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Conserved domains on  [gi|1950807624|gb|QQG35127|]
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ATP-dependent zinc metalloprotease FtsH [Deltaproteobacteria bacterium]

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];
27-609 0e+00

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


:

Pssm-ID: 440233 [Multi-domain]  Cd Length: 583  Bit Score: 932.91  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950807624  27 IGITCAILFQFFGDYNNPVQEKAFSDVVTALNEGQVKNLTIKGREYFGELQDGT--RFYTIGERVSVWYPILNNAheffK 104
Cdd:COG0465     1 IALLLVLLFNLFSSSSSSVKEISYSEFLQLVEAGKVKSVTIQGDRITGTLKDGTktRFTTYRVNDPELVDLLEEK----G 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950807624 105 TKYQFAPEDPVGKSQYIFQWVS-LLVFFGIFFIWVKQSKADGKG-FSFGKNRSRVLVDYESGYTFKDVAGIDECKQELQE 182
Cdd:COG0465    77 VEVTAKPPEESSWLLSLLISLLpILLLIGLWIFFMRRMQGGGGGaMSFGKSKAKLYDEDKPKVTFDDVAGVDEAKEELQE 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950807624 183 IVSFLKDPERYTRLGAEIPKGVLLMGAPGTGKTLLAKAIAGEAGVPFFSVAGSDFVEMFVGVGASRVRDLFEQGKEYAPC 262
Cdd:COG0465   157 IVDFLKDPEKFTRLGAKIPKGVLLVGPPGTGKTLLAKAVAGEAGVPFFSISGSDFVEMFVGVGASRVRDLFEQAKKNAPC 236
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950807624 263 IIFIDEIDAVGRSRGAGSGmGGNDEREQTLNQLLVEMDGFISNEGIIIIAATNRPDVLDPAILRPGRFDRRIIVPRPDLN 342
Cdd:COG0465   237 IIFIDEIDAVGRQRGAGLG-GGHDEREQTLNQLLVEMDGFEGNEGVIVIAATNRPDVLDPALLRPGRFDRQVVVDLPDVK 315
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950807624 343 GRESIFKIHTKNVPLDKDVNLEILARSTPGMSGADIKNLVNEAALIAAQKNQEIVNMQNFEAAREKIIMGTERRSLIMSR 422
Cdd:COG0465   316 GREAILKVHARKKPLAPDVDLEVIARRTPGFSGADLANLVNEAALLAARRNKKAVTMEDFEEAIDRVIAGPERKSRVISE 395
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950807624 423 QEIENTAYHEAGHAIVSILIGHdVDPVHKVTIIPRGQALGLTMQLPTQDRYSISKTYSENQIAIMMGGRIAEELVFGEIT 502
Cdd:COG0465   396 KEKKITAYHEAGHALVAALLPG-ADPVHKVTIIPRGRALGYTMQLPEEDRYLYTKEELLDRIAVLLGGRAAEELVFGEVT 474
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950807624 503 SGAGNDFQKATDLAHSMVCDWGMS-TMGPLYYGTKE-EILLGKSVFQKSAYSELTAQEIDKEVKLIILEQYYRAKDILEQ 580
Cdd:COG0465   475 TGASNDLERATKIARAMVTEYGMSeKLGPVAYGESEgEVFLGRDIGQSRNYSEETAREIDEEVRRIIDEAYERAKEILTE 554
                         570       580
                  ....*....|....*....|....*....
gi 1950807624 581 HMKQLEKVATALVEYETLDGIDVEILLEG 609
Cdd:COG0465   555 NRDKLDALAEALLEKETLDGEELEEILAG 583
 
Name Accession Description Interval E-value
HflB COG0465
ATP-dependent Zn proteases [Posttranslational modification, protein turnover, chaperones];
27-609 0e+00

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


Pssm-ID: 440233 [Multi-domain]  Cd Length: 583  Bit Score: 932.91  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950807624  27 IGITCAILFQFFGDYNNPVQEKAFSDVVTALNEGQVKNLTIKGREYFGELQDGT--RFYTIGERVSVWYPILNNAheffK 104
Cdd:COG0465     1 IALLLVLLFNLFSSSSSSVKEISYSEFLQLVEAGKVKSVTIQGDRITGTLKDGTktRFTTYRVNDPELVDLLEEK----G 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950807624 105 TKYQFAPEDPVGKSQYIFQWVS-LLVFFGIFFIWVKQSKADGKG-FSFGKNRSRVLVDYESGYTFKDVAGIDECKQELQE 182
Cdd:COG0465    77 VEVTAKPPEESSWLLSLLISLLpILLLIGLWIFFMRRMQGGGGGaMSFGKSKAKLYDEDKPKVTFDDVAGVDEAKEELQE 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950807624 183 IVSFLKDPERYTRLGAEIPKGVLLMGAPGTGKTLLAKAIAGEAGVPFFSVAGSDFVEMFVGVGASRVRDLFEQGKEYAPC 262
Cdd:COG0465   157 IVDFLKDPEKFTRLGAKIPKGVLLVGPPGTGKTLLAKAVAGEAGVPFFSISGSDFVEMFVGVGASRVRDLFEQAKKNAPC 236
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950807624 263 IIFIDEIDAVGRSRGAGSGmGGNDEREQTLNQLLVEMDGFISNEGIIIIAATNRPDVLDPAILRPGRFDRRIIVPRPDLN 342
Cdd:COG0465   237 IIFIDEIDAVGRQRGAGLG-GGHDEREQTLNQLLVEMDGFEGNEGVIVIAATNRPDVLDPALLRPGRFDRQVVVDLPDVK 315
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950807624 343 GRESIFKIHTKNVPLDKDVNLEILARSTPGMSGADIKNLVNEAALIAAQKNQEIVNMQNFEAAREKIIMGTERRSLIMSR 422
Cdd:COG0465   316 GREAILKVHARKKPLAPDVDLEVIARRTPGFSGADLANLVNEAALLAARRNKKAVTMEDFEEAIDRVIAGPERKSRVISE 395
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950807624 423 QEIENTAYHEAGHAIVSILIGHdVDPVHKVTIIPRGQALGLTMQLPTQDRYSISKTYSENQIAIMMGGRIAEELVFGEIT 502
Cdd:COG0465   396 KEKKITAYHEAGHALVAALLPG-ADPVHKVTIIPRGRALGYTMQLPEEDRYLYTKEELLDRIAVLLGGRAAEELVFGEVT 474
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950807624 503 SGAGNDFQKATDLAHSMVCDWGMS-TMGPLYYGTKE-EILLGKSVFQKSAYSELTAQEIDKEVKLIILEQYYRAKDILEQ 580
Cdd:COG0465   475 TGASNDLERATKIARAMVTEYGMSeKLGPVAYGESEgEVFLGRDIGQSRNYSEETAREIDEEVRRIIDEAYERAKEILTE 554
                         570       580
                  ....*....|....*....|....*....
gi 1950807624 581 HMKQLEKVATALVEYETLDGIDVEILLEG 609
Cdd:COG0465   555 NRDKLDALAEALLEKETLDGEELEEILAG 583
FtsH_fam TIGR01241
ATP-dependent metalloprotease FtsH; HflB(FtsH) is a pleiotropic protein required for correct ...
118-608 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: 776.46  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950807624 118 SQYIFQWV-SLLVFFGIFFIWVKQSKADGKG-FSFGKNRSRVLVDYESGYTFKDVAGIDECKQELQEIVSFLKDPERYTR 195
Cdd:TIGR01241   3 LGFLFSLLpPILLLVGVWFFFRRQMQGGGGRaFSFGKSKAKLLNEEKPKVTFKDVAGIDEAKEELMEIVDFLKNPSKFTK 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950807624 196 LGAEIPKGVLLMGAPGTGKTLLAKAIAGEAGVPFFSVAGSDFVEMFVGVGASRVRDLFEQGKEYAPCIIFIDEIDAVGRS 275
Cdd:TIGR01241  83 LGAKIPKGVLLVGPPGTGKTLLAKAVAGEAGVPFFSISGSDFVEMFVGVGASRVRDLFEQAKKNAPCIIFIDEIDAVGRQ 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950807624 276 RGAGSGmGGNDEREQTLNQLLVEMDGFISNEGIIIIAATNRPDVLDPAILRPGRFDRRIIVPRPDLNGRESIFKIHTKNV 355
Cdd:TIGR01241 163 RGAGLG-GGNDEREQTLNQLLVEMDGFGTNTGVIVIAATNRPDVLDPALLRPGRFDRQVVVDLPDIKGREEILKVHAKNK 241
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950807624 356 PLDKDVNLEILARSTPGMSGADIKNLVNEAALIAAQKNQEIVNMQNFEAAREKIIMGTERRSLIMSRQEIENTAYHEAGH 435
Cdd:TIGR01241 242 KLAPDVDLKAVARRTPGFSGADLANLLNEAALLAARKNKTEITMNDIEEAIDRVIAGPEKKSRVISEKEKKLVAYHEAGH 321
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950807624 436 AIVSILIgHDVDPVHKVTIIPRGQALGLTMQLPTQDRYSISKTYSENQIAIMMGGRIAEELVFGEITSGAGNDFQKATDL 515
Cdd:TIGR01241 322 ALVGLLL-KDADPVHKVTIIPRGQALGYTQFLPEEDKYLYTKSQLLAQIAVLLGGRAAEEIIFGEVTTGASNDIKQATNI 400
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950807624 516 AHSMVCDWGMS-TMGPLYYGTKE-EILLGKSVFQKSAYSELTAQEIDKEVKLIILEQYYRAKDILEQHMKQLEKVATALV 593
Cdd:TIGR01241 401 ARAMVTEWGMSdKLGPVAYGSDGgDVFLGRGFAKAKEYSEETAREIDEEVKRIIEEAYKRAKQILTENRDELELLAKALL 480
                         490
                  ....*....|....*
gi 1950807624 594 EYETLDGIDVEILLE 608
Cdd:TIGR01241 481 EKETITREEIKELLA 495
hflB PRK10733
ATP-dependent zinc metalloprotease FtsH;
21-613 0e+00

ATP-dependent zinc metalloprotease FtsH;


Pssm-ID: 182683 [Multi-domain]  Cd Length: 644  Bit Score: 636.31  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950807624  21 LVKWIFIGITCAILFQFFGDYNNPVQEKAFSDVVTALNEGQVKNLTIKGREYFGELQDGTRFYTIgerVSVWYP-ILNNA 99
Cdd:PRK10733    5 LILWLVIAVVLMSVFQSFGPSESNGRKVDYSTFLQEVNQDQVREARINGREINVTKKDSNRYTTY---IPVNDPkLLDNL 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950807624 100 HEFFKTKYQFAPEDPVGKSQYIFQWVSLLVFFGIFFIWVKQSKADG-KG-FSFGKNRSRVLVDYESGYTFKDVAGIDECK 177
Cdd:PRK10733   82 LTKNVKVVGEPPEEPSLLASIFISWFPMLLLIGVWIFFMRQMQGGGgKGaMSFGKSKARMLTEDQIKTTFADVAGCDEAK 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950807624 178 QELQEIVSFLKDPERYTRLGAEIPKGVLLMGAPGTGKTLLAKAIAGEAGVPFFSVAGSDFVEMFVGVGASRVRDLFEQGK 257
Cdd:PRK10733  162 EEVAELVEYLREPSRFQKLGGKIPKGVLMVGPPGTGKTLLAKAIAGEAKVPFFTISGSDFVEMFVGVGASRVRDMFEQAK 241
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950807624 258 EYAPCIIFIDEIDAVGRSRGAGSGmGGNDEREQTLNQLLVEMDGFISNEGIIIIAATNRPDVLDPAILRPGRFDRRIIVP 337
Cdd:PRK10733  242 KAAPCIIFIDEIDAVGRQRGAGLG-GGHDEREQTLNQMLVEMDGFEGNEGIIVIAATNRPDVLDPALLRPGRFDRQVVVG 320
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950807624 338 RPDLNGRESIFKIHTKNVPLDKDVNLEILARSTPGMSGADIKNLVNEAALIAAQKNQEIVNMQNFEAAREKIIMGTERRS 417
Cdd:PRK10733  321 LPDVRGREQILKVHMRRVPLAPDIDAAIIARGTPGFSGADLANLVNEAALFAARGNKRVVSMVEFEKAKDKIMMGAERRS 400
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950807624 418 LIMSRQEIENTAYHEAGHAIVSILIGHDvDPVHKVTIIPRGQALGLTMQLPTQDRYSISKTYSENQIAIMMGGRIAEELV 497
Cdd:PRK10733  401 MVMTEAQKESTAYHEAGHAIIGRLVPEH-DPVHKVTIIPRGRALGVTFFLPEGDAISASRQKLESQISTLYGGRLAEEII 479
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950807624 498 FG--EITSGAGNDFQKATDLAHSMVCDWGMS-TMGPLYYGTKE-EILLGKSVFQKSAYSELTAQEIDKEVKLIILEQYYR 573
Cdd:PRK10733  480 YGpeHVSTGASNDIKVATNLARNMVTQWGFSeKLGPLLYAEEEgEVFLGRSVAKAKHMSDETARIIDQEVKALIERNYNR 559
                         570       580       590       600
                  ....*....|....*....|....*....|....*....|
gi 1950807624 574 AKDILEQHMKQLEKVATALVEYETLDGIDVEILLEGKSLK 613
Cdd:PRK10733  560 ARQLLTDNMDILHAMKDALMKYETIDAPQIDDLMARRDVR 599
RecA-like_FtsH cd19501
ATP-dependent zinc metalloprotease FtsH; FtsH ATPase is a processive, ATP-dependent zinc ...
166-336 3.51e-122

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: 361.16  E-value: 3.51e-122
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950807624 166 TFKDVAGIDECKQELQEIVSFLKDPERYTRLGAEIPKGVLLMGAPGTGKTLLAKAIAGEAGVPFFSVAGSDFVEMFVGVG 245
Cdd:cd19501     2 TFKDVAGCEEAKEELKEVVEFLKNPEKFTKLGAKIPKGVLLVGPPGTGKTLLAKAVAGEAGVPFFSISGSDFVEMFVGVG 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950807624 246 ASRVRDLFEQGKEYAPCIIFIDEIDAVGRSRGAGSGmGGNDEREQTLNQLLVEMDGFISNEGIIIIAATNRPDVLDPAIL 325
Cdd:cd19501    82 ASRVRDLFEQAKKNAPCIVFIDEIDAVGRKRGAGLG-GGHDEREQTLNQLLVEMDGFESNTGVIVIAATNRPDVLDPALL 160
                         170
                  ....*....|.
gi 1950807624 326 RPGRFDRRIIV 336
Cdd:cd19501   161 RPGRFDRQVYV 171
Peptidase_M41 pfam01434
Peptidase family M41;
419-606 6.33e-80

Peptidase family M41;


Pssm-ID: 460210 [Multi-domain]  Cd Length: 190  Bit Score: 252.52  E-value: 6.33e-80
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950807624 419 IMSRQEIENTAYHEAGHAIVSILIgHDVDPVHKVTIIPRGQALGLTMQLPTQDRYSISKTYSENQIAIMMGGRIAEELVF 498
Cdd:pfam01434   2 VISEEEKKIVAYHEAGHALVGLLL-PGADPVHKVTIIPRGQALGYTQFLPEEDKLLYTKEQLLARIAVLLGGRAAEELIF 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950807624 499 GEITSGAGNDFQKATDLAHSMVCDWGMS-TMGPLYYG-TKEEILLGKSVFQKSAYSELTAQEIDKEVKLIILEQYYRAKD 576
Cdd:pfam01434  81 GEVTTGASNDLEKATKIARQMVTEFGMSdKLGPVSLEeSDGNVFLGRGMGKRKPYSEETADIIDEEVKRLLEEAYERAKE 160
                         170       180       190
                  ....*....|....*....|....*....|
gi 1950807624 577 ILEQHMKQLEKVATALVEYETLDGIDVEIL 606
Cdd:pfam01434 161 ILTEHRDELEALAEALLEKETLDAEEIREL 190
AAA smart00382
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ...
201-340 7.15e-20

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: 86.66  E-value: 7.15e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950807624  201 PKGVLLMGAPGTGKTLLAKAIAGEA---GVPFFSVAGSDFVE--------------MFVGVGASRVRDLFEQGKEYAPCI 263
Cdd:smart00382   2 GEVILIVGPPGSGKTTLARALARELgppGGGVIYIDGEDILEevldqllliivggkKASGSGELRLRLALALARKLKPDV 81
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1950807624  264 IFIDEIDAVGRSRGagsgmggndEREQTLNQLLVEMDGFISNEGIIIIAATNRPDVLDPAILRPgRFDRRIIVPRPD 340
Cdd:smart00382  82 LILDEITSLLDAEQ---------EALLLLLEELRLLLLLKSEKNLTVILTTNDEKDLGPALLRR-RFDRRIVLLLIL 148
 
Name Accession Description Interval E-value
HflB COG0465
ATP-dependent Zn proteases [Posttranslational modification, protein turnover, chaperones];
27-609 0e+00

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


Pssm-ID: 440233 [Multi-domain]  Cd Length: 583  Bit Score: 932.91  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950807624  27 IGITCAILFQFFGDYNNPVQEKAFSDVVTALNEGQVKNLTIKGREYFGELQDGT--RFYTIGERVSVWYPILNNAheffK 104
Cdd:COG0465     1 IALLLVLLFNLFSSSSSSVKEISYSEFLQLVEAGKVKSVTIQGDRITGTLKDGTktRFTTYRVNDPELVDLLEEK----G 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950807624 105 TKYQFAPEDPVGKSQYIFQWVS-LLVFFGIFFIWVKQSKADGKG-FSFGKNRSRVLVDYESGYTFKDVAGIDECKQELQE 182
Cdd:COG0465    77 VEVTAKPPEESSWLLSLLISLLpILLLIGLWIFFMRRMQGGGGGaMSFGKSKAKLYDEDKPKVTFDDVAGVDEAKEELQE 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950807624 183 IVSFLKDPERYTRLGAEIPKGVLLMGAPGTGKTLLAKAIAGEAGVPFFSVAGSDFVEMFVGVGASRVRDLFEQGKEYAPC 262
Cdd:COG0465   157 IVDFLKDPEKFTRLGAKIPKGVLLVGPPGTGKTLLAKAVAGEAGVPFFSISGSDFVEMFVGVGASRVRDLFEQAKKNAPC 236
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950807624 263 IIFIDEIDAVGRSRGAGSGmGGNDEREQTLNQLLVEMDGFISNEGIIIIAATNRPDVLDPAILRPGRFDRRIIVPRPDLN 342
Cdd:COG0465   237 IIFIDEIDAVGRQRGAGLG-GGHDEREQTLNQLLVEMDGFEGNEGVIVIAATNRPDVLDPALLRPGRFDRQVVVDLPDVK 315
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950807624 343 GRESIFKIHTKNVPLDKDVNLEILARSTPGMSGADIKNLVNEAALIAAQKNQEIVNMQNFEAAREKIIMGTERRSLIMSR 422
Cdd:COG0465   316 GREAILKVHARKKPLAPDVDLEVIARRTPGFSGADLANLVNEAALLAARRNKKAVTMEDFEEAIDRVIAGPERKSRVISE 395
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950807624 423 QEIENTAYHEAGHAIVSILIGHdVDPVHKVTIIPRGQALGLTMQLPTQDRYSISKTYSENQIAIMMGGRIAEELVFGEIT 502
Cdd:COG0465   396 KEKKITAYHEAGHALVAALLPG-ADPVHKVTIIPRGRALGYTMQLPEEDRYLYTKEELLDRIAVLLGGRAAEELVFGEVT 474
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950807624 503 SGAGNDFQKATDLAHSMVCDWGMS-TMGPLYYGTKE-EILLGKSVFQKSAYSELTAQEIDKEVKLIILEQYYRAKDILEQ 580
Cdd:COG0465   475 TGASNDLERATKIARAMVTEYGMSeKLGPVAYGESEgEVFLGRDIGQSRNYSEETAREIDEEVRRIIDEAYERAKEILTE 554
                         570       580
                  ....*....|....*....|....*....
gi 1950807624 581 HMKQLEKVATALVEYETLDGIDVEILLEG 609
Cdd:COG0465   555 NRDKLDALAEALLEKETLDGEELEEILAG 583
FtsH_fam TIGR01241
ATP-dependent metalloprotease FtsH; HflB(FtsH) is a pleiotropic protein required for correct ...
118-608 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: 776.46  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950807624 118 SQYIFQWV-SLLVFFGIFFIWVKQSKADGKG-FSFGKNRSRVLVDYESGYTFKDVAGIDECKQELQEIVSFLKDPERYTR 195
Cdd:TIGR01241   3 LGFLFSLLpPILLLVGVWFFFRRQMQGGGGRaFSFGKSKAKLLNEEKPKVTFKDVAGIDEAKEELMEIVDFLKNPSKFTK 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950807624 196 LGAEIPKGVLLMGAPGTGKTLLAKAIAGEAGVPFFSVAGSDFVEMFVGVGASRVRDLFEQGKEYAPCIIFIDEIDAVGRS 275
Cdd:TIGR01241  83 LGAKIPKGVLLVGPPGTGKTLLAKAVAGEAGVPFFSISGSDFVEMFVGVGASRVRDLFEQAKKNAPCIIFIDEIDAVGRQ 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950807624 276 RGAGSGmGGNDEREQTLNQLLVEMDGFISNEGIIIIAATNRPDVLDPAILRPGRFDRRIIVPRPDLNGRESIFKIHTKNV 355
Cdd:TIGR01241 163 RGAGLG-GGNDEREQTLNQLLVEMDGFGTNTGVIVIAATNRPDVLDPALLRPGRFDRQVVVDLPDIKGREEILKVHAKNK 241
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950807624 356 PLDKDVNLEILARSTPGMSGADIKNLVNEAALIAAQKNQEIVNMQNFEAAREKIIMGTERRSLIMSRQEIENTAYHEAGH 435
Cdd:TIGR01241 242 KLAPDVDLKAVARRTPGFSGADLANLLNEAALLAARKNKTEITMNDIEEAIDRVIAGPEKKSRVISEKEKKLVAYHEAGH 321
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950807624 436 AIVSILIgHDVDPVHKVTIIPRGQALGLTMQLPTQDRYSISKTYSENQIAIMMGGRIAEELVFGEITSGAGNDFQKATDL 515
Cdd:TIGR01241 322 ALVGLLL-KDADPVHKVTIIPRGQALGYTQFLPEEDKYLYTKSQLLAQIAVLLGGRAAEEIIFGEVTTGASNDIKQATNI 400
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950807624 516 AHSMVCDWGMS-TMGPLYYGTKE-EILLGKSVFQKSAYSELTAQEIDKEVKLIILEQYYRAKDILEQHMKQLEKVATALV 593
Cdd:TIGR01241 401 ARAMVTEWGMSdKLGPVAYGSDGgDVFLGRGFAKAKEYSEETAREIDEEVKRIIEEAYKRAKQILTENRDELELLAKALL 480
                         490
                  ....*....|....*
gi 1950807624 594 EYETLDGIDVEILLE 608
Cdd:TIGR01241 481 EKETITREEIKELLA 495
hflB PRK10733
ATP-dependent zinc metalloprotease FtsH;
21-613 0e+00

ATP-dependent zinc metalloprotease FtsH;


Pssm-ID: 182683 [Multi-domain]  Cd Length: 644  Bit Score: 636.31  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950807624  21 LVKWIFIGITCAILFQFFGDYNNPVQEKAFSDVVTALNEGQVKNLTIKGREYFGELQDGTRFYTIgerVSVWYP-ILNNA 99
Cdd:PRK10733    5 LILWLVIAVVLMSVFQSFGPSESNGRKVDYSTFLQEVNQDQVREARINGREINVTKKDSNRYTTY---IPVNDPkLLDNL 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950807624 100 HEFFKTKYQFAPEDPVGKSQYIFQWVSLLVFFGIFFIWVKQSKADG-KG-FSFGKNRSRVLVDYESGYTFKDVAGIDECK 177
Cdd:PRK10733   82 LTKNVKVVGEPPEEPSLLASIFISWFPMLLLIGVWIFFMRQMQGGGgKGaMSFGKSKARMLTEDQIKTTFADVAGCDEAK 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950807624 178 QELQEIVSFLKDPERYTRLGAEIPKGVLLMGAPGTGKTLLAKAIAGEAGVPFFSVAGSDFVEMFVGVGASRVRDLFEQGK 257
Cdd:PRK10733  162 EEVAELVEYLREPSRFQKLGGKIPKGVLMVGPPGTGKTLLAKAIAGEAKVPFFTISGSDFVEMFVGVGASRVRDMFEQAK 241
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950807624 258 EYAPCIIFIDEIDAVGRSRGAGSGmGGNDEREQTLNQLLVEMDGFISNEGIIIIAATNRPDVLDPAILRPGRFDRRIIVP 337
Cdd:PRK10733  242 KAAPCIIFIDEIDAVGRQRGAGLG-GGHDEREQTLNQMLVEMDGFEGNEGIIVIAATNRPDVLDPALLRPGRFDRQVVVG 320
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950807624 338 RPDLNGRESIFKIHTKNVPLDKDVNLEILARSTPGMSGADIKNLVNEAALIAAQKNQEIVNMQNFEAAREKIIMGTERRS 417
Cdd:PRK10733  321 LPDVRGREQILKVHMRRVPLAPDIDAAIIARGTPGFSGADLANLVNEAALFAARGNKRVVSMVEFEKAKDKIMMGAERRS 400
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950807624 418 LIMSRQEIENTAYHEAGHAIVSILIGHDvDPVHKVTIIPRGQALGLTMQLPTQDRYSISKTYSENQIAIMMGGRIAEELV 497
Cdd:PRK10733  401 MVMTEAQKESTAYHEAGHAIIGRLVPEH-DPVHKVTIIPRGRALGVTFFLPEGDAISASRQKLESQISTLYGGRLAEEII 479
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950807624 498 FG--EITSGAGNDFQKATDLAHSMVCDWGMS-TMGPLYYGTKE-EILLGKSVFQKSAYSELTAQEIDKEVKLIILEQYYR 573
Cdd:PRK10733  480 YGpeHVSTGASNDIKVATNLARNMVTQWGFSeKLGPLLYAEEEgEVFLGRSVAKAKHMSDETARIIDQEVKALIERNYNR 559
                         570       580       590       600
                  ....*....|....*....|....*....|....*....|
gi 1950807624 574 AKDILEQHMKQLEKVATALVEYETLDGIDVEILLEGKSLK 613
Cdd:PRK10733  560 ARQLLTDNMDILHAMKDALMKYETIDAPQIDDLMARRDVR 599
ftsH CHL00176
cell division protein; Validated
114-620 0e+00

cell division protein; Validated


Pssm-ID: 214386 [Multi-domain]  Cd Length: 638  Bit Score: 579.70  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950807624 114 PVGKSQYIFQWVSLLVFFGIF---FIWVKQSKADGKG------FSFGKNRSRVLVDYESGYTFKDVAGIDECKQELQEIV 184
Cdd:CHL00176  120 PPVLKSNIVTILSNLLLPLILigvLWFFFQRSSNFKGgpgqnlMNFGKSKARFQMEADTGITFRDIAGIEEAKEEFEEVV 199
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950807624 185 SFLKDPERYTRLGAEIPKGVLLMGAPGTGKTLLAKAIAGEAGVPFFSVAGSDFVEMFVGVGASRVRDLFEQGKEYAPCII 264
Cdd:CHL00176  200 SFLKKPERFTAVGAKIPKGVLLVGPPGTGKTLLAKAIAGEAEVPFFSISGSEFVEMFVGVGAARVRDLFKKAKENSPCIV 279
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950807624 265 FIDEIDAVGRSRGAGSGmGGNDEREQTLNQLLVEMDGFISNEGIIIIAATNRPDVLDPAILRPGRFDRRIIVPRPDLNGR 344
Cdd:CHL00176  280 FIDEIDAVGRQRGAGIG-GGNDEREQTLNQLLTEMDGFKGNKGVIVIAATNRVDILDAALLRPGRFDRQITVSLPDREGR 358
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950807624 345 ESIFKIHTKNVPLDKDVNLEILARSTPGMSGADIKNLVNEAALIAAQKNQEIVNMQNFEAAREKIIMGTERRSLIMSRqe 424
Cdd:CHL00176  359 LDILKVHARNKKLSPDVSLELIARRTPGFSGADLANLLNEAAILTARRKKATITMKEIDTAIDRVIAGLEGTPLEDSK-- 436
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950807624 425 IENT-AYHEAGHAIVSILIGHDvDPVHKVTIIPRGQALGLTMQLPTQDRYSISKTYSENQIAIMMGGRIAEELVFG--EI 501
Cdd:CHL00176  437 NKRLiAYHEVGHAIVGTLLPNH-DPVQKVTLIPRGQAKGLTWFTPEEDQSLVSRSQILARIVGALGGRAAEEVVFGstEV 515
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950807624 502 TSGAGNDFQKATDLAHSMVCDWGMSTMGP--LYYGTKEEILLGKSVFQKSAYSELTAQEIDKEVKLIILEQYYRAKDILE 579
Cdd:CHL00176  516 TTGASNDLQQVTNLARQMVTRFGMSSIGPisLESNNSTDPFLGRFMQRNSEYSEEIADKIDMEVRSILHTCYQYAYQILK 595
                         490       500       510       520
                  ....*....|....*....|....*....|....*....|.
gi 1950807624 580 QHMKQLEKVATALVEYETLDGIDVEILLEGKSLKKDKPYFK 620
Cdd:CHL00176  596 DNRVLIDLLVELLLQKETIDGDEFREIVNSYTILPPKKTWK 636
RecA-like_FtsH cd19501
ATP-dependent zinc metalloprotease FtsH; FtsH ATPase is a processive, ATP-dependent zinc ...
166-336 3.51e-122

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: 361.16  E-value: 3.51e-122
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950807624 166 TFKDVAGIDECKQELQEIVSFLKDPERYTRLGAEIPKGVLLMGAPGTGKTLLAKAIAGEAGVPFFSVAGSDFVEMFVGVG 245
Cdd:cd19501     2 TFKDVAGCEEAKEELKEVVEFLKNPEKFTKLGAKIPKGVLLVGPPGTGKTLLAKAVAGEAGVPFFSISGSDFVEMFVGVG 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950807624 246 ASRVRDLFEQGKEYAPCIIFIDEIDAVGRSRGAGSGmGGNDEREQTLNQLLVEMDGFISNEGIIIIAATNRPDVLDPAIL 325
Cdd:cd19501    82 ASRVRDLFEQAKKNAPCIVFIDEIDAVGRKRGAGLG-GGHDEREQTLNQLLVEMDGFESNTGVIVIAATNRPDVLDPALL 160
                         170
                  ....*....|.
gi 1950807624 326 RPGRFDRRIIV 336
Cdd:cd19501   161 RPGRFDRQVYV 171
RPT1 COG1222
ATP-dependent 26S proteasome regulatory subunit [Posttranslational modification, protein ...
166-415 1.57e-116

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


Pssm-ID: 440835 [Multi-domain]  Cd Length: 326  Bit Score: 352.39  E-value: 1.57e-116
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950807624 166 TFKDVAGIDECKQELQEIVS-FLKDPERYTRLGAEIPKGVLLMGAPGTGKTLLAKAIAGEAGVPFFSVAGSDFVEMFVGV 244
Cdd:COG1222    76 TFDDIGGLDEQIEEIREAVElPLKNPELFRKYGIEPPKGVLLYGPPGTGKTLLAKAVAGELGAPFIRVRGSELVSKYIGE 155
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950807624 245 GASRVRDLFEQGKEYAPCIIFIDEIDAVGRSRGagsGMGGNDEREQTLNQLLVEMDGFISNEGIIIIAATNRPDVLDPAI 324
Cdd:COG1222   156 GARNVREVFELAREKAPSIIFIDEIDAIAARRT---DDGTSGEVQRTVNQLLAELDGFESRGDVLIIAATNRPDLLDPAL 232
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950807624 325 LRPGRFDRRIIVPRPDLNGRESIFKIHTKNVPLDKDVNLEILARSTPGMSGADIKNLVNEAALIAAQKNQEIVNMQNFEA 404
Cdd:COG1222   233 LRPGRFDRVIEVPLPDEEAREEILKIHLRDMPLADDVDLDKLAKLTEGFSGADLKAIVTEAGMFAIREGRDTVTMEDLEK 312
                         250
                  ....*....|.
gi 1950807624 405 AREKIIMGTER 415
Cdd:COG1222   313 AIEKVKKKTET 323
PRK03992 PRK03992
proteasome-activating nucleotidase; Provisional
166-421 2.33e-105

proteasome-activating nucleotidase; Provisional


Pssm-ID: 179699 [Multi-domain]  Cd Length: 389  Bit Score: 326.02  E-value: 2.33e-105
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950807624 166 TFKDVAGIDECKQELQEIVSF-LKDPERYTRLGAEIPKGVLLMGAPGTGKTLLAKAIAGEAGVPFFSVAGSDFVEMFVGV 244
Cdd:PRK03992  129 TYEDIGGLEEQIREVREAVELpLKKPELFEEVGIEPPKGVLLYGPPGTGKTLLAKAVAHETNATFIRVVGSELVQKFIGE 208
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950807624 245 GASRVRDLFEQGKEYAPCIIFIDEIDAVGRSRgAGSGMGGNDEREQTLNQLLVEMDGFISNEGIIIIAATNRPDVLDPAI 324
Cdd:PRK03992  209 GARLVRELFELAREKAPSIIFIDEIDAIAAKR-TDSGTSGDREVQRTLMQLLAEMDGFDPRGNVKIIAATNRIDILDPAI 287
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950807624 325 LRPGRFDRRIIVPRPDLNGRESIFKIHTKNVPLDKDVNLEILARSTPGMSGADIKNLVNEAALIAAQKNQEIVNMQNFEA 404
Cdd:PRK03992  288 LRPGRFDRIIEVPLPDEEGRLEILKIHTRKMNLADDVDLEELAELTEGASGADLKAICTEAGMFAIRDDRTEVTMEDFLK 367
                         250
                  ....*....|....*..
gi 1950807624 405 AREKIIMGTERRSLIMS 421
Cdd:PRK03992  368 AIEKVMGKEEKDSMEEP 384
26Sp45 TIGR01242
26S proteasome subunit P45 family; Many proteins may score above the trusted cutoff because an ...
159-410 1.63e-86

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: 276.29  E-value: 1.63e-86
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950807624 159 VDYESGYTFKDVAGIDECKQELQEIVSF-LKDPERYTRLGAEIPKGVLLMGAPGTGKTLLAKAIAGEAGVPFFSVAGSDF 237
Cdd:TIGR01242 113 VEERPNVSYEDIGGLEEQIREIREAVELpLKHPELFEEVGIEPPKGVLLYGPPGTGKTLLAKAVAHETNATFIRVVGSEL 192
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950807624 238 VEMFVGVGASRVRDLFEQGKEYAPCIIFIDEIDAVGRSRgAGSGMGGNDEREQTLNQLLVEMDGFISNEGIIIIAATNRP 317
Cdd:TIGR01242 193 VRKYIGEGARLVREIFELAKEKAPSIIFIDEIDAIAAKR-TDSGTSGDREVQRTLMQLLAELDGFDPRGNVKVIAATNRP 271
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950807624 318 DVLDPAILRPGRFDRRIIVPRPDLNGRESIFKIHTKNVPLDKDVNLEILARSTPGMSGADIKNLVNEAALIAAQKNQEIV 397
Cdd:TIGR01242 272 DILDPALLRPGRFDRIIEVPLPDFEGRLEILKIHTRKMKLAEDVDLEAIAKMTEGASGADLKAICTEAGMFAIREERDYV 351
                         250
                  ....*....|...
gi 1950807624 398 NMQNFEAAREKII 410
Cdd:TIGR01242 352 TMDDFIKAVEKVL 364
SpoVK COG0464
AAA+-type ATPase, SpoVK/Ycf46/Vps4 family [Cell wall/membrane/envelope biogenesis, Cell cycle ...
167-411 1.78e-81

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: 264.08  E-value: 1.78e-81
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950807624 167 FKDVAGIDECKQELQEIVS-FLKDPERYTRLGAEIPKGVLLMGAPGTGKTLLAKAIAGEAGVPFFSVAGSDFVEMFVGVG 245
Cdd:COG0464   156 LDDLGGLEEVKEELRELVAlPLKRPELREEYGLPPPRGLLLYGPPGTGKTLLARALAGELGLPLIEVDLSDLVSKYVGET 235
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950807624 246 ASRVRDLFEQGKEYAPCIIFIDEIDAVGRSRGAGSGMGGNdereQTLNQLLVEMDGFisNEGIIIIAATNRPDVLDPAIL 325
Cdd:COG0464   236 EKNLREVFDKARGLAPCVLFIDEADALAGKRGEVGDGVGR----RVVNTLLTEMEEL--RSDVVVIAATNRPDLLDPALL 309
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950807624 326 RpgRFDRRIIVPRPDLNGRESIFKIHTKNVPLDKDVNLEILARSTPGMSGADIKNLVNEAALIAAQKNQEIVNMQNFEAA 405
Cdd:COG0464   310 R--RFDEIIFFPLPDAEERLEIFRIHLRKRPLDEDVDLEELAEATEGLSGADIRNVVRRAALQALRLGREPVTTEDLLEA 387

                  ....*.
gi 1950807624 406 REKIIM 411
Cdd:COG0464   388 LEREDI 393
Peptidase_M41 pfam01434
Peptidase family M41;
419-606 6.33e-80

Peptidase family M41;


Pssm-ID: 460210 [Multi-domain]  Cd Length: 190  Bit Score: 252.52  E-value: 6.33e-80
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950807624 419 IMSRQEIENTAYHEAGHAIVSILIgHDVDPVHKVTIIPRGQALGLTMQLPTQDRYSISKTYSENQIAIMMGGRIAEELVF 498
Cdd:pfam01434   2 VISEEEKKIVAYHEAGHALVGLLL-PGADPVHKVTIIPRGQALGYTQFLPEEDKLLYTKEQLLARIAVLLGGRAAEELIF 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950807624 499 GEITSGAGNDFQKATDLAHSMVCDWGMS-TMGPLYYG-TKEEILLGKSVFQKSAYSELTAQEIDKEVKLIILEQYYRAKD 576
Cdd:pfam01434  81 GEVTTGASNDLEKATKIARQMVTEFGMSdKLGPVSLEeSDGNVFLGRGMGKRKPYSEETADIIDEEVKRLLEEAYERAKE 160
                         170       180       190
                  ....*....|....*....|....*....|
gi 1950807624 577 ILEQHMKQLEKVATALVEYETLDGIDVEIL 606
Cdd:pfam01434 161 ILTEHRDELEALAEALLEKETLDAEEIREL 190
CDC48 TIGR01243
AAA family ATPase, CDC48 subfamily; This subfamily of the AAA family ATPases includes two ...
167-410 1.20e-76

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: 260.61  E-value: 1.20e-76
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950807624 167 FKDVAGIDECKQELQEIVSF-LKDPERYTRLGAEIPKGVLLMGAPGTGKTLLAKAIAGEAGVPFFSVAGSDFVEMFVGVG 245
Cdd:TIGR01243 452 WSDIGGLEEVKQELREAVEWpLKHPEIFEKMGIRPPKGVLLFGPPGTGKTLLAKAVATESGANFIAVRGPEILSKWVGES 531
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950807624 246 ASRVRDLFEQGKEYAPCIIFIDEIDAVGRSRGAGSGMGGNDereQTLNQLLVEMDGFISNEGIIIIAATNRPDVLDPAIL 325
Cdd:TIGR01243 532 EKAIREIFRKARQAAPAIIFFDEIDAIAPARGARFDTSVTD---RIVNQLLTEMDGIQELSNVVVIAATNRPDILDPALL 608
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950807624 326 RPGRFDRRIIVPRPDLNGRESIFKIHTKNVPLDKDVNLEILARSTPGMSGADIKNLVNEAALIAAQKNQEIVNMQNFEAA 405
Cdd:TIGR01243 609 RPGRFDRLILVPPPDEEARKEIFKIHTRSMPLAEDVDLEELAEMTEGYTGADIEAVCREAAMAALRESIGSPAKEKLEVG 688

                  ....*
gi 1950807624 406 REKII 410
Cdd:TIGR01243 689 EEEFL 693
RecA-like_PAN_like cd19502
proteasome activating nucleotidase PAN and related proteasome subunits; This subfamily ...
166-334 1.07e-67

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: 219.52  E-value: 1.07e-67
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950807624 166 TFKDVAGIDECKQELQEIVSF-LKDPERYTRLGAEIPKGVLLMGAPGTGKTLLAKAIAGEAGVPFFSVAGSDFVEMFVGV 244
Cdd:cd19502     1 TYEDIGGLDEQIREIREVVELpLKHPELFEELGIEPPKGVLLYGPPGTGKTLLAKAVANHTDATFIRVVGSELVQKYIGE 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950807624 245 GASRVRDLFEQGKEYAPCIIFIDEIDAVGRSRGaGSGMGGNDEREQTLNQLLVEMDGFISNEGIIIIAATNRPDVLDPAI 324
Cdd:cd19502    81 GARLVRELFEMAREKAPSIIFIDEIDAIGAKRF-DSGTGGDREVQRTMLELLNQLDGFDPRGNIKVIMATNRPDILDPAL 159
                         170
                  ....*....|
gi 1950807624 325 LRPGRFDRRI 334
Cdd:cd19502   160 LRPGRFDRKI 169
COG1223 COG1223
Predicted ATPase, AAA+ superfamily [General function prediction only];
167-409 3.26e-65

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


Pssm-ID: 440836 [Multi-domain]  Cd Length: 246  Bit Score: 215.90  E-value: 3.26e-65
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950807624 167 FKDVAGIDECKQELQEIVSFLKDPERYTRLGAEIPKGVLLMGAPGTGKTLLAKAIAGEAGVPFFSVAGSDFVEMFVGVGA 246
Cdd:COG1223     1 LDDVVGQEEAKKKLKLIIKELRRRENLRKFGLWPPRKILFYGPPGTGKTMLAEALAGELKLPLLTVRLDSLIGSYLGETA 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950807624 247 SRVRDLFEQGKEyAPCIIFIDEIDAVGRSRGAGSGMGgndEREQTLNQLLVEMDGFisNEGIIIIAATNRPDVLDPAILR 326
Cdd:COG1223    81 RNLRKLFDFARR-APCVIFFDEFDAIAKDRGDQNDVG---EVKRVVNALLQELDGL--PSGSVVIAATNHPELLDSALWR 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950807624 327 pgRFDRRIIVPRPDLNGRESIFKIHTKNVPLDKDVNLEILARSTPGMSGADIKNLVNEAALIAAQKNQEIVNMQNFEAAR 406
Cdd:COG1223   155 --RFDEVIEFPLPDKEERKEILELNLKKFPLPFELDLKKLAKKLEGLSGADIEKVLKTALKKAILEDREKVTKEDLEEAL 232

                  ...
gi 1950807624 407 EKI 409
Cdd:COG1223   233 KQR 235
PTZ00361 PTZ00361
26 proteosome regulatory subunit 4-like protein; Provisional
166-410 1.07e-64

26 proteosome regulatory subunit 4-like protein; Provisional


Pssm-ID: 185575 [Multi-domain]  Cd Length: 438  Bit Score: 220.80  E-value: 1.07e-64
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950807624 166 TFKDVAGIDECKQELQEIVSF-LKDPERYTRLGAEIPKGVLLMGAPGTGKTLLAKAIAGEAGVPFFSVAGSDFVEMFVGV 244
Cdd:PTZ00361  181 SYADIGGLEQQIQEIKEAVELpLTHPELYDDIGIKPPKGVILYGPPGTGKTLLAKAVANETSATFLRVVGSELIQKYLGD 260
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950807624 245 GASRVRDLFEQGKEYAPCIIFIDEIDAVGRSRgAGSGMGGNDEREQTLNQLLVEMDGFISNEGIIIIAATNRPDVLDPAI 324
Cdd:PTZ00361  261 GPKLVRELFRVAEENAPSIVFIDEIDAIGTKR-YDATSGGEKEIQRTMLELLNQLDGFDSRGDVKVIMATNRIESLDPAL 339
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950807624 325 LRPGRFDRRIIVPRPDLNGRESIFKIHTKNVPLDKDVNLEILARSTPGMSGADIKNLVNEAALIAAQKNQEIVNMQNFEA 404
Cdd:PTZ00361  340 IRPGRIDRKIEFPNPDEKTKRRIFEIHTSKMTLAEDVDLEEFIMAKDELSGADIKAICTEAGLLALRERRMKVTQADFRK 419

                  ....*.
gi 1950807624 405 AREKII 410
Cdd:PTZ00361  420 AKEKVL 425
PTZ00454 PTZ00454
26S protease regulatory subunit 6B-like protein; Provisional
166-416 1.28e-63

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


Pssm-ID: 240423 [Multi-domain]  Cd Length: 398  Bit Score: 216.55  E-value: 1.28e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950807624 166 TFKDVAGIDECKQELQEIVSF-LKDPERYTRLGAEIPKGVLLMGAPGTGKTLLAKAIAGEAGVPFFSVAGSDFVEMFVGV 244
Cdd:PTZ00454  143 TYSDIGGLDIQKQEIREAVELpLTCPELYEQIGIDPPRGVLLYGPPGTGKTMLAKAVAHHTTATFIRVVGSEFVQKYLGE 222
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950807624 245 GASRVRDLFEQGKEYAPCIIFIDEIDAVGRSRgAGSGMGGNDEREQTLNQLLVEMDGFISNEGIIIIAATNRPDVLDPAI 324
Cdd:PTZ00454  223 GPRMVRDVFRLARENAPSIIFIDEVDSIATKR-FDAQTGADREVQRILLELLNQMDGFDQTTNVKVIMATNRADTLDPAL 301
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950807624 325 LRPGRFDRRIIVPRPDLNGRESIFKIHTKNVPLDKDVNLEILARSTPGMSGADIKNLVNEAALIAAQKNQEIVNMQNFEA 404
Cdd:PTZ00454  302 LRPGRLDRKIEFPLPDRRQKRLIFQTITSKMNLSEEVDLEDFVSRPEKISAADIAAICQEAGMQAVRKNRYVILPKDFEK 381
                         250
                  ....*....|..
gi 1950807624 405 AREKIIMGTERR 416
Cdd:PTZ00454  382 GYKTVVRKTDRD 393
CDC48 TIGR01243
AAA family ATPase, CDC48 subfamily; This subfamily of the AAA family ATPases includes two ...
166-407 2.05e-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: 224.40  E-value: 2.05e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950807624 166 TFKDVAGIDECKQELQEIVSF-LKDPERYTRLGAEIPKGVLLMGAPGTGKTLLAKAIAGEAGVPFFSVAGSDFVEMFVGV 244
Cdd:TIGR01243 176 TYEDIGGLKEAKEKIREMVELpMKHPELFEHLGIEPPKGVLLYGPPGTGKTLLAKAVANEAGAYFISINGPEIMSKYYGE 255
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950807624 245 GASRVRDLFEQGKEYAPCIIFIDEIDAVGRSRGAGSGmggnDEREQTLNQLLVEMDGFISNEGIIIIAATNRPDVLDPAI 324
Cdd:TIGR01243 256 SEERLREIFKEAEENAPSIIFIDEIDAIAPKREEVTG----EVEKRVVAQLLTLMDGLKGRGRVIVIGATNRPDALDPAL 331
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950807624 325 LRPGRFDRRIIVPRPDLNGRESIFKIHTKNVPLDKDVNLEILARSTPGMSGADIKNLVNEAALIAAQK--NQEIVNMQNF 402
Cdd:TIGR01243 332 RRPGRFDREIVIRVPDKRARKEILKVHTRNMPLAEDVDLDKLAEVTHGFVGADLAALAKEAAMAALRRfiREGKINFEAE 411

                  ....*
gi 1950807624 403 EAARE 407
Cdd:TIGR01243 412 EIPAE 416
RecA-like_protease cd19481
proteases similar to RecA; RecA-like NTPases. This family includes the NTP binding domain of ...
177-336 3.38e-61

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: 201.74  E-value: 3.38e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950807624 177 KQELQEIVSFLKDPERYTRLGAEIPKGVLLMGAPGTGKTLLAKAIAGEAGVPFFSVAGSDFVEMFVGVGASRVRDLFEQG 256
Cdd:cd19481     2 KASLREAVEAPRRGSRLRRYGLGLPKGILLYGPPGTGKTLLAKALAGELGLPLIVVKLSSLLSKYVGESEKNLRKIFERA 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950807624 257 KEYAPCIIFIDEIDAVGRSRgagSGMGGNDEREQTLNQLLVEMDGFISNEGIIIIAATNRPDVLDPAILRPGRFDRRIIV 336
Cdd:cd19481    82 RRLAPCILFIDEIDAIGRKR---DSSGESGELRRVLNQLLTELDGVNSRSKVLVIAATNRPDLLDPALLRPGRFDEVIEF 158
RecA-like_CDC48_r2-like cd19511
second of two ATPase domains of CDC48/p97, PEX1 and -6, VAT and NVL, and similar ATPase ...
177-336 5.63e-61

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: 201.36  E-value: 5.63e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950807624 177 KQELQEIVSF-LKDPERYTRLGAEIPKGVLLMGAPGTGKTLLAKAIAGEAGVPFFSVAGSDFVEMFVGVGASRVRDLFEQ 255
Cdd:cd19511     2 KRELKEAVEWpLKHPDAFKRLGIRPPKGVLLYGPPGCGKTLLAKALASEAGLNFISVKGPELFSKYVGESERAVREIFQK 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950807624 256 GKEYAPCIIFIDEIDAVGRSRGAGSGMGGNDereQTLNQLLVEMDGFISNEGIIIIAATNRPDVLDPAILRPGRFDRRII 335
Cdd:cd19511    82 ARQAAPCIIFFDEIDSLAPRRGQSDSSGVTD---RVVSQLLTELDGIESLKGVVVIAATNRPDMIDPALLRPGRLDKLIY 158

                  .
gi 1950807624 336 V 336
Cdd:cd19511   159 V 159
RecA-like_CDC48_NLV2_r1-like cd19503
first of two ATPase domains of CDC48 and NLV2, and similar ATPase domains; CDC48 in yeast and ...
169-336 2.78e-58

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: 194.43  E-value: 2.78e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950807624 169 DVAGIDECKQELQEIVSF-LKDPERYTRLGAEIPKGVLLMGAPGTGKTLLAKAIAGEAGVPFFSVAGSDFVEMFVGVGAS 247
Cdd:cd19503     1 DIGGLDEQIASLKELIELpLKYPELFRALGLKPPRGVLLHGPPGTGKTLLARAVANEAGANFLSISGPSIVSKYLGESEK 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950807624 248 RVRDLFEQGKEYAPCIIFIDEIDAVGRSRGAGSGmggndEREQTL-NQLLVEMDGFISNEGIIIIAATNRPDVLDPAILR 326
Cdd:cd19503    81 NLREIFEEARSHAPSIIFIDEIDALAPKREEDQR-----EVERRVvAQLLTLMDGMSSRGKVVVIAATNRPDAIDPALRR 155
                         170
                  ....*....|
gi 1950807624 327 PGRFDRRIIV 336
Cdd:cd19503   156 PGRFDREVEI 165
RecA-like_VCP_r2 cd19529
second of two ATPase domains of Valosin-containing protein-like ATPase (VAT) and similar ...
177-336 6.49e-56

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: 187.70  E-value: 6.49e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950807624 177 KQELQEIVSF-LKDPERYTRLGAEIPKGVLLMGAPGTGKTLLAKAIAGEAGVPFFSVAGSDFVEMFVGVGASRVRDLFEQ 255
Cdd:cd19529     2 KQELKEAVEWpLLKPEVFKRLGIRPPKGILLYGPPGTGKTLLAKAVATESNANFISVKGPELLSKWVGESEKAIREIFRK 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950807624 256 GKEYAPCIIFIDEIDAVGRSRGAGsgmGGNDEREQTLNQLLVEMDGFISNEGIIIIAATNRPDVLDPAILRPGRFDRRII 335
Cdd:cd19529    82 ARQVAPCVIFFDEIDSIAPRRGTT---GDSGVTERVVNQLLTELDGLEEMNGVVVIAATNRPDIIDPALLRAGRFDRLIY 158

                  .
gi 1950807624 336 V 336
Cdd:cd19529   159 I 159
RecA-like_CDC48_r2-like cd19528
second of two ATPase domains of CDC48 and similar ATPase domains; CDC48 in yeast and p97 or ...
177-336 1.84e-54

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: 183.87  E-value: 1.84e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950807624 177 KQELQEIVSF-LKDPERYTRLGAEIPKGVLLMGAPGTGKTLLAKAIAGEAGVPFFSVAGSDFVEMFVGVGASRVRDLFEQ 255
Cdd:cd19528     2 KRELQELVQYpVEHPDKFLKFGMTPSKGVLFYGPPGCGKTLLAKAIANECQANFISVKGPELLTMWFGESEANVRDIFDK 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950807624 256 GKEYAPCIIFIDEIDAVGRSRGAGSGmGGNDEREQTLNQLLVEMDGFISNEGIIIIAATNRPDVLDPAILRPGRFDRRII 335
Cdd:cd19528    82 ARAAAPCVLFFDELDSIAKARGGNIG-DAGGAADRVINQILTEMDGMNTKKNVFIIGATNRPDIIDPAILRPGRLDQLIY 160

                  .
gi 1950807624 336 V 336
Cdd:cd19528   161 I 161
AAA pfam00004
ATPase family associated with various cellular activities (AAA); AAA family proteins often ...
204-338 8.86e-53

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: 178.17  E-value: 8.86e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950807624 204 VLLMGAPGTGKTLLAKAIAGEAGVPFFSVAGSDFVEMFVGVGASRVRDLFEQGKEYAPCIIFIDEIDAVGRSRGAgsgmG 283
Cdd:pfam00004   1 LLLYGPPGTGKTTLAKAVAKELGAPFIEISGSELVSKYVGESEKRLRELFEAAKKLAPCVIFIDEIDALAGSRGS----G 76
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1950807624 284 GNDEREQTLNQLLVEMDGFISNEG-IIIIAATNRPDVLDPAILrpGRFDRRIIVPR 338
Cdd:pfam00004  77 GDSESRRVVNQLLTELDGFTSSNSkVIVIAATNRPDKLDPALL--GRFDRIIEFPL 130
RecA-like_NVL_r2-like cd19530
second of two ATPase domains of NVL (nuclear VCP-like protein) and similar ATPase domains; NVL ...
173-336 1.50e-50

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: 173.44  E-value: 1.50e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950807624 173 IDECKQELQ-EIVSFLKDPERYTRLGAEIPKGVLLMGAPGTGKTLLAKAIAGEAGVPFFSVAGSDFVEMFVGVGASRVRD 251
Cdd:cd19530     1 LDHVREELTmSILRPIKRPDIYKALGIDLPTGVLLYGPPGCGKTLLAKAVANESGANFISVKGPELLNKYVGESERAVRQ 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950807624 252 LFEQGKEYAPCIIFIDEIDAVGRSRGAgsgmGGNDEREQTLNQLLVEMDGFISNEGIIIIAATNRPDVLDPAILRPGRFD 331
Cdd:cd19530    81 VFQRARASAPCVIFFDEVDALVPKRGD----GGSWASERVVNQLLTEMDGLEERSNVFVIAATNRPDIIDPAMLRPGRLD 156

                  ....*
gi 1950807624 332 RRIIV 336
Cdd:cd19530   157 KTLYV 161
RecA-like_NVL_r1-like cd19518
first of two ATPase domains of NVL (nuclear VCP-like protein) and similar ATPase domains; NVL ...
169-334 2.43e-50

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: 172.97  E-value: 2.43e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950807624 169 DVAGIDECKQELQEIVSFLK-DPERYTRLGAEIPKGVLLMGAPGTGKTLLAKAIAGEAGVPFFSVAGSDFVEMFVGVGAS 247
Cdd:cd19518     1 DIGGMDSTLKELCELLIHPIlPPEYFQHLGVEPPRGVLLHGPPGCGKTMLANAIAGELKVPFLKISATEIVSGVSGESEE 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950807624 248 RVRDLFEQGKEYAPCIIFIDEIDAVGRSR-GAGSGMggndEReQTLNQLLVEMDGFISNE----GIIIIAATNRPDVLDP 322
Cdd:cd19518    81 KIRELFDQAISNAPCIVFIDEIDAITPKReSAQREM----ER-RIVSQLLTCMDELNNEKtaggPVLVIGATNRPDSLDP 155
                         170
                  ....*....|..
gi 1950807624 323 AILRPGRFDRRI 334
Cdd:cd19518   156 ALRRAGRFDREI 167
RecA-like_CDC48_r1-like cd19519
first of two ATPase domains of CDC48 and similar ATPase domains; CDC48 in yeast and p97 or VCP ...
169-337 8.52e-48

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


Pssm-ID: 410927 [Multi-domain]  Cd Length: 166  Bit Score: 166.07  E-value: 8.52e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950807624 169 DVAGIDECKQELQEIVSF-LKDPERYTRLGAEIPKGVLLMGAPGTGKTLLAKAIAGEAGVPFFSVAGSDFVEMFVGVGAS 247
Cdd:cd19519     1 DIGGCRKQLAQIREMVELpLRHPELFKAIGIKPPRGILLYGPPGTGKTLIARAVANETGAFFFLINGPEIMSKLAGESES 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950807624 248 RVRDLFEQGKEYAPCIIFIDEIDAVGRSRgagSGMGGNDEReQTLNQLLVEMDGFISNEGIIIIAATNRPDVLDPAILRP 327
Cdd:cd19519    81 NLRKAFEEAEKNAPAIIFIDEIDAIAPKR---EKTHGEVER-RIVSQLLTLMDGLKQRAHVIVMAATNRPNSIDPALRRF 156
                         170
                  ....*....|
gi 1950807624 328 GRFDRRIIVP 337
Cdd:cd19519   157 GRFDREIDIG 166
RecA-like_VPS4-like cd19509
ATPase domain of VPS4, ATAD1, K, KTNA1, Spastin, FIGL-1 and similar ATPase domains; This ...
170-336 2.06e-43

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: 153.66  E-value: 2.06e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950807624 170 VAGIDECKQELQEIVSF-LKDPERYTRLGAeIPKGVLLMGAPGTGKTLLAKAIAGEAGVPFFSVAGSDFVEMFVGVGASR 248
Cdd:cd19509     1 IAGLDDAKEALKEAVILpSLRPDLFPGLRG-PPRGILLYGPPGTGKTLLARAVASESGSTFFSISASSLVSKWVGESEKI 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950807624 249 VRDLFEQGKEYAPCIIFIDEIDAVGRSRGAgsgmgGNDEREQTL-NQLLVEMDGFI--SNEGIIIIAATNRPDVLDPAIL 325
Cdd:cd19509    80 VRALFALARELQPSIIFIDEIDSLLSERGS-----GEHEASRRVkTEFLVQMDGVLnkPEDRVLVLGATNRPWELDEAFL 154
                         170
                  ....*....|.
gi 1950807624 326 RpgRFDRRIIV 336
Cdd:cd19509   155 R--RFEKRIYI 163
RecA-like_PEX6_r2 cd19527
second of two ATPase domains of Peroxisomal biogenesis factor 6 (PEX6); PEX6(also known as ...
177-336 9.31e-43

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: 151.90  E-value: 9.31e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950807624 177 KQELQEIVSF-LKDPERYTrLGAEIPKGVLLMGAPGTGKTLLAKAIAGEAGVPFFSVAGSDFVEMFVGVGASRVRDLFEQ 255
Cdd:cd19527     2 KKEILDTIQLpLEHPELFS-SGLRKRSGILLYGPPGTGKTLLAKAIATECSLNFLSVKGPELINMYIGESEANVREVFQK 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950807624 256 GKEYAPCIIFIDEIDAVGRSRGAGSGMGGNDEReqTLNQLLVEMDGF-ISNEGIIIIAATNRPDVLDPAILRPGRFDRRI 334
Cdd:cd19527    81 ARDAKPCVIFFDELDSLAPSRGNSGDSGGVMDR--VVSQLLAELDGMsSSGQDVFVIGATNRPDLLDPALLRPGRFDKLL 158

                  ..
gi 1950807624 335 IV 336
Cdd:cd19527   159 YL 160
pup_AAA TIGR03689
proteasome ATPase; In the Actinobacteria, as shown for Mycobacterium tuberculosis, some ...
166-407 7.94e-42

proteasome ATPase; In the Actinobacteria, as shown for Mycobacterium tuberculosis, some proteins are modified by ligation between an epsilon-amino group of a lysine side chain and the C-terminal carboxylate of the ubiquitin-like protein Pup. This modification leads to protein degradation by the archaeal-like proteasome found in the Actinobacteria. Members of this protein family belong to the AAA family of ATPases and tend to be clustered with the genes for Pup, the Pup ligase PafA, and structural components of the proteasome. This protein forms hexameric rings with ATPase activity. [Protein fate, Degradation of proteins, peptides, and glycopeptides]


Pssm-ID: 200312 [Multi-domain]  Cd Length: 512  Bit Score: 159.49  E-value: 7.94e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950807624 166 TFKDVAGIDECKQELQEIVS--FLKdPERYTRLGAEIPKGVLLMGAPGTGKTLLAKAIA--------GEAGVP--FFSVA 233
Cdd:TIGR03689 180 TYADIGGLGSQIEQIRDAVElpFLH-PELYREYGLKPPKGVLLYGPPGCGKTLIAKAVAnslaarigAEGGGKsyFLNIK 258
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950807624 234 GSDFVEMFVGVGASRVRDLFEQGKEYA----PCIIFIDEIDAVGRSRGAG--SGMggnderEQTL-NQLLVEMDGFISNE 306
Cdd:TIGR03689 259 GPELLNKYVGETERQIRLIFQRAREKAsegrPVIVFFDEMDSLFRTRGSGvsSDV------ETTVvPQLLAEIDGVESLD 332
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950807624 307 GIIIIAATNRPDVLDPAILRPGRFDRRIIVPRPDLNGRESIFKIH-TKNVPLDKDvnleiLARSTpGMSGADIKNLVNEA 385
Cdd:TIGR03689 333 NVIVIGASNREDMIDPAILRPGRLDVKIRIERPDAEAAADIFAKYlTDDLPLPED-----LAAHD-GDREATAAALIQRV 406
                         250       260
                  ....*....|....*....|....
gi 1950807624 386 --ALIAAQKNQEIVNMQNFEAARE 407
Cdd:TIGR03689 407 vdALYARSEANRYVEVTYANGSTE 430
RecA-like_PEX1_r2 cd19526
second of two ATPase domains of Peroxisomal biogenesis factor 1 (PEX1); PEX1(also known as ...
177-335 4.81e-41

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: 147.19  E-value: 4.81e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950807624 177 KQELQEIVSF-LKDPERYTRLGAEIPKGVLLMGAPGTGKTLLAKAIAGEAGVPFFSVAGSDFVEMFVGVGASRVRDLFEQ 255
Cdd:cd19526     2 KKALEETIEWpSKYPKIFASSPLRLRSGILLYGPPGCGKTLLASAIASECGLNFISVKGPELLNKYIGASEQNVRDLFSR 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950807624 256 GKEYAPCIIFIDEIDAVGRSRGAGSgMGGNDereQTLNQLLVEMDGFISNEGIIIIAATNRPDVLDPAILRPGRFDRRII 335
Cdd:cd19526    82 AQSAKPCILFFDEFDSIAPKRGHDS-TGVTD---RVVNQLLTQLDGVEGLDGVYVLAATSRPDLIDPALLRPGRLDKLVY 157
RecA-like_VPS4 cd19521
ATPase domain of vacuolar protein sorting-associated protein 4; Vacuolar protein ...
169-336 2.23e-38

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: 140.00  E-value: 2.23e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950807624 169 DVAGIDECKQELQEIVSF-LKDPERYTrlGAEIP-KGVLLMGAPGTGKTLLAKAIAGEAGVPFFSVAGSDFVEMFVGVGA 246
Cdd:cd19521     8 DVAGLEGAKEALKEAVILpVKFPHLFT--GNRKPwSGILLYGPPGTGKSYLAKAVATEANSTFFSVSSSDLVSKWMGESE 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950807624 247 SRVRDLFEQGKEYAPCIIFIDEIDAVGRSRGAGSgmggNDEREQTLNQLLVEMDGF-ISNEGIIIIAATNRPDVLDPAIL 325
Cdd:cd19521    86 KLVKQLFAMARENKPSIIFIDEVDSLCGTRGEGE----SEASRRIKTELLVQMNGVgNDSQGVLVLGATNIPWQLDSAIR 161
                         170
                  ....*....|.
gi 1950807624 326 RpgRFDRRIIV 336
Cdd:cd19521   162 R--RFEKRIYI 170
RecA-like_spastin cd19524
ATPase domain of spastin; Spastin is an ATP-dependent microtubule-severing protein involved in ...
169-336 1.34e-35

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: 131.90  E-value: 1.34e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950807624 169 DVAGIDECKQELQEIVSFLKD-PERYTRLGAEiPKGVLLMGAPGTGKTLLAKAIAGEAGVPFFSVAGSDFVEMFVGVGAS 247
Cdd:cd19524     1 DIAGQDLAKQALQEMVILPSLrPELFTGLRAP-ARGLLLFGPPGNGKTMLAKAVAAESNATFFNISAASLTSKYVGEGEK 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950807624 248 RVRDLFEQGKEYAPCIIFIDEIDAVGRSRGAGSgmggNDEREQTLNQLLVEMDGFISN--EGIIIIAATNRPDVLDPAIL 325
Cdd:cd19524    80 LVRALFAVARELQPSIIFIDEVDSLLSERSEGE----HEASRRLKTEFLIEFDGVQSNgdDRVLVMGATNRPQELDDAVL 155
                         170
                  ....*....|.
gi 1950807624 326 RpgRFDRRIIV 336
Cdd:cd19524   156 R--RFTKRVYV 164
RecA-like_Yta7-like cd19517
ATPase domain of Saccharomyces cerevisiae Yta7 and similar ATPase domains; Saccharomyces ...
169-332 4.79e-35

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: 130.71  E-value: 4.79e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950807624 169 DVAGIDECKQELQEIVSF-LKDPERYTRLGAEIPKGVLLMGAPGTGKTLLAKAIAGEAG-----VPFFSVAGSDFVEMFV 242
Cdd:cd19517     1 DIGGLSHYINQLKEMVFFpLLYPEVFAKFKITPPRGVLFHGPPGTGKTLMARALAAECSkggqkVSFFMRKGADCLSKWV 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950807624 243 GVGASRVRDLFEQGKEYAPCIIFIDEIDAVGRSRGAgsgmggndEREQT----LNQLLVEMDGFISNEGIIIIAATNRPD 318
Cdd:cd19517    81 GEAERQLRLLFEEAYRMQPSIIFFDEIDGLAPVRSS--------KQEQIhasiVSTLLALMDGLDNRGQVVVIGATNRPD 152
                         170
                  ....*....|....
gi 1950807624 319 VLDPAILRPGRFDR 332
Cdd:cd19517   153 ALDPALRRPGRFDR 166
RecA-like_Figl-1 cd19525
ATPase domain of Fidgetin-Like 1 (FIGL-1); FIGL-1 may participate in DNA repair in the nucleus; ...
158-336 7.40e-33

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: 125.10  E-value: 7.40e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950807624 158 LVDYESGYTFKDVAGIDECKQELQEIVSF-LKDPERYTRLGAEiPKGVLLMGAPGTGKTLLAKAIAGEAGVPFFSVAGSD 236
Cdd:cd19525    12 IMDHGPPINWADIAGLEFAKKTIKEIVVWpMLRPDIFTGLRGP-PKGILLFGPPGTGKTLIGKCIASQSGATFFSISASS 90
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950807624 237 FVEMFVGVGASRVRDLFEQGKEYAPCIIFIDEIDAVGRSRGAGSgmggNDEREQTLNQLLVEMDGFI--SNEGIIIIAAT 314
Cdd:cd19525    91 LTSKWVGEGEKMVRALFSVARCKQPAVIFIDEIDSLLSQRGEGE----HESSRRIKTEFLVQLDGATtsSEDRILVVGAT 166
                         170       180
                  ....*....|....*....|..
gi 1950807624 315 NRPDVLDPAILRpgRFDRRIIV 336
Cdd:cd19525   167 NRPQEIDEAARR--RLVKRLYI 186
RecA-like_ATAD1 cd19520
ATPase domain of ATPase family AAA domain-containing protein 1 and similar ATPase domains; ...
169-330 1.69e-32

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: 123.30  E-value: 1.69e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950807624 169 DVAGIDECKQELQEIVSF-LKDPERYTR---LGAeiPKGVLLMGAPGTGKTLLAKAIAGEAGVPFFSVAGSDFVEMFVGV 244
Cdd:cd19520     1 DIGGLDEVITELKELVILpLQRPELFDNsrlLQP--PKGVLLYGPPGCGKTMLAKATAKEAGARFINLQVSSLTDKWYGE 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950807624 245 GASRVRDLFEQGKEYAPCIIFIDEIDAVGRSRgagsGMGGNDEREQTLNQLLVEMDGFIS--NEGIIIIAATNRPDVLDP 322
Cdd:cd19520    79 SQKLVAAVFSLASKLQPSIIFIDEIDSFLRQR----SSTDHEATAMMKAEFMSLWDGLSTdgNCRVIVMGATNRPQDLDE 154
                         170
                  ....*....|
gi 1950807624 323 AILR--PGRF 330
Cdd:cd19520   155 AILRrmPKRF 164
RecA-like_KTNA1 cd19522
Katanin p60 ATPase-containing subunit A1; Katanin p60 ATPase-containing subunit A1 (KTNA1) is ...
169-336 9.88e-32

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: 121.24  E-value: 9.88e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950807624 169 DVAGIDECKQELQEIVSF-LKDPERYTrlGAEIP-KGVLLMGAPGTGKTLLAKAIAGEAGVPFFSVAGSDFVEMFVGVGA 246
Cdd:cd19522     1 DIADLEEAKKLLEEAVVLpMWMPEFFK--GIRRPwKGVLMVGPPGTGKTLLAKAVATECGTTFFNVSSSTLTSKYRGESE 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950807624 247 SRVRDLFEQGKEYAPCIIFIDEIDAVGRSRGAGSgmgGNDEREQTLNQLLVEMDGF---ISNEG----IIIIAATNRPDV 319
Cdd:cd19522    79 KLVRLLFEMARFYAPTTIFIDEIDSICSRRGTSE---EHEASRRVKSELLVQMDGVggaSENDDpskmVMVLAATNFPWD 155
                         170
                  ....*....|....*..
gi 1950807624 320 LDPAILRpgRFDRRIIV 336
Cdd:cd19522   156 IDEALRR--RLEKRIYI 170
ycf46 CHL00195
Ycf46; Provisional
153-395 7.22e-31

Ycf46; Provisional


Pssm-ID: 177094 [Multi-domain]  Cd Length: 489  Bit Score: 127.06  E-value: 7.22e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950807624 153 NRSRVLVDYESGYTFKDVAGIDECKQEL-QEIVSFLKDPERYtrlGAEIPKGVLLMGAPGTGKTLLAKAIAGEAGVPFFS 231
Cdd:CHL00195  213 SQTEILEFYSVNEKISDIGGLDNLKDWLkKRSTSFSKQASNY---GLPTPRGLLLVGIQGTGKSLTAKAIANDWQLPLLR 289
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950807624 232 VagsDFVEMF---VGVGASRVRDLFEQGKEYAPCIIFIDEID-AVGRSRGAG-SGmggndereqTLNQLLVEMDGFIS-- 304
Cdd:CHL00195  290 L---DVGKLFggiVGESESRMRQMIRIAEALSPCILWIDEIDkAFSNSESKGdSG---------TTNRVLATFITWLSek 357
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950807624 305 NEGIIIIAATNRPDVLDPAILRPGRFDRRIIVPRPDLNGRESIFKIHTKNV-PLD-KDVNLEILARSTPGMSGADIKNLV 382
Cdd:CHL00195  358 KSPVFVVATANNIDLLPLEILRKGRFDEIFFLDLPSLEEREKIFKIHLQKFrPKSwKKYDIKKLSKLSNKFSGAEIEQSI 437
                         250
                  ....*....|...
gi 1950807624 383 NEAALIAAQKNQE 395
Cdd:CHL00195  438 IEAMYIAFYEKRE 450
AAA cd00009
The AAA+ (ATPases Associated with a wide variety of cellular Activities) superfamily ...
201-337 9.06e-27

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: 106.46  E-value: 9.06e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950807624 201 PKGVLLMGAPGTGKTLLAKAIAGEA---GVPFFSVAGSDFVEMFVG---VGASRVRDLFEQGKEYAPCIIFIDEIDAVGR 274
Cdd:cd00009    19 PKNLLLYGPPGTGKTTLARAIANELfrpGAPFLYLNASDLLEGLVVaelFGHFLVRLLFELAEKAKPGVLFIDEIDSLSR 98
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1950807624 275 srgagsgmggnDEREQTLNQLLVEMDGFISNEGIIIIAATNRPDVLDPAILRPGRFDRRIIVP 337
Cdd:cd00009    99 -----------GAQNALLRVLETLNDLRIDRENVRVIGATNRPLLGDLDRALYDRLDIRIVIP 150
RecA-like_NSF-SEC18_r1-like cd19504
first of two ATPase domains of NSF and SEC18, and similar ATPase domains; ...
190-331 9.45e-27

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: 107.19  E-value: 9.45e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950807624 190 PERYTRLGAEIPKGVLLMGAPGTGKTLLAKAI-----AGEAGVpffsVAGSDFVEMFVGVGASRVRDLFEQGK-EYAPC- 262
Cdd:cd19504    24 PEIVEQLGCKHVKGILLYGPPGTGKTLMARQIgkmlnAREPKI----VNGPEILNKYVGESEANIRKLFADAEeEQRRLg 99
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1950807624 263 ------IIFIDEIDAVGRSRGagSGMGGNDEREQTLNQLLVEMDGFISNEGIIIIAATNRPDVLDPAILRPGRFD 331
Cdd:cd19504   100 ansglhIIIFDEIDAICKQRG--SMAGSTGVHDTVVNQLLSKIDGVEQLNNILVIGMTNRKDLIDEALLRPGRLE 172
RecA-like_Ycf46-like cd19507
ATPase domain of Ycf46 and similar ATPase domains; Ycf46 may play a role in the regulation of ...
169-332 8.63e-24

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: 98.21  E-value: 8.63e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950807624 169 DVAGIDECKQELQE-IVSFLKDPERYtrlGAEIPKGVLLMGAPGTGKTLLAKAIAGEAGVPFFSVAGSDFVEMFVGVGAS 247
Cdd:cd19507     1 DVGGLDNLKDWLKKrKAAFSKQASAY---GLPTPKGLLLVGIQGTGKSLTAKAIAGVWQLPLLRLDMGRLFGGLVGESES 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950807624 248 RVRDLFEQGKEYAPCIIFIDEIDAvGRSRGAGSGMGGNDEReqTLNQLLVEMDGFISNegIIIIAATNRPDVLDPAILRP 327
Cdd:cd19507    78 RLRQMIQTAEAIAPCVLWIDEIEK-GFSNADSKGDSGTSSR--VLGTFLTWLQEKKKP--VFVVATANNVQSLPPELLRK 152

                  ....*
gi 1950807624 328 GRFDR 332
Cdd:cd19507   153 GRFDE 157
RecA-like_BCS1 cd19510
Mitochondrial chaperone BCS1; Mitochondrial chaperone BCS1 is necessary for the assembly of ...
180-336 1.94e-21

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: 91.26  E-value: 1.94e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950807624 180 LQEIVSFLKDPERYTRLGAEIPKGVLLMGAPGTGKTLLAKAIAGEAGVPFFSVAGSDfvemfVGVGASRVRDLFEQGKEY 259
Cdd:cd19510     2 IDDLKDFIKNEDWYNDRGIPYRRGYLLYGPPGTGKSSFIAALAGELDYDICDLNLSE-----VVLTDDRLNHLLNTAPKQ 76
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1950807624 260 ApcIIFIDEIDA--VGRSRGAGSGMGGNDEREQTLNQLLVEMDGFISNEGIIIIAATNRPDVLDPAILRPGRFDRRIIV 336
Cdd:cd19510    77 S--IILLEDIDAafESREHNKKNPSAYGGLSRVTFSGLLNALDGVASSEERIVFMTTNHIERLDPALIRPGRVDMKIYM 153
RecA-like_fidgetin cd19523
ATPase domain of fidgetin; Fidgetin (FIGN) is a ATP-dependent microtubule severing protein. ...
169-336 5.51e-21

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


Pssm-ID: 410931 [Multi-domain]  Cd Length: 163  Bit Score: 90.33  E-value: 5.51e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950807624 169 DVAGIDECKQELQ-EIVSFLKDPERYTRLgAEIPKGVLLMGAPGTGKTLLAKAIAGEAGVPFFSVAGSDFVEMFVGVGAS 247
Cdd:cd19523     1 DIAGLGALKAAIKeEVLWPLLRPDAFSGL-LRLPRSILLFGPRGTGKTLLGRCLASQLGATFLRLRGSTLVAKWAGEGEK 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950807624 248 RVRDLFEQGKEYAPCIIFIDEIDAVGRSRGAGSGMGGndeREQTlnQLLVEMDGFISN--EGIIIIAATNRPDVLDPAIL 325
Cdd:cd19523    80 ILQASFLAARCRQPSVLFISDLDALLSSQDDEASPVG---RLQV--ELLAQLDGVLGSgeDGVLVVCTTSKPEEIDESLR 154
                         170
                  ....*....|.
gi 1950807624 326 RpgRFDRRIIV 336
Cdd:cd19523   155 R--YFSKRLLV 163
AAA smart00382
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ...
201-340 7.15e-20

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: 86.66  E-value: 7.15e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950807624  201 PKGVLLMGAPGTGKTLLAKAIAGEA---GVPFFSVAGSDFVE--------------MFVGVGASRVRDLFEQGKEYAPCI 263
Cdd:smart00382   2 GEVILIVGPPGSGKTTLARALARELgppGGGVIYIDGEDILEevldqllliivggkKASGSGELRLRLALALARKLKPDV 81
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1950807624  264 IFIDEIDAVGRSRGagsgmggndEREQTLNQLLVEMDGFISNEGIIIIAATNRPDVLDPAILRPgRFDRRIIVPRPD 340
Cdd:smart00382  82 LILDEITSLLDAEQ---------EALLLLLEELRLLLLLKSEKNLTVILTTNDEKDLGPALLRR-RFDRRIVLLLIL 148
RecA-like_Ycf2 cd19505
ATPase domain of plant YCF2; Ycf2 is a chloroplast ATPase which has an essential function; ...
195-334 4.00e-13

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


Pssm-ID: 410913 [Multi-domain]  Cd Length: 161  Bit Score: 67.79  E-value: 4.00e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950807624 195 RLGAEIPKGVLLMGAPGTGKTLLAKAIAGEAGVPFFSVAGSDFV--------------EMFVGVGASRVRDLFEQGKEYA 260
Cdd:cd19505     6 RLGLSPSKGILLIGSIETGRSYLIKSLAANSYVPLIRISLNKLLynkpdfgnddwidgMLILKESLHRLNLQFELAKAMS 85
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1950807624 261 PCIIFIDEIDAVGRSRGAGSGMGGNDEREQTLNQLLVEMDGFISNEGIIIIAATNRPDVLDPAILRPGRFDRRI 334
Cdd:cd19505    86 PCIIWIPNIHELNVNRSTQNLEEDPKLLLGLLLNYLSRDFEKSSTRNILVIASTHIPQKVDPALIAPNRLDTCI 159
AAA_lid_3 pfam17862
AAA+ lid domain; This entry represents the alpha helical AAA+ lid domain that is found to the ...
360-404 1.38e-12

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


Pssm-ID: 465537 [Multi-domain]  Cd Length: 45  Bit Score: 62.56  E-value: 1.38e-12
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 1950807624 360 DVNLEILARSTPGMSGADIKNLVNEAALIAAQKNQEIVNMQNFEA 404
Cdd:pfam17862   1 DVDLEELAERTEGFSGADLEALCREAALAALRRGLEAVTQEDLEE 45
RecA-like_ATAD3-like cd19512
ATPase domains of ATPase AAA-domain protein 3A (ATAD3A), -3B, and -3C, and similar ATPase ...
192-324 6.71e-11

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


Pssm-ID: 410920 [Multi-domain]  Cd Length: 150  Bit Score: 61.00  E-value: 6.71e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950807624 192 RYTRLGAEIPKGVLLMGAPGTGKTLLAKAIAGEAGVPFFSVAGSDFVEMfvGV-GASRVRDLFE-QGKEYAPCIIFIDEI 269
Cdd:cd19512    13 RNTKKNKGLYRNILFYGPPGTGKTLFAKKLALHSGMDYAIMTGGDVAPM--GReGVTAIHKVFDwANTSRRGLLLFVDEA 90
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1950807624 270 DAVGRSRgAGSGMggNDEREQTLNQLLVEMdGFISNEgIIIIAATNRPDVLDPAI 324
Cdd:cd19512    91 DAFLRKR-STEKI--SEDLRAALNAFLYRT-GEQSNK-FMLVLASNQPEQFDWAI 140
RecA-like_HslU cd19498
ATP-dependent protease ATPase subunit HslU; HslU is a component of the ATP-dependent protease ...
200-334 7.45e-11

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: 61.63  E-value: 7.45e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950807624 200 IPKGVLLMGAPGTGKTLLAKAIAGEAGVPFFSVAGSDFVEM-FVGVGA-SRVRDLFEQgkeyapcIIFIDEIDAVGRSrg 277
Cdd:cd19498    45 TPKNILMIGPTGVGKTEIARRLAKLAGAPFIKVEATKFTEVgYVGRDVeSIIRDLVEG-------IVFIDEIDKIAKR-- 115
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1950807624 278 aGSGMGGNDEREQTLNQLL--VEMD------GFISNEGIIIIAA----TNRPDVLDPAIlrPGRFDRRI 334
Cdd:cd19498   116 -GGSSGPDVSREGVQRDLLpiVEGStvstkyGPVKTDHILFIAAgafhVAKPSDLIPEL--QGRFPIRV 181
ycf2 CHL00206
Ycf2; Provisional
195-449 1.70e-10

Ycf2; Provisional


Pssm-ID: 214396 [Multi-domain]  Cd Length: 2281  Bit Score: 64.93  E-value: 1.70e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950807624  195 RLGAEIPKGVLLMGAPGTGKTLLAKAIAGEAGVPFFSVAGSDFVE----------------------------------- 239
Cdd:CHL00206  1624 RLALSPSRGILVIGSIGTGRSYLVKYLATNSYVPFITVFLNKFLDnkpkgfliddididdsddiddsddidrdldtellt 1703
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950807624  240 --------MFVGVGASRVRDLFEQGKEYAPCIIFIDEIDAvgrsrgagsgMGGNDEREQTLNQLLVEMDGFISN---EGI 308
Cdd:CHL00206  1704 mmnaltmdMMPKIDRFYITLQFELAKAMSPCIIWIPNIHD----------LNVNESNYLSLGLLVNSLSRDCERcstRNI 1773
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950807624  309 IIIAATNRPDVLDPAILRPGRFDRRIIVPRPDLNGRESIFKI--HTKNVPLDKDV-NLEILARSTPGMSGADIKNLVNEA 385
Cdd:CHL00206  1774 LVIASTHIPQKVDPALIAPNKLNTCIKIRRLLIPQQRKHFFTlsYTRGFHLEKKMfHTNGFGSITMGSNARDLVALTNEA 1853
                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1950807624  386 ALIAAQKNQEIVNMQNFEAAREKiiMGTERRSLIMSRQEIEnTAYHEAGHAIV--SILIGHDVDPV 449
Cdd:CHL00206  1854 LSISITQKKSIIDTNTIRSALHR--QTWDLRSQVRSVQDHG-ILFYQIGRAVAqnVLLSNCPIDPI 1916
PRK04195 PRK04195
replication factor C large subunit; Provisional
166-270 4.54e-10

replication factor C large subunit; Provisional


Pssm-ID: 235250 [Multi-domain]  Cd Length: 482  Bit Score: 62.63  E-value: 4.54e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950807624 166 TFKDVAGIDECKQELQE-IVSFLKdperytrlgAEIPKGVLLMGAPGTGKTLLAKAIAGEAGVPFFSVAGSDF-----VE 239
Cdd:PRK04195   12 TLSDVVGNEKAKEQLREwIESWLK---------GKPKKALLLYGPPGVGKTSLAHALANDYGWEVIELNASDQrtadvIE 82
                          90       100       110
                  ....*....|....*....|....*....|.
gi 1950807624 240 MFVGvGASRVRDLFEQGKEyapcIIFIDEID 270
Cdd:PRK04195   83 RVAG-EAATSGSLFGARRK----LILLDEVD 108
AAA_5 pfam07728
AAA domain (dynein-related subfamily); This Pfam entry includes some of the AAA proteins not ...
203-330 8.84e-09

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: 54.22  E-value: 8.84e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950807624 203 GVLLMGAPGTGKTLLAKAIAgEA--GVPFFSVAGSDF---------VEMFVGVGASRVRDLFEQGKEyaPCIIFIDEIDA 271
Cdd:pfam07728   1 GVLLVGPPGTGKTELAERLA-AAlsNRPVFYVQLTRDtteedlfgrRNIDPGGASWVDGPLVRAARE--GEIAVLDEINR 77
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1950807624 272 vgrsrgagsgmgGNDEREQTLNQLLVE-----MDGF----ISNEGIIIIAATNRPD----VLDPAILRpgRF 330
Cdd:pfam07728  78 ------------ANPDVLNSLLSLLDErrlllPDGGelvkAAPDGFRLIATMNPLDrglnELSPALRS--RF 135
RecA-like_superfamily cd01120
RecA-like_NTPases; RecA-like NTPases. This superfamily includes the NTP binding domain of F1 ...
204-321 1.47e-06

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


Pssm-ID: 410865 [Multi-domain]  Cd Length: 119  Bit Score: 47.50  E-value: 1.47e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950807624 204 VLLMGAPGTGKTLLAKAIAGEAGVPFFSVAGSDFVEMFVgvgaSRVRDLFEQGKeyaPCIIFIDEIDAVGRSRgagsgmg 283
Cdd:cd01120     1 ILITGPPGSGKTTLLLQFAEQALLSDEPVIFISFLDTIL----EAIEDLIEEKK---LDIIIIDSLSSLARAS------- 66
                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 1950807624 284 GNDEREQTLNQLLVEMdGFISNEGIIIIAATNRPDVLD 321
Cdd:cd01120    67 QGDRSSELLEDLAKLL-RAARNTGITVIATIHSDKFDI 103
RarA COG2256
Replication-associated recombination protein RarA (DNA-dependent ATPase) [Replication, ...
204-269 1.69e-06

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


Pssm-ID: 441857 [Multi-domain]  Cd Length: 439  Bit Score: 50.82  E-value: 1.69e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1950807624 204 VLLMGAPGTGKTLLAKAIAGEAGVPFFSV-AGSDfvemfvgvGASRVRDLFEQGKEYA----PCIIFIDEI 269
Cdd:COG2256    52 MILWGPPGTGKTTLARLIANATDAEFVALsAVTS--------GVKDIREVIEEARERRaygrRTILFVDEI 114
PRK13342 PRK13342
recombination factor protein RarA; Reviewed
204-269 4.68e-06

recombination factor protein RarA; Reviewed


Pssm-ID: 237355 [Multi-domain]  Cd Length: 413  Bit Score: 49.70  E-value: 4.68e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1950807624 204 VLLMGAPGTGKTLLAKAIAGEAGVPFFSV-AGSDfvemfvgvGASRVRDLFEQGKEYA----PCIIFIDEI 269
Cdd:PRK13342   39 MILWGPPGTGKTTLARIIAGATDAPFEALsAVTS--------GVKDLREVIEEARQRRsagrRTILFIDEI 101
RecA-like_Pch2-like cd19508
ATPase domain of Pachytene checkpoint 2 (Pch2) and similar ATPase domains; Pch2 (known as ...
204-323 1.87e-05

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


Pssm-ID: 410916 [Multi-domain]  Cd Length: 199  Bit Score: 46.29  E-value: 1.87e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950807624 204 VLLMGAPGTGKTLLAKAIAGEAGVPF-FSVAGSDFVEM--------FVGVGASRVRDLFEQGKEYAP---CIIF--IDEI 269
Cdd:cd19508    55 VLLHGPPGTGKTSLCKALAQKLSIRLsSRYRYGQLIEInshslfskWFSESGKLVTKMFQKIQELIDdkdALVFvlIDEV 134
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1950807624 270 DAVGRSRGAGSgmGGNDERE--QTLNQLLVEMDGFISNEGIIIIAATNRPDVLDPA 323
Cdd:cd19508   135 ESLAAARSASS--SGTEPSDaiRVVNAVLTQIDRIKRYHNNVILLTSNLLEKIDVA 188
MoxR COG0714
MoxR-like ATPase [General function prediction only]; MoxR-like ATPase is part of the Pathway ...
204-270 2.77e-05

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


Pssm-ID: 440478 [Multi-domain]  Cd Length: 292  Bit Score: 46.70  E-value: 2.77e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1950807624 204 VLLMGAPGTGKTLLAKAIAGEAGVPFFSVAG------SDF--VEMFVgvgASRVRDLFEQGKEYAPcIIFIDEID 270
Cdd:COG0714    34 LLLEGVPGVGKTTLAKALARALGLPFIRIQFtpdllpSDIlgTYIYD---QQTGEFEFRPGPLFAN-VLLADEIN 104
TIP49 COG1224
DNA helicase TIP49, TBP-interacting protein [Transcription];
202-237 3.68e-05

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


Pssm-ID: 440837 [Multi-domain]  Cd Length: 452  Bit Score: 46.89  E-value: 3.68e-05
                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 1950807624 202 KGVLLMGAPGTGKTLLAKAIAGEAG--VPFFSVAGSDF 237
Cdd:COG1224    65 KGILIVGPPGTGKTALAVAIARELGedTPFVAISGSEI 102
TIP49 pfam06068
TIP49 P-loop domain; This family consists of the C-terminal region of several eukaryotic and ...
202-237 5.44e-05

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


Pssm-ID: 399217 [Multi-domain]  Cd Length: 347  Bit Score: 45.76  E-value: 5.44e-05
                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 1950807624 202 KGVLLMGAPGTGKTLLAKAIAGEAG--VPFFSVAGSDF 237
Cdd:pfam06068  51 RAVLIAGPPGTGKTALAIAISKELGedTPFTSISGSEV 88
44 PHA02544
clamp loader, small subunit; Provisional
173-273 1.39e-04

clamp loader, small subunit; Provisional


Pssm-ID: 222866 [Multi-domain]  Cd Length: 316  Bit Score: 44.60  E-value: 1.39e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950807624 173 IDEC------KQELQEIVSflkdperytrlGAEIPKGVLLMGAPGTGKTLLAKAIAGEAGVPFFSVAGS----DFVEMFV 242
Cdd:PHA02544   20 IDECilpaadKETFKSIVK-----------KGRIPNMLLHSPSPGTGKTTVAKALCNEVGAEVLFVNGSdcriDFVRNRL 88
                          90       100       110
                  ....*....|....*....|....*....|.
gi 1950807624 243 GVGASRVrDLFEQGKeyapcIIFIDEIDAVG 273
Cdd:PHA02544   89 TRFASTV-SLTGGGK-----VIIIDEFDRLG 113
RecA-like_Lon cd19500
lon protease homolog 2 peroxisomal; Lon protease (also known as Lon peptidase) is an ...
168-275 1.92e-04

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: 42.93  E-value: 1.92e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950807624 168 KDVAGIDECKQELQEIVSFLKdperytrLGAEIpKGVLLM--GAPGTGKTLLAKAIAGEAGVPF--FSVAG-SDFVEM-- 240
Cdd:cd19500    10 ADHYGLEDVKERILEYLAVRK-------LKGSM-KGPILClvGPPGVGKTSLGKSIARALGRKFvrISLGGvRDEAEIrg 81
                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 1950807624 241 ----FVGVGASRVRDLFEQGKEYAPcIIFIDEIDAVGRS 275
Cdd:cd19500    82 hrrtYVGAMPGRIIQALKKAGTNNP-VFLLDEIDKIGSS 119
T7SS_EccA TIGR03922
type VII secretion AAA-ATPase EccA; This model represents the AAA family ATPase, EccA, of the ...
172-334 4.00e-04

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: 43.68  E-value: 4.00e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950807624 172 GIDECKQELQEIVSFLKDPERYTRLGAEIP---KGVLLMGAPGTGKTLLAKAIAGE-AGVPFFS------VAGSDFVEMF 241
Cdd:TIGR03922 280 GLERVKRQVAALKSSTAMALARAERGLPVAqtsNHMLFAGPPGTGKTTIARVVAKIyCGLGVLRkplvreVSRADLIGQY 359
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950807624 242 VGVGASRVRDLFEQGKEyapCIIFIDEIDA-VGRSRGAGSGMGGndereQTLNQLLVEMDGfiSNEGIIIIAATNRPDvL 320
Cdd:TIGR03922 360 IGESEAKTNEIIDSALG---GVLFLDEAYTlVETGYGQKDPFGL-----EAIDTLLARMEN--DRDRLVVIGAGYRKD-L 428
                         170
                  ....*....|....*....
gi 1950807624 321 DPAI-----LRpGRFDRRI 334
Cdd:TIGR03922 429 DKFLevnegLR-SRFTRVI 446
ruvB PRK00080
Holliday junction branch migration DNA helicase RuvB;
204-275 5.07e-04

Holliday junction branch migration DNA helicase RuvB;


Pssm-ID: 234619 [Multi-domain]  Cd Length: 328  Bit Score: 42.81  E-value: 5.07e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1950807624 204 VLLMGAPGTGKTLLAKAIAGEAGVPFFSVAG------SDFVEMFVGVGAsrvRDlfeqgkeyapcIIFIDEIDAVGRS 275
Cdd:PRK00080   54 VLLYGPPGLGKTTLANIIANEMGVNIRITSGpalekpGDLAAILTNLEE---GD-----------VLFIDEIHRLSPV 117
RecA-like_ClpX cd19497
ATP-dependent Clp protease ATP-binding subunit ClpX; ClpX is a component of the ATP-dependent ...
187-281 7.72e-04

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


Pssm-ID: 410905 [Multi-domain]  Cd Length: 251  Bit Score: 41.82  E-value: 7.72e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950807624 187 LKDPERYTRLGAEIPKG-VLLMGAPGTGKTLLAKAIAGEAGVPFfsvAGSDFVEM----FVG--VGASRVRDL------- 252
Cdd:cd19497    35 IRNNLKQKDDDVELEKSnILLIGPTGSGKTLLAQTLAKILDVPF---AIADATTLteagYVGedVENILLKLLqaadydv 111
                          90       100       110
                  ....*....|....*....|....*....|.
gi 1950807624 253 --FEQGkeyapcIIFIDEIDAVGRSRGAGSG 281
Cdd:cd19497   112 erAQRG------IVYIDEIDKIARKSENPSI 136
RuvB_N pfam05496
Holliday junction DNA helicase RuvB P-loop domain; The RuvB protein makes up part of the ...
204-269 1.07e-03

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


Pssm-ID: 398900 [Multi-domain]  Cd Length: 159  Bit Score: 40.18  E-value: 1.07e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1950807624 204 VLLMGAPGTGKTLLAKAIAGEAGVPFFSVAGSDFvemfvgvgaSRVRDL------FEQGKeyapcIIFIDEI 269
Cdd:pfam05496  36 VLLYGPPGLGKTTLANIIANEMGVNIRITSGPAI---------ERPGDLaailtnLEPGD-----VLFIDEI 93
AAA_2 pfam07724
AAA domain (Cdc48 subfamily); This Pfam entry includes some of the AAA proteins not detected ...
201-270 1.36e-03

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: 40.26  E-value: 1.36e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950807624 201 PKGV-LLMGAPGTGKTLLAKAIAGEAGV---PFFSVAGSDFVE-----MFVG-----VGASRVRDLFEQGKEYAPCIIFI 266
Cdd:pfam07724   2 PIGSfLFLGPTGVGKTELAKALAELLFGderALIRIDMSEYMEehsvsRLIGappgyVGYEEGGQLTEAVRRKPYSIVLI 81

                  ....
gi 1950807624 267 DEID 270
Cdd:pfam07724  82 DEIE 85
DnaC COG1484
DNA replication protein DnaC [Replication, recombination and repair];
202-239 2.62e-03

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


Pssm-ID: 441093 [Multi-domain]  Cd Length: 242  Bit Score: 40.15  E-value: 2.62e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 1950807624 202 KGVLLMGAPGTGKTLLAKAIAGEA---GVP--FFSVAgsDFVE 239
Cdd:COG1484   100 ENLILLGPPGTGKTHLAIALGHEAcraGYRvrFTTAP--DLVN 140
ClpX COG1219
ATP-dependent protease Clp, ATPase subunit ClpX [Posttranslational modification, protein ...
199-274 4.69e-03

ATP-dependent protease Clp, ATPase subunit ClpX [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 440832 [Multi-domain]  Cd Length: 409  Bit Score: 40.03  E-value: 4.69e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950807624 199 EIPKG-VLLMGAPGTGKTLLAKAIAGEAGVPfFSVA-----------GSDfVEmfvgvgaSRVRDLF----------EQG 256
Cdd:COG1219   106 ELEKSnILLIGPTGSGKTLLAQTLARILDVP-FAIAdattlteagyvGED-VE-------NILLKLLqaadydvekaERG 176
                          90
                  ....*....|....*...
gi 1950807624 257 keyapcIIFIDEIDAVGR 274
Cdd:COG1219   177 ------IIYIDEIDKIAR 188
GntK COG3265
Gluconate kinase [Carbohydrate transport and metabolism]; Gluconate kinase is part of the ...
201-230 5.10e-03

Gluconate kinase [Carbohydrate transport and metabolism]; Gluconate kinase is part of the Pathway/BioSystem: Non-phosphorylated Entner-Doudoroff pathway


Pssm-ID: 442496 [Multi-domain]  Cd Length: 164  Bit Score: 38.19  E-value: 5.10e-03
                          10        20        30
                  ....*....|....*....|....*....|
gi 1950807624 201 PKGVLLMGAPGTGKTLLAKAIAGEAGVPFF 230
Cdd:COG3265     1 PMVIVVMGVSGSGKSTVGQALAERLGWPFI 30
YifB COG0606
Predicted Mg-chelatase, contains ChlI-like and ATPase domains, YifB family [Posttranslational ...
204-223 7.88e-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: 39.25  E-value: 7.88e-03
                          10        20
                  ....*....|....*....|
gi 1950807624 204 VLLMGAPGTGKTLLAKAIAG 223
Cdd:COG0606   214 LLMIGPPGSGKTMLARRLPG 233
FtsH_ext pfam06480
FtsH Extracellular; This domain is found in the FtsH family of proteins. FtsH is the only ...
24-85 8.82e-03

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


Pssm-ID: 377663 [Multi-domain]  Cd Length: 103  Bit Score: 36.43  E-value: 8.82e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1950807624  24 WIFIGITCAILFQFFGDYNNPVQEKAFSDVVTALNEGQVKNLTIKGRE------YFGELQDGTRFYTI 85
Cdd:pfam06480   5 LLILLVLLLLFLLFLLSSSSSTKEISYSEFLEYLEAGKVKKVVVQDDEilptgvVEGTLKDGSKFTTY 72
 
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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