504
first of two ATPase domains of NSF and SEC18, and similar ATPase domains; ...
363-516 2.99e-29

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


Pssm-ID: 410912 [Multi-domain]  Cd Length: 177  Bit Score: 114.89  E-value: 2.99e-29
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323736  363 FVSFLKEPSRYEKMGAKIPRGAILSGPPGTGKTLLAKA-----TAGEAGVpfyfVSGSEFVEMFVGVGAARVRDLFKTAR 437
Cdd:cd19504  17 FASRVFPPEIVEQLGCKHVKGILLYGPPGTGKTLMARQigkmlNAREPKI----VNGPEILNKYVGESEANIRKLFADAE 92
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323736  438 ENAPS--------IVFIDEIDAIGKarQKGNFSGANDERENTLNQMLVEMDGFTPADHVVVLAGTNRPDILDKALLRPGR 509
Cdd:cd19504  93 EEQRRlgansglhIIIFDEIDAICK--QRGSMAGSTGVHDTVVNQLLSKIDGVEQLNNILVIGMTNRKDLIDEALLRPGR 170

                ....*..
gi 6323736  510 FDRHINI 516
Cdd:cd19504 171 LEVQMEI 177
RecA-like_KTNA1 cd19522
Katanin p60 ATPase-containing subunit A1; Katanin p60 ATPase-containing subunit A1 (KTNA1) is ...
349-516 9.92e-29

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: 113.16  E-value: 9.92e-29
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323736  349 DVAGCDEAKEEIMEFVSF-LKEPSRYEkmGAKIP-RGAILSGPPGTGKTLLAKATAGEAGVPFYFVSGSEFVEMFVGVGA 426
Cdd:cd19522   1 DIADLEEAKKLLEEAVVLpMWMPEFFK--GIRRPwKGVLMVGPPGTGKTLLAKAVATECGTTFFNVSSSTLTSKYRGESE 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323736  427 ARVRDLFKTARENAPSIVFIDEIDAIGKARqkgnfsGANDERENTL---NQMLVEMDGFT-------PADHVVVLAGTNR 496
Cdd:cd19522  79 KLVRLLFEMARFYAPTTIFIDEIDSICSRR------GTSEEHEASRrvkSELLVQMDGVGgasenddPSKMVMVLAATNF 152
                       170       180
                ....*....|....*....|
gi 6323736  497 PDILDKALLRpgRFDRHINI 516
Cdd:cd19522 153 PWDIDEALRR--RLEKRIYI 170
AAA cd00009
The AAA+ (ATPases Associated with a wide variety of cellular Activities) superfamily ...
381-518 3.32e-24

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


Pssm-ID: 99707 [Multi-domain]  Cd Length: 151  Bit Score: 99.53  E-value: 3.32e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323736  381 PRGAILSGPPGTGKTLLAKATAGEA---GVPFYFVSGSEFVEMFVG---VGAARVRDLFKTARENAPSIVFIDEIDAIGK 454
Cdd:cd00009  19 PKNLLLYGPPGTGKTTLARAIANELfrpGAPFLYLNASDLLEGLVVaelFGHFLVRLLFELAEKAKPGVLFIDEIDSLSR 98
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 6323736  455 ARQKGNfsganderentLNQMLVEMDGFTPADHVVVLAGTNRPDILDKALLRPGRFDRHINIDK 518
Cdd:cd00009  99 GAQNAL-----------LRVLETLNDLRIDRENVRVIGATNRPLLGDLDRALYDRLDIRIVIPL 151
ycf46 CHL00195
Ycf46; Provisional
343-571 2.59e-22

Ycf46; Provisional


Pssm-ID: 177094 [Multi-domain]  Cd Length: 489  Bit Score: 101.25  E-value: 2.59e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323736   343 VKIKFKDVAGCDEAKEEI-MEFVSFLKEPSRYekmGAKIPRGAILSGPPGTGKTLLAKATAGEAGVPFYFVSGSEFVEMF 421
Cdd:CHL00195 223 VNEKISDIGGLDNLKDWLkKRSTSFSKQASNY---GLPTPRGLLLVGIQGTGKSLTAKAIANDWQLPLLRLDVGKLFGGI 299
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323736   422 VGVGAARVRDLFKTARENAPSIVFIDEID-AIGKARQKGNfSGANDERENTLNQMLVEMDGFtpadhVVVLAGTNRPDIL 500
Cdd:CHL00195 300 VGESESRMRQMIRIAEALSPCILWIDEIDkAFSNSESKGD-SGTTNRVLATFITWLSEKKSP-----VFVVATANNIDLL 373
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 6323736   501 DKALLRPGRFDRHINIDKPELEGRKAIFAVHLHHLK-LAGEIFDLKnRLAALTPGFSGADIANVCNEAALIA 571
Cdd:CHL00195 374 PLEILRKGRFDEIFFLDLPSLEEREKIFKIHLQKFRpKSWKKYDIK-KLSKLSNKFSGAEIEQSIIEAMYIA 444
RecA-like_BCS1 cd19510
Mitochondrial chaperone BCS1; Mitochondrial chaperone BCS1 is necessary for the assembly of ...
365-516 3.00e-22

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: 93.96  E-value: 3.00e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323736  365 SFLKEPSRYEKMGAKIPRGAILSGPPGTGKTLLAKATAGEAGVPFYFVSGSEfvemfVGVGAARVRDLFKTARENapSIV 444
Cdd:cd19510   7 DFIKNEDWYNDRGIPYRRGYLLYGPPGTGKSSFIAALAGELDYDICDLNLSE-----VVLTDDRLNHLLNTAPKQ--SII 79
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 6323736  445 FIDEIDA--IGKARQKGNFSGANDERENTLNQMLVEMDGFTPADHVVVLAGTNRPDILDKALLRPGRFDRHINI 516
Cdd:cd19510  80 LLEDIDAafESREHNKKNPSAYGGLSRVTFSGLLNALDGVASSEERIVFMTTNHIERLDPALIRPGRVDMKIYM 153
RecA-like_fidgetin cd19523
ATPase domain of fidgetin; Fidgetin (FIGN) is a ATP-dependent microtubule severing protein. ...
349-506 1.07e-21

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: 1.07e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323736  349 DVAGCDEAKEEIMEFVSF-LKEPSRYEKMgAKIPRGAILSGPPGTGKTLLAKATAGEAGVPFYFVSGSEFVEMFVGVGAA 427
Cdd:cd19523   1 DIAGLGALKAAIKEEVLWpLLRPDAFSGL-LRLPRSILLFGPRGTGKTLLGRCLASQLGATFLRLRGSTLVAKWAGEGEK 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323736  428 RVRDLFKTARENAPSIVFIDEIDAIGKARQKGNFSGANDEREntlnqMLVEMDGF--TPADHVVVLAGTNRPDILDKALL 505
Cdd:cd19523  80 ILQASFLAARCRQPSVLFISDLDALLSSQDDEASPVGRLQVE-----LLAQLDGVlgSGEDGVLVVCTTSKPEEIDESLR 154

                .
gi 6323736  506 R 506
Cdd:cd19523 155 R 155
RecA-like_Ycf46-like cd19507
ATPase domain of Ycf46 and similar ATPase domains; Ycf46 may play a role in the regulation of ...
349-512 9.45e-19

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: 83.96  E-value: 9.45e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323736  349 DVAGCDEAKEEIME-FVSFLKEPSRYekmGAKIPRGAILSGPPGTGKTLLAKATAGEAGVPFYFVSGSEFVEMFVGVGAA 427
Cdd:cd19507   1 DVGGLDNLKDWLKKrKAAFSKQASAY---GLPTPKGLLLVGIQGTGKSLTAKAIAGVWQLPLLRLDMGRLFGGLVGESES 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323736  428 RVRDLFKTARENAPSIVFIDEIDaigKARQKGNFSGANDERENTLNQMLVEMDGFTPAdhVVVLAGTNRPDILDKALLRP 507
Cdd:cd19507  78 RLRQMIQTAEAIAPCVLWIDEIE---KGFSNADSKGDSGTSSRVLGTFLTWLQEKKKP--VFVVATANNVQSLPPELLRK 152

                ....*
gi 6323736  508 GRFDR 512
Cdd:cd19507 153 GRFDE 157
AAA smart00382
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ...
381-520 2.50e-17

ATPases associated with a variety of cellular activities; AAA - ATPases associated with a variety of cellular activities. This profile/alignment only detects a fraction of this vast family. The poorly conserved N-terminal helix is missing from the alignment.


Pssm-ID: 214640 [Multi-domain]  Cd Length: 148  Bit Score: 79.72  E-value: 2.50e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323736     381 PRGAILSGPPGTGKTLLAKATAGEA---GVPFYFVSGSEFVE--------------MFVGVGAARVRDLFKTARENAPSI 443
Cdd:smart00382   2 GEVILIVGPPGSGKTTLARALARELgppGGGVIYIDGEDILEevldqllliivggkKASGSGELRLRLALALARKLKPDV 81
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 6323736     444 VFIDEIDAIGKARQkgnfsgandERENTLNQMLVEMDGFTPADHVVVLAGTNRPDILDKALLRPgRFDRHINIDKPE 520
Cdd:smart00382  82 LILDEITSLLDAEQ---------EALLLLLEELRLLLLLKSEKNLTVILTTNDEKDLGPALLRR-RFDRRIVLLLIL 148
AAA_lid_3 pfam17862
AAA+ lid domain; This entry represents the alpha helical AAA+ lid domain that is found to the ...
542-586 5.34e-12

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


Pssm-ID: 465537 [Multi-domain]  Cd Length: 45  Bit Score: 61.02  E-value: 5.34e-12
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 6323736    542 FDLKnRLAALTPGFSGADIANVCNEAALIAARSDEDAVKLNHFEQ 586
Cdd:pfam17862   2 VDLE-ELAERTEGFSGADLEALCREAALAALRRGLEAVTQEDLEE 45
RecA-like_ATAD3-like cd19512
ATPase domains of ATPase AAA-domain protein 3A (ATAD3A), -3B, and -3C, and similar ATPase ...
382-504 1.13e-09

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


Pssm-ID: 410920 [Multi-domain]  Cd Length: 150  Bit Score: 57.54  E-value: 1.13e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323736  382 RGAILSGPPGTGKTLLAKATAGEAGVPFYFVSGSEFVEMFV-GVGAA-RVRDLFKTARENApsIVFIDEIDAIGKARQKG 459
Cdd:cd19512  23 RNILFYGPPGTGKTLFAKKLALHSGMDYAIMTGGDVAPMGReGVTAIhKVFDWANTSRRGL--LLFVDEADAFLRKRSTE 100
                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*
gi 6323736  460 NFSgaNDEREnTLNQMLVEMdGFTPADHVVVLAgTNRPDILDKAL 504
Cdd:cd19512 101 KIS--EDLRA-ALNAFLYRT-GEQSNKFMLVLA-SNQPEQFDWAI 140
PRK13342 PRK13342
recombination factor protein RarA; Reviewed
385-449 2.94e-09

recombination factor protein RarA; Reviewed


Pssm-ID: 237355 [Multi-domain]  Cd Length: 413  Bit Score: 60.10  E-value: 2.94e-09
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 6323736   385 ILSGPPGTGKTLLAKATAGEAGVPFYFVSGSefvemFVGVgaARVRDLFKTARENAPS----IVFIDEI 449
Cdd:PRK13342  40 ILWGPPGTGKTTLARIIAGATDAPFEALSAV-----TSGV--KDLREVIEEARQRRSAgrrtILFIDEI 101
RarA COG2256
Replication-associated recombination protein RarA (DNA-dependent ATPase) [Replication, ...
385-449 3.83e-09

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


Pssm-ID: 441857 [Multi-domain]  Cd Length: 439  Bit Score: 59.68  E-value: 3.83e-09
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 6323736  385 ILSGPPGTGKTLLAKATAGEAGVPFYFVSGsefvemfVGVGAARVRDLFKTARENA----PSIVFIDEI 449
Cdd:COG2256  53 ILWGPPGTGKTTLARLIANATDAEFVALSA-------VTSGVKDIREVIEEARERRaygrRTILFVDEI 114
RecA-like_HslU cd19498
ATP-dependent protease ATPase subunit HslU; HslU is a component of the ATP-dependent protease ...
367-492 5.60e-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: 56.62  E-value: 5.60e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323736  367 LKEPSRYEKMgakiPRGAILSGPPGTGKTLLAKATAGEAGVPFYFVSGSEFVEM-FVGvgaarvRDLFKTARENAPSIVF 445
Cdd:cd19498  36 LPEELRDEVT----PKNILMIGPTGVGKTEIARRLAKLAGAPFIKVEATKFTEVgYVG------RDVESIIRDLVEGIVF 105
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*
gi 6323736  446 IDEIDAIGKarqKGNFSGANDERENTLNQMLVEMDGFT--------PADHVVVLA 492
Cdd:cd19498 106 IDEIDKIAK---RGGSSGPDVSREGVQRDLLPIVEGSTvstkygpvKTDHILFIA 157
PRK04195 PRK04195
replication factor C large subunit; Provisional
346-455 1.09e-08

replication factor C large subunit; Provisional


Pssm-ID: 235250 [Multi-domain]  Cd Length: 482  Bit Score: 58.39  E-value: 1.09e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323736   346 KFKDVAGCDEAKEEIMEFV-SFLKEpsryekmgaKIPRGAILSGPPGTGKTLLAKATAGEAGVPFYFVSGSEF-----VE 419
Cdd:PRK04195  12 TLSDVVGNEKAKEQLREWIeSWLKG---------KPKKALLLYGPPGVGKTSLAHALANDYGWEVIELNASDQrtadvIE 82
                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 6323736   420 MFVGvGAARVRDLFKTARenapSIVFIDEIDAI-GKA 455
Cdd:PRK04195  83 RVAG-EAATSGSLFGARR----KLILLDEVDGIhGNE 114
RecA-like_Lon cd19500
lon protease homolog 2 peroxisomal; Lon protease (also known as Lon peptidase) is an ...
348-457 1.41e-08

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: 55.26  E-value: 1.41e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323736  348 KDVAGCDEAKEEIMEFVSFLKepsRYEKMGAKIprgAILSGPPGTGKTLLAKATAGEAGVPFYFVS-G--SEFVEM---- 420
Cdd:cd19500  10 ADHYGLEDVKERILEYLAVRK---LKGSMKGPI---LCLVGPPGVGKTSLGKSIARALGRKFVRISlGgvRDEAEIrghr 83
                        90       100       110
                ....*....|....*....|....*....|....*....
gi 6323736  421 --FVGVGAARVRDLFKTARENAPSIVfIDEIDAIGKARQ 457
Cdd:cd19500  84 rtYVGAMPGRIIQALKKAGTNNPVFL-LDEIDKIGSSFR 121
RecA-like_Ycf2 cd19505
ATPase domain of plant YCF2; Ycf2 is a chloroplast ATPase which has an essential function; ...
381-516 7.56e-07

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


Pssm-ID: 410913 [Multi-domain]  Cd Length: 161  Bit Score: 49.68  E-value: 7.56e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323736  381 PRGAILSGPPGTGKTLLAKATAGEAGVPFYFVSGSEFV--------------EMFVGVGAARVRDLFKTARENAPSIVFI 446
Cdd:cd19505  12 SKGILLIGSIETGRSYLIKSLAANSYVPLIRISLNKLLynkpdfgnddwidgMLILKESLHRLNLQFELAKAMSPCIIWI 91
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323736  447 DEIDA--IGKARQKG------------NFSGANDERENTLNqmlvemdgftpadhVVVLAGTNRPDILDKALLRPGRFDR 512
Cdd:cd19505  92 PNIHElnVNRSTQNLeedpklllglllNYLSRDFEKSSTRN--------------ILVIASTHIPQKVDPALIAPNRLDT 157

                ....
gi 6323736  513 HINI 516
Cdd:cd19505 158 CINI 161
RecA-like_Pch2-like cd19508
ATPase domain of Pachytene checkpoint 2 (Pch2) and similar ATPase domains; Pch2 (known as ...
382-504 2.18e-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: 2.18e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323736  382 RGAILSGPPGTGKTLLAKATAGEAGVPFYFV----------SGSEFVEMFVGVGAArVRDLFKTARE-----NAPSIVFI 446
Cdd:cd19508  53 RLVLLHGPPGTGKTSLCKALAQKLSIRLSSRyrygqlieinSHSLFSKWFSESGKL-VTKMFQKIQEliddkDALVFVLI 131
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323736  447 DEIDAIGKARQkgNFSGANDERE--NTLNQMLVEMDGFTPADHVVVLAGTNRPDILDKAL 504
Cdd:cd19508 132 DEVESLAAARS--ASSSGTEPSDaiRVVNAVLTQIDRIKRYHNNVILLTSNLLEKIDVAF 189
T7SS_EccA TIGR03922
type VII secretion AAA-ATPase EccA; This model represents the AAA family ATPase, EccA, of the ...
352-517 2.38e-06

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


Pssm-ID: 188437 [Multi-domain]  Cd Length: 557  Bit Score: 51.00  E-value: 2.38e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323736    352 GCDEAKEEIMEFVSFLKEPSRYEKMGAKIP---RGAILSGPPGTGKTLLAKATAGE-AGVPFYF------VSGSEFVEMF 421
Cdd:TIGR03922 280 GLERVKRQVAALKSSTAMALARAERGLPVAqtsNHMLFAGPPGTGKTTIARVVAKIyCGLGVLRkplvreVSRADLIGQY 359
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323736    422 VGVGAARVRDLFKTAREnapSIVFIDEIDA-IGKARQKGNFSGAndereNTLNQMLVEMDgfTPADHVVVLAGTNRPDIl 500
Cdd:TIGR03922 360 IGESEAKTNEIIDSALG---GVLFLDEAYTlVETGYGQKDPFGL-----EAIDTLLARME--NDRDRLVVIGAGYRKDL- 428
                         170       180
                  ....*....|....*....|..
gi 6323736    501 DKAL-----LRpGRFDRHINID 517
Cdd:TIGR03922 429 DKFLevnegLR-SRFTRVIEFP 449
AAA_5 pfam07728
AAA domain (dynein-related subfamily); This Pfam entry includes some of the AAA proteins not ...
385-510 2.78e-06

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


Pssm-ID: 400191 [Multi-domain]  Cd Length: 135  Bit Score: 47.29  E-value: 2.78e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323736    385 ILSGPPGTGKTLLAKATAgEA--GVPFYFVSGSEFVE-------MFVGVGAARVRD--LFKTAREnaPSIVFIDEIDAIG 453
Cdd:pfam07728   3 LLVGPPGTGKTELAERLA-AAlsNRPVFYVQLTRDTTeedlfgrRNIDPGGASWVDgpLVRAARE--GEIAVLDEINRAN 79
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 6323736    454 KARQkGNFSGANDEREntlnqmLVEMDGFT----PADHVVVLAGTNRPDI----LDKALLRpgRF 510
Cdd:pfam07728  80 PDVL-NSLLSLLDERR------LLLPDGGElvkaAPDGFRLIATMNPLDRglneLSPALRS--RF 135
TIP49 COG1224
DNA helicase TIP49, TBP-interacting protein [Transcription];
342-417 1.36e-05

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


Pssm-ID: 440837 [Multi-domain]  Cd Length: 452  Bit Score: 48.43  E-value: 1.36e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323736  342 DVKIKFKDVA----GCDEAKEEIMEFVSFLKEpsryEKMGAkipRGAILSGPPGTGKTLLAKATAGEAG--VPFYFVSGS 415
Cdd:COG1224  28 DENGKAKFVAdglvGQVEAREAAGIVVKMIKE----GKMAG---KGILIVGPPGTGKTALAVAIARELGedTPFVAISGS 100

                ..
gi 6323736  416 EF 417
Cdd:COG1224 101 EI 102
TIP49 pfam06068
TIP49 P-loop domain; This family consists of the C-terminal region of several eukaryotic and ...
382-417 4.39e-05

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


Pssm-ID: 399217 [Multi-domain]  Cd Length: 347  Bit Score: 46.53  E-value: 4.39e-05
                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 6323736    382 RGAILSGPPGTGKTLLAKATAGEAG--VPFYFVSGSEF 417
Cdd:pfam06068  51 RAVLIAGPPGTGKTALAIAISKELGedTPFTSISGSEV 88
AAA_2 pfam07724
AAA domain (Cdc48 subfamily); This Pfam entry includes some of the AAA proteins not detected ...
385-452 5.39e-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: 44.49  E-value: 5.39e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323736    385 ILSGPPGTGKTLLAKATAGEAGV---PFYFVSGSEFVE-----MFVGVGAARVR-----DLFKTARENAPSIVFIDEIDA 451
Cdd:pfam07724   7 LFLGPTGVGKTELAKALAELLFGderALIRIDMSEYMEehsvsRLIGAPPGYVGyeeggQLTEAVRRKPYSIVLIDEIEK 86

                  .
gi 6323736    452 I 452
Cdd:pfam07724  87 A 87
RecA-like_superfamily cd01120
RecA-like_NTPases; RecA-like NTPases. This superfamily includes the NTP binding domain of F1 ...
385-501 6.68e-05

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


Pssm-ID: 410865 [Multi-domain]  Cd Length: 119  Bit Score: 43.26  E-value: 6.68e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323736  385 ILSGPPGTGKTLLAKATAGEA---GVPFYFVSgseFVEMFVgvgaARVRDLfktARENAPSIVFIDEIDAIGKARQkgnf 461
Cdd:cd01120   2 LITGPPGSGKTTLLLQFAEQAllsDEPVIFIS---FLDTIL----EAIEDL---IEEKKLDIIIIDSLSSLARASQ---- 67
                        90       100       110       120
                ....*....|....*....|....*....|....*....|
gi 6323736  462 sgaNDERENTLNQMLVEMDGFTPAdHVVVLAGTNRPDILD 501
Cdd:cd01120  68 ---GDRSSELLEDLAKLLRAARNT-GITVIATIHSDKFDI 103
ycf2 CHL00206
Ycf2; Provisional
375-590 1.29e-04

Ycf2; Provisional


Pssm-ID: 214396 [Multi-domain]  Cd Length: 2281  Bit Score: 46.06  E-value: 1.29e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323736    375 KMGAKIPRGAILSGPPGTGKTLLAKATAGEAGVPFYFVSGSEFVE----------------------------------- 419
Cdd:CHL00206 1624 RLALSPSRGILVIGSIGTGRSYLVKYLATNSYVPFITVFLNKFLDnkpkgfliddididdsddiddsddidrdldtellt 1703
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323736    420 --------MFVGVGAARVRDLFKTARENAPSIVFIDEIDAIGKARQK-------GNFSGANDERENTLNqmlvemdgftp 484
Cdd:CHL00206 1704 mmnaltmdMMPKIDRFYITLQFELAKAMSPCIIWIPNIHDLNVNESNylslgllVNSLSRDCERCSTRN----------- 1772
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323736    485 adhVVVLAGTNRPDILDKALLRPGRFDRHINIDKPEL-EGRKAIFAV-HLHHLKLAGEIFDLkNRLAALTPGFSGADIAN 562
Cdd:CHL00206 1773 ---ILVIASTHIPQKVDPALIAPNKLNTCIKIRRLLIpQQRKHFFTLsYTRGFHLEKKMFHT-NGFGSITMGSNARDLVA 1848
                         250       260
                  ....*....|....*....|....*...
gi 6323736    563 VCNEAALIAARSDEDAVKLNHFEQAIER 590
Cdd:CHL00206 1849 LTNEALSISITQKKSIIDTNTIRSALHR 1876
ruvB PRK00080
Holliday junction branch migration DNA helicase RuvB;
386-455 1.81e-04

Holliday junction branch migration DNA helicase RuvB;


Pssm-ID: 234619 [Multi-domain]  Cd Length: 328  Bit Score: 44.35  E-value: 1.81e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 6323736   386 LSGPPGTGKTLLAKATAGEAGVPFYFVSGSEFvemfvgvgaARVRDL---FKTARENapSIVFIDEIDAIGKA 455
Cdd:PRK00080  56 LYGPPGLGKTTLANIIANEMGVNIRITSGPAL---------EKPGDLaaiLTNLEEG--DVLFIDEIHRLSPV 117
44 PHA02544
clamp loader, small subunit; Provisional
379-455 1.98e-04

clamp loader, small subunit; Provisional


Pssm-ID: 222866 [Multi-domain]  Cd Length: 316  Bit Score: 44.21  E-value: 1.98e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323736   379 KIPRGAILSGPPGTGKTLLAKATAGEAGVPFYFVSGS----EFVEMFVGVGAARVrdlfktARENAPSIVFIDEIDAIGK 454
Cdd:PHA02544  41 RIPNMLLHSPSPGTGKTTVAKALCNEVGAEVLFVNGSdcriDFVRNRLTRFASTV------SLTGGGKVIIIDEFDRLGL 114

                 .
gi 6323736   455 A 455
Cdd:PHA02544 115 A 115
FtsH_ext pfam06480
FtsH Extracellular; This domain is found in the FtsH family of proteins. FtsH is the only ...
205-282 2.46e-04

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


Pssm-ID: 377663 [Multi-domain]  Cd Length: 103  Bit Score: 41.05  E-value: 2.46e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 6323736    205 EITWQDFREKLlAKGYVAKLIVVNKSMVKVMLNDNGKNQADNYgRNFYYFTIGSIDSFEHKLQKAQDELDIDKDFRIP 282
Cdd:pfam06480  28 EISYSEFLEYL-EAGKVKKVVVQDDEILPTGVVEGTLKDGSKF-TTYFIPSLPNVDSLLEKLEDALEEKGVKVSVKPP 103
RuvB_N pfam05496
Holliday junction DNA helicase RuvB P-loop domain; The RuvB protein makes up part of the ...
385-449 2.61e-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: 2.61e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 6323736    385 ILSGPPGTGKTLLAKATAGEAGVPFYFVSGSEFvemfvgvgaARVRDL---FKTARENapSIVFIDEI 449
Cdd:pfam05496  37 LLYGPPGLGKTTLANIIANEMGVNIRITSGPAI---------ERPGDLaaiLTNLEPG--DVLFIDEI 93
McrB COG1401
5-methylcytosine-specific restriction endonuclease McrBC, GTP-binding regulatory subunit McrB ...
379-449 2.94e-03

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


Pssm-ID: 441011 [Multi-domain]  Cd Length: 477  Bit Score: 40.91  E-value: 2.94e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323736  379 KIPRGAILSGPPGTGKT----LLAKATAGEAGVPFYFV------SGSEFVEMFV---GVGAARVRD-LFKTARENA---- 440
Cdd:COG1401 219 KTKKNVILAGPPGTGKTylarRLAEALGGEDNGRIEFVqfhpswSYEDFLLGYRpslDEGKYEPTPgIFLRFCLKAeknp 298
                        90
                ....*....|.
gi 6323736  441 --PSIVFIDEI 449
Cdd:COG1401 299 dkPYVLIIDEI 309
RecA-like_ClpB_Hsp104-like cd19499
Chaperone protein ClpB/Hsp104 subfamily; Bacterial Caseinolytic peptidase B (ClpB) and ...
344-450 4.20e-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: 39.08  E-value: 4.20e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323736  344 KIKFKDVAGCDEAKEEIMEFV----SFLKEPSRyekmgakiPRGA-ILSGPPGTGKTLLAKATAGeagvpFYF------- 411
Cdd:cd19499   7 ERLHERVVGQDEAVKAVSDAIrrarAGLSDPNR--------PIGSfLFLGPTGVGKTELAKALAE-----LLFgdednli 73
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|
gi 6323736  412 -VSGSEFVEMFVG----------VGAARVRDLFKTARENAPSIVFIDEID 450
Cdd:cd19499  74 rIDMSEYMEKHSVsrligappgyVGYTEGGQLTEAVRRKPYSVVLLDEIE 123
PRK13341 PRK13341
AAA family ATPase;
384-457 4.23e-03

AAA family ATPase;


Pssm-ID: 237354 [Multi-domain]  Cd Length: 725  Bit Score: 40.81  E-value: 4.23e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323736   384 AILSGPPGTGKTLLAKATAGeagvpfYFvsGSEFVEM-FVGVGAARVRDLFKTARE-----NAPSIVFIDEIDAIGKARQ 457
Cdd:PRK13341  55 LILYGPPGVGKTTLARIIAN------HT--RAHFSSLnAVLAGVKDLRAEVDRAKErlerhGKRTILFIDEVHRFNKAQQ 126
AAA_17 pfam13207
AAA domain;
387-517 4.83e-03

AAA domain;


Pssm-ID: 463810 [Multi-domain]  Cd Length: 136  Bit Score: 37.99  E-value: 4.83e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323736    387 SGPPGTGKTLLAKATAGEAGVPfYFVSGSEFVEMFVGVGAARVRDLFKTARENAPSIVFIDEIDAIGKARQKGNF--SG- 463
Cdd:pfam13207   1 TGVPGSGKTTQLKKLAEKLGFP-HISAGDLLREEAKERGLVEDRDEMRKLPLEPQKELQKLAAERIAEEAGEGGVivDGh 79
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 6323736    464 -ANDERENTLNQMLVEMDGFTPADHVVVLAgTNRPDILDKALLRPGRFDRHINID 517
Cdd:pfam13207  80 pRIKTPAGYLPGLPVEVLRELKPDAIILLE-ADPEEILERRLKDRTRGRDDDSEE 133
ruvB TIGR00635
Holliday junction DNA helicase, RuvB subunit; All proteins in this family for which functions ...
385-455 5.23e-03

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


Pssm-ID: 129721 [Multi-domain]  Cd Length: 305  Bit Score: 39.98  E-value: 5.23e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 6323736    385 ILSGPPGTGKTLLAKATAGEAGVPFYFVSGSEFVemfvgvgaaRVRDLFK--TAREnAPSIVFIDEIDAIGKA 455
Cdd:TIGR00635  34 LLYGPPGLGKTTLAHIIANEMGVNLKITSGPALE---------KPGDLAAilTNLE-EGDVLFIDEIHRLSPA 96
DnaC COG1484
DNA replication protein DnaC [Replication, recombination and repair];
382-419 9.52e-03

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


Pssm-ID: 441093 [Multi-domain]  Cd Length: 242  Bit Score: 38.61  E-value: 9.52e-03
                        10        20        30        40
                ....*....|....*....|....*....|....*....|.
gi 6323736  382 RGAILSGPPGTGKTLLAKA---TAGEAGVPFYFVSGSEFVE 419
Cdd:COG1484 100 ENLILLGPPGTGKTHLAIAlghEACRAGYRVRFTTAPDLVN 140
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

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