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Conserved domains on  [gi|6325281|ref|NP_015349|]
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i-AAA protease YME1 [Saccharomyces cerevisiae S288C]

Protein Classification

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

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

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
HflB COG0465
ATP-dependent Zn proteases [Posttranslational modification, protein turnover, chaperones];
269-709 0e+00

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


:

Pssm-ID: 440233 [Multi-domain]  Cd Length: 583  Bit Score: 676.37  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325281  269 KSVDVAKTNVKFDDVCGCDEARAELEEIVDFLKDPTKYESLGGKLPKGVLLTGPPGTGKTLLARATAGEAGVDFFFMSGS 348
Cdd:COG0465 130 KLYDEDKPKVTFDDVAGVDEAKEELQEIVDFLKDPEKFTRLGAKIPKGVLLVGPPGTGKTLLAKAVAGEAGVPFFSISGS 209
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325281  349 EFDEVYVGVGAKRIRDLFAQARSRAPAIIFIDELDAIGGKRNpkdqayAK---------QTLNQLLVELDGFSQTSGIII 419
Cdd:COG0465 210 DFVEMFVGVGASRVRDLFEQAKKNAPCIIFIDEIDAVGRQRG------AGlggghdereQTLNQLLVEMDGFEGNEGVIV 283
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325281  420 IGATNFPEALDKALTRPGRFDKVVNVDLPDVRGRADILKHHMKKITLADNVDPTIIARGTPGLSGAELANLVNQAAVYAC 499
Cdd:COG0465 284 IAATNRPDVLDPALLRPGRFDRQVVVDLPDVKGREAILKVHARKKPLAPDVDLEVIARRTPGFSGADLANLVNEAALLAA 363
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325281  500 QKNAVSVDMSHFEWAKDKILMGAERKTMVLTDAARKATAFHEAGHAIMAKYTNGATPLYKATILPRGRALGITFQLPEMD 579
Cdd:COG0465 364 RRNKKAVTMEDFEEAIDRVIAGPERKSRVISEKEKKITAYHEAGHALVAALLPGADPVHKVTIIPRGRALGYTMQLPEED 443
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325281  580 KVDITKRECQARLDVCMGGKIAEELIYGKdnTTSGCGSDLQSATGTARAMVTQYGMSDDVGPVNLSENWESW-------- 651
Cdd:COG0465 444 RYLYTKEELLDRIAVLLGGRAAEELVFGE--VTTGASNDLERATKIARAMVTEYGMSEKLGPVAYGESEGEVflgrdigq 521
                       410       420       430       440       450       460
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 6325281  652 ----SNKIRDIADNEVIELLKDSEERARRLLTKKNVELHRLAQGLIEYETLDAHEIEQVCKG 709
Cdd:COG0465 522 srnySEETAREIDEEVRRIIDEAYERAKEILTENRDKLDALAEALLEKETLDGEELEEILAG 583
 
Name Accession Description Interval E-value
HflB COG0465
ATP-dependent Zn proteases [Posttranslational modification, protein turnover, chaperones];
269-709 0e+00

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


Pssm-ID: 440233 [Multi-domain]  Cd Length: 583  Bit Score: 676.37  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325281  269 KSVDVAKTNVKFDDVCGCDEARAELEEIVDFLKDPTKYESLGGKLPKGVLLTGPPGTGKTLLARATAGEAGVDFFFMSGS 348
Cdd:COG0465 130 KLYDEDKPKVTFDDVAGVDEAKEELQEIVDFLKDPEKFTRLGAKIPKGVLLVGPPGTGKTLLAKAVAGEAGVPFFSISGS 209
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325281  349 EFDEVYVGVGAKRIRDLFAQARSRAPAIIFIDELDAIGGKRNpkdqayAK---------QTLNQLLVELDGFSQTSGIII 419
Cdd:COG0465 210 DFVEMFVGVGASRVRDLFEQAKKNAPCIIFIDEIDAVGRQRG------AGlggghdereQTLNQLLVEMDGFEGNEGVIV 283
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325281  420 IGATNFPEALDKALTRPGRFDKVVNVDLPDVRGRADILKHHMKKITLADNVDPTIIARGTPGLSGAELANLVNQAAVYAC 499
Cdd:COG0465 284 IAATNRPDVLDPALLRPGRFDRQVVVDLPDVKGREAILKVHARKKPLAPDVDLEVIARRTPGFSGADLANLVNEAALLAA 363
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325281  500 QKNAVSVDMSHFEWAKDKILMGAERKTMVLTDAARKATAFHEAGHAIMAKYTNGATPLYKATILPRGRALGITFQLPEMD 579
Cdd:COG0465 364 RRNKKAVTMEDFEEAIDRVIAGPERKSRVISEKEKKITAYHEAGHALVAALLPGADPVHKVTIIPRGRALGYTMQLPEED 443
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325281  580 KVDITKRECQARLDVCMGGKIAEELIYGKdnTTSGCGSDLQSATGTARAMVTQYGMSDDVGPVNLSENWESW-------- 651
Cdd:COG0465 444 RYLYTKEELLDRIAVLLGGRAAEELVFGE--VTTGASNDLERATKIARAMVTEYGMSEKLGPVAYGESEGEVflgrdigq 521
                       410       420       430       440       450       460
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 6325281  652 ----SNKIRDIADNEVIELLKDSEERARRLLTKKNVELHRLAQGLIEYETLDAHEIEQVCKG 709
Cdd:COG0465 522 srnySEETAREIDEEVRRIIDEAYERAKEILTENRDKLDALAEALLEKETLDGEELEEILAG 583
FtsH_fam TIGR01241
ATP-dependent metalloprotease FtsH; HflB(FtsH) is a pleiotropic protein required for correct ...
274-706 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: 597.35  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325281    274 AKTNVKFDDVCGCDEARAELEEIVDFLKDPTKYESLGGKLPKGVLLTGPPGTGKTLLARATAGEAGVDFFFMSGSEFDEV 353
Cdd:TIGR01241  48 EKPKVTFKDVAGIDEAKEELMEIVDFLKNPSKFTKLGAKIPKGVLLVGPPGTGKTLLAKAVAGEAGVPFFSISGSDFVEM 127
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325281    354 YVGVGAKRIRDLFAQARSRAPAIIFIDELDAIGGKR-----NPKDQAyaKQTLNQLLVELDGFSQTSGIIIIGATNFPEA 428
Cdd:TIGR01241 128 FVGVGASRVRDLFEQAKKNAPCIIFIDEIDAVGRQRgaglgGGNDER--EQTLNQLLVEMDGFGTNTGVIVIAATNRPDV 205
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325281    429 LDKALTRPGRFDKVVNVDLPDVRGRADILKHHMKKITLADNVDPTIIARGTPGLSGAELANLVNQAAVYACQKNAVSVDM 508
Cdd:TIGR01241 206 LDPALLRPGRFDRQVVVDLPDIKGREEILKVHAKNKKLAPDVDLKAVARRTPGFSGADLANLLNEAALLAARKNKTEITM 285
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325281    509 SHFEWAKDKILMGAERKTMVLTDAARKATAFHEAGHAIMAKYTNGATPLYKATILPRGRALGITFQLPEMDKVDITKREC 588
Cdd:TIGR01241 286 NDIEEAIDRVIAGPEKKSRVISEKEKKLVAYHEAGHALVGLLLKDADPVHKVTIIPRGQALGYTQFLPEEDKYLYTKSQL 365
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325281    589 QARLDVCMGGKIAEELIYGkdNTTSGCGSDLQSATGTARAMVTQYGMSDDVGPVNLSENWE------------SWSNKIR 656
Cdd:TIGR01241 366 LAQIAVLLGGRAAEEIIFG--EVTTGASNDIKQATNIARAMVTEWGMSDKLGPVAYGSDGGdvflgrgfakakEYSEETA 443
                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|
gi 6325281    657 DIADNEVIELLKDSEERARRLLTKKNVELHRLAQGLIEYETLDAHEIEQV 706
Cdd:TIGR01241 444 REIDEEVKRIIEEAYKRAKQILTENRDELELLAKALLEKETITREEIKEL 493
hflB PRK10733
ATP-dependent zinc metalloprotease FtsH;
272-706 1.50e-163

ATP-dependent zinc metalloprotease FtsH;


Pssm-ID: 182683 [Multi-domain]  Cd Length: 644  Bit Score: 486.85  E-value: 1.50e-163
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325281   272 DVAKTNvkFDDVCGCDEARAELEEIVDFLKDPTKYESLGGKLPKGVLLTGPPGTGKTLLARATAGEAGVDFFFMSGSEFD 351
Cdd:PRK10733 145 DQIKTT--FADVAGCDEAKEEVAELVEYLREPSRFQKLGGKIPKGVLMVGPPGTGKTLLAKAIAGEAKVPFFTISGSDFV 222
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325281   352 EVYVGVGAKRIRDLFAQARSRAPAIIFIDELDAIGGKRNP-----KDQAyaKQTLNQLLVELDGFSQTSGIIIIGATNFP 426
Cdd:PRK10733 223 EMFVGVGASRVRDMFEQAKKAAPCIIFIDEIDAVGRQRGAglgggHDER--EQTLNQMLVEMDGFEGNEGIIVIAATNRP 300
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325281   427 EALDKALTRPGRFDKVVNVDLPDVRGRADILKHHMKKITLADNVDPTIIARGTPGLSGAELANLVNQAAVYACQKNAVSV 506
Cdd:PRK10733 301 DVLDPALLRPGRFDRQVVVGLPDVRGREQILKVHMRRVPLAPDIDAAIIARGTPGFSGADLANLVNEAALFAARGNKRVV 380
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325281   507 DMSHFEWAKDKILMGAERKTMVLTDAARKATAFHEAGHAIMAKYTNGATPLYKATILPRGRALGITFQLPEMDKVDITKR 586
Cdd:PRK10733 381 SMVEFEKAKDKIMMGAERRSMVMTEAQKESTAYHEAGHAIIGRLVPEHDPVHKVTIIPRGRALGVTFFLPEGDAISASRQ 460
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325281   587 ECQARLDVCMGGKIAEELIYGKDNTTSGCGSDLQSATGTARAMVTQYGMSDDVGPVNLSE------------NWESWSNK 654
Cdd:PRK10733 461 KLESQISTLYGGRLAEEIIYGPEHVSTGASNDIKVATNLARNMVTQWGFSEKLGPLLYAEeegevflgrsvaKAKHMSDE 540
                        410       420       430       440       450
                 ....*....|....*....|....*....|....*....|....*....|..
gi 6325281   655 IRDIADNEVIELLKDSEERARRLLTKKNVELHRLAQGLIEYETLDAHEIEQV 706
Cdd:PRK10733 541 TARIIDQEVKALIERNYNRARQLLTDNMDILHAMKDALMKYETIDAPQIDDL 592
RecA-like_FtsH cd19501
ATP-dependent zinc metalloprotease FtsH; FtsH ATPase is a processive, ATP-dependent zinc ...
278-445 5.18e-96

ATP-dependent zinc metalloprotease FtsH; FtsH ATPase is a processive, ATP-dependent zinc metallopeptidase for both cytoplasmic and membrane proteins. It is anchored to the cytoplasmic membrane such that the amino- and carboxy-termini are exposed to the cytoplasm. It presents a membrane-bound hexameric structure that is able to unfold and degrade protein substrates. It is comprised of an N-terminal transmembrane region and the larger C-terminal cytoplasmic region, which consists of an ATPase domain and a protease domain. This RecA-Like FTsH subfamily represents the ATPase domain, and belongs to the RecA-like NTPase family which includes the NTP binding domain of F1 and V1 H(+)ATPases, DnaB and related helicases as well as bacterial RecA and related eukaryotic and archaeal recombinases. The RecA-like NTPase family also includes bacterial conjugation proteins and related DNA transfer proteins involved in type II and type IV secretion.


Pssm-ID: 410909 [Multi-domain]  Cd Length: 171  Bit Score: 294.91  E-value: 5.18e-96
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325281  278 VKFDDVCGCDEARAELEEIVDFLKDPTKYESLGGKLPKGVLLTGPPGTGKTLLARATAGEAGVDFFFMSGSEFDEVYVGV 357
Cdd:cd19501   1 VTFKDVAGCEEAKEELKEVVEFLKNPEKFTKLGAKIPKGVLLVGPPGTGKTLLAKAVAGEAGVPFFSISGSDFVEMFVGV 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325281  358 GAKRIRDLFAQARSRAPAIIFIDELDAIGGKRNPK---DQAYAKQTLNQLLVELDGFSQTSGIIIIGATNFPEALDKALT 434
Cdd:cd19501  81 GASRVRDLFEQAKKNAPCIVFIDEIDAVGRKRGAGlggGHDEREQTLNQLLVEMDGFESNTGVIVIAATNRPDVLDPALL 160
                       170
                ....*....|.
gi 6325281  435 RPGRFDKVVNV 445
Cdd:cd19501 161 RPGRFDRQVYV 171
Peptidase_M41 pfam01434
Peptidase family M41;
527-706 2.83e-83

Peptidase family M41;


Pssm-ID: 460210 [Multi-domain]  Cd Length: 190  Bit Score: 262.54  E-value: 2.83e-83
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325281    527 MVLTDAARKATAFHEAGHAIMAKYTNGATPLYKATILPRGRALGITFQLPEMDKVDITKRECQARLDVCMGGKIAEELIY 606
Cdd:pfam01434   1 RVISEEEKKIVAYHEAGHALVGLLLPGADPVHKVTIIPRGQALGYTQFLPEEDKLLYTKEQLLARIAVLLGGRAAEELIF 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325281    607 GKdnTTSGCGSDLQSATGTARAMVTQYGMSDDVGPVNL---SENWES---------WSNKIRDIADNEVIELLKDSEERA 674
Cdd:pfam01434  81 GE--VTTGASNDLEKATKIARQMVTEFGMSDKLGPVSLeesDGNVFLgrgmgkrkpYSEETADIIDEEVKRLLEEAYERA 158
                         170       180       190
                  ....*....|....*....|....*....|..
gi 6325281    675 RRLLTKKNVELHRLAQGLIEYETLDAHEIEQV 706
Cdd:pfam01434 159 KEILTEHRDELEALAEALLEKETLDAEEIREL 190
AAA smart00382
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ...
314-449 2.08e-19

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


Pssm-ID: 214640 [Multi-domain]  Cd Length: 148  Bit Score: 85.50  E-value: 2.08e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325281     314 PKGVLLTGPPGTGKTLLARATAGEA---GVDFFFMSGSEFDEV--------------YVGVGAKRIRDLFAQARSRAPAI 376
Cdd:smart00382   2 GEVILIVGPPGSGKTTLARALARELgppGGGVIYIDGEDILEEvldqllliivggkkASGSGELRLRLALALARKLKPDV 81
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 6325281     377 IFIDELDAIggkrnPKDQAYAKQTLNQLLVELDGFSQTSGIIIIGATNFPEALDKALTRPgRFDKVVNVDLPD 449
Cdd:smart00382  82 LILDEITSL-----LDAEQEALLLLLEELRLLLLLKSEKNLTVILTTNDEKDLGPALLRR-RFDRRIVLLLIL 148
 
Name Accession Description Interval E-value
HflB COG0465
ATP-dependent Zn proteases [Posttranslational modification, protein turnover, chaperones];
269-709 0e+00

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


Pssm-ID: 440233 [Multi-domain]  Cd Length: 583  Bit Score: 676.37  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325281  269 KSVDVAKTNVKFDDVCGCDEARAELEEIVDFLKDPTKYESLGGKLPKGVLLTGPPGTGKTLLARATAGEAGVDFFFMSGS 348
Cdd:COG0465 130 KLYDEDKPKVTFDDVAGVDEAKEELQEIVDFLKDPEKFTRLGAKIPKGVLLVGPPGTGKTLLAKAVAGEAGVPFFSISGS 209
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325281  349 EFDEVYVGVGAKRIRDLFAQARSRAPAIIFIDELDAIGGKRNpkdqayAK---------QTLNQLLVELDGFSQTSGIII 419
Cdd:COG0465 210 DFVEMFVGVGASRVRDLFEQAKKNAPCIIFIDEIDAVGRQRG------AGlggghdereQTLNQLLVEMDGFEGNEGVIV 283
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325281  420 IGATNFPEALDKALTRPGRFDKVVNVDLPDVRGRADILKHHMKKITLADNVDPTIIARGTPGLSGAELANLVNQAAVYAC 499
Cdd:COG0465 284 IAATNRPDVLDPALLRPGRFDRQVVVDLPDVKGREAILKVHARKKPLAPDVDLEVIARRTPGFSGADLANLVNEAALLAA 363
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325281  500 QKNAVSVDMSHFEWAKDKILMGAERKTMVLTDAARKATAFHEAGHAIMAKYTNGATPLYKATILPRGRALGITFQLPEMD 579
Cdd:COG0465 364 RRNKKAVTMEDFEEAIDRVIAGPERKSRVISEKEKKITAYHEAGHALVAALLPGADPVHKVTIIPRGRALGYTMQLPEED 443
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325281  580 KVDITKRECQARLDVCMGGKIAEELIYGKdnTTSGCGSDLQSATGTARAMVTQYGMSDDVGPVNLSENWESW-------- 651
Cdd:COG0465 444 RYLYTKEELLDRIAVLLGGRAAEELVFGE--VTTGASNDLERATKIARAMVTEYGMSEKLGPVAYGESEGEVflgrdigq 521
                       410       420       430       440       450       460
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 6325281  652 ----SNKIRDIADNEVIELLKDSEERARRLLTKKNVELHRLAQGLIEYETLDAHEIEQVCKG 709
Cdd:COG0465 522 srnySEETAREIDEEVRRIIDEAYERAKEILTENRDKLDALAEALLEKETLDGEELEEILAG 583
FtsH_fam TIGR01241
ATP-dependent metalloprotease FtsH; HflB(FtsH) is a pleiotropic protein required for correct ...
274-706 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: 597.35  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325281    274 AKTNVKFDDVCGCDEARAELEEIVDFLKDPTKYESLGGKLPKGVLLTGPPGTGKTLLARATAGEAGVDFFFMSGSEFDEV 353
Cdd:TIGR01241  48 EKPKVTFKDVAGIDEAKEELMEIVDFLKNPSKFTKLGAKIPKGVLLVGPPGTGKTLLAKAVAGEAGVPFFSISGSDFVEM 127
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325281    354 YVGVGAKRIRDLFAQARSRAPAIIFIDELDAIGGKR-----NPKDQAyaKQTLNQLLVELDGFSQTSGIIIIGATNFPEA 428
Cdd:TIGR01241 128 FVGVGASRVRDLFEQAKKNAPCIIFIDEIDAVGRQRgaglgGGNDER--EQTLNQLLVEMDGFGTNTGVIVIAATNRPDV 205
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325281    429 LDKALTRPGRFDKVVNVDLPDVRGRADILKHHMKKITLADNVDPTIIARGTPGLSGAELANLVNQAAVYACQKNAVSVDM 508
Cdd:TIGR01241 206 LDPALLRPGRFDRQVVVDLPDIKGREEILKVHAKNKKLAPDVDLKAVARRTPGFSGADLANLLNEAALLAARKNKTEITM 285
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325281    509 SHFEWAKDKILMGAERKTMVLTDAARKATAFHEAGHAIMAKYTNGATPLYKATILPRGRALGITFQLPEMDKVDITKREC 588
Cdd:TIGR01241 286 NDIEEAIDRVIAGPEKKSRVISEKEKKLVAYHEAGHALVGLLLKDADPVHKVTIIPRGQALGYTQFLPEEDKYLYTKSQL 365
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325281    589 QARLDVCMGGKIAEELIYGkdNTTSGCGSDLQSATGTARAMVTQYGMSDDVGPVNLSENWE------------SWSNKIR 656
Cdd:TIGR01241 366 LAQIAVLLGGRAAEEIIFG--EVTTGASNDIKQATNIARAMVTEWGMSDKLGPVAYGSDGGdvflgrgfakakEYSEETA 443
                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|
gi 6325281    657 DIADNEVIELLKDSEERARRLLTKKNVELHRLAQGLIEYETLDAHEIEQV 706
Cdd:TIGR01241 444 REIDEEVKRIIEEAYKRAKQILTENRDELELLAKALLEKETITREEIKEL 493
hflB PRK10733
ATP-dependent zinc metalloprotease FtsH;
272-706 1.50e-163

ATP-dependent zinc metalloprotease FtsH;


Pssm-ID: 182683 [Multi-domain]  Cd Length: 644  Bit Score: 486.85  E-value: 1.50e-163
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325281   272 DVAKTNvkFDDVCGCDEARAELEEIVDFLKDPTKYESLGGKLPKGVLLTGPPGTGKTLLARATAGEAGVDFFFMSGSEFD 351
Cdd:PRK10733 145 DQIKTT--FADVAGCDEAKEEVAELVEYLREPSRFQKLGGKIPKGVLMVGPPGTGKTLLAKAIAGEAKVPFFTISGSDFV 222
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325281   352 EVYVGVGAKRIRDLFAQARSRAPAIIFIDELDAIGGKRNP-----KDQAyaKQTLNQLLVELDGFSQTSGIIIIGATNFP 426
Cdd:PRK10733 223 EMFVGVGASRVRDMFEQAKKAAPCIIFIDEIDAVGRQRGAglgggHDER--EQTLNQMLVEMDGFEGNEGIIVIAATNRP 300
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325281   427 EALDKALTRPGRFDKVVNVDLPDVRGRADILKHHMKKITLADNVDPTIIARGTPGLSGAELANLVNQAAVYACQKNAVSV 506
Cdd:PRK10733 301 DVLDPALLRPGRFDRQVVVGLPDVRGREQILKVHMRRVPLAPDIDAAIIARGTPGFSGADLANLVNEAALFAARGNKRVV 380
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325281   507 DMSHFEWAKDKILMGAERKTMVLTDAARKATAFHEAGHAIMAKYTNGATPLYKATILPRGRALGITFQLPEMDKVDITKR 586
Cdd:PRK10733 381 SMVEFEKAKDKIMMGAERRSMVMTEAQKESTAYHEAGHAIIGRLVPEHDPVHKVTIIPRGRALGVTFFLPEGDAISASRQ 460
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325281   587 ECQARLDVCMGGKIAEELIYGKDNTTSGCGSDLQSATGTARAMVTQYGMSDDVGPVNLSE------------NWESWSNK 654
Cdd:PRK10733 461 KLESQISTLYGGRLAEEIIYGPEHVSTGASNDIKVATNLARNMVTQWGFSEKLGPLLYAEeegevflgrsvaKAKHMSDE 540
                        410       420       430       440       450
                 ....*....|....*....|....*....|....*....|....*....|..
gi 6325281   655 IRDIADNEVIELLKDSEERARRLLTKKNVELHRLAQGLIEYETLDAHEIEQV 706
Cdd:PRK10733 541 TARIIDQEVKALIERNYNRARQLLTDNMDILHAMKDALMKYETIDAPQIDDL 592
ftsH CHL00176
cell division protein; Validated
219-706 1.11e-150

cell division protein; Validated


Pssm-ID: 214386 [Multi-domain]  Cd Length: 638  Bit Score: 453.35  E-value: 1.11e-150
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325281   219 HVVVSESTF-TVVSRWVKWLLVFGILTYSFSEGFKYITENTTLLKSSEVADKSVD-VAKTNVKFDDVCGCDEARAELEEI 296
Cdd:CHL00176 119 HPPVLKSNIvTILSNLLLPLILIGVLWFFFQRSSNFKGGPGQNLMNFGKSKARFQmEADTGITFRDIAGIEEAKEEFEEV 198
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325281   297 VDFLKDPTKYESLGGKLPKGVLLTGPPGTGKTLLARATAGEAGVDFFFMSGSEFDEVYVGVGAKRIRDLFAQARSRAPAI 376
Cdd:CHL00176 199 VSFLKKPERFTAVGAKIPKGVLLVGPPGTGKTLLAKAIAGEAEVPFFSISGSEFVEMFVGVGAARVRDLFKKAKENSPCI 278
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325281   377 IFIDELDAIGGKRNPK---DQAYAKQTLNQLLVELDGFSQTSGIIIIGATNFPEALDKALTRPGRFDKVVNVDLPDVRGR 453
Cdd:CHL00176 279 VFIDEIDAVGRQRGAGiggGNDEREQTLNQLLTEMDGFKGNKGVIVIAATNRVDILDAALLRPGRFDRQITVSLPDREGR 358
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325281   454 ADILKHHMKKITLADNVDPTIIARGTPGLSGAELANLVNQAAVYACQKNAVSVDMSHFEWAKDKILMGAERKTMVLTdAA 533
Cdd:CHL00176 359 LDILKVHARNKKLSPDVSLELIARRTPGFSGADLANLLNEAAILTARRKKATITMKEIDTAIDRVIAGLEGTPLEDS-KN 437
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325281   534 RKATAFHEAGHAIMAKYTNGATPLYKATILPRGRALGITFQLPEMDKVDITKRECQARLDVCMGGKIAEELIYGKDNTTS 613
Cdd:CHL00176 438 KRLIAYHEVGHAIVGTLLPNHDPVQKVTLIPRGQAKGLTWFTPEEDQSLVSRSQILARIVGALGGRAAEEVVFGSTEVTT 517
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325281   614 GCGSDLQSATGTARAMVTQYGMSdDVGPVNLSENWES-------------WSNKIRDIADNEVIELLKDSEERARRLLTK 680
Cdd:CHL00176 518 GASNDLQQVTNLARQMVTRFGMS-SIGPISLESNNSTdpflgrfmqrnseYSEEIADKIDMEVRSILHTCYQYAYQILKD 596
                        490       500
                 ....*....|....*....|....*.
gi 6325281   681 KNVELHRLAQGLIEYETLDAHEIEQV 706
Cdd:CHL00176 597 NRVLIDLLVELLLQKETIDGDEFREI 622
RPT1 COG1222
ATP-dependent 26S proteasome regulatory subunit [Posttranslational modification, protein ...
262-527 8.31e-100

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


Pssm-ID: 440835 [Multi-domain]  Cd Length: 326  Bit Score: 310.78  E-value: 8.31e-100
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325281  262 KSSEVADKSVDVAKTNVKFDDVCGCDEARAELEE-IVDFLKDPTKYESLGGKLPKGVLLTGPPGTGKTLLARATAGEAGV 340
Cdd:COG1222  59 RLGTPRGTAVPAESPDVTFDDIGGLDEQIEEIREaVELPLKNPELFRKYGIEPPKGVLLYGPPGTGKTLLAKAVAGELGA 138
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325281  341 DFFFMSGSEFDEVYVGVGAKRIRDLFAQARSRAPAIIFIDELDAIGGKR-NPKDQAYAKQTLNQLLVELDGFSQTSGIII 419
Cdd:COG1222 139 PFIRVRGSELVSKYIGEGARNVREVFELAREKAPSIIFIDEIDAIAARRtDDGTSGEVQRTVNQLLAELDGFESRGDVLI 218
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325281  420 IGATNFPEALDKALTRPGRFDKVVNVDLPDVRGRADILKHHMKKITLADNVDPTIIARGTPGLSGAELANLVNQAAVYAC 499
Cdd:COG1222 219 IAATNRPDLLDPALLRPGRFDRVIEVPLPDEEAREEILKIHLRDMPLADDVDLDKLAKLTEGFSGADLKAIVTEAGMFAI 298
                       250       260
                ....*....|....*....|....*...
gi 6325281  500 QKNAVSVDMSHFEWAKDKILMGAERKTM 527
Cdd:COG1222 299 REGRDTVTMEDLEKAIEKVKKKTETATN 326
RecA-like_FtsH cd19501
ATP-dependent zinc metalloprotease FtsH; FtsH ATPase is a processive, ATP-dependent zinc ...
278-445 5.18e-96

ATP-dependent zinc metalloprotease FtsH; FtsH ATPase is a processive, ATP-dependent zinc metallopeptidase for both cytoplasmic and membrane proteins. It is anchored to the cytoplasmic membrane such that the amino- and carboxy-termini are exposed to the cytoplasm. It presents a membrane-bound hexameric structure that is able to unfold and degrade protein substrates. It is comprised of an N-terminal transmembrane region and the larger C-terminal cytoplasmic region, which consists of an ATPase domain and a protease domain. This RecA-Like FTsH subfamily represents the ATPase domain, and belongs to the RecA-like NTPase family which includes the NTP binding domain of F1 and V1 H(+)ATPases, DnaB and related helicases as well as bacterial RecA and related eukaryotic and archaeal recombinases. The RecA-like NTPase family also includes bacterial conjugation proteins and related DNA transfer proteins involved in type II and type IV secretion.


Pssm-ID: 410909 [Multi-domain]  Cd Length: 171  Bit Score: 294.91  E-value: 5.18e-96
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325281  278 VKFDDVCGCDEARAELEEIVDFLKDPTKYESLGGKLPKGVLLTGPPGTGKTLLARATAGEAGVDFFFMSGSEFDEVYVGV 357
Cdd:cd19501   1 VTFKDVAGCEEAKEELKEVVEFLKNPEKFTKLGAKIPKGVLLVGPPGTGKTLLAKAVAGEAGVPFFSISGSDFVEMFVGV 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325281  358 GAKRIRDLFAQARSRAPAIIFIDELDAIGGKRNPK---DQAYAKQTLNQLLVELDGFSQTSGIIIIGATNFPEALDKALT 434
Cdd:cd19501  81 GASRVRDLFEQAKKNAPCIVFIDEIDAVGRKRGAGlggGHDEREQTLNQLLVEMDGFESNTGVIVIAATNRPDVLDPALL 160
                       170
                ....*....|.
gi 6325281  435 RPGRFDKVVNV 445
Cdd:cd19501 161 RPGRFDRQVYV 171
Peptidase_M41 pfam01434
Peptidase family M41;
527-706 2.83e-83

Peptidase family M41;


Pssm-ID: 460210 [Multi-domain]  Cd Length: 190  Bit Score: 262.54  E-value: 2.83e-83
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325281    527 MVLTDAARKATAFHEAGHAIMAKYTNGATPLYKATILPRGRALGITFQLPEMDKVDITKRECQARLDVCMGGKIAEELIY 606
Cdd:pfam01434   1 RVISEEEKKIVAYHEAGHALVGLLLPGADPVHKVTIIPRGQALGYTQFLPEEDKLLYTKEQLLARIAVLLGGRAAEELIF 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325281    607 GKdnTTSGCGSDLQSATGTARAMVTQYGMSDDVGPVNL---SENWES---------WSNKIRDIADNEVIELLKDSEERA 674
Cdd:pfam01434  81 GE--VTTGASNDLEKATKIARQMVTEFGMSDKLGPVSLeesDGNVFLgrgmgkrkpYSEETADIIDEEVKRLLEEAYERA 158
                         170       180       190
                  ....*....|....*....|....*....|..
gi 6325281    675 RRLLTKKNVELHRLAQGLIEYETLDAHEIEQV 706
Cdd:pfam01434 159 KEILTEHRDELEALAEALLEKETLDAEEIREL 190
PRK03992 PRK03992
proteasome-activating nucleotidase; Provisional
265-533 1.44e-81

proteasome-activating nucleotidase; Provisional


Pssm-ID: 179699 [Multi-domain]  Cd Length: 389  Bit Score: 265.16  E-value: 1.44e-81
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325281   265 EVADKSVDV--------AKTNVKFDDVCGCDEARAELEEIVDF-LKDPTKYESLGGKLPKGVLLTGPPGTGKTLLARATA 335
Cdd:PRK03992 107 EVLPSEKDPrvqameviESPNVTYEDIGGLEEQIREVREAVELpLKKPELFEEVGIEPPKGVLLYGPPGTGKTLLAKAVA 186
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325281   336 GEAGVDFFFMSGSEFDEVYVGVGAKRIRDLFAQARSRAPAIIFIDELDAIGGKRNPKD---QAYAKQTLNQLLVELDGFS 412
Cdd:PRK03992 187 HETNATFIRVVGSELVQKFIGEGARLVRELFELAREKAPSIIFIDEIDAIAAKRTDSGtsgDREVQRTLMQLLAEMDGFD 266
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325281   413 QTSGIIIIGATNFPEALDKALTRPGRFDKVVNVDLPDVRGRADILKHHMKKITLADNVDPTIIARGTPGLSGAELANLVN 492
Cdd:PRK03992 267 PRGNVKIIAATNRIDILDPAILRPGRFDRIIEVPLPDEEGRLEILKIHTRKMNLADDVDLEELAELTEGASGADLKAICT 346
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|.
gi 6325281   493 QAAVYACQKNAVSVDMSHFEWAKDKILMGAERKTMVLTDAA 533
Cdd:PRK03992 347 EAGMFAIRDDRTEVTMEDFLKAIEKVMGKEEKDSMEEPGVM 387
SpoVK COG0464
AAA+-type ATPase, SpoVK/Ycf46/Vps4 family [Cell wall/membrane/envelope biogenesis, Cell cycle ...
280-524 1.39e-76

AAA+-type ATPase, SpoVK/Ycf46/Vps4 family [Cell wall/membrane/envelope biogenesis, Cell cycle control, cell division, chromosome partitioning, Signal transduction mechanisms];


Pssm-ID: 440232 [Multi-domain]  Cd Length: 397  Bit Score: 252.52  E-value: 1.39e-76
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325281  280 FDDVCGCDEARAELEEIVD-FLKDPTKYESLGGKLPKGVLLTGPPGTGKTLLARATAGEAGVDFFFMSGSEFDEVYVGVG 358
Cdd:COG0464 156 LDDLGGLEEVKEELRELVAlPLKRPELREEYGLPPPRGLLLYGPPGTGKTLLARALAGELGLPLIEVDLSDLVSKYVGET 235
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325281  359 AKRIRDLFAQARSRAPAIIFIDELDAIGGKRNPKDQAYAKQTLNQLLVELDGFsqTSGIIIIGATNFPEALDKALTRpgR 438
Cdd:COG0464 236 EKNLREVFDKARGLAPCVLFIDEADALAGKRGEVGDGVGRRVVNTLLTEMEEL--RSDVVVIAATNRPDLLDPALLR--R 311
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325281  439 FDKVVNVDLPDVRGRADILKHHMKKITLADNVDPTIIARGTPGLSGAELANLVNQAAVYACQKNAVSVDMSHFEWAKDKI 518
Cdd:COG0464 312 FDEIIFFPLPDAEERLEIFRIHLRKRPLDEDVDLEELAEATEGLSGADIRNVVRRAALQALRLGREPVTTEDLLEALERE 391

                ....*.
gi 6325281  519 LMGAER 524
Cdd:COG0464 392 DIFLKR 397
26Sp45 TIGR01242
26S proteasome subunit P45 family; Many proteins may score above the trusted cutoff because an ...
275-519 2.97e-69

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: 231.61  E-value: 2.97e-69
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325281    275 KTNVKFDDVCGCDEARAELEEIVDF-LKDPTKYESLGGKLPKGVLLTGPPGTGKTLLARATAGEAGVDFFFMSGSEFDEV 353
Cdd:TIGR01242 116 RPNVSYEDIGGLEEQIREIREAVELpLKHPELFEEVGIEPPKGVLLYGPPGTGKTLLAKAVAHETNATFIRVVGSELVRK 195
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325281    354 YVGVGAKRIRDLFAQARSRAPAIIFIDELDAIGGKRNPKDQA---YAKQTLNQLLVELDGFSQTSGIIIIGATNFPEALD 430
Cdd:TIGR01242 196 YIGEGARLVREIFELAKEKAPSIIFIDEIDAIAAKRTDSGTSgdrEVQRTLMQLLAELDGFDPRGNVKVIAATNRPDILD 275
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325281    431 KALTRPGRFDKVVNVDLPDVRGRADILKHHMKKITLADNVDPTIIARGTPGLSGAELANLVNQAAVYACQKNAVSVDMSH 510
Cdd:TIGR01242 276 PALLRPGRFDRIIEVPLPDFEGRLEILKIHTRKMKLAEDVDLEAIAKMTEGASGADLKAICTEAGMFAIREERDYVTMDD 355

                  ....*....
gi 6325281    511 FEWAKDKIL 519
Cdd:TIGR01242 356 FIKAVEKVL 364
CDC48 TIGR01243
AAA family ATPase, CDC48 subfamily; This subfamily of the AAA family ATPases includes two ...
269-518 9.24e-63

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


Pssm-ID: 273521 [Multi-domain]  Cd Length: 733  Bit Score: 223.63  E-value: 9.24e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325281    269 KSVDVAKTNVKFDDVCGCDEARAELEEIVDF-LKDPTKYESLGGKLPKGVLLTGPPGTGKTLLARATAGEAGVDFFFMSG 347
Cdd:TIGR01243 441 REVLVEVPNVRWSDIGGLEEVKQELREAVEWpLKHPEIFEKMGIRPPKGVLLFGPPGTGKTLLAKAVATESGANFIAVRG 520
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325281    348 SEFDEVYVGVGAKRIRDLFAQARSRAPAIIFIDELDAIGGKRNPK-DQAYAKQTLNQLLVELDGFSQTSGIIIIGATNFP 426
Cdd:TIGR01243 521 PEILSKWVGESEKAIREIFRKARQAAPAIIFFDEIDAIAPARGARfDTSVTDRIVNQLLTEMDGIQELSNVVVIAATNRP 600
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325281    427 EALDKALTRPGRFDKVVNVDLPDVRGRADILKHHMKKITLADNVDPTIIARGTPGLSGAELANLVNQAAVYACQK----- 501
Cdd:TIGR01243 601 DILDPALLRPGRFDRLILVPPPDEEARKEIFKIHTRSMPLAEDVDLEELAEMTEGYTGADIEAVCREAAMAALREsigsp 680
                         250       260       270
                  ....*....|....*....|....*....|
gi 6325281    502 -------------NAVSVDMSHFEWAKDKI 518
Cdd:TIGR01243 681 akeklevgeeeflKDLKVEMRHFLEALKKV 710
RecA-like_protease cd19481
proteases similar to RecA; RecA-like NTPases. This family includes the NTP binding domain of ...
289-445 1.53e-62

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: 206.36  E-value: 1.53e-62
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325281  289 ARAELEEIVDFLKDPTKYESLGGKLPKGVLLTGPPGTGKTLLARATAGEAGVDFFFMSGSEFDEVYVGVGAKRIRDLFAQ 368
Cdd:cd19481   1 LKASLREAVEAPRRGSRLRRYGLGLPKGILLYGPPGTGKTLLAKALAGELGLPLIVVKLSSLLSKYVGESEKNLRKIFER 80
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 6325281  369 ARSRAPAIIFIDELDAIGGKR-NPKDQAYAKQTLNQLLVELDGFSQTSGIIIIGATNFPEALDKALTRPGRFDKVVNV 445
Cdd:cd19481  81 ARRLAPCILFIDEIDAIGRKRdSSGESGELRRVLNQLLTELDGVNSRSKVLVIAATNRPDLLDPALLRPGRFDEVIEF 158
CDC48 TIGR01243
AAA family ATPase, CDC48 subfamily; This subfamily of the AAA family ATPases includes two ...
250-501 7.75e-59

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


Pssm-ID: 273521 [Multi-domain]  Cd Length: 733  Bit Score: 212.46  E-value: 7.75e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325281    250 GFKYITENTTLlkssEVADKSVDVAKT----NVKFDDVCGCDEARAELEEIVDF-LKDPTKYESLGGKLPKGVLLTGPPG 324
Cdd:TIGR01243 147 GFVYVTEATEV----EIREKPVREEIErkvpKVTYEDIGGLKEAKEKIREMVELpMKHPELFEHLGIEPPKGVLLYGPPG 222
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325281    325 TGKTLLARATAGEAGVDFFFMSGSEFDEVYVGVGAKRIRDLFAQARSRAPAIIFIDELDAIGGKRNPKDQAYAKQTLNQL 404
Cdd:TIGR01243 223 TGKTLLAKAVANEAGAYFISINGPEIMSKYYGESEERLREIFKEAEENAPSIIFIDEIDAIAPKREEVTGEVEKRVVAQL 302
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325281    405 LVELDGFSQTSGIIIIGATNFPEALDKALTRPGRFDKVVNVDLPDVRGRADILKHHMKKITLADNVDPTIIARGTPGLSG 484
Cdd:TIGR01243 303 LTLMDGLKGRGRVIVIGATNRPDALDPALRRPGRFDREIVIRVPDKRARKEILKVHTRNMPLAEDVDLDKLAEVTHGFVG 382
                         250
                  ....*....|....*..
gi 6325281    485 AELANLVNQAAVYACQK 501
Cdd:TIGR01243 383 ADLAALAKEAAMAALRR 399
COG1223 COG1223
Predicted ATPase, AAA+ superfamily [General function prediction only];
280-518 3.91e-58

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


Pssm-ID: 440836 [Multi-domain]  Cd Length: 246  Bit Score: 197.80  E-value: 3.91e-58
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325281  280 FDDVCGCDEARAELEEIVDFLKDPTKYESLGGKLPKGVLLTGPPGTGKTLLARATAGEAGVDFFFMSGSEFDEVYVGVGA 359
Cdd:COG1223   1 LDDVVGQEEAKKKLKLIIKELRRRENLRKFGLWPPRKILFYGPPGTGKTMLAEALAGELKLPLLTVRLDSLIGSYLGETA 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325281  360 KRIRDLFAQARsRAPAIIFIDELDAIGGKR-NPKDQAYAKQTLNQLLVELDGFSqtSGIIIIGATNFPEALDKALTRpgR 438
Cdd:COG1223  81 RNLRKLFDFAR-RAPCVIFFDEFDAIAKDRgDQNDVGEVKRVVNALLQELDGLP--SGSVVIAATNHPELLDSALWR--R 155
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325281  439 FDKVVNVDLPDVRGRADILKHHMKKITLADNVDPTIIARGTPGLSGAELANLVNQAAVYACQKNAVSVDMSHFEWAKDKI 518
Cdd:COG1223 156 FDEVIEFPLPDKEERKEILELNLKKFPLPFELDLKKLAKKLEGLSGADIEKVLKTALKKAILEDREKVTKEDLEEALKQR 235
RecA-like_PAN_like cd19502
proteasome activating nucleotidase PAN and related proteasome subunits; This subfamily ...
280-445 9.72e-57

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


Pssm-ID: 410910 [Multi-domain]  Cd Length: 171  Bit Score: 191.01  E-value: 9.72e-57
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325281  280 FDDVCGCDEARAELEEIVDF-LKDPTKYESLGGKLPKGVLLTGPPGTGKTLLARATAGEAGVDFFFMSGSEFDEVYVGVG 358
Cdd:cd19502   2 YEDIGGLDEQIREIREVVELpLKHPELFEELGIEPPKGVLLYGPPGTGKTLLAKAVANHTDATFIRVVGSELVQKYIGEG 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325281  359 AKRIRDLFAQARSRAPAIIFIDELDAIGGKR---NPKDQAYAKQTLNQLLVELDGFSQTSGIIIIGATNFPEALDKALTR 435
Cdd:cd19502  82 ARLVRELFEMAREKAPSIIFIDEIDAIGAKRfdsGTGGDREVQRTMLELLNQLDGFDPRGNIKVIMATNRPDILDPALLR 161
                       170
                ....*....|
gi 6325281  436 PGRFDKVVNV 445
Cdd:cd19502 162 PGRFDRKIEF 171
RecA-like_CDC48_NLV2_r1-like cd19503
first of two ATPase domains of CDC48 and NLV2, and similar ATPase domains; CDC48 in yeast and ...
282-443 2.05e-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: 187.11  E-value: 2.05e-55
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325281  282 DVCGCDEARAELEEIVDF-LKDPTKYESLGGKLPKGVLLTGPPGTGKTLLARATAGEAGVDFFFMSGSEFDEVYVGVGAK 360
Cdd:cd19503   1 DIGGLDEQIASLKELIELpLKYPELFRALGLKPPRGVLLHGPPGTGKTLLARAVANEAGANFLSISGPSIVSKYLGESEK 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325281  361 RIRDLFAQARSRAPAIIFIDELDAIGGKRNPKDQAYAKQTLNQLLVELDGFSQTSGIIIIGATNFPEALDKALTRPGRFD 440
Cdd:cd19503  81 NLREIFEEARSHAPSIIFIDEIDALAPKREEDQREVERRVVAQLLTLMDGMSSRGKVVVIAATNRPDAIDPALRRPGRFD 160

                ...
gi 6325281  441 KVV 443
Cdd:cd19503 161 REV 163
RecA-like_CDC48_r2-like cd19511
second of two ATPase domains of CDC48/p97, PEX1 and -6, VAT and NVL, and similar ATPase ...
292-445 3.60e-52

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: 178.25  E-value: 3.60e-52
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325281  292 ELEEIVDF-LKDPTKYESLGGKLPKGVLLTGPPGTGKTLLARATAGEAGVDFFFMSGSEFDEVYVGVGAKRIRDLFAQAR 370
Cdd:cd19511   4 ELKEAVEWpLKHPDAFKRLGIRPPKGVLLYGPPGCGKTLLAKALASEAGLNFISVKGPELFSKYVGESERAVREIFQKAR 83
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 6325281  371 SRAPAIIFIDELDAIGGKR-NPKDQAYAKQTLNQLLVELDGFSQTSGIIIIGATNFPEALDKALTRPGRFDKVVNV 445
Cdd:cd19511  84 QAAPCIIFFDEIDSLAPRRgQSDSSGVTDRVVSQLLTELDGIESLKGVVVIAATNRPDMIDPALLRPGRLDKLIYV 159
AAA pfam00004
ATPase family associated with various cellular activities (AAA); AAA family proteins often ...
317-447 5.76e-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: 173.93  E-value: 5.76e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325281    317 VLLTGPPGTGKTLLARATAGEAGVDFFFMSGSEFDEVYVGVGAKRIRDLFAQARSRAPAIIFIDELDAIGGKRNPKDQAY 396
Cdd:pfam00004   1 LLLYGPPGTGKTTLAKAVAKELGAPFIEISGSELVSKYVGESEKRLRELFEAAKKLAPCVIFIDEIDALAGSRGSGGDSE 80
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 6325281    397 AKQTLNQLLVELDGFSQ-TSGIIIIGATNFPEALDKALtrPGRFDKVVNVDL 447
Cdd:pfam00004  81 SRRVVNQLLTELDGFTSsNSKVIVIAATNRPDKLDPAL--LGRFDRIIEFPL 130
PTZ00361 PTZ00361
26 proteosome regulatory subunit 4-like protein; Provisional
280-519 8.75e-50

26 proteosome regulatory subunit 4-like protein; Provisional


Pssm-ID: 185575 [Multi-domain]  Cd Length: 438  Bit Score: 180.74  E-value: 8.75e-50
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325281   280 FDDVCGCDEARAELEEIVDF-LKDPTKYESLGGKLPKGVLLTGPPGTGKTLLARATAGEAGVDFFFMSGSEFDEVYVGVG 358
Cdd:PTZ00361 182 YADIGGLEQQIQEIKEAVELpLTHPELYDDIGIKPPKGVILYGPPGTGKTLLAKAVANETSATFLRVVGSELIQKYLGDG 261
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325281   359 AKRIRDLFAQARSRAPAIIFIDELDAIGGKRNPKDQAYAKQ---TLNQLLVELDGFSQTSGIIIIGATNFPEALDKALTR 435
Cdd:PTZ00361 262 PKLVRELFRVAEENAPSIVFIDEIDAIGTKRYDATSGGEKEiqrTMLELLNQLDGFDSRGDVKVIMATNRIESLDPALIR 341
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325281   436 PGRFDKVVNVDLPDVRGRADILKHHMKKITLADNVDPTIIARGTPGLSGAELANLVNQAAVYACQKNAVSVDMSHFEWAK 515
Cdd:PTZ00361 342 PGRIDRKIEFPNPDEKTKRRIFEIHTSKMTLAEDVDLEEFIMAKDELSGADIKAICTEAGLLALRERRMKVTQADFRKAK 421

                 ....
gi 6325281   516 DKIL 519
Cdd:PTZ00361 422 EKVL 425
PTZ00454 PTZ00454
26S protease regulatory subunit 6B-like protein; Provisional
267-512 4.89e-49

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


Pssm-ID: 240423 [Multi-domain]  Cd Length: 398  Bit Score: 177.65  E-value: 4.89e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325281   267 ADKSVDVA----KTNVKFDDVCGCDEARAELEEIVDF-LKDPTKYESLGGKLPKGVLLTGPPGTGKTLLARATAGEAGVD 341
Cdd:PTZ00454 127 ADSSIQLLqmseKPDVTYSDIGGLDIQKQEIREAVELpLTCPELYEQIGIDPPRGVLLYGPPGTGKTMLAKAVAHHTTAT 206
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325281   342 FFFMSGSEFDEVYVGVGAKRIRDLFAQARSRAPAIIFIDELDAIGGKRNPKdQAYAKQTLNQLLVEL----DGFSQTSGI 417
Cdd:PTZ00454 207 FIRVVGSEFVQKYLGEGPRMVRDVFRLARENAPSIIFIDEVDSIATKRFDA-QTGADREVQRILLELlnqmDGFDQTTNV 285
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325281   418 IIIGATNFPEALDKALTRPGRFDKVVNVDLPDVRGRADILKHHMKKITLADNVDPTIIARGTPGLSGAELANLVNQAAVY 497
Cdd:PTZ00454 286 KVIMATNRADTLDPALLRPGRLDRKIEFPLPDRRQKRLIFQTITSKMNLSEEVDLEDFVSRPEKISAADIAAICQEAGMQ 365
                        250
                 ....*....|....*
gi 6325281   498 ACQKNAVSVDMSHFE 512
Cdd:PTZ00454 366 AVRKNRYVILPKDFE 380
RecA-like_CDC48_r1-like cd19519
first of two ATPase domains of CDC48 and similar ATPase domains; CDC48 in yeast and p97 or VCP ...
282-445 5.53e-47

first of two ATPase domains of CDC48 and similar ATPase domains; CDC48 in yeast and p97 or VCP metazoans is an ATP-dependent molecular chaperone which plays an essential role in many cellular processes, by segregating polyubiquitinated proteins from complexes or membranes. Cdc48/p97 consists of an N-terminal domain and two ATPase domains; this subfamily represents the first of the two ATPase domains. CDC48's roles include in the fragmentation of Golgi stacks during mitosis and for their reassembly after mitosis, and in the formation of the nuclear envelope, and of the transitional endoplasmic reticulum (tER). This RecA-like_cdc48_r1-like subfamily belongs to the RecA-like family which includes the NTP binding domain of F1 and V1 H(+)ATPases, DnaB and related helicases as well as bacterial RecA and related eukaryotic and archaeal recombinases. The RecA-like NTPase family also includes bacterial conjugation proteins and related DNA transfer proteins involved in type II and type IV secretion.


Pssm-ID: 410927 [Multi-domain]  Cd Length: 166  Bit Score: 164.15  E-value: 5.53e-47
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325281  282 DVCGCDEARAELEEIVDF-LKDPTKYESLGGKLPKGVLLTGPPGTGKTLLARATAGEAGVDFFFMSGSEFDEVYVGVGAK 360
Cdd:cd19519   1 DIGGCRKQLAQIREMVELpLRHPELFKAIGIKPPRGILLYGPPGTGKTLIARAVANETGAFFFLINGPEIMSKLAGESES 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325281  361 RIRDLFAQARSRAPAIIFIDELDAIGGKRNPKDQAYAKQTLNQLLVELDGFSQTSGIIIIGATNFPEALDKALTRPGRFD 440
Cdd:cd19519  81 NLRKAFEEAEKNAPAIIFIDEIDAIAPKREKTHGEVERRIVSQLLTLMDGLKQRAHVIVMAATNRPNSIDPALRRFGRFD 160

                ....*
gi 6325281  441 KVVNV 445
Cdd:cd19519 161 REIDI 165
RecA-like_VCP_r2 cd19529
second of two ATPase domains of Valosin-containing protein-like ATPase (VAT) and similar ...
289-445 1.68e-46

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: 162.66  E-value: 1.68e-46
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325281  289 ARAELEEIVDF-LKDPTKYESLGGKLPKGVLLTGPPGTGKTLLARATAGEAGVDFFFMSGSEFDEVYVGVGAKRIRDLFA 367
Cdd:cd19529   1 VKQELKEAVEWpLLKPEVFKRLGIRPPKGILLYGPPGTGKTLLAKAVATESNANFISVKGPELLSKWVGESEKAIREIFR 80
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 6325281  368 QARSRAPAIIFIDELDAIGGKRNPK-DQAYAKQTLNQLLVELDGFSQTSGIIIIGATNFPEALDKALTRPGRFDKVVNV 445
Cdd:cd19529  81 KARQVAPCVIFFDEIDSIAPRRGTTgDSGVTERVVNQLLTELDGLEEMNGVVVIAATNRPDIIDPALLRAGRFDRLIYI 159
RecA-like_NVL_r2-like cd19530
second of two ATPase domains of NVL (nuclear VCP-like protein) and similar ATPase domains; NVL ...
287-445 1.87e-44

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: 156.88  E-value: 1.87e-44
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325281  287 DEARAELE-EIVDFLKDPTKYESLGGKLPKGVLLTGPPGTGKTLLARATAGEAGVDFFFMSGSEFDEVYVGVGAKRIRDL 365
Cdd:cd19530   2 DHVREELTmSILRPIKRPDIYKALGIDLPTGVLLYGPPGCGKTLLAKAVANESGANFISVKGPELLNKYVGESERAVRQV 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325281  366 FAQARSRAPAIIFIDELDAIGGKRNPKDQAYAKQTLNQLLVELDGFSQTSGIIIIGATNFPEALDKALTRPGRFDKVVNV 445
Cdd:cd19530  82 FQRARASAPCVIFFDEVDALVPKRGDGGSWASERVVNQLLTEMDGLEERSNVFVIAATNRPDIIDPAMLRPGRLDKTLYV 161
RecA-like_NVL_r1-like cd19518
first of two ATPase domains of NVL (nuclear VCP-like protein) and similar ATPase domains; NVL ...
282-441 1.39e-43

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


Pssm-ID: 410926 [Multi-domain]  Cd Length: 169  Bit Score: 154.87  E-value: 1.39e-43
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325281  282 DVCGCDEARAELEEIVDFLK-DPTKYESLGGKLPKGVLLTGPPGTGKTLLARATAGEAGVDFFFMSGSEFDEVYVGVGAK 360
Cdd:cd19518   1 DIGGMDSTLKELCELLIHPIlPPEYFQHLGVEPPRGVLLHGPPGCGKTMLANAIAGELKVPFLKISATEIVSGVSGESEE 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325281  361 RIRDLFAQARSRAPAIIFIDELDAIGGKRNPKDQAYAKQTLNQLLVELDGF----SQTSGIIIIGATNFPEALDKALTRP 436
Cdd:cd19518  81 KIRELFDQAISNAPCIVFIDEIDAITPKRESAQREMERRIVSQLLTCMDELnnekTAGGPVLVIGATNRPDSLDPALRRA 160

                ....*
gi 6325281  437 GRFDK 441
Cdd:cd19518 161 GRFDR 165
RecA-like_CDC48_r2-like cd19528
second of two ATPase domains of CDC48 and similar ATPase domains; CDC48 in yeast and p97 or ...
290-445 3.90e-42

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: 150.74  E-value: 3.90e-42
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325281  290 RAELEEIVDF-LKDPTKYESLGGKLPKGVLLTGPPGTGKTLLARATAGEAGVDFFFMSGSEFDEVYVGVGAKRIRDLFAQ 368
Cdd:cd19528   2 KRELQELVQYpVEHPDKFLKFGMTPSKGVLFYGPPGCGKTLLAKAIANECQANFISVKGPELLTMWFGESEANVRDIFDK 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325281  369 ARSRAPAIIFIDELDAIGGKRNPK---DQAYAKQTLNQLLVELDGFSQTSGIIIIGATNFPEALDKALTRPGRFDKVVNV 445
Cdd:cd19528  82 ARAAAPCVLFFDELDSIAKARGGNigdAGGAADRVINQILTEMDGMNTKKNVFIIGATNRPDIIDPAILRPGRLDQLIYI 161
RecA-like_VPS4-like cd19509
ATPase domain of VPS4, ATAD1, K, KTNA1, Spastin, FIGL-1 and similar ATPase domains; This ...
283-441 1.21e-39

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: 143.65  E-value: 1.21e-39
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325281  283 VCGCDEARAELEEIVDF-LKDPTKYeSLGGKLPKGVLLTGPPGTGKTLLARATAGEAGVDFFFMSGSEFDEVYVGVGAKR 361
Cdd:cd19509   1 IAGLDDAKEALKEAVILpSLRPDLF-PGLRGPPRGILLYGPPGTGKTLLARAVASESGSTFFSISASSLVSKWVGESEKI 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325281  362 IRDLFAQARSRAPAIIFIDELDAIGGKRNPKDQAYAKQTLNQLLVELDGF--SQTSGIIIIGATNFPEALDKALTRpgRF 439
Cdd:cd19509  80 VRALFALARELQPSIIFIDEIDSLLSERGSGEHEASRRVKTEFLVQMDGVlnKPEDRVLVLGATNRPWELDEAFLR--RF 157

                ..
gi 6325281  440 DK 441
Cdd:cd19509 158 EK 159
RecA-like_PEX1_r2 cd19526
second of two ATPase domains of Peroxisomal biogenesis factor 1 (PEX1); PEX1(also known as ...
289-443 1.47e-39

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: 143.34  E-value: 1.47e-39
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325281  289 ARAELEEIVDF-LKDPTKYESLGGKLPKGVLLTGPPGTGKTLLARATAGEAGVDFFFMSGSEFDEVYVGVGAKRIRDLFA 367
Cdd:cd19526   1 VKKALEETIEWpSKYPKIFASSPLRLRSGILLYGPPGCGKTLLASAIASECGLNFISVKGPELLNKYIGASEQNVRDLFS 80
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 6325281  368 QARSRAPAIIFIDELDAIGGKRNPKDQAYAKQTLNQLLVELDGFSQTSGIIIIGATNFPEALDKALTRPGRFDKVV 443
Cdd:cd19526  81 RAQSAKPCILFFDEFDSIAPKRGHDSTGVTDRVVNQLLTQLDGVEGLDGVYVLAATSRPDLIDPALLRPGRLDKLV 156
RecA-like_PEX6_r2 cd19527
second of two ATPase domains of Peroxisomal biogenesis factor 6 (PEX6); PEX6(also known as ...
295-445 1.40e-37

second of two ATPase domains of Peroxisomal biogenesis factor 6 (PEX6); PEX6(also known as Peroxin61)/PEX1 is a protein unfoldase; PEX6 and PEX1 form a heterohexameric Type-2 AAA-ATPase complex and are essential for peroxisome biogenesis as they are required for the import of folded proteins into the peroxisomal matrix. This subfamily represents the second ATPase domain of PEX6. This subfamily belongs to the RecA-like NTPase family which includes the NTP binding domain of F1 and V1 H(+)ATPases, DnaB and related helicases as well as bacterial RecA and related eukaryotic and archaeal recombinases. The RecA-like NTPase family also includes bacterial conjugation proteins and related DNA transfer proteins involved in type II and type IV secretion.


Pssm-ID: 410935 [Multi-domain]  Cd Length: 160  Bit Score: 137.64  E-value: 1.40e-37
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325281  295 EIVDFLKDPTKYE---SLGGKLPKGVLLTGPPGTGKTLLARATAGEAGVDFFFMSGSEFDEVYVGVGAKRIRDLFAQARS 371
Cdd:cd19527   4 EILDTIQLPLEHPelfSSGLRKRSGILLYGPPGTGKTLLAKAIATECSLNFLSVKGPELINMYIGESEANVREVFQKARD 83
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 6325281  372 RAPAIIFIDELDAIGGKR-NPKDQ-AYAKQTLNQLLVELDGFSQTS-GIIIIGATNFPEALDKALTRPGRFDKVVNV 445
Cdd:cd19527  84 AKPCVIFFDELDSLAPSRgNSGDSgGVMDRVVSQLLAELDGMSSSGqDVFVIGATNRPDLLDPALLRPGRFDKLLYL 160
RecA-like_VPS4 cd19521
ATPase domain of vacuolar protein sorting-associated protein 4; Vacuolar protein ...
275-441 4.95e-37

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


Pssm-ID: 410929 [Multi-domain]  Cd Length: 170  Bit Score: 136.53  E-value: 4.95e-37
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325281  275 KTNVKFDDVCGCDEARAELEEIVDFlkdPTKYESL--GGKLP-KGVLLTGPPGTGKTLLARATAGEAGVDFFFMSGSEFD 351
Cdd:cd19521   1 KPNVKWEDVAGLEGAKEALKEAVIL---PVKFPHLftGNRKPwSGILLYGPPGTGKSYLAKAVATEANSTFFSVSSSDLV 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325281  352 EVYVGVGAKRIRDLFAQARSRAPAIIFIDELDAIGGKRNPKDQAYAKQTLNQLLVELDGFSQ-TSGIIIIGATNFPEALD 430
Cdd:cd19521  78 SKWMGESEKLVKQLFAMARENKPSIIFIDEVDSLCGTRGEGESEASRRIKTELLVQMNGVGNdSQGVLVLGATNIPWQLD 157
                       170
                ....*....|.
gi 6325281  431 KALTRpgRFDK 441
Cdd:cd19521 158 SAIRR--RFEK 166
RecA-like_Figl-1 cd19525
ATPase domain of Fidgetin-Like 1 (FIGL-1); FIGL-1 may participate in DNA repair in the nucleus; ...
278-441 4.56e-35

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: 131.65  E-value: 4.56e-35
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325281  278 VKFDDVCGCDEARAELEEIVDF-LKDPTKYESLGGKlPKGVLLTGPPGTGKTLLARATAGEAGVDFFFMSGSEFDEVYVG 356
Cdd:cd19525  19 INWADIAGLEFAKKTIKEIVVWpMLRPDIFTGLRGP-PKGILLFGPPGTGKTLIGKCIASQSGATFFSISASSLTSKWVG 97
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325281  357 VGAKRIRDLFAQARSRAPAIIFIDELDAIGGKRNPKDQAYAKQTLNQLLVELDGFSQTSG--IIIIGATNFPEALDKALT 434
Cdd:cd19525  98 EGEKMVRALFSVARCKQPAVIFIDEIDSLLSQRGEGEHESSRRIKTEFLVQLDGATTSSEdrILVVGATNRPQEIDEAAR 177

                ....*..
gi 6325281  435 RpgRFDK 441
Cdd:cd19525 178 R--RLVK 182
RecA-like_Yta7-like cd19517
ATPase domain of Saccharomyces cerevisiae Yta7 and similar ATPase domains; Saccharomyces ...
282-441 2.14e-33

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


Pssm-ID: 410925 [Multi-domain]  Cd Length: 170  Bit Score: 126.08  E-value: 2.14e-33
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325281  282 DVCGCDEARAELEEIVDF-LKDPTKYESLGGKLPKGVLLTGPPGTGKTLLARATAGEAG-----VDFFFMSGSEFDEVYV 355
Cdd:cd19517   1 DIGGLSHYINQLKEMVFFpLLYPEVFAKFKITPPRGVLFHGPPGTGKTLMARALAAECSkggqkVSFFMRKGADCLSKWV 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325281  356 GVGAKRIRDLFAQARSRAPAIIFIDELDAIGGKRNPKDQAYAKQTLNQLLVELDGFSQTSGIIIIGATNFPEALDKALTR 435
Cdd:cd19517  81 GEAERQLRLLFEEAYRMQPSIIFFDEIDGLAPVRSSKQEQIHASIVSTLLALMDGLDNRGQVVVIGATNRPDALDPALRR 160

                ....*.
gi 6325281  436 PGRFDK 441
Cdd:cd19517 161 PGRFDR 166
RecA-like_ATAD1 cd19520
ATPase domain of ATPase family AAA domain-containing protein 1 and similar ATPase domains; ...
282-439 6.56e-33

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: 124.84  E-value: 6.56e-33
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325281  282 DVCGCDEARAELEEIVDF-LKDPTKYESlgGKL---PKGVLLTGPPGTGKTLLARATAGEAGVDFFFMSGSEFDEVYVGV 357
Cdd:cd19520   1 DIGGLDEVITELKELVILpLQRPELFDN--SRLlqpPKGVLLYGPPGCGKTMLAKATAKEAGARFINLQVSSLTDKWYGE 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325281  358 GAKRIRDLFAQARSRAPAIIFIDELDAIGGKRNPKDQAYAKQTLNQLLVELDGFS--QTSGIIIIGATNFPEALDKALTR 435
Cdd:cd19520  79 SQKLVAAVFSLASKLQPSIIFIDEIDSFLRQRSSTDHEATAMMKAEFMSLWDGLStdGNCRVIVMGATNRPQDLDEAILR 158

                ....*.
gi 6325281  436 --PGRF 439
Cdd:cd19520 159 rmPKRF 164
RecA-like_spastin cd19524
ATPase domain of spastin; Spastin is an ATP-dependent microtubule-severing protein involved in ...
282-445 6.67e-32

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: 121.88  E-value: 6.67e-32
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325281  282 DVCGCDEARAELEEIVDFlkdPTKYESLGGKL---PKGVLLTGPPGTGKTLLARATAGEAGVDFFFMSGSEFDEVYVGVG 358
Cdd:cd19524   1 DIAGQDLAKQALQEMVIL---PSLRPELFTGLrapARGLLLFGPPGNGKTMLAKAVAAESNATFFNISAASLTSKYVGEG 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325281  359 AKRIRDLFAQARSRAPAIIFIDELDAIGGKRNPKDQAYAKQTLNQLLVELDGFSQTSG--IIIIGATNFPEALDKALTRp 436
Cdd:cd19524  78 EKLVRALFAVARELQPSIIFIDEVDSLLSERSEGEHEASRRLKTEFLIEFDGVQSNGDdrVLVMGATNRPQELDDAVLR- 156

                ....*....
gi 6325281  437 gRFDKVVNV 445
Cdd:cd19524 157 -RFTKRVYV 164
RecA-like_KTNA1 cd19522
Katanin p60 ATPase-containing subunit A1; Katanin p60 ATPase-containing subunit A1 (KTNA1) is ...
282-441 2.48e-31

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: 120.47  E-value: 2.48e-31
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325281  282 DVCGCDEARAELEEIV-------DFLKdptkyeslGGKLP-KGVLLTGPPGTGKTLLARATAGEAGVDFFFMSGSEFDEV 353
Cdd:cd19522   1 DIADLEEAKKLLEEAVvlpmwmpEFFK--------GIRRPwKGVLMVGPPGTGKTLLAKAVATECGTTFFNVSSSTLTSK 72
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325281  354 YVGVGAKRIRDLFAQARSRAPAIIFIDELDAIGGKRNPKDQAYA-KQTLNQLLVELDGFSQTSG-------IIIIGATNF 425
Cdd:cd19522  73 YRGESEKLVRLLFEMARFYAPTTIFIDEIDSICSRRGTSEEHEAsRRVKSELLVQMDGVGGASEnddpskmVMVLAATNF 152
                       170
                ....*....|....*.
gi 6325281  426 PEALDKALTRpgRFDK 441
Cdd:cd19522 153 PWDIDEALRR--RLEK 166
RecA-like_NSF-SEC18_r1-like cd19504
first of two ATPase domains of NSF and SEC18, and similar ATPase domains; ...
303-440 2.36e-26

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: 106.42  E-value: 2.36e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325281  303 PTKYESLGGKLPKGVLLTGPPGTGKTLLARA-----TAGEAGVdfffMSGSEFDEVYVGVGAKRIRDLFAQA----RSRA 373
Cdd:cd19504  24 PEIVEQLGCKHVKGILLYGPPGTGKTLMARQigkmlNAREPKI----VNGPEILNKYVGESEANIRKLFADAeeeqRRLG 99
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 6325281  374 PA----IIFIDELDAIGGKRNPK--DQAYAKQTLNQLLVELDGFSQTSGIIIIGATNFPEALDKALTRPGRFD 440
Cdd:cd19504 100 ANsglhIIIFDEIDAICKQRGSMagSTGVHDTVVNQLLSKIDGVEQLNNILVIGMTNRKDLIDEALLRPGRLE 172
AAA cd00009
The AAA+ (ATPases Associated with a wide variety of cellular Activities) superfamily ...
314-447 3.73e-26

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


Pssm-ID: 99707 [Multi-domain]  Cd Length: 151  Bit Score: 104.92  E-value: 3.73e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325281  314 PKGVLLTGPPGTGKTLLARATAGEA---GVDFFFMSGSEFDEVYVG---VGAKRIRDLFAQARSRAPAIIFIDELDAIGG 387
Cdd:cd00009  19 PKNLLLYGPPGTGKTTLARAIANELfrpGAPFLYLNASDLLEGLVVaelFGHFLVRLLFELAEKAKPGVLFIDEIDSLSR 98
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325281  388 KRNpkdqayaKQTLNQLLVELDGFSQTSGIIIIGATNFPEALDKALTRPGRFDKVVNVDL 447
Cdd:cd00009  99 GAQ-------NALLRVLETLNDLRIDRENVRVIGATNRPLLGDLDRALYDRLDIRIVIPL 151
RecA-like_fidgetin cd19523
ATPase domain of fidgetin; Fidgetin (FIGN) is a ATP-dependent microtubule severing protein. ...
282-441 2.05e-24

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: 100.34  E-value: 2.05e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325281  282 DVCGCDEARAEL-EEIVDFLKDPTKYESLGgKLPKGVLLTGPPGTGKTLLARATAGEAGVDFFFMSGSEFDEVYVGVGAK 360
Cdd:cd19523   1 DIAGLGALKAAIkEEVLWPLLRPDAFSGLL-RLPRSILLFGPRGTGKTLLGRCLASQLGATFLRLRGSTLVAKWAGEGEK 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325281  361 RIRDLFAQARSRAPAIIFIDELDAIGGKRNpKDQAYAKQTLNQLLVELDGF--SQTSGIIIIGATNFPEALDKALTRpgR 438
Cdd:cd19523  80 ILQASFLAARCRQPSVLFISDLDALLSSQD-DEASPVGRLQVELLAQLDGVlgSGEDGVLVVCTTSKPEEIDESLRR--Y 156

                ...
gi 6325281  439 FDK 441
Cdd:cd19523 157 FSK 159
RecA-like_BCS1 cd19510
Mitochondrial chaperone BCS1; Mitochondrial chaperone BCS1 is necessary for the assembly of ...
293-440 3.38e-22

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


Pssm-ID: 410918 [Multi-domain]  Cd Length: 153  Bit Score: 93.57  E-value: 3.38e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325281  293 LEEIVDFLKDPTKYESLGGKLPKGVLLTGPPGTGKTLLARATAGEAGVDFFFMSGSEfdevyVGVGAKRIRDLFaqarSR 372
Cdd:cd19510   2 IDDLKDFIKNEDWYNDRGIPYRRGYLLYGPPGTGKSSFIAALAGELDYDICDLNLSE-----VVLTDDRLNHLL----NT 72
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 6325281  373 AP--AIIFIDELD-AIGGKRNPKDQAYAKQ-----TLNQLLVELDGFSQTSGIIIIGATNFPEALDKALTRPGRFD 440
Cdd:cd19510  73 APkqSIILLEDIDaAFESREHNKKNPSAYGglsrvTFSGLLNALDGVASSEERIVFMTTNHIERLDPALIRPGRVD 148
AAA smart00382
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ...
314-449 2.08e-19

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


Pssm-ID: 214640 [Multi-domain]  Cd Length: 148  Bit Score: 85.50  E-value: 2.08e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325281     314 PKGVLLTGPPGTGKTLLARATAGEA---GVDFFFMSGSEFDEV--------------YVGVGAKRIRDLFAQARSRAPAI 376
Cdd:smart00382   2 GEVILIVGPPGSGKTTLARALARELgppGGGVIYIDGEDILEEvldqllliivggkkASGSGELRLRLALALARKLKPDV 81
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 6325281     377 IFIDELDAIggkrnPKDQAYAKQTLNQLLVELDGFSQTSGIIIIGATNFPEALDKALTRPgRFDKVVNVDLPD 449
Cdd:smart00382  82 LILDEITSL-----LDAEQEALLLLLEELRLLLLLKSEKNLTVILTTNDEKDLGPALLRR-RFDRRIVLLLIL 148
RecA-like_Ycf46-like cd19507
ATPase domain of Ycf46 and similar ATPase domains; Ycf46 may play a role in the regulation of ...
313-442 2.45e-15

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: 73.94  E-value: 2.45e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325281  313 LPKGVLLTGPPGTGKTLLARATAGEAGVDFFFMSGSEFDEVYVGVGAKRIRDLFAQARSRAPAIIFIDELD-AIGGKRNP 391
Cdd:cd19507  30 TPKGLLLVGIQGTGKSLTAKAIAGVWQLPLLRLDMGRLFGGLVGESESRLRQMIQTAEAIAPCVLWIDEIEkGFSNADSK 109
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|.
gi 6325281  392 KDQAYAKQTLNQLLVELDgfSQTSGIIIIGATNFPEALDKALTRPGRFDKV 442
Cdd:cd19507 110 GDSGTSSRVLGTFLTWLQ--EKKKPVFVVATANNVQSLPPELLRKGRFDEI 158
RecA-like_ATAD3-like cd19512
ATPase domains of ATPase AAA-domain protein 3A (ATAD3A), -3B, and -3C, and similar ATPase ...
315-443 1.01e-14

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: 72.17  E-value: 1.01e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325281  315 KGVLLTGPPGTGKTLLARATAGEAGVDFFFMSGSefDEVYVGV-GAKRIRDLFAQA-RSRAPAIIFIDELDAIGGKRNPK 392
Cdd:cd19512  23 RNILFYGPPGTGKTLFAKKLALHSGMDYAIMTGG--DVAPMGReGVTAIHKVFDWAnTSRRGLLLFVDEADAFLRKRSTE 100
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|..
gi 6325281  393 DQAYA-KQTLNQLLVELDgfSQTSGIIIIGATNFPEALDKALTrpGRFDKVV 443
Cdd:cd19512 101 KISEDlRAALNAFLYRTG--EQSNKFMLVLASNQPEQFDWAIN--DRIDEMV 148
ycf46 CHL00195
Ycf46; Provisional
276-487 1.59e-14

Ycf46; Provisional


Pssm-ID: 177094 [Multi-domain]  Cd Length: 489  Bit Score: 76.98  E-value: 1.59e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325281   276 TNVKFDDVCGcdearaeLEEIVDFLKDPT-----KYESLGGKLPKGVLLTGPPGTGKTLLARATAGEAG-----VDFffm 345
Cdd:CHL00195 223 VNEKISDIGG-------LDNLKDWLKKRStsfskQASNYGLPTPRGLLLVGIQGTGKSLTAKAIANDWQlpllrLDV--- 292
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325281   346 sGSEFDEVyVGVGAKRIRDLFAQARSRAPAIIFIDELD-AIGGKRNPKDQAYAKQTLNQLLVELDgfSQTSGIIIIGATN 424
Cdd:CHL00195 293 -GKLFGGI-VGESESRMRQMIRIAEALSPCILWIDEIDkAFSNSESKGDSGTTNRVLATFITWLS--EKKSPVFVVATAN 368
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 6325281   425 FPEALDKALTRPGRFDKVVNVDLPDVRGRADILKHHMKKITLA--DNVDPTIIARGTPGLSGAEL 487
Cdd:CHL00195 369 NIDLLPLEILRKGRFDEIFFLDLPSLEEREKIFKIHLQKFRPKswKKYDIKKLSKLSNKFSGAEI 433
PRK13342 PRK13342
recombination factor protein RarA; Reviewed
317-423 8.39e-10

recombination factor protein RarA; Reviewed


Pssm-ID: 237355 [Multi-domain]  Cd Length: 413  Bit Score: 61.64  E-value: 8.39e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325281   317 VLLTGPPGTGKTLLARATAGEAGVDFFFMSGsefdeVYVGVgaKRIRDLFAQARSRAPA----IIFIDELdaiggKRNPK 392
Cdd:PRK13342  39 MILWGPPGTGKTTLARIIAGATDAPFEALSA-----VTSGV--KDLREVIEEARQRRSAgrrtILFIDEI-----HRFNK 106
                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 6325281   393 DQayakqtlnQ--LL--VEldgfsqtSG-IIIIGAT 423
Cdd:PRK13342 107 AQ--------QdaLLphVE-------DGtITLIGAT 127
RecA-like_Ycf2 cd19505
ATPase domain of plant YCF2; Ycf2 is a chloroplast ATPase which has an essential function; ...
309-445 1.97e-09

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: 57.00  E-value: 1.97e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325281  309 LGGKLPKGVLLTGPPGTGKTLLARATAGEAGV---------------DFFFMSGsEFDEVYVGVGAKRIRDLFAQARSRA 373
Cdd:cd19505   7 LGLSPSKGILLIGSIETGRSYLIKSLAANSYVplirislnkllynkpDFGNDDW-IDGMLILKESLHRLNLQFELAKAMS 85
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 6325281  374 PAIIFIDELDAIGGKRNPKDQAYAKQTLNQLLVEL--DGFSQTS--GIIIIGATNFPEALDKALTRPGRFDKVVNV 445
Cdd:cd19505  86 PCIIWIPNIHELNVNRSTQNLEEDPKLLLGLLLNYlsRDFEKSStrNILVIASTHIPQKVDPALIAPNRLDTCINI 161
RarA COG2256
Replication-associated recombination protein RarA (DNA-dependent ATPase) [Replication, ...
317-423 2.35e-09

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


Pssm-ID: 441857 [Multi-domain]  Cd Length: 439  Bit Score: 60.07  E-value: 2.35e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325281  317 VLLTGPPGTGKTLLARATAGEAGVDFFFMSGsefdeVYVGVgaKRIRDLFAQARSRA----PAIIFIDELDaiggkRNPK 392
Cdd:COG2256  52 MILWGPPGTGKTTLARLIANATDAEFVALSA-----VTSGV--KDIREVIEEARERRaygrRTILFVDEIH-----RFNK 119
                        90       100       110
                ....*....|....*....|....*....|....*.
gi 6325281  393 DQayakqtlnQ--LL--VEldgfsqtSGIII-IGAT 423
Cdd:COG2256 120 AQ--------QdaLLphVE-------DGTITlIGAT 140
PRK04195 PRK04195
replication factor C large subunit; Provisional
279-388 3.30e-09

replication factor C large subunit; Provisional


Pssm-ID: 235250 [Multi-domain]  Cd Length: 482  Bit Score: 59.93  E-value: 3.30e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325281   279 KFDDVCGCDEARAELEE-IVDFLKdptkyeslgGKLPKGVLLTGPPGTGKTLLARATAGEAGVDFFFMSGSEFD-----E 352
Cdd:PRK04195  12 TLSDVVGNEKAKEQLREwIESWLK---------GKPKKALLLYGPPGVGKTSLAHALANDYGWEVIELNASDQRtadviE 82
                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 6325281   353 VYVGVGAKRiRDLFAQARSrapaIIFIDELDAIGGK 388
Cdd:PRK04195  83 RVAGEAATS-GSLFGARRK----LILLDEVDGIHGN 113
RecA-like_HslU cd19498
ATP-dependent protease ATPase subunit HslU; HslU is a component of the ATP-dependent protease ...
313-388 4.12e-09

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


Pssm-ID: 410906 [Multi-domain]  Cd Length: 183  Bit Score: 56.62  E-value: 4.12e-09
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 6325281  313 LPKGVLLTGPPGTGKTLLARATAGEAGVDFFFMSGSEFDEV-YVGvgakriRDLFAQARSRAPAIIFIDELDAIGGK 388
Cdd:cd19498  45 TPKNILMIGPTGVGKTEIARRLAKLAGAPFIKVEATKFTEVgYVG------RDVESIIRDLVEGIVFIDEIDKIAKR 115
TIP49 COG1224
DNA helicase TIP49, TBP-interacting protein [Transcription];
311-350 1.14e-06

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


Pssm-ID: 440837 [Multi-domain]  Cd Length: 452  Bit Score: 51.89  E-value: 1.14e-06
                        10        20        30        40
                ....*....|....*....|....*....|....*....|...
gi 6325281  311 GKLP-KGVLLTGPPGTGKTLLARATAGEAGVD--FFFMSGSEF 350
Cdd:COG1224  60 GKMAgKGILIVGPPGTGKTALAVAIARELGEDtpFVAISGSEI 102
CDC6 COG1474
Cdc6-related protein, AAA superfamily ATPase [Replication, recombination and repair];
291-430 1.59e-06

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


Pssm-ID: 441083 [Multi-domain]  Cd Length: 389  Bit Score: 51.00  E-value: 1.59e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325281  291 AELEEIVDFLKDPTKyeslgGKLPKGVLLTGPPGTGKTLLARA-------TAGEAGVDFFF------MSGSEFDEVY--- 354
Cdd:COG1474  33 EEIEELASALRPALR-----GERPSNVLIYGPTGTGKTAVAKYvleeleeEAEERGVDVRVvyvncrQASTRYRVLSril 107
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325281  355 -----------VGVGAKRIRDLFAQA--RSRAPAIIFIDELDAIgGKRNPKDqayakqTLNQLLVELDGFSQTSgIIIIG 421
Cdd:COG1474 108 eelgsgedipsTGLSTDELFDRLYEAldERDGVLVVVLDEIDYL-VDDEGDD------LLYQLLRANEELEGAR-VGVIG 179
                       170
                ....*....|..
gi 6325281  422 ATN---FPEALD 430
Cdd:COG1474 180 ISNdleFLENLD 191
44 PHA02544
clamp loader, small subunit; Provisional
311-386 1.82e-06

clamp loader, small subunit; Provisional


Pssm-ID: 222866 [Multi-domain]  Cd Length: 316  Bit Score: 50.37  E-value: 1.82e-06
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 6325281   311 GKLPKGVLLTGPPGTGKTLLARATAGEAGVDFFFMSGSEfdevyVGVGAKRIR-DLFAQARSRAPA--IIFIDELDAIG 386
Cdd:PHA02544  40 GRIPNMLLHSPSPGTGKTTVAKALCNEVGAEVLFVNGSD-----CRIDFVRNRlTRFASTVSLTGGgkVIIIDEFDRLG 113
TIP49 pfam06068
TIP49 P-loop domain; This family consists of the C-terminal region of several eukaryotic and ...
285-350 8.48e-06

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: 48.46  E-value: 8.48e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 6325281    285 GCDEARAELEEIVDFLKDPTkyesLGGKlpkGVLLTGPPGTGKTLLARATAGEAGVD--FFFMSGSEF 350
Cdd:pfam06068  28 GQEKAREAAGVIVEMIKEGK----IAGR---AVLIAGPPGTGKTALAIAISKELGEDtpFTSISGSEV 88
AAA_22 pfam13401
AAA domain;
317-429 1.12e-05

AAA domain;


Pssm-ID: 379165 [Multi-domain]  Cd Length: 129  Bit Score: 45.41  E-value: 1.12e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325281    317 VLLTGPPGTGKTLLAR---ATAGEAGVDFFFM---SGSEFDEVY---------VGVGAKRIRDLFAQ-----ARSRAPAI 376
Cdd:pfam13401   8 LVLTGESGTGKTTLLRrllEQLPEVRDSVVFVdlpSGTSPKDLLrallralglPLSGRLSKEELLAAlqqllLALAVAVV 87
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 6325281    377 IFIDELDAIGGKrnpkdqayakqTLNQLLVELDGFSQTSGIIIIGATNFPEAL 429
Cdd:pfam13401  88 LIIDEAQHLSLE-----------ALEELRDLLNLSSKLLQLILVGTPELRELL 129
RecA-like_superfamily cd01120
RecA-like_NTPases; RecA-like NTPases. This superfamily includes the NTP binding domain of F1 ...
317-452 2.54e-05

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


Pssm-ID: 410865 [Multi-domain]  Cd Length: 119  Bit Score: 44.03  E-value: 2.54e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325281  317 VLLTGPPGTGKTLLARATAGEA-GVDFFFMSGSEFDevyvgVGAKRIRDLFAQARsraPAIIFIDELDAIGGKRNPkdqA 395
Cdd:cd01120   1 ILITGPPGSGKTTLLLQFAEQAlLSDEPVIFISFLD-----TILEAIEDLIEEKK---LDIIIIDSLSSLARASQG---D 69
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 6325281  396 YAKQTLNQLLVELDGFSQTSGIIIigatnfpealdkALTRPGRFDKVVNVDLPDVRG 452
Cdd:cd01120  70 RSSELLEDLAKLLRAARNTGITVI------------ATIHSDKFDIDRGGSSNDERL 114
RecA-like_Lon cd19500
lon protease homolog 2 peroxisomal; Lon protease (also known as Lon peptidase) is an ...
294-386 2.92e-05

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


Pssm-ID: 410908 [Multi-domain]  Cd Length: 182  Bit Score: 45.24  E-value: 2.92e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325281  294 EEIVDFLKDPTKYESLGGKLpkgVLLTGPPGTGKTLLARATAGEAGVDFFFMS-GSEFDE--------VYVGVGAKRIRD 364
Cdd:cd19500  20 ERILEYLAVRKLKGSMKGPI---LCLVGPPGVGKTSLGKSIARALGRKFVRISlGGVRDEaeirghrrTYVGAMPGRIIQ 96
                        90       100
                ....*....|....*....|..
gi 6325281  365 LFAQARSRAPaIIFIDELDAIG 386
Cdd:cd19500  97 ALKKAGTNNP-VFLLDEIDKIG 117
RecA-like_IQCA1 cd19506
ATPase domain of IQ and AAA domain-containing protein 1 (IQCA1); IQCA1 (also known as dynein ...
313-426 2.93e-05

ATPase domain of IQ and AAA domain-containing protein 1 (IQCA1); IQCA1 (also known as dynein regulatory complex subunit 11, DRC11 and IQCA) is an ATPase subunit of the nexin-dynein regulatory complex (N-DRC). The 9 + 2 axoneme of most motile cilia and flagella consists of nine outer doublet microtubules arranged in a ring surrounding a central pair of two singlet microtubules. The N-DRC complex maintains alignment between outer doublet microtubules and limits microtubule sliding in motile axonemes. This subfamily belongs to the RecA-like NTPase family which includes the NTP binding domain of F1 and V1 H(+)ATPases, DnaB and related helicases as well as bacterial RecA and related eukaryotic and archaeal recombinases. The RecA-like NTPase family also includes bacterial conjugation proteins and related DNA transfer proteins involved in type II and type IV secretion.


Pssm-ID: 410914 [Multi-domain]  Cd Length: 160  Bit Score: 44.83  E-value: 2.93e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325281  313 LPKGVLLTGPPGTGKTLLARATAGEAGVDFFFMSGSEFDEVYVGVGAKR--IRDLFAQARSRAPAIIFIDELDAIGGKRN 390
Cdd:cd19506  25 LVKSLLLAGPSGVGKKMLVHAICTETGANLFNLSPSNIAGKYPGKNGLQmmLHLVLKVARQLQPSVIWIGDAEKTFYKKV 104
                        90       100       110       120
                ....*....|....*....|....*....|....*....|.
gi 6325281  391 PK-----DQAYAKQTLNQLLVELDGFSQtsgIIIIGATNFP 426
Cdd:cd19506 105 PKtekqlDPKRLKKDLPKILKSLKPEDR---VLIVGTTSRP 142
T7SS_EccA TIGR03922
type VII secretion AAA-ATPase EccA; This model represents the AAA family ATPase, EccA, of the ...
272-446 5.82e-05

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


Pssm-ID: 188437 [Multi-domain]  Cd Length: 557  Bit Score: 46.38  E-value: 5.82e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325281    272 DVAKTNVKFDDVCGCD-------EARAELEEI---------VDFLKDPTKYE----SLGGKLP---KGVLLTGPPGTGKT 328
Cdd:TIGR03922 247 SSAPSRAEFVDPAAAErkakllaEAEAELAEQiglervkrqVAALKSSTAMAlaraERGLPVAqtsNHMLFAGPPGTGKT 326
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325281    329 LLARATAGE-AGVDFFF------MSGSEFDEVYVGVGAKRIRDLFAQARSRapaIIFIDELDAIGGKRNPKDQAYAKQTL 401
Cdd:TIGR03922 327 TIARVVAKIyCGLGVLRkplvreVSRADLIGQYIGESEAKTNEIIDSALGG---VLFLDEAYTLVETGYGQKDPFGLEAI 403
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 6325281    402 NQLLVELDgfSQTSGIIIIGAtNFPEALDKAL-TRPG---RFDKVVNVD 446
Cdd:TIGR03922 404 DTLLARME--NDRDRLVVIGA-GYRKDLDKFLeVNEGlrsRFTRVIEFP 449
KaiC-like cd01124
Circadian Clock Protein KaiC; KaiC is a circadian clock protein, most studied in cyanobacteria. ...
307-371 8.20e-05

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


Pssm-ID: 410869 [Multi-domain]  Cd Length: 222  Bit Score: 44.56  E-value: 8.20e-05
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 6325281  307 ESLGGKLPKG--VLLTGPPGTGKTLLARAtageagvdfFFMSGSEFDE--VYVGVGaKRIRDLFAQARS 371
Cdd:cd01124  10 ELLGGGIPKGsvTLLTGGPGTGKTLFGLQ---------FLYAGAKNGEpgLFFTFE-ESPERLLRNAKS 68
RAD55 COG0467
RecA-superfamily ATPase, KaiC/GvpD/RAD55 family [Signal transduction mechanisms];
309-389 8.21e-05

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


Pssm-ID: 440235 [Multi-domain]  Cd Length: 221  Bit Score: 44.52  E-value: 8.21e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325281  309 LGGKLPKG--VLLTGPPGTGKTLLA------RATAGEAGVDFFF----------MSGSEFD-EVYVGVGAKRIRDLFAQA 369
Cdd:COG0467  13 LGGGLPRGssTLLSGPPGTGKTTLAlqflaeGLRRGEKGLYVSFeespeqllrrAESLGLDlEEYIESGLLRIIDLSPEE 92
                        90       100
                ....*....|....*....|...
gi 6325281  370 RSRAP---AIIFIDELDAIGGKR 389
Cdd:COG0467  93 LGLDLeelLARLREAVEEFGAKR 115
HolB COG0470
DNA polymerase III, delta prime subunit [Replication, recombination and repair];
287-385 9.76e-05

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


Pssm-ID: 440238 [Multi-domain]  Cd Length: 289  Bit Score: 44.97  E-value: 9.76e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325281  287 DEARAELEEIVDflkdptkyeslGGKLPKGVLLTGPPGTGKTLLARATA----GEAGVDFF---------FMSGSEFDEV 353
Cdd:COG0470   2 EEAWEQLLAAAE-----------SGRLPHALLLHGPPGIGKTTLALALArdllCENPEGGKacgqchsrlMAAGNHPDLL 70
                        90       100       110       120
                ....*....|....*....|....*....|....*....|...
gi 6325281  354 YVGVGAKR-------IRDLFAQARSRAPA----IIFIDELDAI 385
Cdd:COG0470  71 ELNPEEKSdqigidqIRELGEFLSLTPLEggrkVVIIDEADAM 113
AAA_2 pfam07724
AAA domain (Cdc48 subfamily); This Pfam entry includes some of the AAA proteins not detected ...
314-425 1.86e-04

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: 42.57  E-value: 1.86e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325281    314 PKGV-LLTGPPGTGKTLLARATAGEAGVDFFFMS---GSEFDE---V---------YVGVGAKRIrdLFAQARSRAPAII 377
Cdd:pfam07724   2 PIGSfLFLGPTGVGKTELAKALAELLFGDERALIridMSEYMEehsVsrligappgYVGYEEGGQ--LTEAVRRKPYSIV 79
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 6325281    378 FIDELDAIggkrnpkdqayAKQTLNQLLVELDG----FSQ-----TSGIIIIGATNF 425
Cdd:pfam07724  80 LIDEIEKA-----------HPGVQNDLLQILEGgtltDKQgrtvdFKNTLFIMTGNF 125
MoxR COG0714
MoxR-like ATPase [General function prediction only]; MoxR-like ATPase is part of the Pathway ...
317-342 2.11e-04

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: 44.00  E-value: 2.11e-04
                        10        20
                ....*....|....*....|....*.
gi 6325281  317 VLLTGPPGTGKTLLARATAGEAGVDF 342
Cdd:COG0714  34 LLLEGVPGVGKTTLAKALARALGLPF 59
AAA_5 pfam07728
AAA domain (dynein-related subfamily); This Pfam entry includes some of the AAA proteins not ...
316-439 2.39e-04

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: 41.89  E-value: 2.39e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325281    316 GVLLTGPPGTGKTLLARATAgEA--GVDFFFMSGSEF---DEVY----VGVGAKRIRDLFAQARSRAPAIIFIDELDaig 386
Cdd:pfam07728   1 GVLLVGPPGTGKTELAERLA-AAlsNRPVFYVQLTRDtteEDLFgrrnIDPGGASWVDGPLVRAAREGEIAVLDEIN--- 76
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 6325281    387 gKRNPKDQAyakqTLNQLL----------VELDGFSQTsGIIIIGATNFPEA----LDKALTRpgRF 439
Cdd:pfam07728  77 -RANPDVLN----SLLSLLderrlllpdgGELVKAAPD-GFRLIATMNPLDRglneLSPALRS--RF 135
rfc PRK00440
replication factor C small subunit; Reviewed
279-384 2.48e-04

replication factor C small subunit; Reviewed


Pssm-ID: 234763 [Multi-domain]  Cd Length: 319  Bit Score: 43.71  E-value: 2.48e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325281   279 KFDDVCGcdearaeLEEIVDFLKDPTKyeslGGKLPKgVLLTGPPGTGKT----LLARATAGEAGVDFFF-MSGSefDEV 353
Cdd:PRK00440  15 TLDEIVG-------QEEIVERLKSYVK----EKNMPH-LLFAGPPGTGKTtaalALARELYGEDWRENFLeLNAS--DER 80
                         90       100       110
                 ....*....|....*....|....*....|....
gi 6325281   354 YVGVGAKRIRDlFAQARSRAPA---IIFIDELDA 384
Cdd:PRK00440  81 GIDVIRNKIKE-FARTAPVGGApfkIIFLDEADN 113
AAA_16 pfam13191
AAA ATPase domain; This family of domains contain a P-loop motif that is characteriztic of the ...
290-408 4.41e-04

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


Pssm-ID: 433025 [Multi-domain]  Cd Length: 167  Bit Score: 41.72  E-value: 4.41e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325281    290 RAELEEIVDFLKDPTKYEslggklPKGVLLTGPPGTGKTLLARA---TAGEAGVDFFFMSGSEFDEVYVGVGAKRIRDLF 366
Cdd:pfam13191   6 EEELEQLLDALDRVRSGR------PPSVLLTGEAGTGKTTLLREllrALERDGGYFLRGKCDENLPYSPLLEALTREGLL 79
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 6325281    367 AQARSRAPAIIFIDELDAIGG--KRNPKDQAYAKQTLNQLLVEL 408
Cdd:pfam13191  80 RQLLDELESSLLEAWRAALLEalAPVPELPGDLAERLLDLLLRL 123
McrB COG1401
5-methylcytosine-specific restriction endonuclease McrBC, GTP-binding regulatory subunit McrB ...
286-382 7.53e-04

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


Pssm-ID: 441011 [Multi-domain]  Cd Length: 477  Bit Score: 42.83  E-value: 7.53e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325281  286 CDEARAELEEIVDFLKDPtkyeslggklpKGVLLTGPPGTGKT----LLARATAGEAGVDFFF------MSGSEFDEVYV 355
Cdd:COG1401 204 REKFEETLEAFLAALKTK-----------KNVILAGPPGTGKTylarRLAEALGGEDNGRIEFvqfhpsWSYEDFLLGYR 272
                        90       100       110
                ....*....|....*....|....*....|....*..
gi 6325281  356 GVGAK---RIRD-LFAQARSRA------PAIIFIDEL 382
Cdd:COG1401 273 PSLDEgkyEPTPgIFLRFCLKAeknpdkPYVLIIDEI 309
RuvB_N pfam05496
Holliday junction DNA helicase RuvB P-loop domain; The RuvB protein makes up part of the ...
317-381 9.88e-04

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


Pssm-ID: 398900 [Multi-domain]  Cd Length: 159  Bit Score: 40.56  E-value: 9.88e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 6325281    317 VLLTGPPGTGKTLLARATAGEAGVDFFFMSGSEFDevyvgvgakRIRDLFAQARSRAPA-IIFIDE 381
Cdd:pfam05496  36 VLLYGPPGLGKTTLANIIANEMGVNIRITSGPAIE---------RPGDLAAILTNLEPGdVLFIDE 92
RecA-like_ClpB_Hsp104-like cd19499
Chaperone protein ClpB/Hsp104 subfamily; Bacterial Caseinolytic peptidase B (ClpB) and ...
300-443 1.20e-03

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


Pssm-ID: 410907 [Multi-domain]  Cd Length: 178  Bit Score: 40.62  E-value: 1.20e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325281  300 LKDPTKyeslggklPKGVLL-TGPPGTGKTLLARATAgeagvDFFFMSG--------SEFDE------------VYVGVG 358
Cdd:cd19499  34 LSDPNR--------PIGSFLfLGPTGVGKTELAKALA-----ELLFGDEdnliridmSEYMEkhsvsrligappGYVGYT 100
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325281  359 AkriRDLFAQA-RSRAPAIIFIDELDaiggKRNPKDQayakqtlNQLLVELD------------GFSQTsgiIIIGATNF 425
Cdd:cd19499 101 E---GGQLTEAvRRKPYSVVLLDEIE----KAHPDVQ-------NLLLQVLDdgrltdshgrtvDFKNT---IIIMTSNH 163
                       170       180
                ....*....|....*....|
gi 6325281  426 --PEALdkaltrpGRFDKVV 443
Cdd:cd19499 164 frPEFL-------NRIDEIV 176
ruvB PRK00080
Holliday junction branch migration DNA helicase RuvB;
317-381 1.44e-03

Holliday junction branch migration DNA helicase RuvB;


Pssm-ID: 234619 [Multi-domain]  Cd Length: 328  Bit Score: 41.65  E-value: 1.44e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325281   317 VLLTGPPGTGKTLLARATAGEAGVDFFFMSGSEFDevyvgvgakRIRDLFA-----QARSrapaIIFIDE 381
Cdd:PRK00080  54 VLLYGPPGLGKTTLANIIANEMGVNIRITSGPALE---------KPGDLAAiltnlEEGD----VLFIDE 110
PRK12402 PRK12402
replication factor C small subunit 2; Reviewed
279-338 1.82e-03

replication factor C small subunit 2; Reviewed


Pssm-ID: 237090 [Multi-domain]  Cd Length: 337  Bit Score: 41.13  E-value: 1.82e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325281   279 KFDDVCGCDEARAELEEIVDflkdptkyeslGGKLPKgVLLTGPPGTGKTLLARATAGEA 338
Cdd:PRK12402  13 LLEDILGQDEVVERLSRAVD-----------SPNLPH-LLVQGPPGSGKTAAVRALAREL 60
ruvB TIGR00635
Holliday junction DNA helicase, RuvB subunit; All proteins in this family for which functions ...
317-386 2.62e-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: 40.75  E-value: 2.62e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 6325281    317 VLLTGPPGTGKTLLARATAGEAGVDFFFMSGSEFDevyvgvgakRIRDLFA-----QARSrapaIIFIDELDAIG 386
Cdd:TIGR00635  33 LLLYGPPGLGKTTLAHIIANEMGVNLKITSGPALE---------KPGDLAAiltnlEEGD----VLFIDEIHRLS 94
DnaC COG1484
DNA replication protein DnaC [Replication, recombination and repair];
315-382 2.96e-03

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


Pssm-ID: 441093 [Multi-domain]  Cd Length: 242  Bit Score: 40.15  E-value: 2.96e-03
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 6325281  315 KGVLLTGPPGTGKTLLARA---TAGEAGVDFFFMSGSEF-DEVYVGVGAKRIRDLFAQArSRAPAIIfIDEL 382
Cdd:COG1484 100 ENLILLGPPGTGKTHLAIAlghEACRAGYRVRFTTAPDLvNELKEARADGRLERLLKRL-AKVDLLI-LDEL 169
PRK08939 PRK08939
primosomal protein DnaI; Reviewed
269-337 4.90e-03

primosomal protein DnaI; Reviewed


Pssm-ID: 236353 [Multi-domain]  Cd Length: 306  Bit Score: 39.85  E-value: 4.90e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 6325281   269 KSVDVAKT--NVKFDDVCGCDEARAE-LEEIVDFLKdptKYESlgGKLPKGVLLTGPPGTGKTLLARATAGE 337
Cdd:PRK08939 113 QSIYMPKDllQASLADIDLDDRDRLDaLMAALDFLE---AYPP--GEKVKGLYLYGDFGVGKSYLLAAIANE 179
YifB COG0606
Predicted Mg-chelatase, contains ChlI-like and ATPase domains, YifB family [Posttranslational ...
317-332 6.00e-03

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


Pssm-ID: 440371 [Multi-domain]  Cd Length: 502  Bit Score: 40.02  E-value: 6.00e-03
                        10
                ....*....|....*.
gi 6325281  317 VLLTGPPGTGKTLLAR 332
Cdd:COG0606 214 LLMIGPPGSGKTMLAR 229
ABC_ATPase cd00267
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ...
312-435 6.37e-03

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


Pssm-ID: 213179 [Multi-domain]  Cd Length: 157  Bit Score: 37.99  E-value: 6.37e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325281  312 KLPKG--VLLTGPPGTGKTLLARATAGEAGVDfffmSGS-EFDEVYVG-VGAKRIRDLF----------------AQARS 371
Cdd:cd00267  21 TLKAGeiVALVGPNGSGKSTLLRAIAGLLKPT----SGEiLIDGKDIAkLPLEELRRRIgyvpqlsggqrqrvalARALL 96
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 6325281  372 RAPAIIFIDE----LDAIGGKRnpkdqayakqtLNQLLVELdgfsQTSGIIIIGATNFPEALDKALTR 435
Cdd:cd00267  97 LNPDLLLLDEptsgLDPASRER-----------LLELLREL----AEEGRTVIIVTHDPELAELAADR 149
DnaA COG0593
Chromosomal replication initiation ATPase DnaA [Replication, recombination and repair];
317-470 6.59e-03

Chromosomal replication initiation ATPase DnaA [Replication, recombination and repair];


Pssm-ID: 440358 [Multi-domain]  Cd Length: 303  Bit Score: 39.40  E-value: 6.59e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325281  317 VLLTGPPGTGKTLLARATAGEAGVDF-----FFMSGSEFDEVYvgVGAKRIRDLFA-QARSRAPAIIFIDELDAIGGKrn 390
Cdd:COG0593  37 LFLYGGVGLGKTHLLHAIGNEALENNpgarvVYLTAEEFTNDF--INAIRNNTIEEfKEKYRSVDVLLIDDIQFLAGK-- 112
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325281  391 PKDQAYAKQTLNQLLveldgfsQTSGIIIIGATNFPEALDKALTR-PGRFDK--VVNVDLPDVRGRADILKH--HMKKIT 465
Cdd:COG0593 113 EATQEEFFHTFNALR-------EAGKQIVLTSDRPPKELPGLEERlRSRLEWglVVDIQPPDLETRIAILRKkaADRGLE 185

                ....*
gi 6325281  466 LADNV 470
Cdd:COG0593 186 LPDEV 190
DnaX COG2812
DNA polymerase III, gamma/tau subunits [Replication, recombination and repair];
279-335 6.64e-03

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


Pssm-ID: 442061 [Multi-domain]  Cd Length: 340  Bit Score: 39.40  E-value: 6.64e-03
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 6325281  279 KFDDVCGcdearaeLEEIVDFLKdptkyESL-GGKLPKGVLLTGPPGTGKTLLARATA 335
Cdd:COG2812   8 TFDDVVG-------QEHVVRTLK-----NALaSGRLAHAYLFTGPRGVGKTTLARILA 53
RuvB COG2255
Holliday junction resolvasome RuvABC, ATP-dependent DNA helicase subunit RuvB [Replication, ...
317-347 8.48e-03

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


Pssm-ID: 441856 [Multi-domain]  Cd Length: 337  Bit Score: 38.91  E-value: 8.48e-03
                        10        20        30
                ....*....|....*....|....*....|.
gi 6325281  317 VLLTGPPGTGKTLLARATAGEAGVDFFFMSG 347
Cdd:COG2255  57 VLLYGPPGLGKTTLAHIIANEMGVNIRITSG 87
 
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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