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Conserved domains on  [gi|489514706|ref|WP_003419543|]
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MULTISPECIES: ATP-dependent zinc metalloprotease FtsH [Mycobacterium]

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];
13-604 0e+00

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


:

Pssm-ID: 440233 [Multi-domain]  Cd Length: 583  Bit Score: 965.65  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489514706  13 IAVVVLLGWSFFYFSddTRGYKPVDTSVAITQINGDNVKSAQIDDreQQLRLILKKGNnetdgSEKVITKYPTGyaVDLF 92
Cdd:COG0465    1 IALLLVLLFNLFSSS--SSSVKEISYSEFLQLVEAGKVKSVTIQG--DRITGTLKDGT-----KTRFTTYRVND--PELV 69
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489514706  93 NALSAKNAKVSTVVNQGS---------------ILGellvyvlpllllvGLFVMFSRMQGGARMGFGFGKSRAKQLSKDM 157
Cdd:COG0465   70 DLLEEKGVEVTAKPPEESswllsllisllpillLIG-------------LWIFFMRRMQGGGGGAMSFGKSKAKLYDEDK 136
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489514706 158 PKTTFADVAGVDEAVEELYEIKDFLQNPSRYQALGAKIPKGVLLYGPPGTGKTLLARAVAGEAGVPFFTISGSDFVEMFV 237
Cdd:COG0465  137 PKVTFDDVAGVDEAKEELQEIVDFLKDPEKFTRLGAKIPKGVLLVGPPGTGKTLLAKAVAGEAGVPFFSISGSDFVEMFV 216
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489514706 238 GVGASRVRDLFEQAKQNSPCIIFVDEIDAVGRQRGAGLGGGHDEREQTLNQLLVEMDGFGDRAGVILIAATNRPDILDPA 317
Cdd:COG0465  217 GVGASRVRDLFEQAKKNAPCIIFIDEIDAVGRQRGAGLGGGHDEREQTLNQLLVEMDGFEGNEGVIVIAATNRPDVLDPA 296
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489514706 318 LLRPGRFDRQIPVSNPDLAGRRAVLRVHSKGKPMAADADLDGLAKRTVGMTGADLANVINEAALLTARENGTVITGPALE 397
Cdd:COG0465  297 LLRPGRFDRQVVVDLPDVKGREAILKVHARKKPLAPDVDLEVIARRTPGFSGADLANLVNEAALLAARRNKKAVTMEDFE 376
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489514706 398 EAVDRVIGGPRRKGRIISEQEKKITAYHEGGHTLAAWAMPDIEPIYKVTILARGRTGGHAVAVPEEDKGLRTRSEMIAQL 477
Cdd:COG0465  377 EAIDRVIAGPERKSRVISEKEKKITAYHEAGHALVAALLPGADPVHKVTIIPRGRALGYTMQLPEEDRYLYTKEELLDRI 456
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489514706 478 VFAMGGRAAEELVFREPTTGAVSDIEQATKIARSMVTEFGMSSKLGAVKYGSEHGDPFLGRTMGTQPDYSHEVAREIDEE 557
Cdd:COG0465  457 AVLLGGRAAEELVFGEVTTGASNDLERATKIARAMVTEYGMSEKLGPVAYGESEGEVFLGRDIGQSRNYSEETAREIDEE 536
                        570       580       590       600
                 ....*....|....*....|....*....|....*....|....*..
gi 489514706 558 VRKLIEAAHTEAWEILTEYRDVLDTLAGELLEKETLHRPELESIFAD 604
Cdd:COG0465  537 VRRIIDEAYERAKEILTENRDKLDALAEALLEKETLDGEELEEILAG 583
PRK10263 super family cl35903
DNA translocase FtsK; Provisional
622-758 1.27e-04

DNA translocase FtsK; Provisional


The actual alignment was detected with superfamily member PRK10263:

Pssm-ID: 236669 [Multi-domain]  Cd Length: 1355  Bit Score: 45.85  E-value: 1.27e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489514706  622 PSDKPPIKTPGELAIERGEPWPQPVPepafkaaiaqatQAAEAARSDAGQTGHGANGSPAGTHRSGDRQYGSTQPDYGAP 701
Cdd:PRK10263  377 PEGYPQQSQYAQPAVQYNEPLQQPVQ------------PQQPYYAPAAEQPAQQPYYAPAPEQPAQQPYYAPAPEQPVAG 444
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 489514706  702 AGWHAPgwPPRSSHRPSYSGEPAPTYP---GQPYPTGQADPGSDESSAEQDDEVSRTKPA 758
Cdd:PRK10263  445 NAWQAE--EQQSTFAPQSTYQTEQTYQqpaAQEPLYQQPQPVEQQPVVEPEPVVEETKPA 502
 
Name Accession Description Interval E-value
HflB COG0465
ATP-dependent Zn proteases [Posttranslational modification, protein turnover, chaperones];
13-604 0e+00

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


Pssm-ID: 440233 [Multi-domain]  Cd Length: 583  Bit Score: 965.65  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489514706  13 IAVVVLLGWSFFYFSddTRGYKPVDTSVAITQINGDNVKSAQIDDreQQLRLILKKGNnetdgSEKVITKYPTGyaVDLF 92
Cdd:COG0465    1 IALLLVLLFNLFSSS--SSSVKEISYSEFLQLVEAGKVKSVTIQG--DRITGTLKDGT-----KTRFTTYRVND--PELV 69
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489514706  93 NALSAKNAKVSTVVNQGS---------------ILGellvyvlpllllvGLFVMFSRMQGGARMGFGFGKSRAKQLSKDM 157
Cdd:COG0465   70 DLLEEKGVEVTAKPPEESswllsllisllpillLIG-------------LWIFFMRRMQGGGGGAMSFGKSKAKLYDEDK 136
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489514706 158 PKTTFADVAGVDEAVEELYEIKDFLQNPSRYQALGAKIPKGVLLYGPPGTGKTLLARAVAGEAGVPFFTISGSDFVEMFV 237
Cdd:COG0465  137 PKVTFDDVAGVDEAKEELQEIVDFLKDPEKFTRLGAKIPKGVLLVGPPGTGKTLLAKAVAGEAGVPFFSISGSDFVEMFV 216
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489514706 238 GVGASRVRDLFEQAKQNSPCIIFVDEIDAVGRQRGAGLGGGHDEREQTLNQLLVEMDGFGDRAGVILIAATNRPDILDPA 317
Cdd:COG0465  217 GVGASRVRDLFEQAKKNAPCIIFIDEIDAVGRQRGAGLGGGHDEREQTLNQLLVEMDGFEGNEGVIVIAATNRPDVLDPA 296
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489514706 318 LLRPGRFDRQIPVSNPDLAGRRAVLRVHSKGKPMAADADLDGLAKRTVGMTGADLANVINEAALLTARENGTVITGPALE 397
Cdd:COG0465  297 LLRPGRFDRQVVVDLPDVKGREAILKVHARKKPLAPDVDLEVIARRTPGFSGADLANLVNEAALLAARRNKKAVTMEDFE 376
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489514706 398 EAVDRVIGGPRRKGRIISEQEKKITAYHEGGHTLAAWAMPDIEPIYKVTILARGRTGGHAVAVPEEDKGLRTRSEMIAQL 477
Cdd:COG0465  377 EAIDRVIAGPERKSRVISEKEKKITAYHEAGHALVAALLPGADPVHKVTIIPRGRALGYTMQLPEEDRYLYTKEELLDRI 456
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489514706 478 VFAMGGRAAEELVFREPTTGAVSDIEQATKIARSMVTEFGMSSKLGAVKYGSEHGDPFLGRTMGTQPDYSHEVAREIDEE 557
Cdd:COG0465  457 AVLLGGRAAEELVFGEVTTGASNDLERATKIARAMVTEYGMSEKLGPVAYGESEGEVFLGRDIGQSRNYSEETAREIDEE 536
                        570       580       590       600
                 ....*....|....*....|....*....|....*....|....*..
gi 489514706 558 VRKLIEAAHTEAWEILTEYRDVLDTLAGELLEKETLHRPELESIFAD 604
Cdd:COG0465  537 VRRIIDEAYERAKEILTENRDKLDALAEALLEKETLDGEELEEILAG 583
FtsH_fam TIGR01241
ATP-dependent metalloprotease FtsH; HflB(FtsH) is a pleiotropic protein required for correct ...
131-603 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: 868.14  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489514706  131 MFSR-MQGGARMGFGFGKSRAKQLSKDMPKTTFADVAGVDEAVEELYEIKDFLQNPSRYQALGAKIPKGVLLYGPPGTGK 209
Cdd:TIGR01241  22 FFRRqMQGGGGRAFSFGKSKAKLLNEEKPKVTFKDVAGIDEAKEELMEIVDFLKNPSKFTKLGAKIPKGVLLVGPPGTGK 101
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489514706  210 TLLARAVAGEAGVPFFTISGSDFVEMFVGVGASRVRDLFEQAKQNSPCIIFVDEIDAVGRQRGAGLGGGHDEREQTLNQL 289
Cdd:TIGR01241 102 TLLAKAVAGEAGVPFFSISGSDFVEMFVGVGASRVRDLFEQAKKNAPCIIFIDEIDAVGRQRGAGLGGGNDEREQTLNQL 181
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489514706  290 LVEMDGFGDRAGVILIAATNRPDILDPALLRPGRFDRQIPVSNPDLAGRRAVLRVHSKGKPMAADADLDGLAKRTVGMTG 369
Cdd:TIGR01241 182 LVEMDGFGTNTGVIVIAATNRPDVLDPALLRPGRFDRQVVVDLPDIKGREEILKVHAKNKKLAPDVDLKAVARRTPGFSG 261
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489514706  370 ADLANVINEAALLTARENGTVITGPALEEAVDRVIGGPRRKGRIISEQEKKITAYHEGGHTLAAWAMPDIEPIYKVTILA 449
Cdd:TIGR01241 262 ADLANLLNEAALLAARKNKTEITMNDIEEAIDRVIAGPEKKSRVISEKEKKLVAYHEAGHALVGLLLKDADPVHKVTIIP 341
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489514706  450 RGRTGGHAVAVPEEDKGLRTRSEMIAQLVFAMGGRAAEELVFREPTTGAVSDIEQATKIARSMVTEFGMSSKLGAVKYGS 529
Cdd:TIGR01241 342 RGQALGYTQFLPEEDKYLYTKSQLLAQIAVLLGGRAAEEIIFGEVTTGASNDIKQATNIARAMVTEWGMSDKLGPVAYGS 421
                         410       420       430       440       450       460       470
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 489514706  530 EHGDPFLGRTMGTQPDYSHEVAREIDEEVRKLIEAAHTEAWEILTEYRDVLDTLAGELLEKETLHRPELESIFA 603
Cdd:TIGR01241 422 DGGDVFLGRGFAKAKEYSEETAREIDEEVKRIIEEAYKRAKQILTENRDELELLAKALLEKETITREEIKELLA 495
ftsH CHL00176
cell division protein; Validated
143-609 0e+00

cell division protein; Validated


Pssm-ID: 214386 [Multi-domain]  Cd Length: 638  Bit Score: 595.88  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489514706 143 FGFGKSRAK-QLSkdmPKT--TFADVAGVDEAVEELYEIKDFLQNPSRYQALGAKIPKGVLLYGPPGTGKTLLARAVAGE 219
Cdd:CHL00176 163 MNFGKSKARfQME---ADTgiTFRDIAGIEEAKEEFEEVVSFLKKPERFTAVGAKIPKGVLLVGPPGTGKTLLAKAIAGE 239
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489514706 220 AGVPFFTISGSDFVEMFVGVGASRVRDLFEQAKQNSPCIIFVDEIDAVGRQRGAGLGGGHDEREQTLNQLLVEMDGFGDR 299
Cdd:CHL00176 240 AEVPFFSISGSEFVEMFVGVGAARVRDLFKKAKENSPCIVFIDEIDAVGRQRGAGIGGGNDEREQTLNQLLTEMDGFKGN 319
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489514706 300 AGVILIAATNRPDILDPALLRPGRFDRQIPVSNPDLAGRRAVLRVHSKGKPMAADADLDGLAKRTVGMTGADLANVINEA 379
Cdd:CHL00176 320 KGVIVIAATNRVDILDAALLRPGRFDRQITVSLPDREGRLDILKVHARNKKLSPDVSLELIARRTPGFSGADLANLLNEA 399
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489514706 380 ALLTARENGTVITGPALEEAVDRVIGGPRRKGRIISeQEKKITAYHEGGHTLAAWAMPDIEPIYKVTILARGRTGGHAVA 459
Cdd:CHL00176 400 AILTARRKKATITMKEIDTAIDRVIAGLEGTPLEDS-KNKRLIAYHEVGHAIVGTLLPNHDPVQKVTLIPRGQAKGLTWF 478
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489514706 460 VPEEDKGLRTRSEMIAQLVFAMGGRAAEELVFREP--TTGAVSDIEQATKIARSMVTEFGMSSkLGAVKYGSEH-GDPFL 536
Cdd:CHL00176 479 TPEEDQSLVSRSQILARIVGALGGRAAEEVVFGSTevTTGASNDLQQVTNLARQMVTRFGMSS-IGPISLESNNsTDPFL 557
                        410       420       430       440       450       460       470
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 489514706 537 GRTMGTQPDYSHEVAREIDEEVRKLIEAAHTEAWEILTEYRDVLDTLAGELLEKETLHRPELESIFADVEKRP 609
Cdd:CHL00176 558 GRFMQRNSEYSEEIADKIDMEVRSILHTCYQYAYQILKDNRVLIDLLVELLLQKETIDGDEFREIVNSYTILP 630
RecA-like_FtsH cd19501
ATP-dependent zinc metalloprotease FtsH; FtsH ATPase is a processive, ATP-dependent zinc ...
160-330 1.48e-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: 363.86  E-value: 1.48e-122
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489514706 160 TTFADVAGVDEAVEELYEIKDFLQNPSRYQALGAKIPKGVLLYGPPGTGKTLLARAVAGEAGVPFFTISGSDFVEMFVGV 239
Cdd:cd19501    1 VTFKDVAGCEEAKEELKEVVEFLKNPEKFTKLGAKIPKGVLLVGPPGTGKTLLAKAVAGEAGVPFFSISGSDFVEMFVGV 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489514706 240 GASRVRDLFEQAKQNSPCIIFVDEIDAVGRQRGAGLGGGHDEREQTLNQLLVEMDGFGDRAGVILIAATNRPDILDPALL 319
Cdd:cd19501   81 GASRVRDLFEQAKKNAPCIVFIDEIDAVGRKRGAGLGGGHDEREQTLNQLLVEMDGFESNTGVIVIAATNRPDVLDPALL 160
                        170
                 ....*....|.
gi 489514706 320 RPGRFDRQIPV 330
Cdd:cd19501  161 RPGRFDRQVYV 171
Peptidase_M41 pfam01434
Peptidase family M41;
412-601 5.86e-99

Peptidase family M41;


Pssm-ID: 460210 [Multi-domain]  Cd Length: 190  Bit Score: 303.75  E-value: 5.86e-99
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489514706  412 RIISEQEKKITAYHEGGHTLAAWAMPDIEPIYKVTILARGRTGGHAVAVPEEDKGLRTRSEMIAQLVFAMGGRAAEELVF 491
Cdd:pfam01434   1 RVISEEEKKIVAYHEAGHALVGLLLPGADPVHKVTIIPRGQALGYTQFLPEEDKLLYTKEQLLARIAVLLGGRAAEELIF 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489514706  492 REPTTGAVSDIEQATKIARSMVTEFGMSSKLGAVKYGSEHGDPFLGRTMGTQPDYSHEVAREIDEEVRKLIEAAHTEAWE 571
Cdd:pfam01434  81 GEVTTGASNDLEKATKIARQMVTEFGMSDKLGPVSLEESDGNVFLGRGMGKRKPYSEETADIIDEEVKRLLEEAYERAKE 160
                         170       180       190
                  ....*....|....*....|....*....|
gi 489514706  572 ILTEYRDVLDTLAGELLEKETLHRPELESI 601
Cdd:pfam01434 161 ILTEHRDELEALAEALLEKETLDAEEIREL 190
AAA smart00382
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ...
196-334 2.70e-22

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: 93.59  E-value: 2.70e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489514706   196 PKGVLLYGPPGTGKTLLARAVAGEA---GVPFFTISGSDFVE--------------MFVGVGASRVRDLFEQAKQNSPCI 258
Cdd:smart00382   2 GEVILIVGPPGSGKTTLARALARELgppGGGVIYIDGEDILEevldqllliivggkKASGSGELRLRLALALARKLKPDV 81
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 489514706   259 IFVDEIDAvgrqrgagLGGGHDEREQTLNQLLVEMDGFGDRAGVILIAATNRPDILDPALLRPgRFDRQIPVSNPD 334
Cdd:smart00382  82 LILDEITS--------LLDAEQEALLLLLEELRLLLLLKSEKNLTVILTTNDEKDLGPALLRR-RFDRRIVLLLIL 148
PRK10263 PRK10263
DNA translocase FtsK; Provisional
622-758 1.27e-04

DNA translocase FtsK; Provisional


Pssm-ID: 236669 [Multi-domain]  Cd Length: 1355  Bit Score: 45.85  E-value: 1.27e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489514706  622 PSDKPPIKTPGELAIERGEPWPQPVPepafkaaiaqatQAAEAARSDAGQTGHGANGSPAGTHRSGDRQYGSTQPDYGAP 701
Cdd:PRK10263  377 PEGYPQQSQYAQPAVQYNEPLQQPVQ------------PQQPYYAPAAEQPAQQPYYAPAPEQPAQQPYYAPAPEQPVAG 444
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 489514706  702 AGWHAPgwPPRSSHRPSYSGEPAPTYP---GQPYPTGQADPGSDESSAEQDDEVSRTKPA 758
Cdd:PRK10263  445 NAWQAE--EQQSTFAPQSTYQTEQTYQqpaAQEPLYQQPQPVEQQPVVEPEPVVEETKPA 502
 
Name Accession Description Interval E-value
HflB COG0465
ATP-dependent Zn proteases [Posttranslational modification, protein turnover, chaperones];
13-604 0e+00

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


Pssm-ID: 440233 [Multi-domain]  Cd Length: 583  Bit Score: 965.65  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489514706  13 IAVVVLLGWSFFYFSddTRGYKPVDTSVAITQINGDNVKSAQIDDreQQLRLILKKGNnetdgSEKVITKYPTGyaVDLF 92
Cdd:COG0465    1 IALLLVLLFNLFSSS--SSSVKEISYSEFLQLVEAGKVKSVTIQG--DRITGTLKDGT-----KTRFTTYRVND--PELV 69
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489514706  93 NALSAKNAKVSTVVNQGS---------------ILGellvyvlpllllvGLFVMFSRMQGGARMGFGFGKSRAKQLSKDM 157
Cdd:COG0465   70 DLLEEKGVEVTAKPPEESswllsllisllpillLIG-------------LWIFFMRRMQGGGGGAMSFGKSKAKLYDEDK 136
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489514706 158 PKTTFADVAGVDEAVEELYEIKDFLQNPSRYQALGAKIPKGVLLYGPPGTGKTLLARAVAGEAGVPFFTISGSDFVEMFV 237
Cdd:COG0465  137 PKVTFDDVAGVDEAKEELQEIVDFLKDPEKFTRLGAKIPKGVLLVGPPGTGKTLLAKAVAGEAGVPFFSISGSDFVEMFV 216
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489514706 238 GVGASRVRDLFEQAKQNSPCIIFVDEIDAVGRQRGAGLGGGHDEREQTLNQLLVEMDGFGDRAGVILIAATNRPDILDPA 317
Cdd:COG0465  217 GVGASRVRDLFEQAKKNAPCIIFIDEIDAVGRQRGAGLGGGHDEREQTLNQLLVEMDGFEGNEGVIVIAATNRPDVLDPA 296
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489514706 318 LLRPGRFDRQIPVSNPDLAGRRAVLRVHSKGKPMAADADLDGLAKRTVGMTGADLANVINEAALLTARENGTVITGPALE 397
Cdd:COG0465  297 LLRPGRFDRQVVVDLPDVKGREAILKVHARKKPLAPDVDLEVIARRTPGFSGADLANLVNEAALLAARRNKKAVTMEDFE 376
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489514706 398 EAVDRVIGGPRRKGRIISEQEKKITAYHEGGHTLAAWAMPDIEPIYKVTILARGRTGGHAVAVPEEDKGLRTRSEMIAQL 477
Cdd:COG0465  377 EAIDRVIAGPERKSRVISEKEKKITAYHEAGHALVAALLPGADPVHKVTIIPRGRALGYTMQLPEEDRYLYTKEELLDRI 456
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489514706 478 VFAMGGRAAEELVFREPTTGAVSDIEQATKIARSMVTEFGMSSKLGAVKYGSEHGDPFLGRTMGTQPDYSHEVAREIDEE 557
Cdd:COG0465  457 AVLLGGRAAEELVFGEVTTGASNDLERATKIARAMVTEYGMSEKLGPVAYGESEGEVFLGRDIGQSRNYSEETAREIDEE 536
                        570       580       590       600
                 ....*....|....*....|....*....|....*....|....*..
gi 489514706 558 VRKLIEAAHTEAWEILTEYRDVLDTLAGELLEKETLHRPELESIFAD 604
Cdd:COG0465  537 VRRIIDEAYERAKEILTENRDKLDALAEALLEKETLDGEELEEILAG 583
FtsH_fam TIGR01241
ATP-dependent metalloprotease FtsH; HflB(FtsH) is a pleiotropic protein required for correct ...
131-603 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: 868.14  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489514706  131 MFSR-MQGGARMGFGFGKSRAKQLSKDMPKTTFADVAGVDEAVEELYEIKDFLQNPSRYQALGAKIPKGVLLYGPPGTGK 209
Cdd:TIGR01241  22 FFRRqMQGGGGRAFSFGKSKAKLLNEEKPKVTFKDVAGIDEAKEELMEIVDFLKNPSKFTKLGAKIPKGVLLVGPPGTGK 101
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489514706  210 TLLARAVAGEAGVPFFTISGSDFVEMFVGVGASRVRDLFEQAKQNSPCIIFVDEIDAVGRQRGAGLGGGHDEREQTLNQL 289
Cdd:TIGR01241 102 TLLAKAVAGEAGVPFFSISGSDFVEMFVGVGASRVRDLFEQAKKNAPCIIFIDEIDAVGRQRGAGLGGGNDEREQTLNQL 181
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489514706  290 LVEMDGFGDRAGVILIAATNRPDILDPALLRPGRFDRQIPVSNPDLAGRRAVLRVHSKGKPMAADADLDGLAKRTVGMTG 369
Cdd:TIGR01241 182 LVEMDGFGTNTGVIVIAATNRPDVLDPALLRPGRFDRQVVVDLPDIKGREEILKVHAKNKKLAPDVDLKAVARRTPGFSG 261
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489514706  370 ADLANVINEAALLTARENGTVITGPALEEAVDRVIGGPRRKGRIISEQEKKITAYHEGGHTLAAWAMPDIEPIYKVTILA 449
Cdd:TIGR01241 262 ADLANLLNEAALLAARKNKTEITMNDIEEAIDRVIAGPEKKSRVISEKEKKLVAYHEAGHALVGLLLKDADPVHKVTIIP 341
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489514706  450 RGRTGGHAVAVPEEDKGLRTRSEMIAQLVFAMGGRAAEELVFREPTTGAVSDIEQATKIARSMVTEFGMSSKLGAVKYGS 529
Cdd:TIGR01241 342 RGQALGYTQFLPEEDKYLYTKSQLLAQIAVLLGGRAAEEIIFGEVTTGASNDIKQATNIARAMVTEWGMSDKLGPVAYGS 421
                         410       420       430       440       450       460       470
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 489514706  530 EHGDPFLGRTMGTQPDYSHEVAREIDEEVRKLIEAAHTEAWEILTEYRDVLDTLAGELLEKETLHRPELESIFA 603
Cdd:TIGR01241 422 DGGDVFLGRGFAKAKEYSEETAREIDEEVKRIIEEAYKRAKQILTENRDELELLAKALLEKETITREEIKELLA 495
ftsH CHL00176
cell division protein; Validated
143-609 0e+00

cell division protein; Validated


Pssm-ID: 214386 [Multi-domain]  Cd Length: 638  Bit Score: 595.88  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489514706 143 FGFGKSRAK-QLSkdmPKT--TFADVAGVDEAVEELYEIKDFLQNPSRYQALGAKIPKGVLLYGPPGTGKTLLARAVAGE 219
Cdd:CHL00176 163 MNFGKSKARfQME---ADTgiTFRDIAGIEEAKEEFEEVVSFLKKPERFTAVGAKIPKGVLLVGPPGTGKTLLAKAIAGE 239
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489514706 220 AGVPFFTISGSDFVEMFVGVGASRVRDLFEQAKQNSPCIIFVDEIDAVGRQRGAGLGGGHDEREQTLNQLLVEMDGFGDR 299
Cdd:CHL00176 240 AEVPFFSISGSEFVEMFVGVGAARVRDLFKKAKENSPCIVFIDEIDAVGRQRGAGIGGGNDEREQTLNQLLTEMDGFKGN 319
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489514706 300 AGVILIAATNRPDILDPALLRPGRFDRQIPVSNPDLAGRRAVLRVHSKGKPMAADADLDGLAKRTVGMTGADLANVINEA 379
Cdd:CHL00176 320 KGVIVIAATNRVDILDAALLRPGRFDRQITVSLPDREGRLDILKVHARNKKLSPDVSLELIARRTPGFSGADLANLLNEA 399
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489514706 380 ALLTARENGTVITGPALEEAVDRVIGGPRRKGRIISeQEKKITAYHEGGHTLAAWAMPDIEPIYKVTILARGRTGGHAVA 459
Cdd:CHL00176 400 AILTARRKKATITMKEIDTAIDRVIAGLEGTPLEDS-KNKRLIAYHEVGHAIVGTLLPNHDPVQKVTLIPRGQAKGLTWF 478
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489514706 460 VPEEDKGLRTRSEMIAQLVFAMGGRAAEELVFREP--TTGAVSDIEQATKIARSMVTEFGMSSkLGAVKYGSEH-GDPFL 536
Cdd:CHL00176 479 TPEEDQSLVSRSQILARIVGALGGRAAEEVVFGSTevTTGASNDLQQVTNLARQMVTRFGMSS-IGPISLESNNsTDPFL 557
                        410       420       430       440       450       460       470
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 489514706 537 GRTMGTQPDYSHEVAREIDEEVRKLIEAAHTEAWEILTEYRDVLDTLAGELLEKETLHRPELESIFADVEKRP 609
Cdd:CHL00176 558 GRFMQRNSEYSEEIADKIDMEVRSILHTCYQYAYQILKDNRVLIDLLVELLLQKETIDGDEFREIVNSYTILP 630
hflB PRK10733
ATP-dependent zinc metalloprotease FtsH;
10-638 0e+00

ATP-dependent zinc metalloprotease FtsH;


Pssm-ID: 182683 [Multi-domain]  Cd Length: 644  Bit Score: 565.04  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489514706  10 ITAIAVVVLLGWSFFYFSDDTRGYKPVDTSVAITQINGDNVKSAQIDDREQQlrlILKKGNNetdgsekvitKYPTGYAV 89
Cdd:PRK10733   6 ILWLVIAVVLMSVFQSFGPSESNGRKVDYSTFLQEVNQDQVREARINGREIN---VTKKDSN----------RYTTYIPV 72
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489514706  90 D---LFNALSAKNAKV-STVVNQGSILGELLVYVLPLLLLVGLFVMFSR-MQGGARMG-FGFGKSRAKQLSKDMPKTTFA 163
Cdd:PRK10733  73 NdpkLLDNLLTKNVKVvGEPPEEPSLLASIFISWFPMLLLIGVWIFFMRqMQGGGGKGaMSFGKSKARMLTEDQIKTTFA 152
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489514706 164 DVAGVDEAVEELYEIKDFLQNPSRYQALGAKIPKGVLLYGPPGTGKTLLARAVAGEAGVPFFTISGSDFVEMFVGVGASR 243
Cdd:PRK10733 153 DVAGCDEAKEEVAELVEYLREPSRFQKLGGKIPKGVLMVGPPGTGKTLLAKAIAGEAKVPFFTISGSDFVEMFVGVGASR 232
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489514706 244 VRDLFEQAKQNSPCIIFVDEIDAVGRQRGAGLGGGHDEREQTLNQLLVEMDGFGDRAGVILIAATNRPDILDPALLRPGR 323
Cdd:PRK10733 233 VRDMFEQAKKAAPCIIFIDEIDAVGRQRGAGLGGGHDEREQTLNQMLVEMDGFEGNEGIIVIAATNRPDVLDPALLRPGR 312
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489514706 324 FDRQIPVSNPDLAGRRAVLRVHSKGKPMAADADLDGLAKRTVGMTGADLANVINEAALLTARENGTVITGPALEEAVDRV 403
Cdd:PRK10733 313 FDRQVVVGLPDVRGREQILKVHMRRVPLAPDIDAAIIARGTPGFSGADLANLVNEAALFAARGNKRVVSMVEFEKAKDKI 392
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489514706 404 IGGPRRKGRIISEQEKKITAYHEGGHTLAAWAMPDIEPIYKVTILARGRTGGHAVAVPEEDKGLRTRSEMIAQLVFAMGG 483
Cdd:PRK10733 393 MMGAERRSMVMTEAQKESTAYHEAGHAIIGRLVPEHDPVHKVTIIPRGRALGVTFFLPEGDAISASRQKLESQISTLYGG 472
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489514706 484 RAAEELVF--REPTTGAVSDIEQATKIARSMVTEFGMSSKLGAVKYGSEHGDPFLGRTMGTQPDYSHEVAREIDEEVRKL 561
Cdd:PRK10733 473 RLAEEIIYgpEHVSTGASNDIKVATNLARNMVTQWGFSEKLGPLLYAEEEGEVFLGRSVAKAKHMSDETARIIDQEVKAL 552
                        570       580       590       600       610       620       630       640
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489514706 562 IEAAHTEAWEILTEYRDVLDTLAGELLEKETLHRPELESIFADVEKRPRLTMFDDFGGR-----------IPSDKPPIKT 630
Cdd:PRK10733 553 IERNYNRARQLLTDNMDILHAMKDALMKYETIDAPQIDDLMARRDVRPPAGWEEPGASNnsddngtpkapRPVDEPRTPN 632

                 ....*...
gi 489514706 631 PGELAIER 638
Cdd:PRK10733 633 PGNTMSEQ 640
RecA-like_FtsH cd19501
ATP-dependent zinc metalloprotease FtsH; FtsH ATPase is a processive, ATP-dependent zinc ...
160-330 1.48e-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: 363.86  E-value: 1.48e-122
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489514706 160 TTFADVAGVDEAVEELYEIKDFLQNPSRYQALGAKIPKGVLLYGPPGTGKTLLARAVAGEAGVPFFTISGSDFVEMFVGV 239
Cdd:cd19501    1 VTFKDVAGCEEAKEELKEVVEFLKNPEKFTKLGAKIPKGVLLVGPPGTGKTLLAKAVAGEAGVPFFSISGSDFVEMFVGV 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489514706 240 GASRVRDLFEQAKQNSPCIIFVDEIDAVGRQRGAGLGGGHDEREQTLNQLLVEMDGFGDRAGVILIAATNRPDILDPALL 319
Cdd:cd19501   81 GASRVRDLFEQAKKNAPCIVFIDEIDAVGRKRGAGLGGGHDEREQTLNQLLVEMDGFESNTGVIVIAATNRPDVLDPALL 160
                        170
                 ....*....|.
gi 489514706 320 RPGRFDRQIPV 330
Cdd:cd19501  161 RPGRFDRQVYV 171
RPT1 COG1222
ATP-dependent 26S proteasome regulatory subunit [Posttranslational modification, protein ...
158-412 9.07e-110

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


Pssm-ID: 440835 [Multi-domain]  Cd Length: 326  Bit Score: 336.98  E-value: 9.07e-110
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489514706 158 PKTTFADVAGVDEAVEELYE-IKDFLQNPSRYQALGAKIPKGVLLYGPPGTGKTLLARAVAGEAGVPFFTISGSDFVEMF 236
Cdd:COG1222   73 PDVTFDDIGGLDEQIEEIREaVELPLKNPELFRKYGIEPPKGVLLYGPPGTGKTLLAKAVAGELGAPFIRVRGSELVSKY 152
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489514706 237 VGVGASRVRDLFEQAKQNSPCIIFVDEIDAVGRQRGAGlgGGHDEREQTLNQLLVEMDGFGDRAGVILIAATNRPDILDP 316
Cdd:COG1222  153 IGEGARNVREVFELAREKAPSIIFIDEIDAIAARRTDD--GTSGEVQRTVNQLLAELDGFESRGDVLIIAATNRPDLLDP 230
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489514706 317 ALLRPGRFDRQIPVSNPDLAGRRAVLRVHSKGKPMAADADLDGLAKRTVGMTGADLANVINEAALLTARENGTVITGPAL 396
Cdd:COG1222  231 ALLRPGRFDRVIEVPLPDEEAREEILKIHLRDMPLADDVDLDKLAKLTEGFSGADLKAIVTEAGMFAIREGRDTVTMEDL 310
                        250
                 ....*....|....*.
gi 489514706 397 EEAVDRVIGGPRRKGR 412
Cdd:COG1222  311 EKAIEKVKKKTETATN 326
Peptidase_M41 pfam01434
Peptidase family M41;
412-601 5.86e-99

Peptidase family M41;


Pssm-ID: 460210 [Multi-domain]  Cd Length: 190  Bit Score: 303.75  E-value: 5.86e-99
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489514706  412 RIISEQEKKITAYHEGGHTLAAWAMPDIEPIYKVTILARGRTGGHAVAVPEEDKGLRTRSEMIAQLVFAMGGRAAEELVF 491
Cdd:pfam01434   1 RVISEEEKKIVAYHEAGHALVGLLLPGADPVHKVTIIPRGQALGYTQFLPEEDKLLYTKEQLLARIAVLLGGRAAEELIF 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489514706  492 REPTTGAVSDIEQATKIARSMVTEFGMSSKLGAVKYGSEHGDPFLGRTMGTQPDYSHEVAREIDEEVRKLIEAAHTEAWE 571
Cdd:pfam01434  81 GEVTTGASNDLEKATKIARQMVTEFGMSDKLGPVSLEESDGNVFLGRGMGKRKPYSEETADIIDEEVKRLLEEAYERAKE 160
                         170       180       190
                  ....*....|....*....|....*....|
gi 489514706  572 ILTEYRDVLDTLAGELLEKETLHRPELESI 601
Cdd:pfam01434 161 ILTEHRDELEALAEALLEKETLDAEEIREL 190
PRK03992 PRK03992
proteasome-activating nucleotidase; Provisional
158-410 9.11e-94

proteasome-activating nucleotidase; Provisional


Pssm-ID: 179699 [Multi-domain]  Cd Length: 389  Bit Score: 297.51  E-value: 9.11e-94
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489514706 158 PKTTFADVAGVDEAVEELYE-IKDFLQNPSRYQALGAKIPKGVLLYGPPGTGKTLLARAVAGEAGVPFFTISGSDFVEMF 236
Cdd:PRK03992 126 PNVTYEDIGGLEEQIREVREaVELPLKKPELFEEVGIEPPKGVLLYGPPGTGKTLLAKAVAHETNATFIRVVGSELVQKF 205
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489514706 237 VGVGASRVRDLFEQAKQNSPCIIFVDEIDAVGRQRGAGLGGGHDEREQTLNQLLVEMDGFGDRAGVILIAATNRPDILDP 316
Cdd:PRK03992 206 IGEGARLVRELFELAREKAPSIIFIDEIDAIAAKRTDSGTSGDREVQRTLMQLLAEMDGFDPRGNVKIIAATNRIDILDP 285
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489514706 317 ALLRPGRFDRQIPVSNPDLAGRRAVLRVHSKGKPMAADADLDGLAKRTVGMTGADLANVINEAALLTARENGTVITGPAL 396
Cdd:PRK03992 286 AILRPGRFDRIIEVPLPDEEGRLEILKIHTRKMNLADDVDLEELAELTEGASGADLKAICTEAGMFAIRDDRTEVTMEDF 365
                        250
                 ....*....|....
gi 489514706 397 EEAVDRVIGGPRRK 410
Cdd:PRK03992 366 LKAIEKVMGKEEKD 379
SpoVK COG0464
AAA+-type ATPase, SpoVK/Ycf46/Vps4 family [Cell wall/membrane/envelope biogenesis, Cell cycle ...
162-403 4.98e-82

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: 267.16  E-value: 4.98e-82
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489514706 162 FADVAGVDEAVEELYEI-KDFLQNPSRYQALGAKIPKGVLLYGPPGTGKTLLARAVAGEAGVPFFTISGSDFVEMFVGVG 240
Cdd:COG0464  156 LDDLGGLEEVKEELRELvALPLKRPELREEYGLPPPRGLLLYGPPGTGKTLLARALAGELGLPLIEVDLSDLVSKYVGET 235
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489514706 241 ASRVRDLFEQAKQNSPCIIFVDEIDAVGRQRGaGLGGGHDEREqtLNQLLVEMDGFgdRAGVILIAATNRPDILDPALLR 320
Cdd:COG0464  236 EKNLREVFDKARGLAPCVLFIDEADALAGKRG-EVGDGVGRRV--VNTLLTEMEEL--RSDVVVIAATNRPDLLDPALLR 310
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489514706 321 pgRFDRQIPVSNPDLAGRRAVLRVHSKGKPMAADADLDGLAKRTVGMTGADLANVINEAALLTARENGTVITGPALEEAV 400
Cdd:COG0464  311 --RFDEIIFFPLPDAEERLEIFRIHLRKRPLDEDVDLEELAEATEGLSGADIRNVVRRAALQALRLGREPVTTEDLLEAL 388

                 ...
gi 489514706 401 DRV 403
Cdd:COG0464  389 ERE 391
26Sp45 TIGR01242
26S proteasome subunit P45 family; Many proteins may score above the trusted cutoff because an ...
158-404 5.70e-82

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: 265.89  E-value: 5.70e-82
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489514706  158 PKTTFADVAGVDEAVEELYEIKDF-LQNPSRYQALGAKIPKGVLLYGPPGTGKTLLARAVAGEAGVPFFTISGSDFVEMF 236
Cdd:TIGR01242 117 PNVSYEDIGGLEEQIREIREAVELpLKHPELFEEVGIEPPKGVLLYGPPGTGKTLLAKAVAHETNATFIRVVGSELVRKY 196
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489514706  237 VGVGASRVRDLFEQAKQNSPCIIFVDEIDAVGRQRGAGLGGGHDEREQTLNQLLVEMDGFGDRAGVILIAATNRPDILDP 316
Cdd:TIGR01242 197 IGEGARLVREIFELAKEKAPSIIFIDEIDAIAAKRTDSGTSGDREVQRTLMQLLAELDGFDPRGNVKVIAATNRPDILDP 276
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489514706  317 ALLRPGRFDRQIPVSNPDLAGRRAVLRVHSKGKPMAADADLDGLAKRTVGMTGADLANVINEAALLTARENGTVITGPAL 396
Cdd:TIGR01242 277 ALLRPGRFDRIIEVPLPDFEGRLEILKIHTRKMKLAEDVDLEAIAKMTEGASGADLKAICTEAGMFAIREERDYVTMDDF 356

                  ....*...
gi 489514706  397 EEAVDRVI 404
Cdd:TIGR01242 357 IKAVEKVL 364
CDC48 TIGR01243
AAA family ATPase, CDC48 subfamily; This subfamily of the AAA family ATPases includes two ...
156-421 7.76e-69

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: 240.96  E-value: 7.76e-69
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489514706  156 DMPKTTFADVAGVDEAVEELYEIKDF-LQNPSRYQALGAKIPKGVLLYGPPGTGKTLLARAVAGEAGVPFFTISGSDFVE 234
Cdd:TIGR01243 446 EVPNVRWSDIGGLEEVKQELREAVEWpLKHPEIFEKMGIRPPKGVLLFGPPGTGKTLLAKAVATESGANFIAVRGPEILS 525
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489514706  235 MFVGVGASRVRDLFEQAKQNSPCIIFVDEIDAVGRQRGAGLGGGHDEReqTLNQLLVEMDGFGDRAGVILIAATNRPDIL 314
Cdd:TIGR01243 526 KWVGESEKAIREIFRKARQAAPAIIFFDEIDAIAPARGARFDTSVTDR--IVNQLLTEMDGIQELSNVVVIAATNRPDIL 603
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489514706  315 DPALLRPGRFDRQIPVSNPDLAGRRAVLRVHSKGKPMAADADLDGLAKRTVGMTGADLANVINEAALLTARENGTVITGP 394
Cdd:TIGR01243 604 DPALLRPGRFDRLILVPPPDEEARKEIFKIHTRSMPLAEDVDLEELAEMTEGYTGADIEAVCREAAMAALRESIGSPAKE 683
                         250       260
                  ....*....|....*....|....*..
gi 489514706  395 ALEEAVDRVIGGPRRKGRIISEQEKKI 421
Cdd:TIGR01243 684 KLEVGEEEFLKDLKVEMRHFLEALKKV 710
RecA-like_PAN_like cd19502
proteasome activating nucleotidase PAN and related proteasome subunits; This subfamily ...
161-330 1.13e-68

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: 223.37  E-value: 1.13e-68
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489514706 161 TFADVAGVDEAVEELYE-IKDFLQNPSRYQALGAKIPKGVLLYGPPGTGKTLLARAVAGEAGVPFFTISGSDFVEMFVGV 239
Cdd:cd19502    1 TYEDIGGLDEQIREIREvVELPLKHPELFEELGIEPPKGVLLYGPPGTGKTLLAKAVANHTDATFIRVVGSELVQKYIGE 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489514706 240 GASRVRDLFEQAKQNSPCIIFVDEIDAVGRQRGAGLGGGHDEREQTLNQLLVEMDGFGDRAGVILIAATNRPDILDPALL 319
Cdd:cd19502   81 GARLVRELFEMAREKAPSIIFIDEIDAIGAKRFDSGTGGDREVQRTMLELLNQLDGFDPRGNIKVIMATNRPDILDPALL 160
                        170
                 ....*....|.
gi 489514706 320 RPGRFDRQIPV 330
Cdd:cd19502  161 RPGRFDRKIEF 171
COG1223 COG1223
Predicted ATPase, AAA+ superfamily [General function prediction only];
162-402 2.33e-65

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


Pssm-ID: 440836 [Multi-domain]  Cd Length: 246  Bit Score: 217.44  E-value: 2.33e-65
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489514706 162 FADVAGVDEAVEELYEIKDFLQNPSRYQALGAKIPKGVLLYGPPGTGKTLLARAVAGEAGVPFFTISGSDFVEMFVGVGA 241
Cdd:COG1223    1 LDDVVGQEEAKKKLKLIIKELRRRENLRKFGLWPPRKILFYGPPGTGKTMLAEALAGELKLPLLTVRLDSLIGSYLGETA 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489514706 242 SRVRDLFEQAKQNsPCIIFVDEIDAVGRQRGAglGGGHDEREQTLNQLLVEMDGFgdRAGVILIAATNRPDILDPALLRp 321
Cdd:COG1223   81 RNLRKLFDFARRA-PCVIFFDEFDAIAKDRGD--QNDVGEVKRVVNALLQELDGL--PSGSVVIAATNHPELLDSALWR- 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489514706 322 gRFDRQIPVSNPDLAGRRAVLRVHSKGKPMAADADLDGLAKRTVGMTGADLANVINEAALLTARENGTVITGPALEEAVD 401
Cdd:COG1223  155 -RFDEVIEFPLPDKEERKEILELNLKKFPLPFELDLKKLAKKLEGLSGADIEKVLKTALKKAILEDREKVTKEDLEEALK 233

                 .
gi 489514706 402 R 402
Cdd:COG1223  234 Q 234
RecA-like_protease cd19481
proteases similar to RecA; RecA-like NTPases. This family includes the NTP binding domain of ...
171-330 2.94e-64

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: 210.99  E-value: 2.94e-64
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489514706 171 AVEELYEIKDFLQNPSRYQALGAKIPKGVLLYGPPGTGKTLLARAVAGEAGVPFFTISGSDFVEMFVGVGASRVRDLFEQ 250
Cdd:cd19481    1 LKASLREAVEAPRRGSRLRRYGLGLPKGILLYGPPGTGKTLLAKALAGELGLPLIVVKLSSLLSKYVGESEKNLRKIFER 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489514706 251 AKQNSPCIIFVDEIDAVGRQRGAglGGGHDEREQTLNQLLVEMDGFGDRAGVILIAATNRPDILDPALLRPGRFDRQIPV 330
Cdd:cd19481   81 ARRLAPCILFIDEIDAIGRKRDS--SGESGELRRVLNQLLTELDGVNSRSKVLVIAATNRPDLLDPALLRPGRFDEVIEF 158
CDC48 TIGR01243
AAA family ATPase, CDC48 subfamily; This subfamily of the AAA family ATPases includes two ...
157-385 1.19e-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: 226.33  E-value: 1.19e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489514706  157 MPKTTFADVAGVDEAVEELYEIKDF-LQNPSRYQALGAKIPKGVLLYGPPGTGKTLLARAVAGEAGVPFFTISGSDFVEM 235
Cdd:TIGR01243 172 VPKVTYEDIGGLKEAKEKIREMVELpMKHPELFEHLGIEPPKGVLLYGPPGTGKTLLAKAVANEAGAYFISINGPEIMSK 251
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489514706  236 FVGVGASRVRDLFEQAKQNSPCIIFVDEIDAVGRQRGAGLGgghDEREQTLNQLLVEMDGFGDRAGVILIAATNRPDILD 315
Cdd:TIGR01243 252 YYGESEERLREIFKEAEENAPSIIFIDEIDAIAPKREEVTG---EVEKRVVAQLLTLMDGLKGRGRVIVIGATNRPDALD 328
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489514706  316 PALLRPGRFDRQIPVSNPDLAGRRAVLRVHSKGKPMAADADLDGLAKRTVGMTGADLANVINEAALLTAR 385
Cdd:TIGR01243 329 PALRRPGRFDREIVIRVPDKRARKEILKVHTRNMPLAEDVDLDKLAEVTHGFVGADLAALAKEAAMAALR 398
PTZ00361 PTZ00361
26 proteosome regulatory subunit 4-like protein; Provisional
158-413 1.16e-62

26 proteosome regulatory subunit 4-like protein; Provisional


Pssm-ID: 185575 [Multi-domain]  Cd Length: 438  Bit Score: 216.56  E-value: 1.16e-62
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489514706 158 PKTTFADVAGVDEAVEELYEIKDF-LQNPSRYQALGAKIPKGVLLYGPPGTGKTLLARAVAGEAGVPFFTISGSDFVEMF 236
Cdd:PTZ00361 178 PLESYADIGGLEQQIQEIKEAVELpLTHPELYDDIGIKPPKGVILYGPPGTGKTLLAKAVANETSATFLRVVGSELIQKY 257
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489514706 237 VGVGASRVRDLFEQAKQNSPCIIFVDEIDAVGRQRGAGLGGGHDEREQTLNQLLVEMDGFGDRAGVILIAATNRPDILDP 316
Cdd:PTZ00361 258 LGDGPKLVRELFRVAEENAPSIVFIDEIDAIGTKRYDATSGGEKEIQRTMLELLNQLDGFDSRGDVKVIMATNRIESLDP 337
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489514706 317 ALLRPGRFDRQIPVSNPDLAGRRAVLRVHSKGKPMAADADLDGLAKRTVGMTGADLANVINEAALLTARENGTVITGPAL 396
Cdd:PTZ00361 338 ALIRPGRIDRKIEFPNPDEKTKRRIFEIHTSKMTLAEDVDLEEFIMAKDELSGADIKAICTEAGLLALRERRMKVTQADF 417
                        250
                 ....*....|....*..
gi 489514706 397 EEAVDRVIggPRRKGRI 413
Cdd:PTZ00361 418 RKAKEKVL--YRKKGNI 432
PTZ00454 PTZ00454
26S protease regulatory subunit 6B-like protein; Provisional
156-404 7.29e-61

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


Pssm-ID: 240423 [Multi-domain]  Cd Length: 398  Bit Score: 210.39  E-value: 7.29e-61
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489514706 156 DMPKTTFADVAGVDEAVEELYEIKDF-LQNPSRYQALGAKIPKGVLLYGPPGTGKTLLARAVAGEAGVPFFTISGSDFVE 234
Cdd:PTZ00454 138 EKPDVTYSDIGGLDIQKQEIREAVELpLTCPELYEQIGIDPPRGVLLYGPPGTGKTMLAKAVAHHTTATFIRVVGSEFVQ 217
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489514706 235 MFVGVGASRVRDLFEQAKQNSPCIIFVDEIDAVGRQRGAGLGGGHDEREQTLNQLLVEMDGFGDRAGVILIAATNRPDIL 314
Cdd:PTZ00454 218 KYLGEGPRMVRDVFRLARENAPSIIFIDEVDSIATKRFDAQTGADREVQRILLELLNQMDGFDQTTNVKVIMATNRADTL 297
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489514706 315 DPALLRPGRFDRQIPVSNPDLAGRRAVLRVHSKGKPMAADADLDGLAKRTVGMTGADLANVINEAALLTARENGTVITGP 394
Cdd:PTZ00454 298 DPALLRPGRLDRKIEFPLPDRRQKRLIFQTITSKMNLSEEVDLEDFVSRPEKISAADIAAICQEAGMQAVRKNRYVILPK 377
                        250
                 ....*....|
gi 489514706 395 ALEEAVDRVI 404
Cdd:PTZ00454 378 DFEKGYKTVV 387
RecA-like_CDC48_NLV2_r1-like cd19503
first of two ATPase domains of CDC48 and NLV2, and similar ATPase domains; CDC48 in yeast and ...
164-330 2.01e-60

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: 200.98  E-value: 2.01e-60
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489514706 164 DVAGVDEAVEELYEIKDF-LQNPSRYQALGAKIPKGVLLYGPPGTGKTLLARAVAGEAGVPFFTISGSDFVEMFVGVGAS 242
Cdd:cd19503    1 DIGGLDEQIASLKELIELpLKYPELFRALGLKPPRGVLLHGPPGTGKTLLARAVANEAGANFLSISGPSIVSKYLGESEK 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489514706 243 RVRDLFEQAKQNSPCIIFVDEIDAVGRQRGAglggGHDEREQTL-NQLLVEMDGFGDRAGVILIAATNRPDILDPALLRP 321
Cdd:cd19503   81 NLREIFEEARSHAPSIIFIDEIDALAPKREE----DQREVERRVvAQLLTLMDGMSSRGKVVVIAATNRPDAIDPALRRP 156

                 ....*....
gi 489514706 322 GRFDRQIPV 330
Cdd:cd19503  157 GRFDREVEI 165
RecA-like_CDC48_r2-like cd19511
second of two ATPase domains of CDC48/p97, PEX1 and -6, VAT and NVL, and similar ATPase ...
182-330 1.11e-59

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: 198.66  E-value: 1.11e-59
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489514706 182 LQNPSRYQALGAKIPKGVLLYGPPGTGKTLLARAVAGEAGVPFFTISGSDFVEMFVGVGASRVRDLFEQAKQNSPCIIFV 261
Cdd:cd19511   13 LKHPDAFKRLGIRPPKGVLLYGPPGCGKTLLAKALASEAGLNFISVKGPELFSKYVGESERAVREIFQKARQAAPCIIFF 92
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 489514706 262 DEIDAVGRQRGAGLGGGHDEReqTLNQLLVEMDGFGDRAGVILIAATNRPDILDPALLRPGRFDRQIPV 330
Cdd:cd19511   93 DEIDSLAPRRGQSDSSGVTDR--VVSQLLTELDGIESLKGVVVIAATNRPDMIDPALLRPGRLDKLIYV 159
AAA pfam00004
ATPase family associated with various cellular activities (AAA); AAA family proteins often ...
199-331 3.30e-57

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: 190.88  E-value: 3.30e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489514706  199 VLLYGPPGTGKTLLARAVAGEAGVPFFTISGSDFVEMFVGVGASRVRDLFEQAKQNSPCIIFVDEIDAVGRQRGaglGGG 278
Cdd:pfam00004   1 LLLYGPPGTGKTTLAKAVAKELGAPFIEISGSELVSKYVGESEKRLRELFEAAKKLAPCVIFIDEIDALAGSRG---SGG 77
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 489514706  279 HDEREQTLNQLLVEMDGFGDRAG-VILIAATNRPDILDPALLrpGRFDRQIPVS 331
Cdd:pfam00004  78 DSESRRVVNQLLTELDGFTSSNSkVIVIAATNRPDKLDPALL--GRFDRIIEFP 129
RecA-like_VCP_r2 cd19529
second of two ATPase domains of Valosin-containing protein-like ATPase (VAT) and similar ...
182-330 2.57e-53

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: 181.54  E-value: 2.57e-53
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489514706 182 LQNPSRYQALGAKIPKGVLLYGPPGTGKTLLARAVAGEAGVPFFTISGSDFVEMFVGVGASRVRDLFEQAKQNSPCIIFV 261
Cdd:cd19529   13 LLKPEVFKRLGIRPPKGILLYGPPGTGKTLLAKAVATESNANFISVKGPELLSKWVGESEKAIREIFRKARQVAPCVIFF 92
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 489514706 262 DEIDAVGRQRGAGLGGGHDEReqTLNQLLVEMDGFGDRAGVILIAATNRPDILDPALLRPGRFDRQIPV 330
Cdd:cd19529   93 DEIDSIAPRRGTTGDSGVTER--VVNQLLTELDGLEEMNGVVVIAATNRPDIIDPALLRAGRFDRLIYI 159
RecA-like_CDC48_r2-like cd19528
second of two ATPase domains of CDC48 and similar ATPase domains; CDC48 in yeast and p97 or ...
173-330 1.09e-52

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: 180.01  E-value: 1.09e-52
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489514706 173 EELYEIKDF-LQNPSRYQALGAKIPKGVLLYGPPGTGKTLLARAVAGEAGVPFFTISGSDFVEMFVGVGASRVRDLFEQA 251
Cdd:cd19528    3 RELQELVQYpVEHPDKFLKFGMTPSKGVLFYGPPGCGKTLLAKAIANECQANFISVKGPELLTMWFGESEANVRDIFDKA 82
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 489514706 252 KQNSPCIIFVDEIDAVGRQRGAGLGGGHDEREQTLNQLLVEMDGFGDRAGVILIAATNRPDILDPALLRPGRFDRQIPV 330
Cdd:cd19528   83 RAAAPCVLFFDELDSIAKARGGNIGDAGGAADRVINQILTEMDGMNTKKNVFIIGATNRPDIIDPAILRPGRLDQLIYI 161
RecA-like_NVL_r2-like cd19530
second of two ATPase domains of NVL (nuclear VCP-like protein) and similar ATPase domains; NVL ...
182-330 2.03e-51

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: 176.52  E-value: 2.03e-51
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489514706 182 LQNPSRYQALGAKIPKGVLLYGPPGTGKTLLARAVAGEAGVPFFTISGSDFVEMFVGVGASRVRDLFEQAKQNSPCIIFV 261
Cdd:cd19530   16 IKRPDIYKALGIDLPTGVLLYGPPGCGKTLLAKAVANESGANFISVKGPELLNKYVGESERAVRQVFQRARASAPCVIFF 95
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 489514706 262 DEIDAVGRQRGAGLGGGhdeREQTLNQLLVEMDGFGDRAGVILIAATNRPDILDPALLRPGRFDRQIPV 330
Cdd:cd19530   96 DEVDALVPKRGDGGSWA---SERVVNQLLTEMDGLEERSNVFVIAATNRPDIIDPAMLRPGRLDKTLYV 161
RecA-like_CDC48_r1-like cd19519
first of two ATPase domains of CDC48 and similar ATPase domains; CDC48 in yeast and p97 or VCP ...
164-328 2.65e-51

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: 176.09  E-value: 2.65e-51
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489514706 164 DVAGVDEAVEELYEIKDF-LQNPSRYQALGAKIPKGVLLYGPPGTGKTLLARAVAGEAGVPFFTISGSDFVEMFVGVGAS 242
Cdd:cd19519    1 DIGGCRKQLAQIREMVELpLRHPELFKAIGIKPPRGILLYGPPGTGKTLIARAVANETGAFFFLINGPEIMSKLAGESES 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489514706 243 RVRDLFEQAKQNSPCIIFVDEIDAVGRQRGAglggGHDEREQTL-NQLLVEMDGFGDRAGVILIAATNRPDILDPALLRP 321
Cdd:cd19519   81 NLRKAFEEAEKNAPAIIFIDEIDAIAPKREK----THGEVERRIvSQLLTLMDGLKQRAHVIVMAATNRPNSIDPALRRF 156

                 ....*..
gi 489514706 322 GRFDRQI 328
Cdd:cd19519  157 GRFDREI 163
RecA-like_NVL_r1-like cd19518
first of two ATPase domains of NVL (nuclear VCP-like protein) and similar ATPase domains; NVL ...
164-328 2.36e-49

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


Pssm-ID: 410926 [Multi-domain]  Cd Length: 169  Bit Score: 171.05  E-value: 2.36e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489514706 164 DVAGVDEAVEELYEIKDFL-QNPSRYQALGAKIPKGVLLYGPPGTGKTLLARAVAGEAGVPFFTISGSDFVEMFVGVGAS 242
Cdd:cd19518    1 DIGGMDSTLKELCELLIHPiLPPEYFQHLGVEPPRGVLLHGPPGCGKTMLANAIAGELKVPFLKISATEIVSGVSGESEE 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489514706 243 RVRDLFEQAKQNSPCIIFVDEIDAVGRQRGaglGGGHDEREQTLNQLLVEMDGFG----DRAGVILIAATNRPDILDPAL 318
Cdd:cd19518   81 KIRELFDQAISNAPCIVFIDEIDAITPKRE---SAQREMERRIVSQLLTCMDELNnektAGGPVLVIGATNRPDSLDPAL 157
                        170
                 ....*....|
gi 489514706 319 LRPGRFDRQI 328
Cdd:cd19518  158 RRAGRFDREI 167
RecA-like_PEX1_r2 cd19526
second of two ATPase domains of Peroxisomal biogenesis factor 1 (PEX1); PEX1(also known as ...
178-328 1.02e-43

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: 154.89  E-value: 1.02e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489514706 178 IKDFLQNPSRY----QALGAKIPKGVLLYGPPGTGKTLLARAVAGEAGVPFFTISGSDFVEMFVGVGASRVRDLFEQAKQ 253
Cdd:cd19526    5 LEETIEWPSKYpkifASSPLRLRSGILLYGPPGCGKTLLASAIASECGLNFISVKGPELLNKYIGASEQNVRDLFSRAQS 84
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 489514706 254 NSPCIIFVDEIDAVGRQRgaglggGHDER---EQTLNQLLVEMDGFGDRAGVILIAATNRPDILDPALLRPGRFDRQI 328
Cdd:cd19526   85 AKPCILFFDEFDSIAPKR------GHDSTgvtDRVVNQLLTQLDGVEGLDGVYVLAATSRPDLIDPALLRPGRLDKLV 156
RecA-like_PEX6_r2 cd19527
second of two ATPase domains of Peroxisomal biogenesis factor 6 (PEX6); PEX6(also known as ...
177-326 2.45e-42

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: 151.13  E-value: 2.45e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489514706 177 EIKDFLQNPSRYQ---ALGAKIPKGVLLYGPPGTGKTLLARAVAGEAGVPFFTISGSDFVEMFVGVGASRVRDLFEQAKQ 253
Cdd:cd19527    4 EILDTIQLPLEHPelfSSGLRKRSGILLYGPPGTGKTLLAKAIATECSLNFLSVKGPELINMYIGESEANVREVFQKARD 83
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 489514706 254 NSPCIIFVDEIDAVGRQRGA-GLGGGHDEReqTLNQLLVEMDGFGDRA-GVILIAATNRPDILDPALLRPGRFDR 326
Cdd:cd19527   84 AKPCVIFFDELDSLAPSRGNsGDSGGVMDR--VVSQLLAELDGMSSSGqDVFVIGATNRPDLLDPALLRPGRFDK 156
RecA-like_VPS4-like cd19509
ATPase domain of VPS4, ATAD1, K, KTNA1, Spastin, FIGL-1 and similar ATPase domains; This ...
165-328 2.47e-40

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: 145.57  E-value: 2.47e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489514706 165 VAGVDEAVEELYEIKDF-LQNPSRYQaLGAKIPKGVLLYGPPGTGKTLLARAVAGEAGVPFFTISGSDFVEMFVGVGASR 243
Cdd:cd19509    1 IAGLDDAKEALKEAVILpSLRPDLFP-GLRGPPRGILLYGPPGTGKTLLARAVASESGSTFFSISASSLVSKWVGESEKI 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489514706 244 VRDLFEQAKQNSPCIIFVDEIDAVGRQRGAglgGGHDEREQTLNQLLVEMDGFGDRA--GVILIAATNRPDILDPALLRp 321
Cdd:cd19509   80 VRALFALARELQPSIIFIDEIDSLLSERGS---GEHEASRRVKTEFLVQMDGVLNKPedRVLVLGATNRPWELDEAFLR- 155

                 ....*..
gi 489514706 322 gRFDRQI 328
Cdd:cd19509  156 -RFEKRI 161
RecA-like_Yta7-like cd19517
ATPase domain of Saccharomyces cerevisiae Yta7 and similar ATPase domains; Saccharomyces ...
164-327 2.44e-38

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: 140.34  E-value: 2.44e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489514706 164 DVAGVDEAVEELYEIKDF-LQNPSRYQALGAKIPKGVLLYGPPGTGKTLLARAVAGEAG-----VPFFTISGSDFVEMFV 237
Cdd:cd19517    1 DIGGLSHYINQLKEMVFFpLLYPEVFAKFKITPPRGVLFHGPPGTGKTLMARALAAECSkggqkVSFFMRKGADCLSKWV 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489514706 238 GVGASRVRDLFEQAKQNSPCIIFVDEIDAVGRQRGAglggghdEREQT----LNQLLVEMDGFGDRAGVILIAATNRPDI 313
Cdd:cd19517   81 GEAERQLRLLFEEAYRMQPSIIFFDEIDGLAPVRSS-------KQEQIhasiVSTLLALMDGLDNRGQVVVIGATNRPDA 153
                        170
                 ....*....|....
gi 489514706 314 LDPALLRPGRFDRQ 327
Cdd:cd19517  154 LDPALRRPGRFDRE 167
RecA-like_VPS4 cd19521
ATPase domain of vacuolar protein sorting-associated protein 4; Vacuolar protein ...
158-328 1.06e-36

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


Pssm-ID: 410929 [Multi-domain]  Cd Length: 170  Bit Score: 135.76  E-value: 1.06e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489514706 158 PKTTFADVAGVDEAVEELYEIKDFlqnPSRYQAL--GAKIP-KGVLLYGPPGTGKTLLARAVAGEAGVPFFTISGSDFVE 234
Cdd:cd19521    2 PNVKWEDVAGLEGAKEALKEAVIL---PVKFPHLftGNRKPwSGILLYGPPGTGKSYLAKAVATEANSTFFSVSSSDLVS 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489514706 235 MFVGVGASRVRDLFEQAKQNSPCIIFVDEIDAVGRQRGAglgGGHDEREQTLNQLLVEMDGFG-DRAGVILIAATNRPDI 313
Cdd:cd19521   79 KWMGESEKLVKQLFAMARENKPSIIFIDEVDSLCGTRGE---GESEASRRIKTELLVQMNGVGnDSQGVLVLGATNIPWQ 155
                        170
                 ....*....|....*
gi 489514706 314 LDPALLRpgRFDRQI 328
Cdd:cd19521  156 LDSAIRR--RFEKRI 168
RecA-like_ATAD1 cd19520
ATPase domain of ATPase family AAA domain-containing protein 1 and similar ATPase domains; ...
164-324 9.58e-34

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: 127.16  E-value: 9.58e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489514706 164 DVAGVDEAVEELYEIKDF-LQNPSRY---QALGAkiPKGVLLYGPPGTGKTLLARAVAGEAGVPFFTISGSDFVEMFVGV 239
Cdd:cd19520    1 DIGGLDEVITELKELVILpLQRPELFdnsRLLQP--PKGVLLYGPPGCGKTMLAKATAKEAGARFINLQVSSLTDKWYGE 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489514706 240 GASRVRDLFEQAKQNSPCIIFVDEIDAVGRQRGAglgGGHDEREQTLNQLLVEMDGF--GDRAGVILIAATNRPDILDPA 317
Cdd:cd19520   79 SQKLVAAVFSLASKLQPSIIFIDEIDSFLRQRSS---TDHEATAMMKAEFMSLWDGLstDGNCRVIVMGATNRPQDLDEA 155

                 ....*....
gi 489514706 318 LLR--PGRF 324
Cdd:cd19520  156 ILRrmPKRF 164
RecA-like_Figl-1 cd19525
ATPase domain of Fidgetin-Like 1 (FIGL-1); FIGL-1 may participate in DNA repair in the nucleus; ...
158-328 4.10e-31

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


Pssm-ID: 410933 [Multi-domain]  Cd Length: 186  Bit Score: 120.48  E-value: 4.10e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489514706 158 PKTTFADVAGVDEAVEELYEIKDF-LQNPSRYQALGAKiPKGVLLYGPPGTGKTLLARAVAGEAGVPFFTISGSDFVEMF 236
Cdd:cd19525   17 PPINWADIAGLEFAKKTIKEIVVWpMLRPDIFTGLRGP-PKGILLFGPPGTGKTLIGKCIASQSGATFFSISASSLTSKW 95
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489514706 237 VGVGASRVRDLFEQAKQNSPCIIFVDEIDAVGRQRGAglgGGHDEREQTLNQLLVEMDGFG----DRagVILIAATNRPD 312
Cdd:cd19525   96 VGEGEKMVRALFSVARCKQPAVIFIDEIDSLLSQRGE---GEHESSRRIKTEFLVQLDGATtsseDR--ILVVGATNRPQ 170
                        170
                 ....*....|....*.
gi 489514706 313 ILDPALLRpgRFDRQI 328
Cdd:cd19525  171 EIDEAARR--RLVKRL 184
RecA-like_KTNA1 cd19522
Katanin p60 ATPase-containing subunit A1; Katanin p60 ATPase-containing subunit A1 (KTNA1) is ...
164-328 9.22e-31

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


Pssm-ID: 410930 [Multi-domain]  Cd Length: 170  Bit Score: 118.55  E-value: 9.22e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489514706 164 DVAGVDEAVEELYE-------IKDFLQnpsryqalGAKIP-KGVLLYGPPGTGKTLLARAVAGEAGVPFFTISGSDFVEM 235
Cdd:cd19522    1 DIADLEEAKKLLEEavvlpmwMPEFFK--------GIRRPwKGVLMVGPPGTGKTLLAKAVATECGTTFFNVSSSTLTSK 72
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489514706 236 FVGVGASRVRDLFEQAKQNSPCIIFVDEIDAVGRQRGAglGGGHDEREQTLNQLLVEMDGFGDRAG-------VILIAAT 308
Cdd:cd19522   73 YRGESEKLVRLLFEMARFYAPTTIFIDEIDSICSRRGT--SEEHEASRRVKSELLVQMDGVGGASEnddpskmVMVLAAT 150
                        170       180
                 ....*....|....*....|
gi 489514706 309 NRPDILDPALLRpgRFDRQI 328
Cdd:cd19522  151 NFPWDIDEALRR--RLEKRI 168
RecA-like_NSF-SEC18_r1-like cd19504
first of two ATPase domains of NSF and SEC18, and similar ATPase domains; ...
185-330 1.04e-30

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: 118.75  E-value: 1.04e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489514706 185 PSRYQALGAKIPKGVLLYGPPGTGKTLLARAV-----AGEAGVpfftISGSDFVEMFVGVGASRVRDLFEQAKQ------ 253
Cdd:cd19504   24 PEIVEQLGCKHVKGILLYGPPGTGKTLMARQIgkmlnAREPKI----VNGPEILNKYVGESEANIRKLFADAEEeqrrlg 99
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 489514706 254 -NSPC-IIFVDEIDAVGRQRGAGlGGGHDEREQTLNQLLVEMDGFGDRAGVILIAATNRPDILDPALLRPGRFDRQIPV 330
Cdd:cd19504  100 aNSGLhIIIFDEIDAICKQRGSM-AGSTGVHDTVVNQLLSKIDGVEQLNNILVIGMTNRKDLIDEALLRPGRLEVQMEI 177
AAA cd00009
The AAA+ (ATPases Associated with a wide variety of cellular Activities) superfamily ...
189-331 1.16e-30

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: 117.63  E-value: 1.16e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489514706 189 QALGAKIPKGVLLYGPPGTGKTLLARAVAGEA---GVPFFTISGSDFVEMFVG---VGASRVRDLFEQAKQNSPCIIFVD 262
Cdd:cd00009   12 EALELPPPKNLLLYGPPGTGKTTLARAIANELfrpGAPFLYLNASDLLEGLVVaelFGHFLVRLLFELAEKAKPGVLFID 91
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 489514706 263 EIDAVGRqrgaglggghDEREQTLNQLLVEMDGFGDRAGVILIAATNRPDILDPALLRPGRFDRQIPVS 331
Cdd:cd00009   92 EIDSLSR----------GAQNALLRVLETLNDLRIDRENVRVIGATNRPLLGDLDRALYDRLDIRIVIP 150
RecA-like_spastin cd19524
ATPase domain of spastin; Spastin is an ATP-dependent microtubule-severing protein involved in ...
164-330 1.82e-29

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: 114.95  E-value: 1.82e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489514706 164 DVAGVDEAVEELYEIKdFLQN--PSRYQALGAKiPKGVLLYGPPGTGKTLLARAVAGEAGVPFFTISGSDFVEMFVGVGA 241
Cdd:cd19524    1 DIAGQDLAKQALQEMV-ILPSlrPELFTGLRAP-ARGLLLFGPPGNGKTMLAKAVAAESNATFFNISAASLTSKYVGEGE 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489514706 242 SRVRDLFEQAKQNSPCIIFVDEIDAVGRQRGAglgGGHDEREQTLNQLLVEMDGF----GDRagVILIAATNRPDILDPA 317
Cdd:cd19524   79 KLVRALFAVARELQPSIIFIDEVDSLLSERSE---GEHEASRRLKTEFLIEFDGVqsngDDR--VLVMGATNRPQELDDA 153
                        170
                 ....*....|...
gi 489514706 318 LLRpgRFDRQIPV 330
Cdd:cd19524  154 VLR--RFTKRVYV 164
RecA-like_BCS1 cd19510
Mitochondrial chaperone BCS1; Mitochondrial chaperone BCS1 is necessary for the assembly of ...
177-328 5.54e-23

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: 95.88  E-value: 5.54e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489514706 177 EIKDFLQNPSRYQALGAKIPKGVLLYGPPGTGKTLLARAVAGEAGVPFFTISGSDfvemfVGVGASRVRDLFEQAKQNSp 256
Cdd:cd19510    4 DLKDFIKNEDWYNDRGIPYRRGYLLYGPPGTGKSSFIAALAGELDYDICDLNLSE-----VVLTDDRLNHLLNTAPKQS- 77
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 489514706 257 cIIFVDEIDAV---GRQRGAGLGGGHDEREQTLNQLLVEMDGFGDRAGVILIAATNRPDILDPALLRPGRFDRQI 328
Cdd:cd19510   78 -IILLEDIDAAfesREHNKKNPSAYGGLSRVTFSGLLNALDGVASSEERIVFMTTNHIERLDPALIRPGRVDMKI 151
AAA smart00382
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ...
196-334 2.70e-22

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: 93.59  E-value: 2.70e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489514706   196 PKGVLLYGPPGTGKTLLARAVAGEA---GVPFFTISGSDFVE--------------MFVGVGASRVRDLFEQAKQNSPCI 258
Cdd:smart00382   2 GEVILIVGPPGSGKTTLARALARELgppGGGVIYIDGEDILEevldqllliivggkKASGSGELRLRLALALARKLKPDV 81
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 489514706   259 IFVDEIDAvgrqrgagLGGGHDEREQTLNQLLVEMDGFGDRAGVILIAATNRPDILDPALLRPgRFDRQIPVSNPD 334
Cdd:smart00382  82 LILDEITS--------LLDAEQEALLLLLEELRLLLLLKSEKNLTVILTTNDEKDLGPALLRR-RFDRRIVLLLIL 148
RecA-like_Ycf46-like cd19507
ATPase domain of Ycf46 and similar ATPase domains; Ycf46 may play a role in the regulation of ...
164-326 6.26e-21

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: 90.12  E-value: 6.26e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489514706 164 DVAGVDEaveelyeIKDFLQNPS-----RYQALGAKIPKGVLLYGPPGTGKTLLARAVAGEAGVPFFTISGSDFVEMFVG 238
Cdd:cd19507    1 DVGGLDN-------LKDWLKKRKaafskQASAYGLPTPKGLLLVGIQGTGKSLTAKAIAGVWQLPLLRLDMGRLFGGLVG 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489514706 239 VGASRVRDLFEQAKQNSPCIIFVDEID-AVGRQRGAGLGGGHDEREQTLNQLLVEmdgfgDRAGVILIAATNRPDILDPA 317
Cdd:cd19507   74 ESESRLRQMIQTAEAIAPCVLWIDEIEkGFSNADSKGDSGTSSRVLGTFLTWLQE-----KKKPVFVVATANNVQSLPPE 148

                 ....*....
gi 489514706 318 LLRPGRFDR 326
Cdd:cd19507  149 LLRKGRFDE 157
ycf46 CHL00195
Ycf46; Provisional
158-379 6.87e-21

Ycf46; Provisional


Pssm-ID: 177094 [Multi-domain]  Cd Length: 489  Bit Score: 96.63  E-value: 6.87e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489514706 158 PKTTFADVAGVDEaveelyeIKDFLQNPSR---YQAL--GAKIPKGVLLYGPPGTGKTLLARAVAGEAGVPFFTIsgsDF 232
Cdd:CHL00195 223 VNEKISDIGGLDN-------LKDWLKKRSTsfsKQASnyGLPTPRGLLLVGIQGTGKSLTAKAIANDWQLPLLRL---DV 292
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489514706 233 VEMF---VGVGASRVRDLFEQAKQNSPCIIFVDEID-AVGRQRGAGLGGGHDEREQTLNQLLVEmdgfgDRAGVILIAAT 308
Cdd:CHL00195 293 GKLFggiVGESESRMRQMIRIAEALSPCILWIDEIDkAFSNSESKGDSGTTNRVLATFITWLSE-----KKSPVFVVATA 367
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 489514706 309 NRPDILDPALLRPGRFDRQIPVSNPDLAGRRAVLRVH-SKGKPMA-ADADLDGLAKRTVGMTGADLANVINEA 379
Cdd:CHL00195 368 NNIDLLPLEILRKGRFDEIFFLDLPSLEEREKIFKIHlQKFRPKSwKKYDIKKLSKLSNKFSGAEIEQSIIEA 440
RecA-like_fidgetin cd19523
ATPase domain of fidgetin; Fidgetin (FIGN) is a ATP-dependent microtubule severing protein. ...
164-320 1.20e-17

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: 80.70  E-value: 1.20e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489514706 164 DVAGVD---EAVEElyEIKDFLQNPSRYQALgAKIPKGVLLYGPPGTGKTLLARAVAGEAGVPFFTISGSDFVEMFVGVG 240
Cdd:cd19523    1 DIAGLGalkAAIKE--EVLWPLLRPDAFSGL-LRLPRSILLFGPRGTGKTLLGRCLASQLGATFLRLRGSTLVAKWAGEG 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489514706 241 ASRVRDLFEQAKQNSPCIIFVDEIDAV--GRQRGAGLGGghdeREQTlnQLLVEMDGFGDRA--GVILIAATNRPDILDP 316
Cdd:cd19523   78 EKILQASFLAARCRQPSVLFISDLDALlsSQDDEASPVG----RLQV--ELLAQLDGVLGSGedGVLVVCTTSKPEEIDE 151

                 ....
gi 489514706 317 ALLR 320
Cdd:cd19523  152 SLRR 155
RarA COG2256
Replication-associated recombination protein RarA (DNA-dependent ATPase) [Replication, ...
188-402 3.78e-14

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


Pssm-ID: 441857 [Multi-domain]  Cd Length: 439  Bit Score: 75.48  E-value: 3.78e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489514706 188 YQALGAKIPKGVLLYGPPGTGKTLLARAVAGEAGVPFFTISGsdfvemfVGVGASRVRDLFEQAKQNS----PCIIFVDE 263
Cdd:COG2256   41 RRAIEAGRLSSMILWGPPGTGKTTLARLIANATDAEFVALSA-------VTSGVKDIREVIEEARERRaygrRTILFVDE 113
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489514706 264 I--------DAvgrqrgaglggghdereqtlnqLL--VEmDGFgdragVILIAAT--NrPDI-LDPALLrpgrfDR-QI- 328
Cdd:COG2256  114 IhrfnkaqqDA----------------------LLphVE-DGT-----ITLIGATteN-PSFeVNSALL-----SRcRVf 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489514706 329 ---PVSNPDLAG--RRAV----LRVHSKGKPMAADAdLDGLAkrtvGMTGADLANVIN--EAALLTARENGT-VITGPAL 396
Cdd:COG2256  160 vlkPLSEEDLEQllERALaddeRGLGGYKLELDDEA-LEALA----RLADGDARRALNalELAVLSAPPDGViEITLELV 234

                 ....*.
gi 489514706 397 EEAVDR 402
Cdd:COG2256  235 EEALQR 240
RecA-like_ATAD3-like cd19512
ATPase domains of ATPase AAA-domain protein 3A (ATAD3A), -3B, and -3C, and similar ATPase ...
197-318 1.44e-13

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


Pssm-ID: 410920 [Multi-domain]  Cd Length: 150  Bit Score: 68.71  E-value: 1.44e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489514706 197 KGVLLYGPPGTGKTLLARAVAGEAGVPFFTISGSDFVEMFVGvGASRVRDLFEQA-KQNSPCIIFVDEIDAVGRQRgAGL 275
Cdd:cd19512   23 RNILFYGPPGTGKTLFAKKLALHSGMDYAIMTGGDVAPMGRE-GVTAIHKVFDWAnTSRRGLLLFVDEADAFLRKR-STE 100
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 489514706 276 GGGHDEReQTLNQLLVEMdgfGDRAG-VILIAATNRPDILDPAL 318
Cdd:cd19512  101 KISEDLR-AALNAFLYRT---GEQSNkFMLVLASNQPEQFDWAI 140
PRK13342 PRK13342
recombination factor protein RarA; Reviewed
188-402 2.19e-13

recombination factor protein RarA; Reviewed


Pssm-ID: 237355 [Multi-domain]  Cd Length: 413  Bit Score: 72.81  E-value: 2.19e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489514706 188 YQALGAKIPKGVLLYGPPGTGKTLLARAVAGEAGVPFFTISGSDFvemfvgvGASRVRDLFEQAKQNS----PCIIFVDE 263
Cdd:PRK13342  28 RRMIEAGRLSSMILWGPPGTGKTTLARIIAGATDAPFEALSAVTS-------GVKDLREVIEEARQRRsagrRTILFIDE 100
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489514706 264 IdavgrqrgaglgggHdeReqtLN---Q--LL--VEmDGFgdragVILIAAT--NrPDI-LDPALLrpgrfDR-QI---- 328
Cdd:PRK13342 101 I--------------H--R---FNkaqQdaLLphVE-DGT-----ITLIGATteN-PSFeVNPALL-----SRaQVfelk 149
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 489514706 329 PVSNPDLAG--RRAvLRVHSKGKPMAADADLDGLAKrtvgMTGADLANVINeaALLTARENGTVITGPALEEAVDR 402
Cdd:PRK13342 150 PLSEEDIEQllKRA-LEDKERGLVELDDEALDALAR----LANGDARRALN--LLELAALGVDSITLELLEEALQK 218
RecA-like_Ycf2 cd19505
ATPase domain of plant YCF2; Ycf2 is a chloroplast ATPase which has an essential function; ...
191-330 8.43e-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: 67.02  E-value: 8.43e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489514706 191 LGAKIPKGVLLYGPPGTGKTLLARAVAGEAGVPFFTISGSDFV--------------EMFVGVGASRVRDLFEQAKQNSP 256
Cdd:cd19505    7 LGLSPSKGILLIGSIETGRSYLIKSLAANSYVPLIRISLNKLLynkpdfgnddwidgMLILKESLHRLNLQFELAKAMSP 86
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 489514706 257 CIIFVDEIDAVGRQRgagLGGGHDEREQTLNQLLVEM--DGFGDRA--GVILIAATNRPDILDPALLRPGRFDRQIPV 330
Cdd:cd19505   87 CIIWIPNIHELNVNR---STQNLEEDPKLLLGLLLNYlsRDFEKSStrNILVIASTHIPQKVDPALIAPNRLDTCINI 161
PRK04195 PRK04195
replication factor C large subunit; Provisional
158-265 2.32e-12

replication factor C large subunit; Provisional


Pssm-ID: 235250 [Multi-domain]  Cd Length: 482  Bit Score: 69.95  E-value: 2.32e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489514706 158 PKTtFADVAGVDEAVEELYE-IKDFLQNpsryqalgaKIPKGVLLYGPPGTGKTLLARAVAGEAGVPFFTISGSDF---- 232
Cdd:PRK04195  10 PKT-LSDVVGNEKAKEQLREwIESWLKG---------KPKKALLLYGPPGVGKTSLAHALANDYGWEVIELNASDQrtad 79
                         90       100       110
                 ....*....|....*....|....*....|....
gi 489514706 233 -VEMFVGvGASRVRDLFEQAKQnspcIIFVDEID 265
Cdd:PRK04195  80 vIERVAG-EAATSGSLFGARRK----LILLDEVD 108
AAA_5 pfam07728
AAA domain (dynein-related subfamily); This Pfam entry includes some of the AAA proteins not ...
198-324 4.61e-10

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: 58.07  E-value: 4.61e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489514706  198 GVLLYGPPGTGKTLLARAVAgEA--GVPFFTISGSDF---------VEMFVGVGASRVRDLFEQAKqnSPCIIFVDEIDA 266
Cdd:pfam07728   1 GVLLVGPPGTGKTELAERLA-AAlsNRPVFYVQLTRDtteedlfgrRNIDPGGASWVDGPLVRAAR--EGEIAVLDEINR 77
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 489514706  267 vgrqrgaglggGHDEREQTLNQLLVE-----MDGFG----DRAGVILIAATNRPDI----LDPALLRpgRF 324
Cdd:pfam07728  78 -----------ANPDVLNSLLSLLDErrlllPDGGElvkaAPDGFRLIATMNPLDRglneLSPALRS--RF 135
RecA-like_HslU cd19498
ATP-dependent protease ATPase subunit HslU; HslU is a component of the ATP-dependent protease ...
182-280 7.46e-10

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


Pssm-ID: 410906 [Multi-domain]  Cd Length: 183  Bit Score: 58.93  E-value: 7.46e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489514706 182 LQNPSRYQALGAKI-----PKGVLLYGPPGTGKTLLARAVAGEAGVPFFTISGSDFVEM-FVGVGA-SRVRDLFEQakqn 254
Cdd:cd19498   27 LRNRWRRMQLPEELrdevtPKNILMIGPTGVGKTEIARRLAKLAGAPFIKVEATKFTEVgYVGRDVeSIIRDLVEG---- 102
                         90       100
                 ....*....|....*....|....*.
gi 489514706 255 spcIIFVDEIDAVGRQRGaglGGGHD 280
Cdd:cd19498  103 ---IVFIDEIDKIAKRGG---SSGPD 122
AAA_lid_3 pfam17862
AAA+ lid domain; This entry represents the alpha helical AAA+ lid domain that is found to the ...
354-398 1.64e-09

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: 53.70  E-value: 1.64e-09
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 489514706  354 DADLDGLAKRTVGMTGADLANVINEAALLTARENGTVITGPALEE 398
Cdd:pfam17862   1 DVDLEELAERTEGFSGADLEALCREAALAALRRGLEAVTQEDLEE 45
ycf2 CHL00206
Ycf2; Provisional
191-442 2.70e-09

Ycf2; Provisional


Pssm-ID: 214396 [Multi-domain]  Cd Length: 2281  Bit Score: 61.08  E-value: 2.70e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489514706  191 LGAKIPKGVLLYGPPGTGKTLLARAVAGEAGVPFFT--------------------ISGSDFVE---------------- 234
Cdd:CHL00206 1625 LALSPSRGILVIGSIGTGRSYLVKYLATNSYVPFITvflnkfldnkpkgfliddidIDDSDDIDdsddidrdldtelltm 1704
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489514706  235 -------MFVGVGASRVRDLFEQAKQNSPCIIFVDEIDAVGRqrgaglgggHDEREQTLNQLLVEMDGFGDRAGV---IL 304
Cdd:CHL00206 1705 mnaltmdMMPKIDRFYITLQFELAKAMSPCIIWIPNIHDLNV---------NESNYLSLGLLVNSLSRDCERCSTrniLV 1775
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489514706  305 IAATNRPDILDPALLRPGRFDRQIPVSNPDLAGRR----AVLRV---HSKGKPMaadaDLDGLAKRTVGMTGADLANVIN 377
Cdd:CHL00206 1776 IASTHIPQKVDPALIAPNKLNTCIKIRRLLIPQQRkhffTLSYTrgfHLEKKMF----HTNGFGSITMGSNARDLVALTN 1851
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 489514706  378 EAALLTARENGTVITGPALEEAVDRVIGGPRRKGRiiSEQEKKITAYHEGGHTL--AAWAMPDIEPI 442
Cdd:CHL00206 1852 EALSISITQKKSIIDTNTIRSALHRQTWDLRSQVR--SVQDHGILFYQIGRAVAqnVLLSNCPIDPI 1916
FtsH_ext pfam06480
FtsH Extracellular; This domain is found in the FtsH family of proteins. FtsH is the only ...
10-107 1.07e-07

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: 50.68  E-value: 1.07e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489514706   10 ITAIAVVVLLGWSFFYFSDDTRGYKPVDTSVAITQINGDNVKSAQIDDREQQLRLILKKGNNetDGSEKVITKYPTGYAV 89
Cdd:pfam06480   3 LWLLILLVLLLLFLLFLLSSSSSTKEISYSEFLEYLEAGKVKKVVVQDDEILPTGVVEGTLK--DGSKFTTYFIPSLPNV 80
                          90       100
                  ....*....|....*....|...
gi 489514706   90 DLF-----NALSAKNAKVSTVVN 107
Cdd:pfam06480  81 DSLlekleDALEEKGVKVSVKPP 103
RecA-like_superfamily cd01120
RecA-like_NTPases; RecA-like NTPases. This superfamily includes the NTP binding domain of F1 ...
199-315 1.68e-07

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: 50.58  E-value: 1.68e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489514706 199 VLLYGPPGTGKTLLARAVAGEA---GVPFFTISgsdFVEMFVgvgaSRVRDLFEQAKqnsPCIIFVDEIDAVGRQRGAgl 275
Cdd:cd01120    1 ILITGPPGSGKTTLLLQFAEQAllsDEPVIFIS---FLDTIL----EAIEDLIEEKK---LDIIIIDSLSSLARASQG-- 68
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 489514706 276 ggghDEREQTLNQLLVEMDGFGDrAGVILIAATNRPDILD 315
Cdd:cd01120   69 ----DRSSELLEDLAKLLRAARN-TGITVIATIHSDKFDI 103
CDC6 COG1474
Cdc6-related protein, AAA superfamily ATPase [Replication, recombination and repair];
196-315 6.12e-07

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


Pssm-ID: 441083 [Multi-domain]  Cd Length: 389  Bit Score: 52.54  E-value: 6.12e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489514706 196 PKGVLLYGPPGTGKTLLARAV-------AGEAGVPFFTI----------------------SGSDFVEmfVGVGASRVRD 246
Cdd:COG1474   51 PSNVLIYGPTGTGKTAVAKYVleeleeeAEERGVDVRVVyvncrqastryrvlsrileelgSGEDIPS--TGLSTDELFD 128
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 489514706 247 LFEQA--KQNSPCIIFVDEIDAVgrqrgaglggGHDEREQTLNQLLVEMDGF-GDRAGVILIaaTNRPDILD 315
Cdd:COG1474  129 RLYEAldERDGVLVVVLDEIDYL----------VDDEGDDLLYQLLRANEELeGARVGVIGI--SNDLEFLE 188
T7SS_EccA TIGR03922
type VII secretion AAA-ATPase EccA; This model represents the AAA family ATPase, EccA, of the ...
167-328 9.41e-07

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: 52.15  E-value: 9.41e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489514706  167 GVDEAVEELYEIKDFLQNPSRYQALGAKIP---KGVLLYGPPGTGKTLLARAVAGE-AGVPFFT------ISGSDFVEMF 236
Cdd:TIGR03922 280 GLERVKRQVAALKSSTAMALARAERGLPVAqtsNHMLFAGPPGTGKTTIARVVAKIyCGLGVLRkplvreVSRADLIGQY 359
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489514706  237 VGVGASRVRDLFEQAKQNspcIIFVDEIDAVGRQRGaglGGGHDEREQTLNQLLVEMDgfGDRAGVILIAATNRPDIlDP 316
Cdd:TIGR03922 360 IGESEAKTNEIIDSALGG---VLFLDEAYTLVETGY---GQKDPFGLEAIDTLLARME--NDRDRLVVIGAGYRKDL-DK 430
                         170
                  ....*....|....*..
gi 489514706  317 AL-----LRpGRFDRQI 328
Cdd:TIGR03922 431 FLevnegLR-SRFTRVI 446
TIP49 COG1224
DNA helicase TIP49, TBP-interacting protein [Transcription];
197-232 1.10e-06

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


Pssm-ID: 440837 [Multi-domain]  Cd Length: 452  Bit Score: 51.89  E-value: 1.10e-06
                         10        20        30
                 ....*....|....*....|....*....|....*...
gi 489514706 197 KGVLLYGPPGTGKTLLARAVAGEAG--VPFFTISGSDF 232
Cdd:COG1224   65 KGILIVGPPGTGKTALAVAIARELGedTPFVAISGSEI 102
ruvB PRK00080
Holliday junction branch migration DNA helicase RuvB;
199-264 1.45e-06

Holliday junction branch migration DNA helicase RuvB;


Pssm-ID: 234619 [Multi-domain]  Cd Length: 328  Bit Score: 50.90  E-value: 1.45e-06
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 489514706 199 VLLYGPPGTGKTLLARAVAGEAGVPFFTISG------SDFVEMFVGVGAsrvRDlfeqakqnspcIIFVDEI 264
Cdd:PRK00080  54 VLLYGPPGLGKTTLANIIANEMGVNIRITSGpalekpGDLAAILTNLEE---GD-----------VLFIDEI 111
RecA-like_ClpB_Hsp104-like cd19499
Chaperone protein ClpB/Hsp104 subfamily; Bacterial Caseinolytic peptidase B (ClpB) and ...
155-265 3.81e-06

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


Pssm-ID: 410907 [Multi-domain]  Cd Length: 178  Bit Score: 47.94  E-value: 3.81e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489514706 155 KDMPKTTFADVAGVDEAVEE----LYEIKDFLQNPSRyqalgakiPKGVLLY-GPPGTGKTLLARAVAGE---AGVPFFT 226
Cdd:cd19499    3 LNLEERLHERVVGQDEAVKAvsdaIRRARAGLSDPNR--------PIGSFLFlGPTGVGKTELAKALAELlfgDEDNLIR 74
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 489514706 227 ISGSDFVEMFVG----------VGASRVRDLFEQAKQNSPCIIFVDEID 265
Cdd:cd19499   75 IDMSEYMEKHSVsrligappgyVGYTEGGQLTEAVRRKPYSVVLLDEIE 123
RecA-like_Lon cd19500
lon protease homolog 2 peroxisomal; Lon protease (also known as Lon peptidase) is an ...
200-269 7.21e-06

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: 47.17  E-value: 7.21e-06
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 489514706 200 LLYGPPGTGKTLLARAVAGEAGVPFFTIS-G--SDFVEM------FVGVGASRVRDLFEQAKQNSPcIIFVDEIDAVGR 269
Cdd:cd19500   41 CLVGPPGVGKTSLGKSIARALGRKFVRISlGgvRDEAEIrghrrtYVGAMPGRIIQALKKAGTNNP-VFLLDEIDKIGS 118
RuvB_N pfam05496
Holliday junction DNA helicase RuvB P-loop domain; The RuvB protein makes up part of the ...
199-229 8.15e-06

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: 46.34  E-value: 8.15e-06
                          10        20        30
                  ....*....|....*....|....*....|.
gi 489514706  199 VLLYGPPGTGKTLLARAVAGEAGVPFFTISG 229
Cdd:pfam05496  36 VLLYGPPGLGKTTLANIIANEMGVNIRITSG 66
DnaA COG0593
Chromosomal replication initiation ATPase DnaA [Replication, recombination and repair];
199-425 8.37e-06

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


Pssm-ID: 440358 [Multi-domain]  Cd Length: 303  Bit Score: 48.26  E-value: 8.37e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489514706 199 VLLYGPPGTGKTLLARAVAGEA-----GVPFFTISGSDFVEMFvgVGASRVRDLFE-QAKQNSPCIIFVDEIdavgrQRG 272
Cdd:COG0593   37 LFLYGGVGLGKTHLLHAIGNEAlennpGARVVYLTAEEFTNDF--INAIRNNTIEEfKEKYRSVDVLLIDDI-----QFL 109
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489514706 273 AGlggghDEREQ-----TLNQLLvemdgfgDRAGVILIAATNRP---DILDPALLRpgRFDR--QIPVSNPDLAGRRAVL 342
Cdd:COG0593  110 AG-----KEATQeeffhTFNALR-------EAGKQIVLTSDRPPkelPGLEERLRS--RLEWglVVDIQPPDLETRIAIL 175
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489514706 343 RVHSKGKPMAADAD-LDGLAKRtVGMTGADLanvinEAALLT----ARENGTVITGPALEEAVDRVIGGPRRkgRIISEQ 417
Cdd:COG0593  176 RKKAADRGLELPDEvLEYLARR-IERNVREL-----EGALNRldayALLTGRPITLELAREVLKDLLRAQKK--EITIED 247

                 ....*...
gi 489514706 418 EKKITAYH 425
Cdd:COG0593  248 IQKAVAEY 255
McrB COG1401
5-methylcytosine-specific restriction endonuclease McrBC, GTP-binding regulatory subunit McrB ...
162-264 9.94e-06

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


Pssm-ID: 441011 [Multi-domain]  Cd Length: 477  Bit Score: 49.00  E-value: 9.94e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489514706 162 FADVAGVDEAVEELYEIKDFLQNPSR------YQALgaKIPKGVLLYGPPGTGKT----LLARAVAGEAGVPFFTI---- 227
Cdd:COG1401  183 AAEELYSEDLESEDDYLKDLLREKFEetleafLAAL--KTKKNVILAGPPGTGKTylarRLAEALGGEDNGRIEFVqfhp 260
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 489514706 228 --SGSDFVEMFVGVGAS---RVRD-LF----EQAKQNS--PCIIFVDEI 264
Cdd:COG1401  261 swSYEDFLLGYRPSLDEgkyEPTPgIFlrfcLKAEKNPdkPYVLIIDEI 309
TIP49 pfam06068
TIP49 P-loop domain; This family consists of the C-terminal region of several eukaryotic and ...
197-232 1.35e-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: 48.07  E-value: 1.35e-05
                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 489514706  197 KGVLLYGPPGTGKTLLARAVAGEAG--VPFFTISGSDF 232
Cdd:pfam06068  51 RAVLIAGPPGTGKTALAIAISKELGedTPFTSISGSEV 88
ruvB TIGR00635
Holliday junction DNA helicase, RuvB subunit; All proteins in this family for which functions ...
199-270 2.12e-05

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


Pssm-ID: 129721 [Multi-domain]  Cd Length: 305  Bit Score: 47.29  E-value: 2.12e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 489514706  199 VLLYGPPGTGKTLLARAVAGEAGVPFFTISG------SDFVEMFVGVGAsrvRDlfeqakqnspcIIFVDEIDAVGRQ 270
Cdd:TIGR00635  33 LLLYGPPGLGKTTLAHIIANEMGVNLKITSGpalekpGDLAAILTNLEE---GD-----------VLFIDEIHRLSPA 96
AAA_22 pfam13401
AAA domain;
199-314 2.19e-05

AAA domain;


Pssm-ID: 379165 [Multi-domain]  Cd Length: 129  Bit Score: 44.64  E-value: 2.19e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489514706  199 VLLYGPPGTGKTLLARAVA---GEAGVPFFTI------SGSDFVEMFV---------GVGASRVRDLFEQA--KQNSPCI 258
Cdd:pfam13401   8 LVLTGESGTGKTTLLRRLLeqlPEVRDSVVFVdlpsgtSPKDLLRALLralglplsgRLSKEELLAALQQLllALAVAVV 87
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 489514706  259 IFVDEIDAVgrqrgaglggghdeREQTLNQLLVEMDGFGDRAGVILIAATNRPDIL 314
Cdd:pfam13401  88 LIIDEAQHL--------------SLEALEELRDLLNLSSKLLQLILVGTPELRELL 129
RuvB COG2255
Holliday junction resolvasome RuvABC, ATP-dependent DNA helicase subunit RuvB [Replication, ...
199-229 2.98e-05

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


Pssm-ID: 441856 [Multi-domain]  Cd Length: 337  Bit Score: 47.00  E-value: 2.98e-05
                         10        20        30
                 ....*....|....*....|....*....|.
gi 489514706 199 VLLYGPPGTGKTLLARAVAGEAGVPFFTISG 229
Cdd:COG2255   57 VLLYGPPGLGKTTLAHIIANEMGVNIRITSG 87
RecA-like_Pch2-like cd19508
ATPase domain of Pachytene checkpoint 2 (Pch2) and similar ATPase domains; Pch2 (known as ...
199-318 3.49e-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: 45.52  E-value: 3.49e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489514706 199 VLLYGPPGTGKTLLARAVAGEAGVPF-FTISGSDFVEM--------FVGVGASRVRDLFEQAKQ---NSPCIIFV--DEI 264
Cdd:cd19508   55 VLLHGPPGTGKTSLCKALAQKLSIRLsSRYRYGQLIEInshslfskWFSESGKLVTKMFQKIQElidDKDALVFVliDEV 134
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 489514706 265 DAVGRQRGAGLGGGH-DEREQTLNQLLVEMDGFGDRAGVILIAATNRPDILDPAL 318
Cdd:cd19508  135 ESLAAARSASSSGTEpSDAIRVVNAVLTQIDRIKRYHNNVILLTSNLLEKIDVAF 189
AAA_2 pfam07724
AAA domain (Cdc48 subfamily); This Pfam entry includes some of the AAA proteins not detected ...
196-265 4.73e-05

AAA domain (Cdc48 subfamily); This Pfam entry includes some of the AAA proteins not detected by the pfam00004 model.


Pssm-ID: 400187 [Multi-domain]  Cd Length: 168  Bit Score: 44.49  E-value: 4.73e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489514706  196 PKGV-LLYGPPGTGKTLLARAVAGEAGV---PFFTISGSDFVE-----MFVG-----VGASRVRDLFEQAKQNSPCIIFV 261
Cdd:pfam07724   2 PIGSfLFLGPTGVGKTELAKALAELLFGderALIRIDMSEYMEehsvsRLIGappgyVGYEEGGQLTEAVRRKPYSIVLI 81

                  ....
gi 489514706  262 DEID 265
Cdd:pfam07724  82 DEIE 85
MoxR COG0714
MoxR-like ATPase [General function prediction only]; MoxR-like ATPase is part of the Pathway ...
199-227 1.13e-04

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


Pssm-ID: 440478 [Multi-domain]  Cd Length: 292  Bit Score: 44.77  E-value: 1.13e-04
                         10        20
                 ....*....|....*....|....*....
gi 489514706 199 VLLYGPPGTGKTLLARAVAGEAGVPFFTI 227
Cdd:COG0714   34 LLLEGVPGVGKTTLAKALARALGLPFIRI 62
PRK10263 PRK10263
DNA translocase FtsK; Provisional
622-758 1.27e-04

DNA translocase FtsK; Provisional


Pssm-ID: 236669 [Multi-domain]  Cd Length: 1355  Bit Score: 45.85  E-value: 1.27e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489514706  622 PSDKPPIKTPGELAIERGEPWPQPVPepafkaaiaqatQAAEAARSDAGQTGHGANGSPAGTHRSGDRQYGSTQPDYGAP 701
Cdd:PRK10263  377 PEGYPQQSQYAQPAVQYNEPLQQPVQ------------PQQPYYAPAAEQPAQQPYYAPAPEQPAQQPYYAPAPEQPVAG 444
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 489514706  702 AGWHAPgwPPRSSHRPSYSGEPAPTYP---GQPYPTGQADPGSDESSAEQDDEVSRTKPA 758
Cdd:PRK10263  445 NAWQAE--EQQSTFAPQSTYQTEQTYQqpaAQEPLYQQPQPVEQQPVVEPEPVVEETKPA 502
HolB COG0470
DNA polymerase III, delta prime subunit [Replication, recombination and repair];
177-266 2.70e-04

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


Pssm-ID: 440238 [Multi-domain]  Cd Length: 289  Bit Score: 43.43  E-value: 2.70e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489514706 177 EIKDFLQNpsryQALGAKIPKGVLLYGPPGTGKTLLARAVA-------GEAGVPFFTISG--------SDFVEMFVGV-- 239
Cdd:COG0470    3 EAWEQLLA----AAESGRLPHALLLHGPPGIGKTTLALALArdllcenPEGGKACGQCHSrlmaagnhPDLLELNPEEks 78
                         90       100       110
                 ....*....|....*....|....*....|....
gi 489514706 240 ---GASRVRDLFEQAKQNSPC----IIFVDEIDA 266
Cdd:COG0470   79 dqiGIDQIRELGEFLSLTPLEggrkVVIIDEADA 112
AAA_16 pfam13191
AAA ATPase domain; This family of domains contain a P-loop motif that is characteriztic of the ...
173-291 3.29e-04

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


Pssm-ID: 433025 [Multi-domain]  Cd Length: 167  Bit Score: 42.11  E-value: 3.29e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489514706  173 EELYEIKDFLQNPSRYQalgakiPKGVLLYGPPGTGKTLLARAV---AGEAGVPFFTISGSDFVEMFVGVGASRVRDLFE 249
Cdd:pfam13191   7 EELEQLLDALDRVRSGR------PPSVLLTGEAGTGKTTLLRELlraLERDGGYFLRGKCDENLPYSPLLEALTREGLLR 80
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 489514706  250 QAKQNSPCIIFV---DEIDAVGRQRGAGLGGGHDEREQTLNQLLV 291
Cdd:pfam13191  81 QLLDELESSLLEawrAALLEALAPVPELPGDLAERLLDLLLRLLD 125
PRK11361 PRK11361
acetoacetate metabolism transcriptional regulator AtoC;
163-339 3.42e-04

acetoacetate metabolism transcriptional regulator AtoC;


Pssm-ID: 183099 [Multi-domain]  Cd Length: 457  Bit Score: 43.68  E-value: 3.42e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489514706 163 ADVAGVDEAVEELYEIKDFLQNPSRYQAL---GAKIPKG---VLLYGPPGTGKTLLARAV---AGEAGVPFFTISGSDFV 233
Cdd:PRK11361 127 KEIRHLHQALSTSWQWGHILTNSPAMMDIckdTAKIALSqasVLISGESGTGKELIARAIhynSRRAKGPFIKVNCAALP 206
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489514706 234 E-------------MFVGVGASRvRDLFEQAKQNSpciIFVDEIDAVGRQRGAGLGGGHDEREqtlnqllVEMDGFGD-- 298
Cdd:PRK11361 207 EslleselfghekgAFTGAQTLR-QGLFERANEGT---LLLDEIGEMPLVLQAKLLRILQERE-------FERIGGHQti 275
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 489514706 299 RAGVILIAATNRpDIldPALLRPGRFdRQ--------IPVSNPDLAGRR 339
Cdd:PRK11361 276 KVDIRIIAATNR-DL--QAMVKEGTF-REdlfyrlnvIHLILPPLRDRR 320
44 PHA02544
clamp loader, small subunit; Provisional
194-231 3.53e-04

clamp loader, small subunit; Provisional


Pssm-ID: 222866 [Multi-domain]  Cd Length: 316  Bit Score: 43.44  E-value: 3.53e-04
                         10        20        30
                 ....*....|....*....|....*....|....*...
gi 489514706 194 KIPKGVLLYGPPGTGKTLLARAVAGEAGVPFFTISGSD 231
Cdd:PHA02544  41 RIPNMLLHSPSPGTGKTTVAKALCNEVGAEVLFVNGSD 78
NACHT COG5635
Predicted NTPase, NACHT family domain [Signal transduction mechanisms];
161-320 4.03e-04

Predicted NTPase, NACHT family domain [Signal transduction mechanisms];


Pssm-ID: 444362 [Multi-domain]  Cd Length: 935  Bit Score: 44.03  E-value: 4.03e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489514706 161 TFADVAGVDEAVEELY---EIKDFLQNPSRYQALGAKIPKgVLLYGPPGTGKTLLARAVA---------GEAGVPFF--- 225
Cdd:COG5635  143 LLLDADGLLVSLDDLYvplNLLERIESLKRLELLEAKKKR-LLILGEPGSGKTTLLRYLAlelaeryldAEDPIPILiel 221
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489514706 226 -TISGS----DFVEMFVGVGASRVRDLFEQAKQNSPCIIFVDEIDAVGRQrgaglggghDEREQTLNQLLVEMDGFgDRA 300
Cdd:COG5635  222 rDLAEEasleDLLAEALEKRGGEPEDALERLLRNGRLLLLLDGLDEVPDE---------ADRDEVLNQLRRFLERY-PKA 291
                        170       180
                 ....*....|....*....|
gi 489514706 301 GVILiaaTNRPDILDPALLR 320
Cdd:COG5635  292 RVII---TSRPEGYDSSELE 308
PRK13341 PRK13341
AAA family ATPase;
200-264 4.25e-04

AAA family ATPase;


Pssm-ID: 237354 [Multi-domain]  Cd Length: 725  Bit Score: 43.89  E-value: 4.25e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489514706 200 LLYGPPGTGKTLLARAVAGEAGVPFFTISGsdfvemfVGVGASRVRDLFEQAKQ-----NSPCIIFVDEI 264
Cdd:PRK13341  56 ILYGPPGVGKTTLARIIANHTRAHFSSLNA-------VLAGVKDLRAEVDRAKErlerhGKRTILFIDEV 118
fbpC PRK11432
ferric ABC transporter ATP-binding protein;
195-340 4.69e-04

ferric ABC transporter ATP-binding protein;


Pssm-ID: 183133 [Multi-domain]  Cd Length: 351  Bit Score: 43.17  E-value: 4.69e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489514706 195 IPKG--VLLYGPPGTGKTLLARAVAG----EAGVPFftISGSDfvemfVGVGASRVRDLfeqakqnspCIIFVDEI---- 264
Cdd:PRK11432  29 IKQGtmVTLLGPSGCGKTTVLRLVAGlekpTEGQIF--IDGED-----VTHRSIQQRDI---------CMVFQSYAlfph 92
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489514706 265 DAVGRQRGAGL---GGGHDEREQTLNQLL--VEMDGFGDR------AGVILIAATNRPDILDPALLrpgRFDRqiPVSNP 333
Cdd:PRK11432  93 MSLGENVGYGLkmlGVPKEERKQRVKEALelVDLAGFEDRyvdqisGGQQQRVALARALILKPKVL---LFDE--PLSNL 167

                 ....*..
gi 489514706 334 DLAGRRA 340
Cdd:PRK11432 168 DANLRRS 174
RecA-like_ClpX cd19497
ATP-dependent Clp protease ATP-binding subunit ClpX; ClpX is a component of the ATP-dependent ...
182-269 7.18e-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: 42.20  E-value: 7.18e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489514706 182 LQNPSRYQALGAKIPKG-VLLYGPPGTGKTLLARAVAGEAGVPfFTIS-----------GSDfVEMFVgvgasrVRDL-- 247
Cdd:cd19497   35 IRNNLKQKDDDVELEKSnILLIGPTGSGKTLLAQTLAKILDVP-FAIAdattlteagyvGED-VENIL------LKLLqa 106
                         90       100
                 ....*....|....*....|....*.
gi 489514706 248 ----FEQAKQNspcIIFVDEIDAVGR 269
Cdd:cd19497  107 adydVERAQRG---IVYIDEIDKIAR 129
PRK01318 PRK01318
membrane protein insertase; Provisional
1-79 2.04e-03

membrane protein insertase; Provisional


Pssm-ID: 234942 [Multi-domain]  Cd Length: 521  Bit Score: 41.40  E-value: 2.04e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489514706   1 MNRKNVTRTItAIAVVVLLGWSFFYFsDDTRGYKPVDTSVAITQINGDNV------KSAQIDDreqqlrLILKKGNNETD 74
Cdd:PRK01318   1 MDNKRLLLAI-ALSFVIFLGWQYWQQ-DKAQAAAQAPAPQARITVETDVLrlsidtKGGRIDD------LLLKKYKETLD 72

                 ....*
gi 489514706  75 GSEKV 79
Cdd:PRK01318  73 SSPPV 77
PRK12402 PRK12402
replication factor C small subunit 2; Reviewed
160-252 2.19e-03

replication factor C small subunit 2; Reviewed


Pssm-ID: 237090 [Multi-domain]  Cd Length: 337  Bit Score: 41.13  E-value: 2.19e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489514706 160 TTFADVAGVDEAVEELYEikdflqnpsryqALGAKIPKGVLLYGPPGTGKTLLARAVAGEA-GVPFftisGSDFVEMfvg 238
Cdd:PRK12402  12 ALLEDILGQDEVVERLSR------------AVDSPNLPHLLVQGPPGSGKTAAVRALARELyGDPW----ENNFTEF--- 72
                         90
                 ....*....|....
gi 489514706 239 vgasRVRDLFEQAK 252
Cdd:PRK12402  73 ----NVADFFDQGK 82
Sigma54_activat pfam00158
Sigma-54 interaction domain;
193-264 2.56e-03

Sigma-54 interaction domain;


Pssm-ID: 425491 [Multi-domain]  Cd Length: 168  Bit Score: 39.31  E-value: 2.56e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489514706  193 AKIPKGVLLYGPPGTGKTLLARAV---AGEAGVPFFTISGSDFV------EMFvGV------GASRVRD-LFEQAKQNsp 256
Cdd:pfam00158  19 APTDAPVLITGESGTGKELFARAIhqlSPRADGPFVAVNCAAIPeellesELF-GHekgaftGADSDRKgLFELADGG-- 95

                  ....*...
gi 489514706  257 cIIFVDEI 264
Cdd:pfam00158  96 -TLFLDEI 102
clpX PRK05342
ATP-dependent Clp protease ATP-binding subunit ClpX;
199-269 2.59e-03

ATP-dependent Clp protease ATP-binding subunit ClpX;


Pssm-ID: 235422 [Multi-domain]  Cd Length: 412  Bit Score: 40.91  E-value: 2.59e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489514706 199 VLLYGPPGTGKTLLARAVAGEAGVPfFTIS-----------GSDfVEMFVgvgasrVRDLF------EQAKQNspcIIFV 261
Cdd:PRK05342 111 ILLIGPTGSGKTLLAQTLARILDVP-FAIAdattlteagyvGED-VENIL------LKLLQaadydvEKAQRG---IVYI 179

                 ....*...
gi 489514706 262 DEIDAVGR 269
Cdd:PRK05342 180 DEIDKIAR 187
ABCC_Protease_Secretion cd03246
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ...
184-314 2.81e-03

ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of the protease secretion system PrtD, a 60-kDa integral membrane protein sharing 37% identity with HlyB, the ABC component of the alpha-hemolysin secretion pathway, in the C-terminal domain. They export degradative enzymes by using a type I protein secretion system and lack an N-terminal signal peptide, but contain a C-terminal secretion signal. The Type I secretion apparatus is made up of three components, an ABC transporter, a membrane fusion protein (MFP), and an outer membrane protein (OMP). For the HlyA transporter complex, HlyB (ABC transporter) and HlyD (MFP) reside in the inner membrane of E. coli. The OMP component is TolC, which is thought to interact with the MFP to form a continuous channel across the periplasm from the cytoplasm to the exterior. HlyB belongs to the family of ABC transporters, which are ubiquitous, ATP-dependent transmembrane pumps or channels. The spectrum of transport substrates ranges from inorganic ions, nutrients such as amino acids, sugars, or peptides, hydrophobic drugs, to large polypeptides, such as HlyA.


Pssm-ID: 213213 [Multi-domain]  Cd Length: 173  Bit Score: 39.51  E-value: 2.81e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489514706 184 NPSRYQALGAKIPKG--VLLYGPPGTGKTLLARAVAGEA----------GVPFFTISGSDF----------VEMFVGV-- 239
Cdd:cd03246   14 EPPVLRNVSFSIEPGesLAIIGPSGSGKSTLARLILGLLrptsgrvrldGADISQWDPNELgdhvgylpqdDELFSGSia 93
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489514706 240 -----GASRVRDLFEQAKQNSPCIIFVDEIDAvgrqrgaglgggH--DEREQTLNQLLVEMDGfgdrAGVILIAATNRPD 312
Cdd:cd03246   94 enilsGGQRQRLGLARALYGNPRILVLDEPNS------------HldVEGERALNQAIAALKA----AGATRIVIAHRPE 157

                 ..
gi 489514706 313 IL 314
Cdd:cd03246  158 TL 159
KaiC-like cd01124
Circadian Clock Protein KaiC; KaiC is a circadian clock protein, most studied in cyanobacteria. ...
191-253 3.34e-03

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


Pssm-ID: 410869 [Multi-domain]  Cd Length: 222  Bit Score: 39.55  E-value: 3.34e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 489514706 191 LGAKIPKG--VLLYGPPGTGKTL-----LARAVA-GEAGVpFFTisgsdFVEmfvgvgasRVRDLFEQAKQ 253
Cdd:cd01124   12 LGGGIPKGsvTLLTGGPGTGKTLfglqfLYAGAKnGEPGL-FFT-----FEE--------SPERLLRNAKS 68
ClpX COG1219
ATP-dependent protease Clp, ATPase subunit ClpX [Posttranslational modification, protein ...
199-269 3.49e-03

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


Pssm-ID: 440832 [Multi-domain]  Cd Length: 409  Bit Score: 40.42  E-value: 3.49e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489514706 199 VLLYGPPGTGKTLLARAVAGEAGVPfFTIS-----------GSDfVEMFVgvgasrVR-------DLfEQAKQNspcIIF 260
Cdd:COG1219  112 ILLIGPTGSGKTLLAQTLARILDVP-FAIAdattlteagyvGED-VENIL------LKllqaadyDV-EKAERG---IIY 179

                 ....*....
gi 489514706 261 VDEIDAVGR 269
Cdd:COG1219  180 IDEIDKIAR 188
DnaC COG1484
DNA replication protein DnaC [Replication, recombination and repair];
197-220 3.55e-03

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


Pssm-ID: 441093 [Multi-domain]  Cd Length: 242  Bit Score: 39.76  E-value: 3.55e-03
                         10        20
                 ....*....|....*....|....
gi 489514706 197 KGVLLYGPPGTGKTLLARAVAGEA 220
Cdd:COG1484  100 ENLILLGPPGTGKTHLAIALGHEA 123
PRK08116 PRK08116
hypothetical protein; Validated
198-219 3.82e-03

hypothetical protein; Validated


Pssm-ID: 236153 [Multi-domain]  Cd Length: 268  Bit Score: 40.00  E-value: 3.82e-03
                         10        20
                 ....*....|....*....|..
gi 489514706 198 GVLLYGPPGTGKTLLARAVAGE 219
Cdd:PRK08116 116 GLLLWGSVGTGKTYLAACIANE 137
TsaE pfam02367
Threonylcarbamoyl adenosine biosynthesis protein TsaE; This family of proteins is involved in ...
189-227 3.97e-03

Threonylcarbamoyl adenosine biosynthesis protein TsaE; This family of proteins is involved in the synthesis of threonylcarbamoyl adenosine (t(6)A).


Pssm-ID: 460540  Cd Length: 127  Bit Score: 38.18  E-value: 3.97e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 489514706  189 QALGAKIPKG--VLLYGPPGTGKTLLARAVAGEAGV------PFFTI 227
Cdd:pfam02367  12 KRLAALLKPGdvILLSGDLGAGKTTFTRGLARGLGVtgpvtsPTFTL 58
RecA-like_IQCA1 cd19506
ATPase domain of IQ and AAA domain-containing protein 1 (IQCA1); IQCA1 (also known as dynein ...
189-263 4.03e-03

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


Pssm-ID: 410914 [Multi-domain]  Cd Length: 160  Bit Score: 38.66  E-value: 4.03e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 489514706 189 QALGAKIP--KGVLLYGPPGTGKTLLARAVAGEAGVPFFTISGSDFVEMFVGVGASR--VRDLFEQAKQNSPCIIFVDE 263
Cdd:cd19506   17 QAVHEKAPlvKSLLLAGPSGVGKKMLVHAICTETGANLFNLSPSNIAGKYPGKNGLQmmLHLVLKVARQLQPSVIWIGD 95
TIGR02928 TIGR02928
orc1/cdc6 family replication initiation protein; Members of this protein family are found ...
173-265 4.06e-03

orc1/cdc6 family replication initiation protein; Members of this protein family are found exclusively in the archaea. This set of DNA binding proteins shows homology to the origin recognition complex subunit 1/cell division control protein 6 family in eukaryotes. Several members may be found in genome and interact with each other. [DNA metabolism, DNA replication, recombination, and repair]


Pssm-ID: 274354 [Multi-domain]  Cd Length: 365  Bit Score: 40.31  E-value: 4.06e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489514706  173 EELYEIKDFLQnpsryQALGAKIPKGVLLYGPPGTGKTLLARAV-------AGEAGVPFFTI---------SGSDFVEMF 236
Cdd:TIGR02928  22 EQIEELAKALR-----PILRGSRPSNVFIYGKTGTGKTAVTKYVmkeleeaAEDRDVRVVTVyvncqildtLYQVLVELA 96
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 489514706  237 ------------VGVGASRV-RDLFEQAKQNSPCIIFV-DEID 265
Cdd:TIGR02928  97 nqlrgsgeevptTGLSTSEVfRRLYKELNERGDSLIIVlDEID 139
Parvo_NS1 pfam01057
Parvovirus non-structural protein NS1; This family also contains the NS2 protein. Parvoviruses ...
199-227 6.87e-03

Parvovirus non-structural protein NS1; This family also contains the NS2 protein. Parvoviruses encode two non-structural proteins, NS1 and NS2. The mRNA for NS2 contains the coding sequence for the first 87 amino acids of NS1, then by an alternative splicing mechanism mRNA from a different reading frame, encoding the last 78 amino acids, makes up the full length of the NS2 mRNA. NS1, is the major non-structural protein. It is essential for DNA replication. It is an 83-kDa nuclear phosphoprotein. It has DNA helicase and ATPase activity.


Pssm-ID: 426020  Cd Length: 271  Bit Score: 39.21  E-value: 6.87e-03
                          10        20
                  ....*....|....*....|....*....
gi 489514706  199 VLLYGPPGTGKTLLARAVAgeAGVPFFTI 227
Cdd:pfam01057 116 VWFYGPASTGKTNLAQAIA--HAVPLYGC 142
YifB COG0606
Predicted Mg-chelatase, contains ChlI-like and ATPase domains, YifB family [Posttranslational ...
199-218 7.79e-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: 39.64  E-value: 7.79e-03
                         10        20
                 ....*....|....*....|
gi 489514706 199 VLLYGPPGTGKTLLARAVAG 218
Cdd:COG0606  214 LLMIGPPGSGKTMLARRLPG 233
RAD55 COG0467
RecA-superfamily ATPase, KaiC/GvpD/RAD55 family [Signal transduction mechanisms];
195-271 8.01e-03

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


Pssm-ID: 440235 [Multi-domain]  Cd Length: 221  Bit Score: 38.74  E-value: 8.01e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489514706 195 IPKG--VLLYGPPGTGKTLLA------RAVAGEAGVPF-FTISGSDFVEMFVGVGAS----------RVRDLFEQAKQNS 255
Cdd:COG0467   17 LPRGssTLLSGPPGTGKTTLAlqflaeGLRRGEKGLYVsFEESPEQLLRRAESLGLDleeyiesgllRIIDLSPEELGLD 96
                         90
                 ....*....|....*....
gi 489514706 256 PCIIFV---DEIDAVGRQR 271
Cdd:COG0467   97 LEELLArlrEAVEEFGAKR 115
 
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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