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Conserved domains on  [gi|961788553|gb|KTB13536|]
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Mitochondrial respiratory chain complexes assembly protein YTA12 [Nakaseomyces glabratus]

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 ...
209-703 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: 809.59  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961788553  209 NWARALFQMLPTVLMLVGIIWLTRKSMQSAGntrGGIFGISRSKAKKFNTEtDVKVKFKDVAGCDEAKEEIMEFVSFLRN 288
Cdd:TIGR01241   1 SLLGFLFSLLPPILLLVGVWFFFRRQMQGGG---GRAFSFGKSKAKLLNEE-KPKVTFKDVAGIDEAKEELMEIVDFLKN 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961788553  289 PQRYEKMGAKIPRGAILSGPPGTGKTLLAKATAGEAGVPFYFVSGSEFVEMFVGVGAARVRDLFKTARENAPSIVFIDEI 368
Cdd:TIGR01241  77 PSKFTKLGAKIPKGVLLVGPPGTGKTLLAKAVAGEAGVPFFSISGSDFVEMFVGVGASRVRDLFEQAKKNAPCIIFIDEI 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961788553  369 DAIGKARQKGnFSGANDERENTLNQMLVEMDGFTSADHVVVLAGTNRPDILDNALLRPGRFDRRIHIDRPELEGRKAIFE 448
Cdd:TIGR01241 157 DAVGRQRGAG-LGGGNDEREQTLNQLLVEMDGFGTNTGVIVIAATNRPDVLDPALLRPGRFDRQVVVDLPDIKGREEILK 235
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961788553  449 VHLQKLKLAgSIFDLKnRLAALTPGFSGADIANVCNEAALIAARHDENAVKLSHFEQAIERVIGGVERKTRLLSPEEKQV 528
Cdd:TIGR01241 236 VHAKNKKLA-PDVDLK-AVARRTPGFSGADLANLLNEAALLAARKNKTEITMNDIEEAIDRVIAGPEKKSRVISEKEKKL 313
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961788553  529 VAYHEAGHAVCGWYLKYADPLLKVSIIPRGQgALGYAQYLP-GDVFLLSKQQLLDRMTMALGGRVSEELHFQWVTSGASD 607
Cdd:TIGR01241 314 VAYHEAGHALVGLLLKDADPVHKVTIIPRGQ-ALGYTQFLPeEDKYLYTKSQLLAQIAVLLGGRAAEEIIFGEVTTGASN 392
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961788553  608 DFKKVTNMATAMVTELGMSEKIGWINYKKNDDN-------DLTKAFSEETGVIIDSEVYRIVQECHKRCTDLLKEKAEDV 680
Cdd:TIGR01241 393 DIKQATNIARAMVTEWGMSDKLGPVAYGSDGGDvflgrgfAKAKEYSEETAREIDEEVKRIIEEAYKRAKQILTENRDEL 472
                         490       500
                  ....*....|....*....|...
gi 961788553  681 EKIAQLLLKKEVLTREDMINLLG 703
Cdd:TIGR01241 473 ELLAKALLEKETITREEIKELLA 495
FtsH_ext pfam06480
FtsH Extracellular; This domain is found in the FtsH family of proteins. FtsH is the only ...
116-201 1.08e-05

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: 44.90  E-value: 1.08e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961788553  116 VNDTEGQKEITWQDFRErYLAKGYVQRLEVVNKSYVKVVLNDMGKNQPENYGQEVVyFNLGSVENFEHKLEKAQNEMDID 195
Cdd:pfam06480  20 LSSSSSTKEISYSEFLE-YLEAGKVKKVVVQDDEILPTGVVEGTLKDGSKFTTYFI-PSLPNVDSLLEKLEDALEEKGVK 97

                  ....*.
gi 961788553  196 QDFRVP 201
Cdd:pfam06480  98 VSVKPP 103
 
Name Accession Description Interval E-value
FtsH_fam TIGR01241
ATP-dependent metalloprotease FtsH; HflB(FtsH) is a pleiotropic protein required for correct ...
209-703 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: 809.59  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961788553  209 NWARALFQMLPTVLMLVGIIWLTRKSMQSAGntrGGIFGISRSKAKKFNTEtDVKVKFKDVAGCDEAKEEIMEFVSFLRN 288
Cdd:TIGR01241   1 SLLGFLFSLLPPILLLVGVWFFFRRQMQGGG---GRAFSFGKSKAKLLNEE-KPKVTFKDVAGIDEAKEELMEIVDFLKN 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961788553  289 PQRYEKMGAKIPRGAILSGPPGTGKTLLAKATAGEAGVPFYFVSGSEFVEMFVGVGAARVRDLFKTARENAPSIVFIDEI 368
Cdd:TIGR01241  77 PSKFTKLGAKIPKGVLLVGPPGTGKTLLAKAVAGEAGVPFFSISGSDFVEMFVGVGASRVRDLFEQAKKNAPCIIFIDEI 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961788553  369 DAIGKARQKGnFSGANDERENTLNQMLVEMDGFTSADHVVVLAGTNRPDILDNALLRPGRFDRRIHIDRPELEGRKAIFE 448
Cdd:TIGR01241 157 DAVGRQRGAG-LGGGNDEREQTLNQLLVEMDGFGTNTGVIVIAATNRPDVLDPALLRPGRFDRQVVVDLPDIKGREEILK 235
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961788553  449 VHLQKLKLAgSIFDLKnRLAALTPGFSGADIANVCNEAALIAARHDENAVKLSHFEQAIERVIGGVERKTRLLSPEEKQV 528
Cdd:TIGR01241 236 VHAKNKKLA-PDVDLK-AVARRTPGFSGADLANLLNEAALLAARKNKTEITMNDIEEAIDRVIAGPEKKSRVISEKEKKL 313
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961788553  529 VAYHEAGHAVCGWYLKYADPLLKVSIIPRGQgALGYAQYLP-GDVFLLSKQQLLDRMTMALGGRVSEELHFQWVTSGASD 607
Cdd:TIGR01241 314 VAYHEAGHALVGLLLKDADPVHKVTIIPRGQ-ALGYTQFLPeEDKYLYTKSQLLAQIAVLLGGRAAEEIIFGEVTTGASN 392
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961788553  608 DFKKVTNMATAMVTELGMSEKIGWINYKKNDDN-------DLTKAFSEETGVIIDSEVYRIVQECHKRCTDLLKEKAEDV 680
Cdd:TIGR01241 393 DIKQATNIARAMVTEWGMSDKLGPVAYGSDGGDvflgrgfAKAKEYSEETAREIDEEVKRIIEEAYKRAKQILTENRDEL 472
                         490       500
                  ....*....|....*....|...
gi 961788553  681 EKIAQLLLKKEVLTREDMINLLG 703
Cdd:TIGR01241 473 ELLAKALLEKETITREEIKELLA 495
HflB COG0465
ATP-dependent Zn proteases [Posttranslational modification, protein turnover, chaperones];
117-704 0e+00

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


Pssm-ID: 440233 [Multi-domain]  Cd Length: 583  Bit Score: 808.49  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961788553 117 NDTEGQKEITWQDFRErYLAKGYVQRLEVVNkSYVKVVLNDmGKNQPenygqevVYFNLGSVENFEHKLEKAqnemDIDQ 196
Cdd:COG0465   14 SSSSSVKEISYSEFLQ-LVEAGKVKSVTIQG-DRITGTLKD-GTKTR-------FTTYRVNDPELVDLLEEK----GVEV 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961788553 197 DFRVPVQyvqQGNWARALFQMLPTVLMLVGIIWLTRKsMQSAGntrGGIFGISRSKAKKFnTETDVKVKFKDVAGCDEAK 276
Cdd:COG0465   80 TAKPPEE---SSWLLSLLISLLPILLLIGLWIFFMRR-MQGGG---GGAMSFGKSKAKLY-DEDKPKVTFDDVAGVDEAK 151
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961788553 277 EEIMEFVSFLRNPQRYEKMGAKIPRGAILSGPPGTGKTLLAKATAGEAGVPFYFVSGSEFVEMFVGVGAARVRDLFKTAR 356
Cdd:COG0465  152 EELQEIVDFLKDPEKFTRLGAKIPKGVLLVGPPGTGKTLLAKAVAGEAGVPFFSISGSDFVEMFVGVGASRVRDLFEQAK 231
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961788553 357 ENAPSIVFIDEIDAIGKARQKGNfSGANDERENTLNQMLVEMDGFTSADHVVVLAGTNRPDILDNALLRPGRFDRRIHID 436
Cdd:COG0465  232 KNAPCIIFIDEIDAVGRQRGAGL-GGGHDEREQTLNQLLVEMDGFEGNEGVIVIAATNRPDVLDPALLRPGRFDRQVVVD 310
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961788553 437 RPELEGRKAIFEVHLQKLKLAGSIfDLKnRLAALTPGFSGADIANVCNEAALIAARHDENAVKLSHFEQAIERVIGGVER 516
Cdd:COG0465  311 LPDVKGREAILKVHARKKPLAPDV-DLE-VIARRTPGFSGADLANLVNEAALLAARRNKKAVTMEDFEEAIDRVIAGPER 388
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961788553 517 KTRLLSPEEKQVVAYHEAGHAVCGWYLKYADPLLKVSIIPRGqGALGYAQYLP-GDVFLLSKQQLLDRMTMALGGRVSEE 595
Cdd:COG0465  389 KSRVISEKEKKITAYHEAGHALVAALLPGADPVHKVTIIPRG-RALGYTMQLPeEDRYLYTKEELLDRIAVLLGGRAAEE 467
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961788553 596 LHFQWVTSGASDDFKKVTNMATAMVTELGMSEKIGWINYKKNDDNDL-------TKAFSEETGVIIDSEVYRIVQECHKR 668
Cdd:COG0465  468 LVFGEVTTGASNDLERATKIARAMVTEYGMSEKLGPVAYGESEGEVFlgrdigqSRNYSEETAREIDEEVRRIIDEAYER 547
                        570       580       590
                 ....*....|....*....|....*....|....*.
gi 961788553 669 CTDLLKEKAEDVEKIAQLLLKKEVLTREDMINLLGK 704
Cdd:COG0465  548 AKEILTENRDKLDALAEALLEKETLDGEELEEILAG 583
ftsH CHL00176
cell division protein; Validated
133-694 1.33e-175

cell division protein; Validated


Pssm-ID: 214386 [Multi-domain]  Cd Length: 638  Bit Score: 517.30  E-value: 1.33e-175
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961788553 133 RYLAKGYVQRLEVVNKSYVKVVLNdmgkNQPENyGQEVVYFNLG-SVENFE--HKLEKAqnemDIDQDFRVPVQYVQQGN 209
Cdd:CHL00176  59 EYLDMGWIKKVDLYDNGRTAIVEA----SSPEL-GNRPQRIRVElPVGASEliQKLKEA----NIDFDAHPPVLKSNIVT 129
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961788553 210 WARALFqmLPtVLMLVGIIWLTRKSMQSAGNTRGGIFGISRSKAKkFNTETDVKVKFKDVAGCDEAKEEIMEFVSFLRNP 289
Cdd:CHL00176 130 ILSNLL--LP-LILIGVLWFFFQRSSNFKGGPGQNLMNFGKSKAR-FQMEADTGITFRDIAGIEEAKEEFEEVVSFLKKP 205
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961788553 290 QRYEKMGAKIPRGAILSGPPGTGKTLLAKATAGEAGVPFYFVSGSEFVEMFVGVGAARVRDLFKTARENAPSIVFIDEID 369
Cdd:CHL00176 206 ERFTAVGAKIPKGVLLVGPPGTGKTLLAKAIAGEAEVPFFSISGSEFVEMFVGVGAARVRDLFKKAKENSPCIVFIDEID 285
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961788553 370 AIGKARQKGnFSGANDERENTLNQMLVEMDGFTSADHVVVLAGTNRPDILDNALLRPGRFDRRIHIDRPELEGRKAIFEV 449
Cdd:CHL00176 286 AVGRQRGAG-IGGGNDEREQTLNQLLTEMDGFKGNKGVIVIAATNRVDILDAALLRPGRFDRQITVSLPDREGRLDILKV 364
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961788553 450 HLQKLKLAGSIfdLKNRLAALTPGFSGADIANVCNEAALIAARHDENAVKLSHFEQAIERVIGGVErKTRLLSPEEKQVV 529
Cdd:CHL00176 365 HARNKKLSPDV--SLELIARRTPGFSGADLANLLNEAAILTARRKKATITMKEIDTAIDRVIAGLE-GTPLEDSKNKRLI 441
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961788553 530 AYHEAGHAVCGWYLKYADPLLKVSIIPRGQgALGYAQYLPG-DVFLLSKQQLLDRMTMALGGRVSEELHFQ--WVTSGAS 606
Cdd:CHL00176 442 AYHEVGHAIVGTLLPNHDPVQKVTLIPRGQ-AKGLTWFTPEeDQSLVSRSQILARIVGALGGRAAEEVVFGstEVTTGAS 520
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961788553 607 DDFKKVTNMATAMVTELGMSeKIGWINYKKNDDNDL--------TKAFSEETGVIIDSEVYRIVQECHKRCTDLLKEKAE 678
Cdd:CHL00176 521 NDLQQVTNLARQMVTRFGMS-SIGPISLESNNSTDPflgrfmqrNSEYSEEIADKIDMEVRSILHTCYQYAYQILKDNRV 599
                        570
                 ....*....|....*.
gi 961788553 679 DVEKIAQLLLKKEVLT 694
Cdd:CHL00176 600 LIDLLVELLLQKETID 615
RecA-like_FtsH cd19501
ATP-dependent zinc metalloprotease FtsH; FtsH ATPase is a processive, ATP-dependent zinc ...
264-435 1.18e-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: 1.18e-114
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961788553 264 VKFKDVAGCDEAKEEIMEFVSFLRNPQRYEKMGAKIPRGAILSGPPGTGKTLLAKATAGEAGVPFYFVSGSEFVEMFVGV 343
Cdd:cd19501    1 VTFKDVAGCEEAKEELKEVVEFLKNPEKFTKLGAKIPKGVLLVGPPGTGKTLLAKAVAGEAGVPFFSISGSDFVEMFVGV 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961788553 344 GAARVRDLFKTARENAPSIVFIDEIDAIGKARQKGnFSGANDERENTLNQMLVEMDGFTSADHVVVLAGTNRPDILDNAL 423
Cdd:cd19501   81 GASRVRDLFEQAKKNAPCIVFIDEIDAVGRKRGAG-LGGGHDEREQTLNQLLVEMDGFESNTGVIVIAATNRPDVLDPAL 159
                        170
                 ....*....|..
gi 961788553 424 LRPGRFDRRIHI 435
Cdd:cd19501  160 LRPGRFDRQVYV 171
Peptidase_M41 pfam01434
Peptidase family M41;
519-701 1.39e-88

Peptidase family M41;


Pssm-ID: 460210 [Multi-domain]  Cd Length: 190  Bit Score: 276.02  E-value: 1.39e-88
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961788553  519 RLLSPEEKQVVAYHEAGHAVCGWYLKYADPLLKVSIIPRGQgALGYAQYLP-GDVFLLSKQQLLDRMTMALGGRVSEELH 597
Cdd:pfam01434   1 RVISEEEKKIVAYHEAGHALVGLLLPGADPVHKVTIIPRGQ-ALGYTQFLPeEDKLLYTKEQLLARIAVLLGGRAAEELI 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961788553  598 FQWVTSGASDDFKKVTNMATAMVTELGMSEKIGWINYKKNDDN-------DLTKAFSEETGVIIDSEVYRIVQECHKRCT 670
Cdd:pfam01434  80 FGEVTTGASNDLEKATKIARQMVTEFGMSDKLGPVSLEESDGNvflgrgmGKRKPYSEETADIIDEEVKRLLEEAYERAK 159
                         170       180       190
                  ....*....|....*....|....*....|.
gi 961788553  671 DLLKEKAEDVEKIAQLLLKKEVLTREDMINL 701
Cdd:pfam01434 160 EILTEHRDELEALAEALLEKETLDAEEIREL 190
AAA smart00382
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ...
300-439 9.49e-18

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: 80.50  E-value: 9.49e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961788553   300 PRGAILSGPPGTGKTLLAKATAGEA---GVPFYFVSGSEFVE--------------MFVGVGAARVRDLFKTARENAPSI 362
Cdd:smart00382   2 GEVILIVGPPGSGKTTLARALARELgppGGGVIYIDGEDILEevldqllliivggkKASGSGELRLRLALALARKLKPDV 81
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 961788553   363 VFIDEIDAIGKARQkgnfsgandERENTLNQMLVEMDGFTSADHVVVLAGTNRPDILDNALLRPgRFDRRIHIDRPE 439
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 ...
116-201 1.08e-05

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: 44.90  E-value: 1.08e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961788553  116 VNDTEGQKEITWQDFRErYLAKGYVQRLEVVNKSYVKVVLNDMGKNQPENYGQEVVyFNLGSVENFEHKLEKAQNEMDID 195
Cdd:pfam06480  20 LSSSSSTKEISYSEFLE-YLEAGKVKKVVVQDDEILPTGVVEGTLKDGSKFTTYFI-PSLPNVDSLLEKLEDALEEKGVK 97

                  ....*.
gi 961788553  196 QDFRVP 201
Cdd:pfam06480  98 VSVKPP 103
 
Name Accession Description Interval E-value
FtsH_fam TIGR01241
ATP-dependent metalloprotease FtsH; HflB(FtsH) is a pleiotropic protein required for correct ...
209-703 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: 809.59  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961788553  209 NWARALFQMLPTVLMLVGIIWLTRKSMQSAGntrGGIFGISRSKAKKFNTEtDVKVKFKDVAGCDEAKEEIMEFVSFLRN 288
Cdd:TIGR01241   1 SLLGFLFSLLPPILLLVGVWFFFRRQMQGGG---GRAFSFGKSKAKLLNEE-KPKVTFKDVAGIDEAKEELMEIVDFLKN 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961788553  289 PQRYEKMGAKIPRGAILSGPPGTGKTLLAKATAGEAGVPFYFVSGSEFVEMFVGVGAARVRDLFKTARENAPSIVFIDEI 368
Cdd:TIGR01241  77 PSKFTKLGAKIPKGVLLVGPPGTGKTLLAKAVAGEAGVPFFSISGSDFVEMFVGVGASRVRDLFEQAKKNAPCIIFIDEI 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961788553  369 DAIGKARQKGnFSGANDERENTLNQMLVEMDGFTSADHVVVLAGTNRPDILDNALLRPGRFDRRIHIDRPELEGRKAIFE 448
Cdd:TIGR01241 157 DAVGRQRGAG-LGGGNDEREQTLNQLLVEMDGFGTNTGVIVIAATNRPDVLDPALLRPGRFDRQVVVDLPDIKGREEILK 235
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961788553  449 VHLQKLKLAgSIFDLKnRLAALTPGFSGADIANVCNEAALIAARHDENAVKLSHFEQAIERVIGGVERKTRLLSPEEKQV 528
Cdd:TIGR01241 236 VHAKNKKLA-PDVDLK-AVARRTPGFSGADLANLLNEAALLAARKNKTEITMNDIEEAIDRVIAGPEKKSRVISEKEKKL 313
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961788553  529 VAYHEAGHAVCGWYLKYADPLLKVSIIPRGQgALGYAQYLP-GDVFLLSKQQLLDRMTMALGGRVSEELHFQWVTSGASD 607
Cdd:TIGR01241 314 VAYHEAGHALVGLLLKDADPVHKVTIIPRGQ-ALGYTQFLPeEDKYLYTKSQLLAQIAVLLGGRAAEEIIFGEVTTGASN 392
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961788553  608 DFKKVTNMATAMVTELGMSEKIGWINYKKNDDN-------DLTKAFSEETGVIIDSEVYRIVQECHKRCTDLLKEKAEDV 680
Cdd:TIGR01241 393 DIKQATNIARAMVTEWGMSDKLGPVAYGSDGGDvflgrgfAKAKEYSEETAREIDEEVKRIIEEAYKRAKQILTENRDEL 472
                         490       500
                  ....*....|....*....|...
gi 961788553  681 EKIAQLLLKKEVLTREDMINLLG 703
Cdd:TIGR01241 473 ELLAKALLEKETITREEIKELLA 495
HflB COG0465
ATP-dependent Zn proteases [Posttranslational modification, protein turnover, chaperones];
117-704 0e+00

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


Pssm-ID: 440233 [Multi-domain]  Cd Length: 583  Bit Score: 808.49  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961788553 117 NDTEGQKEITWQDFRErYLAKGYVQRLEVVNkSYVKVVLNDmGKNQPenygqevVYFNLGSVENFEHKLEKAqnemDIDQ 196
Cdd:COG0465   14 SSSSSVKEISYSEFLQ-LVEAGKVKSVTIQG-DRITGTLKD-GTKTR-------FTTYRVNDPELVDLLEEK----GVEV 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961788553 197 DFRVPVQyvqQGNWARALFQMLPTVLMLVGIIWLTRKsMQSAGntrGGIFGISRSKAKKFnTETDVKVKFKDVAGCDEAK 276
Cdd:COG0465   80 TAKPPEE---SSWLLSLLISLLPILLLIGLWIFFMRR-MQGGG---GGAMSFGKSKAKLY-DEDKPKVTFDDVAGVDEAK 151
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961788553 277 EEIMEFVSFLRNPQRYEKMGAKIPRGAILSGPPGTGKTLLAKATAGEAGVPFYFVSGSEFVEMFVGVGAARVRDLFKTAR 356
Cdd:COG0465  152 EELQEIVDFLKDPEKFTRLGAKIPKGVLLVGPPGTGKTLLAKAVAGEAGVPFFSISGSDFVEMFVGVGASRVRDLFEQAK 231
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961788553 357 ENAPSIVFIDEIDAIGKARQKGNfSGANDERENTLNQMLVEMDGFTSADHVVVLAGTNRPDILDNALLRPGRFDRRIHID 436
Cdd:COG0465  232 KNAPCIIFIDEIDAVGRQRGAGL-GGGHDEREQTLNQLLVEMDGFEGNEGVIVIAATNRPDVLDPALLRPGRFDRQVVVD 310
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961788553 437 RPELEGRKAIFEVHLQKLKLAGSIfDLKnRLAALTPGFSGADIANVCNEAALIAARHDENAVKLSHFEQAIERVIGGVER 516
Cdd:COG0465  311 LPDVKGREAILKVHARKKPLAPDV-DLE-VIARRTPGFSGADLANLVNEAALLAARRNKKAVTMEDFEEAIDRVIAGPER 388
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961788553 517 KTRLLSPEEKQVVAYHEAGHAVCGWYLKYADPLLKVSIIPRGqGALGYAQYLP-GDVFLLSKQQLLDRMTMALGGRVSEE 595
Cdd:COG0465  389 KSRVISEKEKKITAYHEAGHALVAALLPGADPVHKVTIIPRG-RALGYTMQLPeEDRYLYTKEELLDRIAVLLGGRAAEE 467
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961788553 596 LHFQWVTSGASDDFKKVTNMATAMVTELGMSEKIGWINYKKNDDNDL-------TKAFSEETGVIIDSEVYRIVQECHKR 668
Cdd:COG0465  468 LVFGEVTTGASNDLERATKIARAMVTEYGMSEKLGPVAYGESEGEVFlgrdigqSRNYSEETAREIDEEVRRIIDEAYER 547
                        570       580       590
                 ....*....|....*....|....*....|....*.
gi 961788553 669 CTDLLKEKAEDVEKIAQLLLKKEVLTREDMINLLGK 704
Cdd:COG0465  548 AKEILTENRDKLDALAEALLEKETLDGEELEEILAG 583
ftsH CHL00176
cell division protein; Validated
133-694 1.33e-175

cell division protein; Validated


Pssm-ID: 214386 [Multi-domain]  Cd Length: 638  Bit Score: 517.30  E-value: 1.33e-175
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961788553 133 RYLAKGYVQRLEVVNKSYVKVVLNdmgkNQPENyGQEVVYFNLG-SVENFE--HKLEKAqnemDIDQDFRVPVQYVQQGN 209
Cdd:CHL00176  59 EYLDMGWIKKVDLYDNGRTAIVEA----SSPEL-GNRPQRIRVElPVGASEliQKLKEA----NIDFDAHPPVLKSNIVT 129
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961788553 210 WARALFqmLPtVLMLVGIIWLTRKSMQSAGNTRGGIFGISRSKAKkFNTETDVKVKFKDVAGCDEAKEEIMEFVSFLRNP 289
Cdd:CHL00176 130 ILSNLL--LP-LILIGVLWFFFQRSSNFKGGPGQNLMNFGKSKAR-FQMEADTGITFRDIAGIEEAKEEFEEVVSFLKKP 205
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961788553 290 QRYEKMGAKIPRGAILSGPPGTGKTLLAKATAGEAGVPFYFVSGSEFVEMFVGVGAARVRDLFKTARENAPSIVFIDEID 369
Cdd:CHL00176 206 ERFTAVGAKIPKGVLLVGPPGTGKTLLAKAIAGEAEVPFFSISGSEFVEMFVGVGAARVRDLFKKAKENSPCIVFIDEID 285
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961788553 370 AIGKARQKGnFSGANDERENTLNQMLVEMDGFTSADHVVVLAGTNRPDILDNALLRPGRFDRRIHIDRPELEGRKAIFEV 449
Cdd:CHL00176 286 AVGRQRGAG-IGGGNDEREQTLNQLLTEMDGFKGNKGVIVIAATNRVDILDAALLRPGRFDRQITVSLPDREGRLDILKV 364
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961788553 450 HLQKLKLAGSIfdLKNRLAALTPGFSGADIANVCNEAALIAARHDENAVKLSHFEQAIERVIGGVErKTRLLSPEEKQVV 529
Cdd:CHL00176 365 HARNKKLSPDV--SLELIARRTPGFSGADLANLLNEAAILTARRKKATITMKEIDTAIDRVIAGLE-GTPLEDSKNKRLI 441
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961788553 530 AYHEAGHAVCGWYLKYADPLLKVSIIPRGQgALGYAQYLPG-DVFLLSKQQLLDRMTMALGGRVSEELHFQ--WVTSGAS 606
Cdd:CHL00176 442 AYHEVGHAIVGTLLPNHDPVQKVTLIPRGQ-AKGLTWFTPEeDQSLVSRSQILARIVGALGGRAAEEVVFGstEVTTGAS 520
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961788553 607 DDFKKVTNMATAMVTELGMSeKIGWINYKKNDDNDL--------TKAFSEETGVIIDSEVYRIVQECHKRCTDLLKEKAE 678
Cdd:CHL00176 521 NDLQQVTNLARQMVTRFGMS-SIGPISLESNNSTDPflgrfmqrNSEYSEEIADKIDMEVRSILHTCYQYAYQILKDNRV 599
                        570
                 ....*....|....*.
gi 961788553 679 DVEKIAQLLLKKEVLT 694
Cdd:CHL00176 600 LIDLLVELLLQKETID 615
hflB PRK10733
ATP-dependent zinc metalloprotease FtsH;
221-705 1.37e-154

ATP-dependent zinc metalloprotease FtsH;


Pssm-ID: 182683 [Multi-domain]  Cd Length: 644  Bit Score: 463.74  E-value: 1.37e-154
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961788553 221 VLMLVGIIWLTRKSMQSAGNTRGGIFGisRSKAKKFnTETDVKVKFKDVAGCDEAKEEIMEFVSFLRNPQRYEKMGAKIP 300
Cdd:PRK10733 109 MLLLIGVWIFFMRQMQGGGGKGAMSFG--KSKARML-TEDQIKTTFADVAGCDEAKEEVAELVEYLREPSRFQKLGGKIP 185
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961788553 301 RGAILSGPPGTGKTLLAKATAGEAGVPFYFVSGSEFVEMFVGVGAARVRDLFKTARENAPSIVFIDEIDAIGKARQKGnF 380
Cdd:PRK10733 186 KGVLMVGPPGTGKTLLAKAIAGEAKVPFFTISGSDFVEMFVGVGASRVRDMFEQAKKAAPCIIFIDEIDAVGRQRGAG-L 264
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961788553 381 SGANDERENTLNQMLVEMDGFTSADHVVVLAGTNRPDILDNALLRPGRFDRRIHIDRPELEGRKAIFEVHLQKLKLAGSI 460
Cdd:PRK10733 265 GGGHDEREQTLNQMLVEMDGFEGNEGIIVIAATNRPDVLDPALLRPGRFDRQVVVGLPDVRGREQILKVHMRRVPLAPDI 344
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961788553 461 FdlKNRLAALTPGFSGADIANVCNEAALIAARHDENAVKLSHFEQAIERVIGGVERKTRLLSPEEKQVVAYHEAGHAVCG 540
Cdd:PRK10733 345 D--AAIIARGTPGFSGADLANLVNEAALFAARGNKRVVSMVEFEKAKDKIMMGAERRSMVMTEAQKESTAYHEAGHAIIG 422
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961788553 541 WYLKYADPLLKVSIIPRGQgALGYAQYLP-GDVFLLSKQQLLDRMTMALGGRVSEELHF--QWVTSGASDDFKKVTNMAT 617
Cdd:PRK10733 423 RLVPEHDPVHKVTIIPRGR-ALGVTFFLPeGDAISASRQKLESQISTLYGGRLAEEIIYgpEHVSTGASNDIKVATNLAR 501
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961788553 618 AMVTELGMSEKIGWINYKKNDDNDL-------TKAFSEETGVIIDSEVYRIVQECHKRCTDLLKEKAEDVEKIAQLLLKK 690
Cdd:PRK10733 502 NMVTQWGFSEKLGPLLYAEEEGEVFlgrsvakAKHMSDETARIIDQEVKALIERNYNRARQLLTDNMDILHAMKDALMKY 581
                        490
                 ....*....|....*
gi 961788553 691 EVLTREDMINLLGKR 705
Cdd:PRK10733 582 ETIDAPQIDDLMARR 596
RecA-like_FtsH cd19501
ATP-dependent zinc metalloprotease FtsH; FtsH ATPase is a processive, ATP-dependent zinc ...
264-435 1.18e-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: 1.18e-114
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961788553 264 VKFKDVAGCDEAKEEIMEFVSFLRNPQRYEKMGAKIPRGAILSGPPGTGKTLLAKATAGEAGVPFYFVSGSEFVEMFVGV 343
Cdd:cd19501    1 VTFKDVAGCEEAKEELKEVVEFLKNPEKFTKLGAKIPKGVLLVGPPGTGKTLLAKAVAGEAGVPFFSISGSDFVEMFVGV 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961788553 344 GAARVRDLFKTARENAPSIVFIDEIDAIGKARQKGnFSGANDERENTLNQMLVEMDGFTSADHVVVLAGTNRPDILDNAL 423
Cdd:cd19501   81 GASRVRDLFEQAKKNAPCIVFIDEIDAVGRKRGAG-LGGGHDEREQTLNQLLVEMDGFESNTGVIVIAATNRPDVLDPAL 159
                        170
                 ....*....|..
gi 961788553 424 LRPGRFDRRIHI 435
Cdd:cd19501  160 LRPGRFDRQVYV 171
RPT1 COG1222
ATP-dependent 26S proteasome regulatory subunit [Posttranslational modification, protein ...
264-519 2.57e-108

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


Pssm-ID: 440835 [Multi-domain]  Cd Length: 326  Bit Score: 332.74  E-value: 2.57e-108
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961788553 264 VKFKDVAGCDEAKEEIMEFVS-FLRNPQRYEKMGAKIPRGAILSGPPGTGKTLLAKATAGEAGVPFYFVSGSEFVEMFVG 342
Cdd:COG1222   75 VTFDDIGGLDEQIEEIREAVElPLKNPELFRKYGIEPPKGVLLYGPPGTGKTLLAKAVAGELGAPFIRVRGSELVSKYIG 154
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961788553 343 VGAARVRDLFKTARENAPSIVFIDEIDAIGKARQKGNFSGANDereNTLNQMLVEMDGFTSADHVVVLAGTNRPDILDNA 422
Cdd:COG1222  155 EGARNVREVFELAREKAPSIIFIDEIDAIAARRTDDGTSGEVQ---RTVNQLLAELDGFESRGDVLIIAATNRPDLLDPA 231
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961788553 423 LLRPGRFDRRIHIDRPELEGRKAIFEVHLQKLKLAGSIfDLKnRLAALTPGFSGADIANVCNEAALIAARHDENAVKLSH 502
Cdd:COG1222  232 LLRPGRFDRVIEVPLPDEEAREEILKIHLRDMPLADDV-DLD-KLAKLTEGFSGADLKAIVTEAGMFAIREGRDTVTMED 309
                        250
                 ....*....|....*..
gi 961788553 503 FEQAIERVIGGVERKTR 519
Cdd:COG1222  310 LEKAIEKVKKKTETATN 326
PRK03992 PRK03992
proteasome-activating nucleotidase; Provisional
263-517 5.78e-91

proteasome-activating nucleotidase; Provisional


Pssm-ID: 179699 [Multi-domain]  Cd Length: 389  Bit Score: 289.81  E-value: 5.78e-91
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961788553 263 KVKFKDVAGCDEAKEEIMEFVSF-LRNPQRYEKMGAKIPRGAILSGPPGTGKTLLAKATAGEAGVPFYFVSGSEFVEMFV 341
Cdd:PRK03992 127 NVTYEDIGGLEEQIREVREAVELpLKKPELFEEVGIEPPKGVLLYGPPGTGKTLLAKAVAHETNATFIRVVGSELVQKFI 206
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961788553 342 GVGAARVRDLFKTARENAPSIVFIDEIDAIGKARQKGNFSGandERE--NTLNQMLVEMDGFTSADHVVVLAGTNRPDIL 419
Cdd:PRK03992 207 GEGARLVRELFELAREKAPSIIFIDEIDAIAAKRTDSGTSG---DREvqRTLMQLLAEMDGFDPRGNVKIIAATNRIDIL 283
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961788553 420 DNALLRPGRFDRRIHIDRPELEGRKAIFEVHLQKLKLAGSIfDLKnRLAALTPGFSGADIANVCNEAALIAARHDENAVK 499
Cdd:PRK03992 284 DPAILRPGRFDRIIEVPLPDEEGRLEILKIHTRKMNLADDV-DLE-ELAELTEGASGADLKAICTEAGMFAIRDDRTEVT 361
                        250
                 ....*....|....*...
gi 961788553 500 LSHFEQAIERVIGGVERK 517
Cdd:PRK03992 362 MEDFLKAIEKVMGKEEKD 379
Peptidase_M41 pfam01434
Peptidase family M41;
519-701 1.39e-88

Peptidase family M41;


Pssm-ID: 460210 [Multi-domain]  Cd Length: 190  Bit Score: 276.02  E-value: 1.39e-88
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961788553  519 RLLSPEEKQVVAYHEAGHAVCGWYLKYADPLLKVSIIPRGQgALGYAQYLP-GDVFLLSKQQLLDRMTMALGGRVSEELH 597
Cdd:pfam01434   1 RVISEEEKKIVAYHEAGHALVGLLLPGADPVHKVTIIPRGQ-ALGYTQFLPeEDKLLYTKEQLLARIAVLLGGRAAEELI 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961788553  598 FQWVTSGASDDFKKVTNMATAMVTELGMSEKIGWINYKKNDDN-------DLTKAFSEETGVIIDSEVYRIVQECHKRCT 670
Cdd:pfam01434  80 FGEVTTGASNDLEKATKIARQMVTEFGMSDKLGPVSLEESDGNvflgrgmGKRKPYSEETADIIDEEVKRLLEEAYERAK 159
                         170       180       190
                  ....*....|....*....|....*....|.
gi 961788553  671 DLLKEKAEDVEKIAQLLLKKEVLTREDMINL 701
Cdd:pfam01434 160 EILTEHRDELEALAEALLEKETLDAEEIREL 190
SpoVK COG0464
AAA+-type ATPase, SpoVK/Ycf46/Vps4 family [Cell wall/membrane/envelope biogenesis, Cell cycle ...
266-510 5.16e-79

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: 258.69  E-value: 5.16e-79
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961788553 266 FKDVAGCDEAKEEIMEFVS-FLRNPQRYEKMGAKIPRGAILSGPPGTGKTLLAKATAGEAGVPFYFVSGSEFVEMFVGVG 344
Cdd:COG0464  156 LDDLGGLEEVKEELRELVAlPLKRPELREEYGLPPPRGLLLYGPPGTGKTLLARALAGELGLPLIEVDLSDLVSKYVGET 235
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961788553 345 AARVRDLFKTARENAPSIVFIDEIDAIGKARqkgnfSGANDERENT-LNQMLVEMDGFTsaDHVVVLAGTNRPDILDNAL 423
Cdd:COG0464  236 EKNLREVFDKARGLAPCVLFIDEADALAGKR-----GEVGDGVGRRvVNTLLTEMEELR--SDVVVIAATNRPDLLDPAL 308
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961788553 424 LRpgRFDRRIHIDRPELEGRKAIFEVHLQKLKLAGSiFDLkNRLAALTPGFSGADIANVCNEAALIAARHDENAVKLSHF 503
Cdd:COG0464  309 LR--RFDEIIFFPLPDAEERLEIFRIHLRKRPLDED-VDL-EELAEATEGLSGADIRNVVRRAALQALRLGREPVTTEDL 384

                 ....*..
gi 961788553 504 EQAIERV 510
Cdd:COG0464  385 LEALERE 391
26Sp45 TIGR01242
26S proteasome subunit P45 family; Many proteins may score above the trusted cutoff because an ...
253-511 1.69e-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: 256.26  E-value: 1.69e-78
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961788553  253 AKKFNTETDVKVKFKDVAGCDEAKEEIMEFVSF-LRNPQRYEKMGAKIPRGAILSGPPGTGKTLLAKATAGEAGVPFYFV 331
Cdd:TIGR01242 108 VKGMEVEERPNVSYEDIGGLEEQIREIREAVELpLKHPELFEEVGIEPPKGVLLYGPPGTGKTLLAKAVAHETNATFIRV 187
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961788553  332 SGSEFVEMFVGVGAARVRDLFKTARENAPSIVFIDEIDAIGKARQKGNFSGaNDERENTLNQMLVEMDGFTSADHVVVLA 411
Cdd:TIGR01242 188 VGSELVRKYIGEGARLVREIFELAKEKAPSIIFIDEIDAIAAKRTDSGTSG-DREVQRTLMQLLAELDGFDPRGNVKVIA 266
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961788553  412 GTNRPDILDNALLRPGRFDRRIHIDRPELEGRKAIFEVHLQKLKLAGSIfDLKnRLAALTPGFSGADIANVCNEAALIAA 491
Cdd:TIGR01242 267 ATNRPDILDPALLRPGRFDRIIEVPLPDFEGRLEILKIHTRKMKLAEDV-DLE-AIAKMTEGASGADLKAICTEAGMFAI 344
                         250       260
                  ....*....|....*....|
gi 961788553  492 RHDENAVKLSHFEQAIERVI 511
Cdd:TIGR01242 345 REERDYVTMDDFIKAVEKVL 364
RecA-like_PAN_like cd19502
proteasome activating nucleotidase PAN and related proteasome subunits; This subfamily ...
266-435 2.98e-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: 213.74  E-value: 2.98e-65
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961788553 266 FKDVAGCDEAKEEIMEFVSF-LRNPQRYEKMGAKIPRGAILSGPPGTGKTLLAKATAGEAGVPFYFVSGSEFVEMFVGVG 344
Cdd:cd19502    2 YEDIGGLDEQIREIREVVELpLKHPELFEELGIEPPKGVLLYGPPGTGKTLLAKAVANHTDATFIRVVGSELVQKYIGEG 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961788553 345 AARVRDLFKTARENAPSIVFIDEIDAIGKARQKGNfSGANDERENTLNQMLVEMDGFTSADHVVVLAGTNRPDILDNALL 424
Cdd:cd19502   82 ARLVRELFEMAREKAPSIIFIDEIDAIGAKRFDSG-TGGDREVQRTMLELLNQLDGFDPRGNIKVIMATNRPDILDPALL 160
                        170
                 ....*....|.
gi 961788553 425 RPGRFDRRIHI 435
Cdd:cd19502  161 RPGRFDRKIEF 171
CDC48 TIGR01243
AAA family ATPase, CDC48 subfamily; This subfamily of the AAA family ATPases includes two ...
264-510 4.74e-65

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: 229.79  E-value: 4.74e-65
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961788553  264 VKFKDVAGCDEAKEEIMEFVSF-LRNPQRYEKMGAKIPRGAILSGPPGTGKTLLAKATAGEAGVPFYFVSGSEFVEMFVG 342
Cdd:TIGR01243 450 VRWSDIGGLEEVKQELREAVEWpLKHPEIFEKMGIRPPKGVLLFGPPGTGKTLLAKAVATESGANFIAVRGPEILSKWVG 529
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961788553  343 VGAARVRDLFKTARENAPSIVFIDEIDAIGKARQKGNFSGANDErenTLNQMLVEMDGFTSADHVVVLAGTNRPDILDNA 422
Cdd:TIGR01243 530 ESEKAIREIFRKARQAAPAIIFFDEIDAIAPARGARFDTSVTDR---IVNQLLTEMDGIQELSNVVVIAATNRPDILDPA 606
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961788553  423 LLRPGRFDRRIHIDRPELEGRKAIFEVHLQKLKLAGSIfDLKnRLAALTPGFSGADIANVCNEAALIAARH--------- 493
Cdd:TIGR01243 607 LLRPGRFDRLILVPPPDEEARKEIFKIHTRSMPLAEDV-DLE-ELAEMTEGYTGADIEAVCREAAMAALREsigspakek 684
                         250       260
                  ....*....|....*....|....*.
gi 961788553  494 ---------DENAVKLSHFEQAIERV 510
Cdd:TIGR01243 685 levgeeeflKDLKVEMRHFLEALKKV 710
COG1223 COG1223
Predicted ATPase, AAA+ superfamily [General function prediction only];
266-527 4.25e-63

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


Pssm-ID: 440836 [Multi-domain]  Cd Length: 246  Bit Score: 210.90  E-value: 4.25e-63
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961788553 266 FKDVAGCDEAKEEIMEFVSFLRNPQRYEKMGAKIPRGAILSGPPGTGKTLLAKATAGEAGVPFYFVSGSEFVEMFVGVGA 345
Cdd:COG1223    1 LDDVVGQEEAKKKLKLIIKELRRRENLRKFGLWPPRKILFYGPPGTGKTMLAEALAGELKLPLLTVRLDSLIGSYLGETA 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961788553 346 ARVRDLFKTAREnAPSIVFIDEIDAIGKARQKGNFSGandERENTLNQMLVEMDGFTSadHVVVLAGTNRPDILDNALLR 425
Cdd:COG1223   81 RNLRKLFDFARR-APCVIFFDEFDAIAKDRGDQNDVG---EVKRVVNALLQELDGLPS--GSVVIAATNHPELLDSALWR 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961788553 426 pgRFDRRIHIDRPELEGRKAIFEVHLQKLKLAGSiFDLKnRLAALTPGFSGADIANVCNEAALIAARHDENAVKLSHFEQ 505
Cdd:COG1223  155 --RFDEVIEFPLPDKEERKEILELNLKKFPLPFE-LDLK-KLAKKLEGLSGADIEKVLKTALKKAILEDREKVTKEDLEE 230
                        250       260
                 ....*....|....*....|..
gi 961788553 506 AIErviggvERKTRLLSPEEKQ 527
Cdd:COG1223  231 ALK------QRKERKKEPKKEG 246
PTZ00454 PTZ00454
26S protease regulatory subunit 6B-like protein; Provisional
264-516 7.57e-62

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


Pssm-ID: 240423 [Multi-domain]  Cd Length: 398  Bit Score: 212.70  E-value: 7.57e-62
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961788553 264 VKFKDVAGCDEAKEEIMEFVSF-LRNPQRYEKMGAKIPRGAILSGPPGTGKTLLAKATAGEAGVPFYFVSGSEFVEMFVG 342
Cdd:PTZ00454 142 VTYSDIGGLDIQKQEIREAVELpLTCPELYEQIGIDPPRGVLLYGPPGTGKTMLAKAVAHHTTATFIRVVGSEFVQKYLG 221
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961788553 343 VGAARVRDLFKTARENAPSIVFIDEIDAIGKARQKGNfSGANDERENTLNQMLVEMDGFTSADHVVVLAGTNRPDILDNA 422
Cdd:PTZ00454 222 EGPRMVRDVFRLARENAPSIIFIDEVDSIATKRFDAQ-TGADREVQRILLELLNQMDGFDQTTNVKVIMATNRADTLDPA 300
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961788553 423 LLRPGRFDRRIHIDRPELEGRKAIFEVHLQKLKLAGSIfDLKNrLAALTPGFSGADIANVCNEAALIAARHDENAVKLSH 502
Cdd:PTZ00454 301 LLRPGRLDRKIEFPLPDRRQKRLIFQTITSKMNLSEEV-DLED-FVSRPEKISAADIAAICQEAGMQAVRKNRYVILPKD 378
                        250
                 ....*....|....
gi 961788553 503 FEQAIERVIGGVER 516
Cdd:PTZ00454 379 FEKGYKTVVRKTDR 392
PTZ00361 PTZ00361
26 proteosome regulatory subunit 4-like protein; Provisional
248-511 3.67e-60

26 proteosome regulatory subunit 4-like protein; Provisional


Pssm-ID: 185575 [Multi-domain]  Cd Length: 438  Bit Score: 209.24  E-value: 3.67e-60
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961788553 248 ISRSKAKKFNTETdvkvkFKDVAGCDEAKEEIMEFVSF-LRNPQRYEKMGAKIPRGAILSGPPGTGKTLLAKATAGEAGV 326
Cdd:PTZ00361 169 VSVMKVDKAPLES-----YADIGGLEQQIQEIKEAVELpLTHPELYDDIGIKPPKGVILYGPPGTGKTLLAKAVANETSA 243
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961788553 327 PFYFVSGSEFVEMFVGVGAARVRDLFKTARENAPSIVFIDEIDAIGKARQKGNfSGANDERENTLNQMLVEMDGFTSADH 406
Cdd:PTZ00361 244 TFLRVVGSELIQKYLGDGPKLVRELFRVAEENAPSIVFIDEIDAIGTKRYDAT-SGGEKEIQRTMLELLNQLDGFDSRGD 322
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961788553 407 VVVLAGTNRPDILDNALLRPGRFDRRIHIDRPELEGRKAIFEVHLQKLKLAGSIfDLKNRLAAlTPGFSGADIANVCNEA 486
Cdd:PTZ00361 323 VKVIMATNRIESLDPALIRPGRIDRKIEFPNPDEKTKRRIFEIHTSKMTLAEDV-DLEEFIMA-KDELSGADIKAICTEA 400
                        250       260
                 ....*....|....*....|....*
gi 961788553 487 ALIAARHDENAVKLSHFEQAIERVI 511
Cdd:PTZ00361 401 GLLALRERRMKVTQADFRKAKEKVL 425
RecA-like_protease cd19481
proteases similar to RecA; RecA-like NTPases. This family includes the NTP binding domain of ...
275-435 2.61e-59

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: 197.51  E-value: 2.61e-59
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961788553 275 AKEEIMEFVSFLRNPQRYEKMGAKIPRGAILSGPPGTGKTLLAKATAGEAGVPFYFVSGSEFVEMFVGVGAARVRDLFKT 354
Cdd:cd19481    1 LKASLREAVEAPRRGSRLRRYGLGLPKGILLYGPPGTGKTLLAKALAGELGLPLIVVKLSSLLSKYVGESEKNLRKIFER 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961788553 355 ARENAPSIVFIDEIDAIGKARQKgnfSGANDERENTLNQMLVEMDGFTSADHVVVLAGTNRPDILDNALLRPGRFDRRIH 434
Cdd:cd19481   81 ARRLAPCILFIDEIDAIGRKRDS---SGESGELRRVLNQLLTELDGVNSRSKVLVIAATNRPDLLDPALLRPGRFDEVIE 157

                 .
gi 961788553 435 I 435
Cdd:cd19481  158 F 158
RecA-like_CDC48_r2-like cd19511
second of two ATPase domains of CDC48/p97, PEX1 and -6, VAT and NVL, and similar ATPase ...
275-435 1.71e-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: 195.19  E-value: 1.71e-58
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961788553 275 AKEEIMEFVSF-LRNPQRYEKMGAKIPRGAILSGPPGTGKTLLAKATAGEAGVPFYFVSGSEFVEMFVGVGAARVRDLFK 353
Cdd:cd19511    1 VKRELKEAVEWpLKHPDAFKRLGIRPPKGVLLYGPPGCGKTLLAKALASEAGLNFISVKGPELFSKYVGESERAVREIFQ 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961788553 354 TARENAPSIVFIDEIDAIGKARQKGNFSGANDErenTLNQMLVEMDGFTSADHVVVLAGTNRPDILDNALLRPGRFDRRI 433
Cdd:cd19511   81 KARQAAPCIIFFDEIDSLAPRRGQSDSSGVTDR---VVSQLLTELDGIESLKGVVVIAATNRPDMIDPALLRPGRLDKLI 157

                 ..
gi 961788553 434 HI 435
Cdd:cd19511  158 YV 159
CDC48 TIGR01243
AAA family ATPase, CDC48 subfamily; This subfamily of the AAA family ATPases includes two ...
250-492 2.18e-58

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


Pssm-ID: 273521 [Multi-domain]  Cd Length: 733  Bit Score: 211.30  E-value: 2.18e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961788553  250 RSKAKKFNTETDV-KVKFKDVAGCDEAKEEIMEFVSF-LRNPQRYEKMGAKIPRGAILSGPPGTGKTLLAKATAGEAGVP 327
Cdd:TIGR01243 160 REKPVREEIERKVpKVTYEDIGGLKEAKEKIREMVELpMKHPELFEHLGIEPPKGVLLYGPPGTGKTLLAKAVANEAGAY 239
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961788553  328 FYFVSGSEFVEMFVGVGAARVRDLFKTARENAPSIVFIDEIDAIGKARQKgnFSGANDERenTLNQMLVEMDGFTSADHV 407
Cdd:TIGR01243 240 FISINGPEIMSKYYGESEERLREIFKEAEENAPSIIFIDEIDAIAPKREE--VTGEVEKR--VVAQLLTLMDGLKGRGRV 315
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961788553  408 VVLAGTNRPDILDNALLRPGRFDRRIHIDRPELEGRKAIFEVHLQKLKLAGSIfDLkNRLAALTPGFSGADIANVCNEAA 487
Cdd:TIGR01243 316 IVIGATNRPDALDPALRRPGRFDREIVIRVPDKRARKEILKVHTRNMPLAEDV-DL-DKLAEVTHGFVGADLAALAKEAA 393

                  ....*
gi 961788553  488 LIAAR 492
Cdd:TIGR01243 394 MAALR 398
RecA-like_CDC48_NLV2_r1-like cd19503
first of two ATPase domains of CDC48 and NLV2, and similar ATPase domains; CDC48 in yeast and ...
268-435 4.91e-55

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: 186.34  E-value: 4.91e-55
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961788553 268 DVAGCDEAKEEIMEFVSF-LRNPQRYEKMGAKIPRGAILSGPPGTGKTLLAKATAGEAGVPFYFVSGSEFVEMFVGVGAA 346
Cdd:cd19503    1 DIGGLDEQIASLKELIELpLKYPELFRALGLKPPRGVLLHGPPGTGKTLLARAVANEAGANFLSISGPSIVSKYLGESEK 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961788553 347 RVRDLFKTARENAPSIVFIDEIDAIGKARQKGnfSGANDERenTLNQMLVEMDGFTSADHVVVLAGTNRPDILDNALLRP 426
Cdd:cd19503   81 NLREIFEEARSHAPSIIFIDEIDALAPKREED--QREVERR--VVAQLLTLMDGMSSRGKVVVIAATNRPDAIDPALRRP 156

                 ....*....
gi 961788553 427 GRFDRRIHI 435
Cdd:cd19503  157 GRFDREVEI 165
AAA pfam00004
ATPase family associated with various cellular activities (AAA); AAA family proteins often ...
304-437 1.09e-51

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: 175.86  E-value: 1.09e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961788553  304 ILSGPPGTGKTLLAKATAGEAGVPFYFVSGSEFVEMFVGVGAARVRDLFKTARENAPSIVFIDEIDAIGKARqkgnFSGA 383
Cdd:pfam00004   2 LLYGPPGTGKTTLAKAVAKELGAPFIEISGSELVSKYVGESEKRLRELFEAAKKLAPCVIFIDEIDALAGSR----GSGG 77
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 961788553  384 NDERENTLNQMLVEMDGFTSADH-VVVLAGTNRPDILDNALLrpGRFDRRIHIDR 437
Cdd:pfam00004  78 DSESRRVVNQLLTELDGFTSSNSkVIVIAATNRPDKLDPALL--GRFDRIIEFPL 130
RecA-like_VCP_r2 cd19529
second of two ATPase domains of Valosin-containing protein-like ATPase (VAT) and similar ...
275-435 2.38e-50

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


Pssm-ID: 410937 [Multi-domain]  Cd Length: 159  Bit Score: 173.07  E-value: 2.38e-50
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961788553 275 AKEEIMEFVSF-LRNPQRYEKMGAKIPRGAILSGPPGTGKTLLAKATAGEAGVPFYFVSGSEFVEMFVGVGAARVRDLFK 353
Cdd:cd19529    1 VKQELKEAVEWpLLKPEVFKRLGIRPPKGILLYGPPGTGKTLLAKAVATESNANFISVKGPELLSKWVGESEKAIREIFR 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961788553 354 TARENAPSIVFIDEIDAIGKARQKGNFSGANderENTLNQMLVEMDGFTSADHVVVLAGTNRPDILDNALLRPGRFDRRI 433
Cdd:cd19529   81 KARQVAPCVIFFDEIDSIAPRRGTTGDSGVT---ERVVNQLLTELDGLEEMNGVVVIAATNRPDIIDPALLRAGRFDRLI 157

                 ..
gi 961788553 434 HI 435
Cdd:cd19529  158 YI 159
RecA-like_CDC48_r2-like cd19528
second of two ATPase domains of CDC48 and similar ATPase domains; CDC48 in yeast and p97 or ...
276-435 7.48e-50

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: 171.92  E-value: 7.48e-50
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961788553 276 KEEIMEFVSF-LRNPQRYEKMGAKIPRGAILSGPPGTGKTLLAKATAGEAGVPFYFVSGSEFVEMFVGVGAARVRDLFKT 354
Cdd:cd19528    2 KRELQELVQYpVEHPDKFLKFGMTPSKGVLFYGPPGCGKTLLAKAIANECQANFISVKGPELLTMWFGESEANVRDIFDK 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961788553 355 ARENAPSIVFIDEIDAIGKARqKGNFSGANDERENTLNQMLVEMDGFTSADHVVVLAGTNRPDILDNALLRPGRFDRRIH 434
Cdd:cd19528   82 ARAAAPCVLFFDELDSIAKAR-GGNIGDAGGAADRVINQILTEMDGMNTKKNVFIIGATNRPDIIDPAILRPGRLDQLIY 160

                 .
gi 961788553 435 I 435
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 ...
268-435 1.24e-49

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: 171.47  E-value: 1.24e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961788553 268 DVAGCDEAKEEIMEFVSF-LRNPQRYEKMGAKIPRGAILSGPPGTGKTLLAKATAGEAGVPFYFVSGSEFVEMFVGVGAA 346
Cdd:cd19519    1 DIGGCRKQLAQIREMVELpLRHPELFKAIGIKPPRGILLYGPPGTGKTLIARAVANETGAFFFLINGPEIMSKLAGESES 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961788553 347 RVRDLFKTARENAPSIVFIDEIDAIGKARQKgnfsgANDERENTL-NQMLVEMDGFTSADHVVVLAGTNRPDILDNALLR 425
Cdd:cd19519   81 NLRKAFEEAEKNAPAIIFIDEIDAIAPKREK-----THGEVERRIvSQLLTLMDGLKQRAHVIVMAATNRPNSIDPALRR 155
                        170
                 ....*....|
gi 961788553 426 PGRFDRRIHI 435
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 ...
268-433 3.48e-47

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: 164.89  E-value: 3.48e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961788553 268 DVAGCDEAKEEIMEFVSFL-RNPQRYEKMGAKIPRGAILSGPPGTGKTLLAKATAGEAGVPFYFVSGSEFVEMFVGVGAA 346
Cdd:cd19518    1 DIGGMDSTLKELCELLIHPiLPPEYFQHLGVEPPRGVLLHGPPGCGKTMLANAIAGELKVPFLKISATEIVSGVSGESEE 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961788553 347 RVRDLFKTARENAPSIVFIDEIDAIGKARQkgnfsGANDERENTL-NQMLVEMDGF----TSADHVVVLAGTNRPDILDN 421
Cdd:cd19518   81 KIRELFDQAISNAPCIVFIDEIDAITPKRE-----SAQREMERRIvSQLLTCMDELnnekTAGGPVLVIGATNRPDSLDP 155
                        170
                 ....*....|..
gi 961788553 422 ALLRPGRFDRRI 433
Cdd:cd19518  156 ALRRAGRFDREI 167
RecA-like_NVL_r2-like cd19530
second of two ATPase domains of NVL (nuclear VCP-like protein) and similar ATPase domains; NVL ...
273-435 2.62e-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: 151.10  E-value: 2.62e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961788553 273 DEAKEEI-MEFVSFLRNPQRYEKMGAKIPRGAILSGPPGTGKTLLAKATAGEAGVPFYFVSGSEFVEMFVGVGAARVRDL 351
Cdd:cd19530    2 DHVREELtMSILRPIKRPDIYKALGIDLPTGVLLYGPPGCGKTLLAKAVANESGANFISVKGPELLNKYVGESERAVRQV 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961788553 352 FKTARENAPSIVFIDEIDAIGKARQKGNFSGAnderENTLNQMLVEMDGFTSADHVVVLAGTNRPDILDNALLRPGRFDR 431
Cdd:cd19530   82 FQRARASAPCVIFFDEVDALVPKRGDGGSWAS----ERVVNQLLTEMDGLEERSNVFVIAATNRPDIIDPAMLRPGRLDK 157

                 ....
gi 961788553 432 RIHI 435
Cdd:cd19530  158 TLYV 161
RecA-like_VPS4-like cd19509
ATPase domain of VPS4, ATAD1, K, KTNA1, Spastin, FIGL-1 and similar ATPase domains; This ...
269-435 1.29e-38

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: 140.57  E-value: 1.29e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961788553 269 VAGCDEAKEEIMEFVSF-LRNPQRYeKMGAKIPRGAILSGPPGTGKTLLAKATAGEAGVPFYFVSGSEFVEMFVGVGAAR 347
Cdd:cd19509    1 IAGLDDAKEALKEAVILpSLRPDLF-PGLRGPPRGILLYGPPGTGKTLLARAVASESGSTFFSISASSLVSKWVGESEKI 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961788553 348 VRDLFKTARENAPSIVFIDEIDAIGKARQKGNFSGANDERentlNQMLVEMDGFTSA--DHVVVLAGTNRPDILDNALLR 425
Cdd:cd19509   80 VRALFALARELQPSIIFIDEIDSLLSERGSGEHEASRRVK----TEFLVQMDGVLNKpeDRVLVLGATNRPWELDEAFLR 155
                        170
                 ....*....|
gi 961788553 426 pgRFDRRIHI 435
Cdd:cd19509  156 --RFEKRIYI 163
RecA-like_PEX6_r2 cd19527
second of two ATPase domains of Peroxisomal biogenesis factor 6 (PEX6); PEX6(also known as ...
276-435 2.22e-38

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: 139.96  E-value: 2.22e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961788553 276 KEEIMEFVSF-LRNPQRYEKmGAKIPRGAILSGPPGTGKTLLAKATAGEAGVPFYFVSGSEFVEMFVGVGAARVRDLFKT 354
Cdd:cd19527    2 KKEILDTIQLpLEHPELFSS-GLRKRSGILLYGPPGTGKTLLAKAIATECSLNFLSVKGPELINMYIGESEANVREVFQK 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961788553 355 ARENAPSIVFIDEIDAIGKARQKGNFSGANDERenTLNQMLVEMDGF-TSADHVVVLAGTNRPDILDNALLRPGRFDRRI 433
Cdd:cd19527   81 ARDAKPCVIFFDELDSLAPSRGNSGDSGGVMDR--VVSQLLAELDGMsSSGQDVFVIGATNRPDLLDPALLRPGRFDKLL 158

                 ..
gi 961788553 434 HI 435
Cdd:cd19527  159 YL 160
RecA-like_PEX1_r2 cd19526
second of two ATPase domains of Peroxisomal biogenesis factor 1 (PEX1); PEX1(also known as ...
274-433 6.16e-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: 138.72  E-value: 6.16e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961788553 274 EAKEEIMEFVSflRNPQRYEKMGAKIPRGAILSGPPGTGKTLLAKATAGEAGVPFYFVSGSEFVEMFVGVGAARVRDLFK 353
Cdd:cd19526    3 KALEETIEWPS--KYPKIFASSPLRLRSGILLYGPPGCGKTLLASAIASECGLNFISVKGPELLNKYIGASEQNVRDLFS 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961788553 354 TARENAPSIVFIDEIDAIGKARQKGNfSGANDErenTLNQMLVEMDGFTSADHVVVLAGTNRPDILDNALLRPGRFDRRI 433
Cdd:cd19526   81 RAQSAKPCILFFDEFDSIAPKRGHDS-TGVTDR---VVNQLLTQLDGVEGLDGVYVLAATSRPDLIDPALLRPGRLDKLV 156
RecA-like_VPS4 cd19521
ATPase domain of vacuolar protein sorting-associated protein 4; Vacuolar protein ...
263-435 9.66e-37

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


Pssm-ID: 410929 [Multi-domain]  Cd Length: 170  Bit Score: 135.76  E-value: 9.66e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961788553 263 KVKFKDVAGCDEAKEEIMEFVSF-LRNPQRYEkmGAKIP-RGAILSGPPGTGKTLLAKATAGEAGVPFYFVSGSEFVEMF 340
Cdd:cd19521    3 NVKWEDVAGLEGAKEALKEAVILpVKFPHLFT--GNRKPwSGILLYGPPGTGKSYLAKAVATEANSTFFSVSSSDLVSKW 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961788553 341 VGVGAARVRDLFKTARENAPSIVFIDEIDAIGKARQKGNfsgaNDERENTLNQMLVEMDGF-TSADHVVVLAGTNRPDIL 419
Cdd:cd19521   81 MGESEKLVKQLFAMARENKPSIIFIDEVDSLCGTRGEGE----SEASRRIKTELLVQMNGVgNDSQGVLVLGATNIPWQL 156
                        170
                 ....*....|....*.
gi 961788553 420 DNALLRpgRFDRRIHI 435
Cdd:cd19521  157 DSAIRR--RFEKRIYI 170
RecA-like_spastin cd19524
ATPase domain of spastin; Spastin is an ATP-dependent microtubule-severing protein involved in ...
268-435 7.41e-33

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


Pssm-ID: 410932 [Multi-domain]  Cd Length: 164  Bit Score: 124.58  E-value: 7.41e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961788553 268 DVAGCDEAKEEIMEFVsFLRNPQRYEKMGAKIP-RGAILSGPPGTGKTLLAKATAGEAGVPFYFVSGSEFVEMFVGVGAA 346
Cdd:cd19524    1 DIAGQDLAKQALQEMV-ILPSLRPELFTGLRAPaRGLLLFGPPGNGKTMLAKAVAAESNATFFNISAASLTSKYVGEGEK 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961788553 347 RVRDLFKTARENAPSIVFIDEIDAIGKARQkgnfSGANDERENTLNQMLVEMDGFTSA--DHVVVLAGTNRPDILDNALL 424
Cdd:cd19524   80 LVRALFAVARELQPSIIFIDEVDSLLSERS----EGEHEASRRLKTEFLIEFDGVQSNgdDRVLVMGATNRPQELDDAVL 155
                        170
                 ....*....|.
gi 961788553 425 RpgRFDRRIHI 435
Cdd:cd19524  156 R--RFTKRVYV 164
RecA-like_Yta7-like cd19517
ATPase domain of Saccharomyces cerevisiae Yta7 and similar ATPase domains; Saccharomyces ...
268-431 1.83e-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: 123.39  E-value: 1.83e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961788553 268 DVAGCDEAKEEIMEFVSF-LRNPQRYEKMGAKIPRGAILSGPPGTGKTLLAKATAGEAG-----VPFYFVSGSEFVEMFV 341
Cdd:cd19517    1 DIGGLSHYINQLKEMVFFpLLYPEVFAKFKITPPRGVLFHGPPGTGKTLMARALAAECSkggqkVSFFMRKGADCLSKWV 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961788553 342 GVGAARVRDLFKTARENAPSIVFIDEIDAIGKARqkgnfSGANDERENTL-NQMLVEMDGFTSADHVVVLAGTNRPDILD 420
Cdd:cd19517   81 GEAERQLRLLFEEAYRMQPSIIFFDEIDGLAPVR-----SSKQEQIHASIvSTLLALMDGLDNRGQVVVIGATNRPDALD 155
                        170
                 ....*....|.
gi 961788553 421 NALLRPGRFDR 431
Cdd:cd19517  156 PALRRPGRFDR 166
RecA-like_ATAD1 cd19520
ATPase domain of ATPase family AAA domain-containing protein 1 and similar ATPase domains; ...
268-435 2.71e-31

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


Pssm-ID: 410928 [Multi-domain]  Cd Length: 166  Bit Score: 120.22  E-value: 2.71e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961788553 268 DVAGCDEAKEEIMEFVSF-LRNPQRYEKMG-AKIPRGAILSGPPGTGKTLLAKATAGEAGVPFYFVSGSEFVEMFVGVGA 345
Cdd:cd19520    1 DIGGLDEVITELKELVILpLQRPELFDNSRlLQPPKGVLLYGPPGCGKTMLAKATAKEAGARFINLQVSSLTDKWYGESQ 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961788553 346 ARVRDLFKTARENAPSIVFIDEIDAIGKARQkgnfSGANDERENTLNQMLVEMDGFTSADH--VVVLAGTNRPDILDNAL 423
Cdd:cd19520   81 KLVAAVFSLASKLQPSIIFIDEIDSFLRQRS----STDHEATAMMKAEFMSLWDGLSTDGNcrVIVMGATNRPQDLDEAI 156
                        170
                 ....*....|..
gi 961788553 424 LRpgRFDRRIHI 435
Cdd:cd19520  157 LR--RMPKRFHI 166
RecA-like_Figl-1 cd19525
ATPase domain of Fidgetin-Like 1 (FIGL-1); FIGL-1 may participate in DNA repair in the nucleus; ...
264-435 4.00e-31

ATPase domain of Fidgetin-Like 1 (FIGL-1); FIGL-1 may participate in DNA repair in the nucleus; it may be involved in DNA double-strand break repair via homologous recombination. Caenorhabditis elegans FIGL-1 is a nuclear protein and controls the mitotic progression in the germ line and mouse FIGL-1 may be involved in the control of male meiosis. human FIGL-1 has been shown to be a centrosome protein involved in ciliogenesis perhaps as a microtubule-severing protein. This subfamily belongs to the RecA-like NTPase family which includes the NTP binding domain of F1 and V1 H(+)ATPases, DnaB and related helicases as well as bacterial RecA and related eukaryotic and archaeal recombinases. The RecA-like NTPase family also includes bacterial conjugation proteins and related DNA transfer proteins involved in type II and type IV secretion.


Pssm-ID: 410933 [Multi-domain]  Cd Length: 186  Bit Score: 120.48  E-value: 4.00e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961788553 264 VKFKDVAGCDEAKEEIMEFV--SFLRnPQRYEKMGAKiPRGAILSGPPGTGKTLLAKATAGEAGVPFYFVSGSEFVEMFV 341
Cdd:cd19525   19 INWADIAGLEFAKKTIKEIVvwPMLR-PDIFTGLRGP-PKGILLFGPPGTGKTLIGKCIASQSGATFFSISASSLTSKWV 96
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961788553 342 GVGAARVRDLFKTARENAPSIVFIDEIDAIGKARQKGNfsgaNDERENTLNQMLVEMDGFTSA--DHVVVLAGTNRPDIL 419
Cdd:cd19525   97 GEGEKMVRALFSVARCKQPAVIFIDEIDSLLSQRGEGE----HESSRRIKTEFLVQLDGATTSseDRILVVGATNRPQEI 172
                        170
                 ....*....|....*.
gi 961788553 420 DNALLRpgRFDRRIHI 435
Cdd:cd19525  173 DEAARR--RLVKRLYI 186
RecA-like_KTNA1 cd19522
Katanin p60 ATPase-containing subunit A1; Katanin p60 ATPase-containing subunit A1 (KTNA1) is ...
268-435 5.57e-30

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: 116.62  E-value: 5.57e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961788553 268 DVAGCDEAKEEIMEFVSF-LRNPQRYEkmGAKIP-RGAILSGPPGTGKTLLAKATAGEAGVPFYFVSGSEFVEMFVGVGA 345
Cdd:cd19522    1 DIADLEEAKKLLEEAVVLpMWMPEFFK--GIRRPwKGVLMVGPPGTGKTLLAKAVATECGTTFFNVSSSTLTSKYRGESE 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961788553 346 ARVRDLFKTARENAPSIVFIDEIDAIGKARqkgnfsGANDERENTL---NQMLVEMDGFT-------SADHVVVLAGTNR 415
Cdd:cd19522   79 KLVRLLFEMARFYAPTTIFIDEIDSICSRR------GTSEEHEASRrvkSELLVQMDGVGgasenddPSKMVMVLAATNF 152
                        170       180
                 ....*....|....*....|
gi 961788553 416 PDILDNALLRpgRFDRRIHI 435
Cdd:cd19522  153 PWDIDEALRR--RLEKRIYI 170
RecA-like_NSF-SEC18_r1-like cd19504
first of two ATPase domains of NSF and SEC18, and similar ATPase domains; ...
282-435 6.24e-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: 113.74  E-value: 6.24e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961788553 282 FVSFLRNPQRYEKMGAKIPRGAILSGPPGTGKTLLAKA-----TAGEAGVpfyfVSGSEFVEMFVGVGAARVRDLFKTAR 356
Cdd:cd19504   17 FASRVFPPEIVEQLGCKHVKGILLYGPPGTGKTLMARQigkmlNAREPKI----VNGPEILNKYVGESEANIRKLFADAE 92
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961788553 357 ENAPS--------IVFIDEIDAIGKarQKGNFSGANDERENTLNQMLVEMDGFTSADHVVVLAGTNRPDILDNALLRPGR 428
Cdd:cd19504   93 EEQRRlgansglhIIIFDEIDAICK--QRGSMAGSTGVHDTVVNQLLSKIDGVEQLNNILVIGMTNRKDLIDEALLRPGR 170

                 ....*..
gi 961788553 429 FDRRIHI 435
Cdd:cd19504  171 LEVQMEI 177
ycf46 CHL00195
Ycf46; Provisional
262-490 5.84e-26

Ycf46; Provisional


Pssm-ID: 177094 [Multi-domain]  Cd Length: 489  Bit Score: 112.42  E-value: 5.84e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961788553 262 VKVKFKDVAGCDEAKEEI-MEFVSFLRNPQRYekmGAKIPRGAILSGPPGTGKTLLAKATAGEAGVPFYFVSGSEFVEMF 340
Cdd:CHL00195 223 VNEKISDIGGLDNLKDWLkKRSTSFSKQASNY---GLPTPRGLLLVGIQGTGKSLTAKAIANDWQLPLLRLDVGKLFGGI 299
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961788553 341 VGVGAARVRDLFKTARENAPSIVFIDEIDaigKARQKGNFSGANDERENTLNQMLVEMDGFTSAdhVVVLAGTNRPDILD 420
Cdd:CHL00195 300 VGESESRMRQMIRIAEALSPCILWIDEID---KAFSNSESKGDSGTTNRVLATFITWLSEKKSP--VFVVATANNIDLLP 374
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 961788553 421 NALLRPGRFDRRIHIDRPELEGRKAIFEVHLQKLK-LAGSIFDLKnRLAALTPGFSGADIANVCNEAALIA 490
Cdd:CHL00195 375 LEILRKGRFDEIFFLDLPSLEEREKIFKIHLQKFRpKSWKKYDIK-KLSKLSNKFSGAEIEQSIIEAMYIA 444
RecA-like_BCS1 cd19510
Mitochondrial chaperone BCS1; Mitochondrial chaperone BCS1 is necessary for the assembly of ...
284-435 2.93e-24

Mitochondrial chaperone BCS1; Mitochondrial chaperone BCS1 is necessary for the assembly of mitochondrial respiratory chain complex III and plays an important role in the maintenance of mitochondrial tubular networks, respiratory chain assembly and formation of the LETM1 complex. RecA-like NTPases. This family includes the NTP binding domain of F1 and V1 H(+)ATPases, DnaB and related helicases as well as bacterial RecA and related eukaryotic and archaeal recombinases. This group also includes bacterial conjugation proteins and related DNA transfer proteins involved in type II and type IV secretion.


Pssm-ID: 410918 [Multi-domain]  Cd Length: 153  Bit Score: 99.35  E-value: 2.93e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961788553 284 SFLRNPQRYEKMGAKIPRGAILSGPPGTGKTLLAKATAGEAGVPFYFVSGSEfvemfVGVGAARVRDLFKTARENapSIV 363
Cdd:cd19510    7 DFIKNEDWYNDRGIPYRRGYLLYGPPGTGKSSFIAALAGELDYDICDLNLSE-----VVLTDDRLNHLLNTAPKQ--SII 79
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 961788553 364 FIDEIDA--IGKARQKGNFSGANDERENTLNQMLVEMDGFTSADHVVVLAGTNRPDILDNALLRPGRFDRRIHI 435
Cdd:cd19510   80 LLEDIDAafESREHNKKNPSAYGGLSRVTFSGLLNALDGVASSEERIVFMTTNHIERLDPALIRPGRVDMKIYM 153
AAA cd00009
The AAA+ (ATPases Associated with a wide variety of cellular Activities) superfamily ...
274-436 5.96e-24

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


Pssm-ID: 99707 [Multi-domain]  Cd Length: 151  Bit Score: 98.37  E-value: 5.96e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961788553 274 EAKEEIMEFVSFLRNPQryekmgakiPRGAILSGPPGTGKTLLAKATAGEA---GVPFYFVSGSEFVEMFVG---VGAAR 347
Cdd:cd00009    2 GQEEAIEALREALELPP---------PKNLLLYGPPGTGKTTLARAIANELfrpGAPFLYLNASDLLEGLVVaelFGHFL 72
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961788553 348 VRDLFKTARENAPSIVFIDEIDAIGKARQKGNfsganderentLNQMLVEMDGFTSADHVVVLAGTNRPDILDNALLRPG 427
Cdd:cd00009   73 VRLLFELAEKAKPGVLFIDEIDSLSRGAQNAL-----------LRVLETLNDLRIDRENVRVIGATNRPLLGDLDRALYD 141

                 ....*....
gi 961788553 428 RFDRRIHID 436
Cdd:cd00009  142 RLDIRIVIP 150
RecA-like_fidgetin cd19523
ATPase domain of fidgetin; Fidgetin (FIGN) is a ATP-dependent microtubule severing protein. ...
268-435 4.69e-22

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


Pssm-ID: 410931 [Multi-domain]  Cd Length: 163  Bit Score: 93.41  E-value: 4.69e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961788553 268 DVAGCDEAKEEIMEFVSF-LRNPQRYEKMgAKIPRGAILSGPPGTGKTLLAKATAGEAGVPFYFVSGSEFVEMFVGVGAA 346
Cdd:cd19523    1 DIAGLGALKAAIKEEVLWpLLRPDAFSGL-LRLPRSILLFGPRGTGKTLLGRCLASQLGATFLRLRGSTLVAKWAGEGEK 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961788553 347 RVRDLFKTARENAPSIVFIDEIDAIGKARQKGNFSGANDEREntlnqMLVEMDGFTSA--DHVVVLAGTNRPDILDNALL 424
Cdd:cd19523   80 ILQASFLAARCRQPSVLFISDLDALLSSQDDEASPVGRLQVE-----LLAQLDGVLGSgeDGVLVVCTTSKPEEIDESLR 154
                        170
                 ....*....|.
gi 961788553 425 RpgRFDRRIHI 435
Cdd:cd19523  155 R--YFSKRLLV 163
RecA-like_Ycf46-like cd19507
ATPase domain of Ycf46 and similar ATPase domains; Ycf46 may play a role in the regulation of ...
268-431 3.14e-18

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: 82.42  E-value: 3.14e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961788553 268 DVAGCDEAKEEIME-FVSFLRNPQRYekmGAKIPRGAILSGPPGTGKTLLAKATAGEAGVPFYFVSGSEFVEMFVGVGAA 346
Cdd:cd19507    1 DVGGLDNLKDWLKKrKAAFSKQASAY---GLPTPKGLLLVGIQGTGKSLTAKAIAGVWQLPLLRLDMGRLFGGLVGESES 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961788553 347 RVRDLFKTARENAPSIVFIDEIDaigKARQKGNFSGANDERENTLNQMLVEMDGFTSAdhVVVLAGTNRPDILDNALLRP 426
Cdd:cd19507   78 RLRQMIQTAEAIAPCVLWIDEIE---KGFSNADSKGDSGTSSRVLGTFLTWLQEKKKP--VFVVATANNVQSLPPELLRK 152

                 ....*
gi 961788553 427 GRFDR 431
Cdd:cd19507  153 GRFDE 157
AAA smart00382
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ...
300-439 9.49e-18

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: 80.50  E-value: 9.49e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961788553   300 PRGAILSGPPGTGKTLLAKATAGEA---GVPFYFVSGSEFVE--------------MFVGVGAARVRDLFKTARENAPSI 362
Cdd:smart00382   2 GEVILIVGPPGSGKTTLARALARELgppGGGVIYIDGEDILEevldqllliivggkKASGSGELRLRLALALARKLKPDV 81
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 961788553   363 VFIDEIDAIGKARQkgnfsgandERENTLNQMLVEMDGFTSADHVVVLAGTNRPDILDNALLRPgRFDRRIHIDRPE 439
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 ...
461-505 5.67e-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: 60.63  E-value: 5.67e-12
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 961788553  461 FDLKnRLAALTPGFSGADIANVCNEAALIAARHDENAVKLSHFEQ 505
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 ...
301-434 1.86e-11

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: 62.54  E-value: 1.86e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961788553 301 RGAILSGPPGTGKTLLAKATAGEAGVPFYFVSGSEFVEMFV-GVGAA-RVRDLFKTARENApsIVFIDEIDAIGKARQKG 378
Cdd:cd19512   23 RNILFYGPPGTGKTLFAKKLALHSGMDYAIMTGGDVAPMGReGVTAIhKVFDWANTSRRGL--LLFVDEADAFLRKRSTE 100
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 961788553 379 NFSgaNDEREnTLNQMLVEMdGFTSADHVVVLAgTNRPDILDNALlrPGRFDRRIH 434
Cdd:cd19512  101 KIS--EDLRA-ALNAFLYRT-GEQSNKFMLVLA-SNQPEQFDWAI--NDRIDEMVE 149
RecA-like_HslU cd19498
ATP-dependent protease ATPase subunit HslU; HslU is a component of the ATP-dependent protease ...
267-446 4.22e-10

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


Pssm-ID: 410906 [Multi-domain]  Cd Length: 183  Bit Score: 59.70  E-value: 4.22e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961788553 267 KDVAGCDEAKEEImefVSFLRNPQRYEKMGAKI-----PRGAILSGPPGTGKTLLAKATAGEAGVPFYFVSGSEFVEM-F 340
Cdd:cd19498   11 KYIIGQDEAKRAV---AIALRNRWRRMQLPEELrdevtPKNILMIGPTGVGKTEIARRLAKLAGAPFIKVEATKFTEVgY 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961788553 341 VGvgaarvRDLFKTARENAPSIVFIDEIDAIGKarqKGNFSGANDERENTLNQMLVEMDGFT--------SADHVVVLAG 412
Cdd:cd19498   88 VG------RDVESIIRDLVEGIVFIDEIDKIAK---RGGSSGPDVSREGVQRDLLPIVEGSTvstkygpvKTDHILFIAA 158
                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 961788553 413 tnrpdildnallrpGRFdrriHIDRP-----ELEGRKAI 446
Cdd:cd19498  159 --------------GAF----HVAKPsdlipELQGRFPI 179
PRK13342 PRK13342
recombination factor protein RarA; Reviewed
304-368 2.06e-09

recombination factor protein RarA; Reviewed


Pssm-ID: 237355 [Multi-domain]  Cd Length: 413  Bit Score: 60.10  E-value: 2.06e-09
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 961788553 304 ILSGPPGTGKTLLAKATAGEAGVPFYFVSGSefvemFVGVgaARVRDLFKTARENAPS----IVFIDEI 368
Cdd:PRK13342  40 ILWGPPGTGKTTLARIIAGATDAPFEALSAV-----TSGV--KDLREVIEEARQRRSAgrrtILFIDEI 101
RarA COG2256
Replication-associated recombination protein RarA (DNA-dependent ATPase) [Replication, ...
304-368 3.39e-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: 3.39e-09
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 961788553 304 ILSGPPGTGKTLLAKATAGEAGVPFYFVSGsefvemfVGVGAARVRDLFKTARENA----PSIVFIDEI 368
Cdd:COG2256   53 ILWGPPGTGKTTLARLIANATDAEFVALSA-------VTSGVKDIREVIEEARERRaygrRTILFVDEI 114
PRK04195 PRK04195
replication factor C large subunit; Provisional
265-374 7.60e-09

replication factor C large subunit; Provisional


Pssm-ID: 235250 [Multi-domain]  Cd Length: 482  Bit Score: 58.78  E-value: 7.60e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961788553 265 KFKDVAGCDEAKEEIMEFV-SFLRNpqryekmgaKIPRGAILSGPPGTGKTLLAKATAGEAGVPFYFVSGSEF-----VE 338
Cdd:PRK04195  12 TLSDVVGNEKAKEQLREWIeSWLKG---------KPKKALLLYGPPGVGKTSLAHALANDYGWEVIELNASDQrtadvIE 82
                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 961788553 339 MFVGvGAARVRDLFKTARenapSIVFIDEIDAI-GKA 374
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 ...
267-383 1.55e-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: 54.87  E-value: 1.55e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961788553 267 KDVAGCDEAKEEIMEFVSFLrnpQRYEKMGAKIprgAILSGPPGTGKTLLAKATAGEAGVPFYFVS-G--SEFVEM---- 339
Cdd:cd19500   10 ADHYGLEDVKERILEYLAVR---KLKGSMKGPI---LCLVGPPGVGKTSLGKSIARALGRKFVRISlGgvRDEAEIrghr 83
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 961788553 340 --FVGVGAARVRDLFKTARENAPSIVfIDEIDAIGKARQkGNFSGA 383
Cdd:cd19500   84 rtYVGAMPGRIIQALKKAGTNNPVFL-LDEIDKIGSSFR-GDPASA 127
RecA-like_Pch2-like cd19508
ATPase domain of Pachytene checkpoint 2 (Pch2) and similar ATPase domains; Pch2 (known as ...
301-423 8.20e-07

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: 50.14  E-value: 8.20e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961788553 301 RGAILSGPPGTGKTLLAKATAGEAGVPFYFV----------SGSEFVEMFVGVGAArVRDLFKTARE-----NAPSIVFI 365
Cdd:cd19508   53 RLVLLHGPPGTGKTSLCKALAQKLSIRLSSRyrygqlieinSHSLFSKWFSESGKL-VTKMFQKIQEliddkDALVFVLI 131
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 961788553 366 DEIDAIGKARQkgNFSGANDERE--NTLNQMLVEMDGFTSADHVVVLAGTNRPDILDNAL 423
Cdd:cd19508  132 DEVESLAAARS--ASSSGTEPSDaiRVVNAVLTQIDRIKRYHNNVILLTSNLLEKIDVAF 189
RecA-like_Ycf2 cd19505
ATPase domain of plant YCF2; Ycf2 is a chloroplast ATPase which has an essential function; ...
300-435 3.62e-06

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: 47.76  E-value: 3.62e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961788553 300 PRGAILSGPPGTGKTLLAKATAGEAGVPFYFVSGSEFV--------------EMFVGVGAARVRDLFKTARENAPSIVFI 365
Cdd:cd19505   12 SKGILLIGSIETGRSYLIKSLAANSYVPLIRISLNKLLynkpdfgnddwidgMLILKESLHRLNLQFELAKAMSPCIIWI 91
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961788553 366 DEIDAIGKARQKGNFSGANDERENTLNQMLVEMDGFTSADHVVVLAGTNRPDILDNALLRPGRFDRRIHI 435
Cdd:cd19505   92 PNIHELNVNRSTQNLEEDPKLLLGLLLNYLSRDFEKSSTRNILVIASTHIPQKVDPALIAPNRLDTCINI 161
T7SS_EccA TIGR03922
type VII secretion AAA-ATPase EccA; This model represents the AAA family ATPase, EccA, of the ...
271-436 3.97e-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: 50.23  E-value: 3.97e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961788553  271 GCDEAKEEIMEFVSFLRNPQRYEKMGAKIP---RGAILSGPPGTGKTLLAKATAGE-AGVPFYF------VSGSEFVEMF 340
Cdd:TIGR03922 280 GLERVKRQVAALKSSTAMALARAERGLPVAqtsNHMLFAGPPGTGKTTIARVVAKIyCGLGVLRkplvreVSRADLIGQY 359
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961788553  341 VGVGAARVRDLFKTAREnapSIVFIDEIDA-IGKARQKGNFSGAndereNTLNQMLVEMDgfTSADHVVVLAGTNRPDI- 418
Cdd:TIGR03922 360 IGESEAKTNEIIDSALG---GVLFLDEAYTlVETGYGQKDPFGL-----EAIDTLLARME--NDRDRLVVIGAGYRKDLd 429
                         170       180
                  ....*....|....*....|.
gi 961788553  419 --LD-NALLRpGRFDRRIHID 436
Cdd:TIGR03922 430 kfLEvNEGLR-SRFTRVIEFP 449
CDC6 COG1474
Cdc6-related protein, AAA superfamily ATPase [Replication, recombination and repair];
277-528 6.57e-06

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


Pssm-ID: 441083 [Multi-domain]  Cd Length: 389  Bit Score: 49.08  E-value: 6.57e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961788553 277 EEIMEFVSFLRNPQRYEKmgakiPRGAILSGPPGTGKTLLAKA-------TAGEAGVPFYFV------SGSEF------V 337
Cdd:COG1474   33 EEIEELASALRPALRGER-----PSNVLIYGPTGTGKTAVAKYvleeleeEAEERGVDVRVVyvncrqASTRYrvlsriL 107
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961788553 338 EMFV--------GVGAARVRDLFKTA--RENAPSIVFIDEIDAIGKarqkgnfsganDERENTLNQmLVEMDGFTSADHV 407
Cdd:COG1474  108 EELGsgedipstGLSTDELFDRLYEAldERDGVLVVVLDEIDYLVD-----------DEGDDLLYQ-LLRANEELEGARV 175
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961788553 408 VVLAGTNRPDILDNalLRP---GRF-DRRIHI---DRPELegrKAIfevhlqklklagsifdLKNRL-AALTPGFSGADI 479
Cdd:COG1474  176 GVIGISNDLEFLEN--LDPrvkSSLgEEEIVFppyDADEL---RDI----------------LEDRAeLAFYDGVLSDEV 234
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 961788553 480 ANVCNE------------------AALIAARHDENAVKLSHFEQAIERV-IGGVERKTRLLSPEEKQV 528
Cdd:COG1474  235 IPLIAAlaaqehgdarkaidllrvAGEIAEREGSDRVTEEHVREAREKIeRDRLLEVLRGLPTHEKLV 302
RecA-like_superfamily cd01120
RecA-like_NTPases; RecA-like NTPases. This superfamily includes the NTP binding domain of F1 ...
304-421 8.44e-06

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: 45.57  E-value: 8.44e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961788553 304 ILSGPPGTGKTLLAKATAGEA---GVPFYFVSgseFVEMFVgvgaARVRDLfktARENAPSIVFIDEIDAIGKARQkgnf 380
Cdd:cd01120    2 LITGPPGSGKTTLLLQFAEQAllsDEPVIFIS---FLDTIL----EAIEDL---IEEKKLDIIIIDSLSSLARASQ---- 67
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 961788553 381 sgaNDERENTLNQMLVEMDGFTSAdHVVVLAGTNRPDILDN 421
Cdd:cd01120   68 ---GDRSSELLEDLAKLLRAARNT-GITVIATIHSDKFDID 104
FtsH_ext pfam06480
FtsH Extracellular; This domain is found in the FtsH family of proteins. FtsH is the only ...
116-201 1.08e-05

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: 44.90  E-value: 1.08e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961788553  116 VNDTEGQKEITWQDFRErYLAKGYVQRLEVVNKSYVKVVLNDMGKNQPENYGQEVVyFNLGSVENFEHKLEKAQNEMDID 195
Cdd:pfam06480  20 LSSSSSTKEISYSEFLE-YLEAGKVKKVVVQDDEILPTGVVEGTLKDGSKFTTYFI-PSLPNVDSLLEKLEDALEEKGVK 97

                  ....*.
gi 961788553  196 QDFRVP 201
Cdd:pfam06480  98 VSVKPP 103
AAA_5 pfam07728
AAA domain (dynein-related subfamily); This Pfam entry includes some of the AAA proteins not ...
304-429 3.07e-05

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: 44.21  E-value: 3.07e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961788553  304 ILSGPPGTGKTLLAKATAgEA--GVPFYFVSGSEFVE-------MFVGVGAARVRD--LFKTAREnaPSIVFIDEIDAIG 372
Cdd:pfam07728   3 LLVGPPGTGKTELAERLA-AAlsNRPVFYVQLTRDTTeedlfgrRNIDPGGASWVDgpLVRAARE--GEIAVLDEINRAN 79
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 961788553  373 KARQkGNFSGANDEREntlnqmLVEMDGFT----SADHVVVLAGTNRPDI----LDNALLRpgRF 429
Cdd:pfam07728  80 PDVL-NSLLSLLDERR------LLLPDGGElvkaAPDGFRLIATMNPLDRglneLSPALRS--RF 135
TIP49 pfam06068
TIP49 P-loop domain; This family consists of the C-terminal region of several eukaryotic and ...
301-336 3.43e-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: 3.43e-05
                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 961788553  301 RGAILSGPPGTGKTLLAKATAGEAG--VPFYFVSGSEF 336
Cdd:pfam06068  51 RAVLIAGPPGTGKTALAIAISKELGedTPFTSISGSEV 88
AAA_2 pfam07724
AAA domain (Cdc48 subfamily); This Pfam entry includes some of the AAA proteins not detected ...
304-371 3.67e-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: 44.88  E-value: 3.67e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961788553  304 ILSGPPGTGKTLLAKATAGEAGV---PFYFVSGSEFVE-----MFVGVGAARVR-----DLFKTARENAPSIVFIDEIDA 370
Cdd:pfam07724   7 LFLGPTGVGKTELAKALAELLFGderALIRIDMSEYMEehsvsRLIGAPPGYVGyeeggQLTEAVRRKPYSIVLIDEIEK 86

                  .
gi 961788553  371 I 371
Cdd:pfam07724  87 A 87
TIP49 COG1224
DNA helicase TIP49, TBP-interacting protein [Transcription];
294-336 7.59e-05

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


Pssm-ID: 440837 [Multi-domain]  Cd Length: 452  Bit Score: 45.73  E-value: 7.59e-05
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*
gi 961788553 294 KMGAkipRGAILSGPPGTGKTLLAKATAGEAG--VPFYFVSGSEF 336
Cdd:COG1224   61 KMAG---KGILIVGPPGTGKTALAVAIARELGedTPFVAISGSEI 102
44 PHA02544
clamp loader, small subunit; Provisional
298-374 1.24e-04

clamp loader, small subunit; Provisional


Pssm-ID: 222866 [Multi-domain]  Cd Length: 316  Bit Score: 44.60  E-value: 1.24e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961788553 298 KIPRGAILSGPPGTGKTLLAKATAGEAGVPFYFVSGS----EFVEMFVGVGAARVrdlfktARENAPSIVFIDEIDAIGK 373
Cdd:PHA02544  41 RIPNMLLHSPSPGTGKTTVAKALCNEVGAEVLFVNGSdcriDFVRNRLTRFASTV------SLTGGGKVIIIDEFDRLGL 114

                 .
gi 961788553 374 A 374
Cdd:PHA02544 115 A 115
ruvB PRK00080
Holliday junction branch migration DNA helicase RuvB;
305-374 1.25e-04

Holliday junction branch migration DNA helicase RuvB;


Pssm-ID: 234619 [Multi-domain]  Cd Length: 328  Bit Score: 44.74  E-value: 1.25e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 961788553 305 LSGPPGTGKTLLAKATAGEAGVPFYFVSGSEFvemfvgvgaARVRDL---FKTARENapSIVFIDEIDAIGKA 374
Cdd:PRK00080  56 LYGPPGLGKTTLANIIANEMGVNIRITSGPAL---------EKPGDLaaiLTNLEEG--DVLFIDEIHRLSPV 117
McrB COG1401
5-methylcytosine-specific restriction endonuclease McrBC, GTP-binding regulatory subunit McrB ...
298-368 1.25e-03

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


Pssm-ID: 441011 [Multi-domain]  Cd Length: 477  Bit Score: 42.06  E-value: 1.25e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961788553 298 KIPRGAILSGPPGTGKT----LLAKATAGEAGVPFYFV------SGSEFVEMFV---GVGAARVRD-LFKTARENA---- 359
Cdd:COG1401  219 KTKKNVILAGPPGTGKTylarRLAEALGGEDNGRIEFVqfhpswSYEDFLLGYRpslDEGKYEPTPgIFLRFCLKAeknp 298
                         90
                 ....*....|.
gi 961788553 360 --PSIVFIDEI 368
Cdd:COG1401  299 dkPYVLIIDEI 309
MoxR COG0714
MoxR-like ATPase [General function prediction only]; MoxR-like ATPase is part of the Pathway ...
305-499 1.49e-03

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


Pssm-ID: 440478 [Multi-domain]  Cd Length: 292  Bit Score: 41.31  E-value: 1.49e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961788553 305 LSGPPGTGKTLLAKATAGEAGVPFY----------------FVSGSEFVEMFVGVGAarvrdLFKtarenapSIVFIDEI 368
Cdd:COG0714   36 LEGVPGVGKTTLAKALARALGLPFIriqftpdllpsdilgtYIYDQQTGEFEFRPGP-----LFA-------NVLLADEI 103
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961788553 369 DaigKARQKgnfsganderenTLNQML-------VEMDGFT-SADH-VVVLA--------GTNR-PDildnALLRpgRFD 430
Cdd:COG0714  104 N---RAPPK------------TQSALLeameerqVTIPGGTyKLPEpFLVIAtqnpieqeGTYPlPE----AQLD--RFL 162
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 961788553 431 RRIHIDRPELEGRKAIFEVHLQklklagsifdlkNRLAALTPGFSGADIANVcneAALIAARHDENAVK 499
Cdd:COG0714  163 LKLYIGYPDAEEEREILRRHTG------------RHLAEVEPVLSPEELLAL---QELVRQVHVSEAVL 216
RuvB_N pfam05496
Holliday junction DNA helicase RuvB P-loop domain; The RuvB protein makes up part of the ...
304-368 2.31e-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: 2.31e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 961788553  304 ILSGPPGTGKTLLAKATAGEAGVPFYFVSGSEFvemfvgvgaARVRDL---FKTARENapSIVFIDEI 368
Cdd:pfam05496  37 LLYGPPGLGKTTLANIIANEMGVNIRITSGPAI---------ERPGDLaaiLTNLEPG--DVLFIDEI 93
RecA-like_ClpB_Hsp104-like cd19499
Chaperone protein ClpB/Hsp104 subfamily; Bacterial Caseinolytic peptidase B (ClpB) and ...
263-369 3.27e-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: 3.27e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961788553 263 KVKFKDVAGCDEAKEEIMEFV----SFLRNPQRyekmgakiPRGA-ILSGPPGTGKTLLAKATAGeagvpFYF------- 330
Cdd:cd19499    7 ERLHERVVGQDEAVKAVSDAIrrarAGLSDPNR--------PIGSfLFLGPTGVGKTELAKALAE-----LLFgdednli 73
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 961788553 331 -VSGSEFVEMFVG----------VGAARVRDLFKTARENAPSIVFIDEID 369
Cdd:cd19499   74 rIDMSEYMEKHSVsrligappgyVGYTEGGQLTEAVRRKPYSVVLLDEIE 123
ruvB TIGR00635
Holliday junction DNA helicase, RuvB subunit; All proteins in this family for which functions ...
304-374 4.40e-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: 4.40e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 961788553  304 ILSGPPGTGKTLLAKATAGEAGVPFYFVSGSEFVemfvgvgaaRVRDLFK--TAREnAPSIVFIDEIDAIGKA 374
Cdd:TIGR00635  34 LLYGPPGLGKTTLAHIIANEMGVNLKITSGPALE---------KPGDLAAilTNLE-EGDVLFIDEIHRLSPA 96
PRK13341 PRK13341
AAA family ATPase;
303-376 4.96e-03

AAA family ATPase;


Pssm-ID: 237354 [Multi-domain]  Cd Length: 725  Bit Score: 40.42  E-value: 4.96e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961788553 303 AILSGPPGTGKTLLAKATAGeagvpfYFvsGSEFVEM-FVGVGAARVRDLFKTARE-----NAPSIVFIDEIDAIGKARQ 376
Cdd:PRK13341  55 LILYGPPGVGKTTLARIIAN------HT--RAHFSSLnAVLAGVKDLRAEVDRAKErlerhGKRTILFIDEVHRFNKAQQ 126
AAA_22 pfam13401
AAA domain;
304-420 6.09e-03

AAA domain;


Pssm-ID: 379165 [Multi-domain]  Cd Length: 129  Bit Score: 37.71  E-value: 6.09e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961788553  304 ILSGPPGTGKTLLAK---ATAGEAGVPFYFV------SGSEFVEMFV------GVGAARVRDLFKTAREN-----APSIV 363
Cdd:pfam13401   9 VLTGESGTGKTTLLRrllEQLPEVRDSVVFVdlpsgtSPKDLLRALLralglpLSGRLSKEELLAALQQLllalaVAVVL 88
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 961788553  364 FIDEIDAIgkarqkgnfsgandeRENTLNQmLVEMDGFTSADHVVVLAGTnrPDILD 420
Cdd:pfam13401  89 IIDEAQHL---------------SLEALEE-LRDLLNLSSKLLQLILVGT--PELRE 127
DnaC COG1484
DNA replication protein DnaC [Replication, recombination and repair];
301-338 8.33e-03

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


Pssm-ID: 441093 [Multi-domain]  Cd Length: 242  Bit Score: 38.61  E-value: 8.33e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|.
gi 961788553 301 RGAILSGPPGTGKTLLAKA---TAGEAGVPFYFVSGSEFVE 338
Cdd:COG1484  100 ENLILLGPPGTGKTHLAIAlghEACRAGYRVRFTTAPDLVN 140
AAA_17 pfam13207
AAA domain;
306-428 8.55e-03

AAA domain;


Pssm-ID: 463810 [Multi-domain]  Cd Length: 136  Bit Score: 37.22  E-value: 8.55e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961788553  306 SGPPGTGKTLLAKATAGEAGVPfYFVSGSEFVEMFVGVGAARVRDLFKTARENAPSIVFIDEIDAIGKARQKGNF--SG- 382
Cdd:pfam13207   1 TGVPGSGKTTQLKKLAEKLGFP-HISAGDLLREEAKERGLVEDRDEMRKLPLEPQKELQKLAAERIAEEAGEGGVivDGh 79
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 961788553  383 -ANDERENTLNQMLVEMDGFTSADHVVVLAgTNRPDILDNALLRPGR 428
Cdd:pfam13207  80 pRIKTPAGYLPGLPVEVLRELKPDAIILLE-ADPEEILERRLKDRTR 125
 
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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