NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|46397258|sp|Q96TA2|]
View 

RecName: Full=ATP-dependent zinc metalloprotease YME1L1; AltName: Full=ATP-dependent metalloprotease FtsH1; AltName: Full=Meg-4; AltName: Full=Presenilin-associated metalloprotease; Short=PAMP; AltName: Full=YME1-like protein 1

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

CATH:  1.20.58.760|3.40.50.300
EC:  3.4.24.-
Gene Ontology:  GO:0016020|GO:0030163|GO:0005524|GO:0016887|GO:0004176|GO:0004222|GO:0008270
PubMed:  29097521|16966379|21925212|8355690|7900428|22498346
SCOP:  4001627|4006040
TCDB:  3.A.29

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
HflB COG0465
ATP-dependent Zn proteases [Posttranslational modification, protein turnover, chaperones];
332-767 0e+00

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


:

Pssm-ID: 440233 [Multi-domain]  Cd Length: 583  Bit Score: 703.33  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46397258 332 QMKNVTFEHVKGVEEAKQELQEVVEFLKNPQKFTILGGKLPKGILLVGPPGTGKTLLARAVAGEADVPFYYASGSEFDEM 411
Cdd:COG0465 135 DKPKVTFDDVAGVDEAKEELQEIVDFLKDPEKFTRLGAKIPKGVLLVGPPGTGKTLLAKAVAGEAGVPFFSISGSDFVEM 214

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46397258 412 FVGVGASRIRNLFREAKANAPCVIFIDELDSVGGKRIESPM--HPYSRQTINQLLAEMDGFKPNEGVIIIGATNFPEALD 489
Cdd:COG0465 215 FVGVGASRVRDLFEQAKKNAPCIIFIDEIDAVGRQRGAGLGggHDEREQTLNQLLVEMDGFEGNEGVIVIAATNRPDVLD 294

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46397258 490 NALIRPGRFDMQVTVPRPDVKGRTEILKWYLNKIKFDQSVDPEIIARGTVGFSGAELENLVNQAALKAAVDGKEMVTMKE 569
Cdd:COG0465 295 PALLRPGRFDRQVVVDLPDVKGREAILKVHARKKPLAPDVDLEVIARRTPGFSGADLANLVNEAALLAARRNKKAVTMED 374

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46397258 570 LEFSKDKILMGPERRSVEIDNKNKTITAYHESGHAIIAYYTKDAMPINKATIMPRGPTLGHVSLLPENDRWNETRAQLLA 649
Cdd:COG0465 375 FEEAIDRVIAGPERKSRVISEKEKKITAYHEAGHALVAALLPGADPVHKVTIIPRGRALGYTMQLPEEDRYLYTKEELLD 454

                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46397258 650 QMDVSMGGRVAEELIFGtdHITTGASSDFDNATKIAKRMVTKFGMSEKLGVMTYSDTG-------------KLSPETQSA 716
Cdd:COG0465 455 RIAVLLGGRAAEELVFG--EVTTGASNDLERATKIARAMVTEYGMSEKLGPVAYGESEgevflgrdigqsrNYSEETARE 532

                       410       420       430       440       450
                ....*....|....*....|....*....|....*....|....*....|.
gi 46397258 717 IEQEIRILLRDSYERAKHILKTHAKEHKNLAEALLTYETLDAKEIQIVLEG 767
Cdd:COG0465 533 IDEEVRRIIDEAYERAKEILTENRDKLDALAEALLEKETLDGEELEEILAG 583
 
Name Accession Description Interval E-value
HflB COG0465
ATP-dependent Zn proteases [Posttranslational modification, protein turnover, chaperones];
332-767 0e+00

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


Pssm-ID: 440233 [Multi-domain]  Cd Length: 583  Bit Score: 703.33  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46397258 332 QMKNVTFEHVKGVEEAKQELQEVVEFLKNPQKFTILGGKLPKGILLVGPPGTGKTLLARAVAGEADVPFYYASGSEFDEM 411
Cdd:COG0465 135 DKPKVTFDDVAGVDEAKEELQEIVDFLKDPEKFTRLGAKIPKGVLLVGPPGTGKTLLAKAVAGEAGVPFFSISGSDFVEM 214

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46397258 412 FVGVGASRIRNLFREAKANAPCVIFIDELDSVGGKRIESPM--HPYSRQTINQLLAEMDGFKPNEGVIIIGATNFPEALD 489
Cdd:COG0465 215 FVGVGASRVRDLFEQAKKNAPCIIFIDEIDAVGRQRGAGLGggHDEREQTLNQLLVEMDGFEGNEGVIVIAATNRPDVLD 294

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46397258 490 NALIRPGRFDMQVTVPRPDVKGRTEILKWYLNKIKFDQSVDPEIIARGTVGFSGAELENLVNQAALKAAVDGKEMVTMKE 569
Cdd:COG0465 295 PALLRPGRFDRQVVVDLPDVKGREAILKVHARKKPLAPDVDLEVIARRTPGFSGADLANLVNEAALLAARRNKKAVTMED 374

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46397258 570 LEFSKDKILMGPERRSVEIDNKNKTITAYHESGHAIIAYYTKDAMPINKATIMPRGPTLGHVSLLPENDRWNETRAQLLA 649
Cdd:COG0465 375 FEEAIDRVIAGPERKSRVISEKEKKITAYHEAGHALVAALLPGADPVHKVTIIPRGRALGYTMQLPEEDRYLYTKEELLD 454

                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46397258 650 QMDVSMGGRVAEELIFGtdHITTGASSDFDNATKIAKRMVTKFGMSEKLGVMTYSDTG-------------KLSPETQSA 716
Cdd:COG0465 455 RIAVLLGGRAAEELVFG--EVTTGASNDLERATKIARAMVTEYGMSEKLGPVAYGESEgevflgrdigqsrNYSEETARE 532

                       410       420       430       440       450
                ....*....|....*....|....*....|....*....|....*....|.
gi 46397258 717 IEQEIRILLRDSYERAKHILKTHAKEHKNLAEALLTYETLDAKEIQIVLEG 767
Cdd:COG0465 533 IDEEVRRIIDEAYERAKEILTENRDKLDALAEALLEKETLDGEELEEILAG 583
FtsH_fam TIGR01241
ATP-dependent metalloprotease FtsH; HflB(FtsH) is a pleiotropic protein required for correct ...
 333-766 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: 622.38  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46397258   333 MKNVTFEHVKGVEEAKQELQEVVEFLKNPQKFTILGGKLPKGILLVGPPGTGKTLLARAVAGEADVPFYYASGSEFDEMF 412
Cdd:TIGR01241  49 KPKVTFKDVAGIDEAKEELMEIVDFLKNPSKFTKLGAKIPKGVLLVGPPGTGKTLLAKAVAGEAGVPFFSISGSDFVEMF 128

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46397258   413 VGVGASRIRNLFREAKANAPCVIFIDELDSVGGKR--IESPMHPYSRQTINQLLAEMDGFKPNEGVIIIGATNFPEALDN 490
Cdd:TIGR01241 129 VGVGASRVRDLFEQAKKNAPCIIFIDEIDAVGRQRgaGLGGGNDEREQTLNQLLVEMDGFGTNTGVIVIAATNRPDVLDP 208

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46397258   491 ALIRPGRFDMQVTVPRPDVKGRTEILKWYLNKIKFDQSVDPEIIARGTVGFSGAELENLVNQAALKAAVDGKEMVTMKEL 570
Cdd:TIGR01241 209 ALLRPGRFDRQVVVDLPDIKGREEILKVHAKNKKLAPDVDLKAVARRTPGFSGADLANLLNEAALLAARKNKTEITMNDI 288

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46397258   571 EFSKDKILMGPERRSVEIDNKNKTITAYHESGHAIIAYYTKDAMPINKATIMPRGPTLGHVSLLPENDRWNETRAQLLAQ 650
Cdd:TIGR01241 289 EEAIDRVIAGPEKKSRVISEKEKKLVAYHEAGHALVGLLLKDADPVHKVTIIPRGQALGYTQFLPEEDKYLYTKSQLLAQ 368

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46397258   651 MDVSMGGRVAEELIFGtdHITTGASSDFDNATKIAKRMVTKFGMSEKLGVMTYSDTGK-------------LSPETQSAI 717
Cdd:TIGR01241 369 IAVLLGGRAAEEIIFG--EVTTGASNDIKQATNIARAMVTEWGMSDKLGPVAYGSDGGdvflgrgfakakeYSEETAREI 446

                         410       420       430       440
                  ....*....|....*....|....*....|....*....|....*....
gi 46397258   718 EQEIRILLRDSYERAKHILKTHAKEHKNLAEALLTYETLDAKEIQIVLE 766
Cdd:TIGR01241 447 DEEVKRIIEEAYKRAKQILTENRDELELLAKALLEKETITREEIKELLA 495
hflB PRK10733
ATP-dependent zinc metalloprotease FtsH;
332-773 1.20e-161

ATP-dependent zinc metalloprotease FtsH;


Pssm-ID: 182683 [Multi-domain]  Cd Length: 644  Bit Score: 483.00  E-value: 1.20e-161
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46397258  332 QMKNvTFEHVKGVEEAKQELQEVVEFLKNPQKFTILGGKLPKGILLVGPPGTGKTLLARAVAGEADVPFYYASGSEFDEM 411
Cdd:PRK10733 146 QIKT-TFADVAGCDEAKEEVAELVEYLREPSRFQKLGGKIPKGVLMVGPPGTGKTLLAKAIAGEAKVPFFTISGSDFVEM 224

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46397258  412 FVGVGASRIRNLFREAKANAPCVIFIDELDSVGGKRIES--PMHPYSRQTINQLLAEMDGFKPNEGVIIIGATNFPEALD 489
Cdd:PRK10733 225 FVGVGASRVRDMFEQAKKAAPCIIFIDEIDAVGRQRGAGlgGGHDEREQTLNQMLVEMDGFEGNEGIIVIAATNRPDVLD 304

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46397258  490 NALIRPGRFDMQVTVPRPDVKGRTEILKWYLNKIKFDQSVDPEIIARGTVGFSGAELENLVNQAALKAAVDGKEMVTMKE 569
Cdd:PRK10733 305 PALLRPGRFDRQVVVGLPDVRGREQILKVHMRRVPLAPDIDAAIIARGTPGFSGADLANLVNEAALFAARGNKRVVSMVE 384

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46397258  570 LEFSKDKILMGPERRSVEIDNKNKTITAYHESGHAIIAYYTKDAMPINKATIMPRGPTLGHVSLLPENDRWNETRAQLLA 649
Cdd:PRK10733 385 FEKAKDKIMMGAERRSMVMTEAQKESTAYHEAGHAIIGRLVPEHDPVHKVTIIPRGRALGVTFFLPEGDAISASRQKLES 464

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46397258  650 QMDVSMGGRVAEELIFGTDHITTGASSDFDNATKIAKRMVTKFGMSEKLGVMTYSD-------------TGKLSPETQSA 716
Cdd:PRK10733 465 QISTLYGGRLAEEIIYGPEHVSTGASNDIKVATNLARNMVTQWGFSEKLGPLLYAEeegevflgrsvakAKHMSDETARI 544

                        410       420       430       440       450
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 46397258  717 IEQEIRILLRDSYERAKHILKTHAKEHKNLAEALLTYETLDAKEIQIVLEGKklEVR 773
Cdd:PRK10733 545 IDQEVKALIERNYNRARQLLTDNMDILHAMKDALMKYETIDAPQIDDLMARR--DVR 599
RecA-like_FtsH cd19501
ATP-dependent zinc metalloprotease FtsH; FtsH ATPase is a processive, ATP-dependent zinc ...
 336-504 1.17e-104

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: 318.02  E-value: 1.17e-104
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46397258 336 VTFEHVKGVEEAKQELQEVVEFLKNPQKFTILGGKLPKGILLVGPPGTGKTLLARAVAGEADVPFYYASGSEFDEMFVGV 415
Cdd:cd19501   1 VTFKDVAGCEEAKEELKEVVEFLKNPEKFTKLGAKIPKGVLLVGPPGTGKTLLAKAVAGEAGVPFFSISGSDFVEMFVGV 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46397258 416 GASRIRNLFREAKANAPCVIFIDELDSVGGKR--IESPMHPYSRQTINQLLAEMDGFKPNEGVIIIGATNFPEALDNALI 493
Cdd:cd19501  81 GASRVRDLFEQAKKNAPCIVFIDEIDAVGRKRgaGLGGGHDEREQTLNQLLVEMDGFESNTGVIVIAATNRPDVLDPALL 160

                       170
                ....*....|.
gi 46397258 494 RPGRFDMQVTV 504
Cdd:cd19501 161 RPGRFDRQVYV 171
Peptidase_M41 pfam01434
Peptidase family M41;
586-764 1.38e-86

Peptidase family M41;


Pssm-ID: 460210 [Multi-domain]  Cd Length: 190  Bit Score: 271.78  E-value: 1.38e-86
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46397258   586 VEIDNKNKTITAYHESGHAIIAYYTKDAMPINKATIMPRGPTLGHVSLLPENDRWNETRAQLLAQMDVSMGGRVAEELIF 665
Cdd:pfam01434   1 RVISEEEKKIVAYHEAGHALVGLLLPGADPVHKVTIIPRGQALGYTQFLPEEDKLLYTKEQLLARIAVLLGGRAAEELIF 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46397258   666 GtdHITTGASSDFDNATKIAKRMVTKFGMSEKLGVMTYSDTG-------------KLSPETQSAIEQEIRILLRDSYERA 732
Cdd:pfam01434  81 G--EVTTGASNDLEKATKIARQMVTEFGMSDKLGPVSLEESDgnvflgrgmgkrkPYSEETADIIDEEVKRLLEEAYERA 158

                         170       180       190
                  ....*....|....*....|....*....|..
gi 46397258   733 KHILKTHAKEHKNLAEALLTYETLDAKEIQIV 764
Cdd:pfam01434 159 KEILTEHRDELEALAEALLEKETLDAEEIREL 190
AAA smart00382
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ...
 372-508 4.17e-18

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


Pssm-ID: 214640 [Multi-domain]  Cd Length: 148  Bit Score: 81.65  E-value: 4.17e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46397258    372 PKGILLVGPPGTGKTLLARAVAGEADVP---FYYASGSEFDE--------------MFVGVGASRIRNLFREAKANAPCV 434
Cdd:smart00382   2 GEVILIVGPPGSGKTTLARALARELGPPgggVIYIDGEDILEevldqllliivggkKASGSGELRLRLALALARKLKPDV 81

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 46397258    435 IFIDELDSVGGKRIESPMhpysrqTINQLLAEMDGFKPNEGVIIIGATNFPEALDNALIRPgRFDMQVTVPRPD 508
Cdd:smart00382  82 LILDEITSLLDAEQEALL------LLLEELRLLLLLKSEKNLTVILTTNDEKDLGPALLRR-RFDRRIVLLLIL 148
 
Name Accession Description Interval E-value
HflB COG0465
ATP-dependent Zn proteases [Posttranslational modification, protein turnover, chaperones];
332-767 0e+00

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


Pssm-ID: 440233 [Multi-domain]  Cd Length: 583  Bit Score: 703.33  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46397258 332 QMKNVTFEHVKGVEEAKQELQEVVEFLKNPQKFTILGGKLPKGILLVGPPGTGKTLLARAVAGEADVPFYYASGSEFDEM 411
Cdd:COG0465 135 DKPKVTFDDVAGVDEAKEELQEIVDFLKDPEKFTRLGAKIPKGVLLVGPPGTGKTLLAKAVAGEAGVPFFSISGSDFVEM 214

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46397258 412 FVGVGASRIRNLFREAKANAPCVIFIDELDSVGGKRIESPM--HPYSRQTINQLLAEMDGFKPNEGVIIIGATNFPEALD 489
Cdd:COG0465 215 FVGVGASRVRDLFEQAKKNAPCIIFIDEIDAVGRQRGAGLGggHDEREQTLNQLLVEMDGFEGNEGVIVIAATNRPDVLD 294

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46397258 490 NALIRPGRFDMQVTVPRPDVKGRTEILKWYLNKIKFDQSVDPEIIARGTVGFSGAELENLVNQAALKAAVDGKEMVTMKE 569
Cdd:COG0465 295 PALLRPGRFDRQVVVDLPDVKGREAILKVHARKKPLAPDVDLEVIARRTPGFSGADLANLVNEAALLAARRNKKAVTMED 374

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46397258 570 LEFSKDKILMGPERRSVEIDNKNKTITAYHESGHAIIAYYTKDAMPINKATIMPRGPTLGHVSLLPENDRWNETRAQLLA 649
Cdd:COG0465 375 FEEAIDRVIAGPERKSRVISEKEKKITAYHEAGHALVAALLPGADPVHKVTIIPRGRALGYTMQLPEEDRYLYTKEELLD 454

                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46397258 650 QMDVSMGGRVAEELIFGtdHITTGASSDFDNATKIAKRMVTKFGMSEKLGVMTYSDTG-------------KLSPETQSA 716
Cdd:COG0465 455 RIAVLLGGRAAEELVFG--EVTTGASNDLERATKIARAMVTEYGMSEKLGPVAYGESEgevflgrdigqsrNYSEETARE 532

                       410       420       430       440       450
                ....*....|....*....|....*....|....*....|....*....|.
gi 46397258 717 IEQEIRILLRDSYERAKHILKTHAKEHKNLAEALLTYETLDAKEIQIVLEG 767
Cdd:COG0465 533 IDEEVRRIIDEAYERAKEILTENRDKLDALAEALLEKETLDGEELEEILAG 583
FtsH_fam TIGR01241
ATP-dependent metalloprotease FtsH; HflB(FtsH) is a pleiotropic protein required for correct ...
 333-766 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: 622.38  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46397258   333 MKNVTFEHVKGVEEAKQELQEVVEFLKNPQKFTILGGKLPKGILLVGPPGTGKTLLARAVAGEADVPFYYASGSEFDEMF 412
Cdd:TIGR01241  49 KPKVTFKDVAGIDEAKEELMEIVDFLKNPSKFTKLGAKIPKGVLLVGPPGTGKTLLAKAVAGEAGVPFFSISGSDFVEMF 128

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46397258   413 VGVGASRIRNLFREAKANAPCVIFIDELDSVGGKR--IESPMHPYSRQTINQLLAEMDGFKPNEGVIIIGATNFPEALDN 490
Cdd:TIGR01241 129 VGVGASRVRDLFEQAKKNAPCIIFIDEIDAVGRQRgaGLGGGNDEREQTLNQLLVEMDGFGTNTGVIVIAATNRPDVLDP 208

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46397258   491 ALIRPGRFDMQVTVPRPDVKGRTEILKWYLNKIKFDQSVDPEIIARGTVGFSGAELENLVNQAALKAAVDGKEMVTMKEL 570
Cdd:TIGR01241 209 ALLRPGRFDRQVVVDLPDIKGREEILKVHAKNKKLAPDVDLKAVARRTPGFSGADLANLLNEAALLAARKNKTEITMNDI 288

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46397258   571 EFSKDKILMGPERRSVEIDNKNKTITAYHESGHAIIAYYTKDAMPINKATIMPRGPTLGHVSLLPENDRWNETRAQLLAQ 650
Cdd:TIGR01241 289 EEAIDRVIAGPEKKSRVISEKEKKLVAYHEAGHALVGLLLKDADPVHKVTIIPRGQALGYTQFLPEEDKYLYTKSQLLAQ 368

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46397258   651 MDVSMGGRVAEELIFGtdHITTGASSDFDNATKIAKRMVTKFGMSEKLGVMTYSDTGK-------------LSPETQSAI 717
Cdd:TIGR01241 369 IAVLLGGRAAEEIIFG--EVTTGASNDIKQATNIARAMVTEWGMSDKLGPVAYGSDGGdvflgrgfakakeYSEETAREI 446

                         410       420       430       440
                  ....*....|....*....|....*....|....*....|....*....
gi 46397258   718 EQEIRILLRDSYERAKHILKTHAKEHKNLAEALLTYETLDAKEIQIVLE 766
Cdd:TIGR01241 447 DEEVKRIIEEAYKRAKQILTENRDELELLAKALLEKETITREEIKELLA 495
hflB PRK10733
ATP-dependent zinc metalloprotease FtsH;
332-773 1.20e-161

ATP-dependent zinc metalloprotease FtsH;


Pssm-ID: 182683 [Multi-domain]  Cd Length: 644  Bit Score: 483.00  E-value: 1.20e-161
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46397258  332 QMKNvTFEHVKGVEEAKQELQEVVEFLKNPQKFTILGGKLPKGILLVGPPGTGKTLLARAVAGEADVPFYYASGSEFDEM 411
Cdd:PRK10733 146 QIKT-TFADVAGCDEAKEEVAELVEYLREPSRFQKLGGKIPKGVLMVGPPGTGKTLLAKAIAGEAKVPFFTISGSDFVEM 224

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46397258  412 FVGVGASRIRNLFREAKANAPCVIFIDELDSVGGKRIES--PMHPYSRQTINQLLAEMDGFKPNEGVIIIGATNFPEALD 489
Cdd:PRK10733 225 FVGVGASRVRDMFEQAKKAAPCIIFIDEIDAVGRQRGAGlgGGHDEREQTLNQMLVEMDGFEGNEGIIVIAATNRPDVLD 304

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46397258  490 NALIRPGRFDMQVTVPRPDVKGRTEILKWYLNKIKFDQSVDPEIIARGTVGFSGAELENLVNQAALKAAVDGKEMVTMKE 569
Cdd:PRK10733 305 PALLRPGRFDRQVVVGLPDVRGREQILKVHMRRVPLAPDIDAAIIARGTPGFSGADLANLVNEAALFAARGNKRVVSMVE 384

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46397258  570 LEFSKDKILMGPERRSVEIDNKNKTITAYHESGHAIIAYYTKDAMPINKATIMPRGPTLGHVSLLPENDRWNETRAQLLA 649
Cdd:PRK10733 385 FEKAKDKIMMGAERRSMVMTEAQKESTAYHEAGHAIIGRLVPEHDPVHKVTIIPRGRALGVTFFLPEGDAISASRQKLES 464

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46397258  650 QMDVSMGGRVAEELIFGTDHITTGASSDFDNATKIAKRMVTKFGMSEKLGVMTYSD-------------TGKLSPETQSA 716
Cdd:PRK10733 465 QISTLYGGRLAEEIIYGPEHVSTGASNDIKVATNLARNMVTQWGFSEKLGPLLYAEeegevflgrsvakAKHMSDETARI 544

                        410       420       430       440       450
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 46397258  717 IEQEIRILLRDSYERAKHILKTHAKEHKNLAEALLTYETLDAKEIQIVLEGKklEVR 773
Cdd:PRK10733 545 IDQEVKALIERNYNRARQLLTDNMDILHAMKDALMKYETIDAPQIDDLMARR--DVR 599
ftsH CHL00176
cell division protein; Validated
 334-766 2.49e-161

cell division protein; Validated


Pssm-ID: 214386 [Multi-domain]  Cd Length: 638  Bit Score: 481.86  E-value: 2.49e-161
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46397258  334 KNVTFEHVKGVEEAKQELQEVVEFLKNPQKFTILGGKLPKGILLVGPPGTGKTLLARAVAGEADVPFYYASGSEFDEMFV 413
Cdd:CHL00176 178 TGITFRDIAGIEEAKEEFEEVVSFLKKPERFTAVGAKIPKGVLLVGPPGTGKTLLAKAIAGEAEVPFFSISGSEFVEMFV 257

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46397258  414 GVGASRIRNLFREAKANAPCVIFIDELDSVG---GKRIESPMHPySRQTINQLLAEMDGFKPNEGVIIIGATNFPEALDN 490
Cdd:CHL00176 258 GVGAARVRDLFKKAKENSPCIVFIDEIDAVGrqrGAGIGGGNDE-REQTLNQLLTEMDGFKGNKGVIVIAATNRVDILDA 336

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46397258  491 ALIRPGRFDMQVTVPRPDVKGRTEILKWYLNKIKFDQSVDPEIIARGTVGFSGAELENLVNQAALKAAVDGKEMVTMKEL 570
Cdd:CHL00176 337 ALLRPGRFDRQITVSLPDREGRLDILKVHARNKKLSPDVSLELIARRTPGFSGADLANLLNEAAILTARRKKATITMKEI 416

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46397258  571 EFSKDKILMGPERRSVEiDNKNKTITAYHESGHAIIAYYTKDAMPINKATIMPRGPTLGHVSLLPENDRWNETRAQLLAQ 650
Cdd:CHL00176 417 DTAIDRVIAGLEGTPLE-DSKNKRLIAYHEVGHAIVGTLLPNHDPVQKVTLIPRGQAKGLTWFTPEEDQSLVSRSQILAR 495

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46397258  651 MDVSMGGRVAEELIFGTDHITTGASSDFDNATKIAKRMVTKFGMSeKLGVMTYSDTG--------------KLSPETQSA 716
Cdd:CHL00176 496 IVGALGGRAAEEVVFGSTEVTTGASNDLQQVTNLARQMVTRFGMS-SIGPISLESNNstdpflgrfmqrnsEYSEEIADK 574

                        410       420       430       440       450
                 ....*....|....*....|....*....|....*....|....*....|
gi 46397258  717 IEQEIRILLRDSYERAKHILKTHAKEHKNLAEALLTYETLDAKEIQIVLE 766
Cdd:CHL00176 575 IDMEVRSILHTCYQYAYQILKDNRVLIDLLVELLLQKETIDGDEFREIVN 624
RPT1 COG1222
ATP-dependent 26S proteasome regulatory subunit [Posttranslational modification, protein ...
 335-583 4.85e-106

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


Pssm-ID: 440835 [Multi-domain]  Cd Length: 326  Bit Score: 327.73  E-value: 4.85e-106
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46397258 335 NVTFEHVKGVEEAKQELQEVVE-FLKNPQKFTILGGKLPKGILLVGPPGTGKTLLARAVAGEADVPFYYASGSEFDEMFV 413
Cdd:COG1222  74 DVTFDDIGGLDEQIEEIREAVElPLKNPELFRKYGIEPPKGVLLYGPPGTGKTLLAKAVAGELGAPFIRVRGSELVSKYI 153

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46397258 414 GVGASRIRNLFREAKANAPCVIFIDELDSVGGKRIESPMHPYSRQTINQLLAEMDGFKPNEGVIIIGATNFPEALDNALI 493
Cdd:COG1222 154 GEGARNVREVFELAREKAPSIIFIDEIDAIAARRTDDGTSGEVQRTVNQLLAELDGFESRGDVLIIAATNRPDLLDPALL 233

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46397258 494 RPGRFDMQVTVPRPDVKGRTEILKWYLNKIKFDQSVDPEIIARGTVGFSGAELENLVNQAALKAAVDGKEMVTMKELEFS 573
Cdd:COG1222 234 RPGRFDRVIEVPLPDEEAREEILKIHLRDMPLADDVDLDKLAKLTEGFSGADLKAIVTEAGMFAIREGRDTVTMEDLEKA 313

                       250
                ....*....|
gi 46397258 574 KDKILMGPER 583
Cdd:COG1222 314 IEKVKKKTET 323
RecA-like_FtsH cd19501
ATP-dependent zinc metalloprotease FtsH; FtsH ATPase is a processive, ATP-dependent zinc ...
 336-504 1.17e-104

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: 318.02  E-value: 1.17e-104
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46397258 336 VTFEHVKGVEEAKQELQEVVEFLKNPQKFTILGGKLPKGILLVGPPGTGKTLLARAVAGEADVPFYYASGSEFDEMFVGV 415
Cdd:cd19501   1 VTFKDVAGCEEAKEELKEVVEFLKNPEKFTKLGAKIPKGVLLVGPPGTGKTLLAKAVAGEAGVPFFSISGSDFVEMFVGV 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46397258 416 GASRIRNLFREAKANAPCVIFIDELDSVGGKR--IESPMHPYSRQTINQLLAEMDGFKPNEGVIIIGATNFPEALDNALI 493
Cdd:cd19501  81 GASRVRDLFEQAKKNAPCIVFIDEIDAVGRKRgaGLGGGHDEREQTLNQLLVEMDGFESNTGVIVIAATNRPDVLDPALL 160

                       170
                ....*....|.
gi 46397258 494 RPGRFDMQVTV 504
Cdd:cd19501 161 RPGRFDRQVYV 171
Peptidase_M41 pfam01434
Peptidase family M41;
586-764 1.38e-86

Peptidase family M41;


Pssm-ID: 460210 [Multi-domain]  Cd Length: 190  Bit Score: 271.78  E-value: 1.38e-86
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46397258   586 VEIDNKNKTITAYHESGHAIIAYYTKDAMPINKATIMPRGPTLGHVSLLPENDRWNETRAQLLAQMDVSMGGRVAEELIF 665
Cdd:pfam01434   1 RVISEEEKKIVAYHEAGHALVGLLLPGADPVHKVTIIPRGQALGYTQFLPEEDKLLYTKEQLLARIAVLLGGRAAEELIF 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46397258   666 GtdHITTGASSDFDNATKIAKRMVTKFGMSEKLGVMTYSDTG-------------KLSPETQSAIEQEIRILLRDSYERA 732
Cdd:pfam01434  81 G--EVTTGASNDLEKATKIARQMVTEFGMSDKLGPVSLEESDgnvflgrgmgkrkPYSEETADIIDEEVKRLLEEAYERA 158

                         170       180       190
                  ....*....|....*....|....*....|..
gi 46397258   733 KHILKTHAKEHKNLAEALLTYETLDAKEIQIV 764
Cdd:pfam01434 159 KEILTEHRDELEALAEALLEKETLDAEEIREL 190
PRK03992 PRK03992
proteasome-activating nucleotidase; Provisional
 335-587 1.11e-81

proteasome-activating nucleotidase; Provisional


Pssm-ID: 179699 [Multi-domain]  Cd Length: 389  Bit Score: 265.93  E-value: 1.11e-81
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46397258  335 NVTFEHVKGVEEAKQELQEVVEF-LKNPQKFTILGGKLPKGILLVGPPGTGKTLLARAVAGEADVPFYYASGSEFDEMFV 413
Cdd:PRK03992 127 NVTYEDIGGLEEQIREVREAVELpLKKPELFEEVGIEPPKGVLLYGPPGTGKTLLAKAVAHETNATFIRVVGSELVQKFI 206

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46397258  414 GVGASRIRNLFREAKANAPCVIFIDELDSVGGKRIESpMHPYSRQ---TINQLLAEMDGFKPNEGVIIIGATNFPEALDN 490
Cdd:PRK03992 207 GEGARLVRELFELAREKAPSIIFIDEIDAIAAKRTDS-GTSGDREvqrTLMQLLAEMDGFDPRGNVKIIAATNRIDILDP 285

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46397258  491 ALIRPGRFDMQVTVPRPDVKGRTEILKWYLNKIKFDQSVDPEIIARGTVGFSGAELENLVNQAALKAAVDGKEMVTMKEL 570
Cdd:PRK03992 286 AILRPGRFDRIIEVPLPDEEGRLEILKIHTRKMNLADDVDLEELAELTEGASGADLKAICTEAGMFAIRDDRTEVTMEDF 365

                        250
                 ....*....|....*..
gi 46397258  571 EFSKDKILMGPERRSVE 587
Cdd:PRK03992 366 LKAIEKVMGKEEKDSME 382
SpoVK COG0464
AAA+-type ATPase, SpoVK/Ycf46/Vps4 family [Cell wall/membrane/envelope biogenesis, Cell cycle ...
 338-571 4.65e-76

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


Pssm-ID: 440232 [Multi-domain]  Cd Length: 397  Bit Score: 251.37  E-value: 4.65e-76
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46397258 338 FEHVKGVEEAKQELQEVVE-FLKNPQKFTILGGKLPKGILLVGPPGTGKTLLARAVAGEADVPFYYASGSEFDEMFVGVG 416
Cdd:COG0464 156 LDDLGGLEEVKEELRELVAlPLKRPELREEYGLPPPRGLLLYGPPGTGKTLLARALAGELGLPLIEVDLSDLVSKYVGET 235

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46397258 417 ASRIRNLFREAKANAPCVIFIDELDSVGGKRiESPMHPYSRQTINQLLAEMDGFkpNEGVIIIGATNFPEALDNALIRpg 496
Cdd:COG0464 236 EKNLREVFDKARGLAPCVLFIDEADALAGKR-GEVGDGVGRRVVNTLLTEMEEL--RSDVVVIAATNRPDLLDPALLR-- 310

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 46397258 497 RFDMQVTVPRPDVKGRTEILKWYLNKIKFDQSVDPEIIARGTVGFSGAELENLVNQAALKAAVDGKEMVTMKELE 571
Cdd:COG0464 311 RFDEIIFFPLPDAEERLEIFRIHLRKRPLDEDVDLEELAEATEGLSGADIRNVVRRAALQALRLGREPVTTEDLL 385
26Sp45 TIGR01242
26S proteasome subunit P45 family; Many proteins may score above the trusted cutoff because an ...
 335-578 1.36e-72

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: 241.24  E-value: 1.36e-72
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46397258   335 NVTFEHVKGVEEAKQELQEVVEF-LKNPQKFTILGGKLPKGILLVGPPGTGKTLLARAVAGEADVPFYYASGSEFDEMFV 413
Cdd:TIGR01242 118 NVSYEDIGGLEEQIREIREAVELpLKHPELFEEVGIEPPKGVLLYGPPGTGKTLLAKAVAHETNATFIRVVGSELVRKYI 197

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46397258   414 GVGASRIRNLFREAKANAPCVIFIDELDSVGGKRIESPM--HPYSRQTINQLLAEMDGFKPNEGVIIIGATNFPEALDNA 491
Cdd:TIGR01242 198 GEGARLVREIFELAKEKAPSIIFIDEIDAIAAKRTDSGTsgDREVQRTLMQLLAELDGFDPRGNVKVIAATNRPDILDPA 277

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46397258   492 LIRPGRFDMQVTVPRPDVKGRTEILKWYLNKIKFDQSVDPEIIARGTVGFSGAELENLVNQAALKAAVDGKEMVTMKELE 571
Cdd:TIGR01242 278 LLRPGRFDRIIEVPLPDFEGRLEILKIHTRKMKLAEDVDLEAIAKMTEGASGADLKAICTEAGMFAIREERDYVTMDDFI 357


                  ....*..
gi 46397258   572 FSKDKIL 578
Cdd:TIGR01242 358 KAVEKVL 364
COG1223 COG1223
Predicted ATPase, AAA+ superfamily [General function prediction only];
338-583 1.18e-64

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


Pssm-ID: 440836 [Multi-domain]  Cd Length: 246  Bit Score: 215.52  E-value: 1.18e-64
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46397258 338 FEHVKGVEEAKQELQEVVEFLK---NPQKFtilGGKLPKGILLVGPPGTGKTLLARAVAGEADVPFYYASGSEFDEMFVG 414
Cdd:COG1223   1 LDDVVGQEEAKKKLKLIIKELRrreNLRKF---GLWPPRKILFYGPPGTGKTMLAEALAGELKLPLLTVRLDSLIGSYLG 77

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46397258 415 VGASRIRNLFREAKaNAPCVIFIDELDSVGGKRIESPMHPYSRQTINQLLAEMDGFkpNEGVIIIGATNFPEALDNALIR 494
Cdd:COG1223  78 ETARNLRKLFDFAR-RAPCVIFFDEFDAIAKDRGDQNDVGEVKRVVNALLQELDGL--PSGSVVIAATNHPELLDSALWR 154

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46397258 495 pgRFDMQVTVPRPDVKGRTEILKWYLNKIKFDQSVDPEIIARGTVGFSGAELENLVNQAALKAAVDGKEMVTMKELE--- 571
Cdd:COG1223 155 --RFDEVIEFPLPDKEERKEILELNLKKFPLPFELDLKKLAKKLEGLSGADIEKVLKTALKKAILEDREKVTKEDLEeal 232

                       250
                ....*....|....
gi 46397258 572 --FSKDKILMGPER 583
Cdd:COG1223 233 kqRKERKKEPKKEG 246
CDC48 TIGR01243
AAA family ATPase, CDC48 subfamily; This subfamily of the AAA family ATPases includes two ...
 331-578 1.70e-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: 1.70e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46397258   331 VQMKNVTFEHVKGVEEAKQELQEVVEF-LKNPQKFTILGGKLPKGILLVGPPGTGKTLLARAVAGEADVPFYYASGSEFD 409
Cdd:TIGR01243 445 VEVPNVRWSDIGGLEEVKQELREAVEWpLKHPEIFEKMGIRPPKGVLLFGPPGTGKTLLAKAVATESGANFIAVRGPEIL 524

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46397258   410 EMFVGVGASRIRNLFREAKANAPCVIFIDELDSVGGKRIESPMHPYSRQTINQLLAEMDGFKPNEGVIIIGATNFPEALD 489
Cdd:TIGR01243 525 SKWVGESEKAIREIFRKARQAAPAIIFFDEIDAIAPARGARFDTSVTDRIVNQLLTEMDGIQELSNVVVIAATNRPDILD 604

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46397258   490 NALIRPGRFDMQVTVPRPDVKGRTEILKWYLNKIKFDQSVDPEIIARGTVGFSGAELENLVNQAALKAAVDGKEMVTMKE 569
Cdd:TIGR01243 605 PALLRPGRFDRLILVPPPDEEARKEIFKIHTRSMPLAEDVDLEELAEMTEGYTGADIEAVCREAAMAALRESIGSPAKEK 684


                  ....*....
gi 46397258   570 LEFSKDKIL 578
Cdd:TIGR01243 685 LEVGEEEFL 693
RecA-like_protease cd19481
proteases similar to RecA; RecA-like NTPases. This family includes the NTP binding domain of ...
 347-504 2.11e-61

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


Pssm-ID: 410889 [Multi-domain]  Cd Length: 158  Bit Score: 203.67  E-value: 2.11e-61
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46397258 347 AKQELQEVVEFLKNPQKFTILGGKLPKGILLVGPPGTGKTLLARAVAGEADVPFYYASGSEFDEMFVGVGASRIRNLFRE 426
Cdd:cd19481   1 LKASLREAVEAPRRGSRLRRYGLGLPKGILLYGPPGTGKTLLAKALAGELGLPLIVVKLSSLLSKYVGESEKNLRKIFER 80

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 46397258 427 AKANAPCVIFIDELDSVGGKRIESPMHPYSRQTINQLLAEMDGFKPNEGVIIIGATNFPEALDNALIRPGRFDMQVTV 504
Cdd:cd19481  81 ARRLAPCILFIDEIDAIGRKRDSSGESGELRRVLNQLLTELDGVNSRSKVLVIAATNRPDLLDPALLRPGRFDEVIEF 158
RecA-like_PAN_like cd19502
proteasome activating nucleotidase PAN and related proteasome subunits; This subfamily ...
 337-504 1.47e-57

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


Pssm-ID: 410910 [Multi-domain]  Cd Length: 171  Bit Score: 193.71  E-value: 1.47e-57
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46397258 337 TFEHVKGVEEAKQELQEVVEF-LKNPQKFTILGGKLPKGILLVGPPGTGKTLLARAVAGEADVPFYYASGSEFDEMFVGV 415
Cdd:cd19502   1 TYEDIGGLDEQIREIREVVELpLKHPELFEELGIEPPKGVLLYGPPGTGKTLLAKAVANHTDATFIRVVGSELVQKYIGE 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46397258 416 GASRIRNLFREAKANAPCVIFIDELDSVGGKRIESPMHPYS--RQTINQLLAEMDGFKPNEGVIIIGATNFPEALDNALI 493
Cdd:cd19502  81 GARLVRELFEMAREKAPSIIFIDEIDAIGAKRFDSGTGGDRevQRTMLELLNQLDGFDPRGNIKVIMATNRPDILDPALL 160

                       170
                ....*....|.
gi 46397258 494 RPGRFDMQVTV 504
Cdd:cd19502 161 RPGRFDRKIEF 171
CDC48 TIGR01243
AAA family ATPase, CDC48 subfamily; This subfamily of the AAA family ATPases includes two ...
 336-557 3.36e-57

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


Pssm-ID: 273521 [Multi-domain]  Cd Length: 733  Bit Score: 208.22  E-value: 3.36e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46397258   336 VTFEHVKGVEEAKQELQEVVEF-LKNPQKFTILGGKLPKGILLVGPPGTGKTLLARAVAGEADVPFYYASGSEFDEMFVG 414
Cdd:TIGR01243 175 VTYEDIGGLKEAKEKIREMVELpMKHPELFEHLGIEPPKGVLLYGPPGTGKTLLAKAVANEAGAYFISINGPEIMSKYYG 254

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46397258   415 VGASRIRNLFREAKANAPCVIFIDELDSVGGKRiESPMHPYSRQTINQLLAEMDGFKPNEGVIIIGATNFPEALDNALIR 494
Cdd:TIGR01243 255 ESEERLREIFKEAEENAPSIIFIDEIDAIAPKR-EEVTGEVEKRVVAQLLTLMDGLKGRGRVIVIGATNRPDALDPALRR 333

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 46397258   495 PGRFDMQVTVPRPDVKGRTEILKWYLNKIKFDQSVDPEIIARGTVGFSGAELENLVNQAALKA 557
Cdd:TIGR01243 334 PGRFDREIVIRVPDKRARKEILKVHTRNMPLAEDVDLDKLAEVTHGFVGADLAALAKEAAMAA 396
RecA-like_CDC48_r2-like cd19511
second of two ATPase domains of CDC48/p97, PEX1 and -6, VAT and NVL, and similar ATPase ...
 347-499 3.05e-54

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: 184.02  E-value: 3.05e-54
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46397258 347 AKQELQEVVEF-LKNPQKFTILGGKLPKGILLVGPPGTGKTLLARAVAGEADVPFYYASGSEFDEMFVGVGASRIRNLFR 425
Cdd:cd19511   1 VKRELKEAVEWpLKHPDAFKRLGIRPPKGVLLYGPPGCGKTLLAKALASEAGLNFISVKGPELFSKYVGESERAVREIFQ 80

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 46397258 426 EAKANAPCVIFIDELDSVGGKRIESPMHPYSRQTINQLLAEMDGFKPNEGVIIIGATNFPEALDNALIRPGRFD 499
Cdd:cd19511  81 KARQAAPCIIFFDEIDSLAPRRGQSDSSGVTDRVVSQLLTELDGIESLKGVVVIAATNRPDMIDPALLRPGRLD 154
RecA-like_CDC48_NLV2_r1-like cd19503
first of two ATPase domains of CDC48 and NLV2, and similar ATPase domains; CDC48 in yeast and ...
 341-502 2.90e-53

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: 181.72  E-value: 2.90e-53
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46397258 341 VKGVEEAKQELQEVVEF-LKNPQKFTILGGKLPKGILLVGPPGTGKTLLARAVAGEADVPFYYASGSEFDEMFVGVGASR 419
Cdd:cd19503   2 IGGLDEQIASLKELIELpLKYPELFRALGLKPPRGVLLHGPPGTGKTLLARAVANEAGANFLSISGPSIVSKYLGESEKN 81

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46397258 420 IRNLFREAKANAPCVIFIDELDSVGGKRiESPMHPYSRQTINQLLAEMDGFKPNEGVIIIGATNFPEALDNALIRPGRFD 499
Cdd:cd19503  82 LREIFEEARSHAPSIIFIDEIDALAPKR-EEDQREVERRVVAQLLTLMDGMSSRGKVVVIAATNRPDAIDPALRRPGRFD 160


                ...
gi 46397258 500 MQV 502
Cdd:cd19503 161 REV 163
RecA-like_VCP_r2 cd19529
second of two ATPase domains of Valosin-containing protein-like ATPase (VAT) and similar ...
 347-504 2.95e-51

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


Pssm-ID: 410937 [Multi-domain]  Cd Length: 159  Bit Score: 176.15  E-value: 2.95e-51
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46397258 347 AKQELQEVVEF-LKNPQKFTILGGKLPKGILLVGPPGTGKTLLARAVAGEADVPFYYASGSEFDEMFVGVGASRIRNLFR 425
Cdd:cd19529   1 VKQELKEAVEWpLLKPEVFKRLGIRPPKGILLYGPPGTGKTLLAKAVATESNANFISVKGPELLSKWVGESEKAIREIFR 80

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 46397258 426 EAKANAPCVIFIDELDSVGGKRIESPMHPYSRQTINQLLAEMDGFKPNEGVIIIGATNFPEALDNALIRPGRFDMQVTV 504
Cdd:cd19529  81 KARQVAPCVIFFDEIDSIAPRRGTTGDSGVTERVVNQLLTELDGLEEMNGVVVIAATNRPDIIDPALLRAGRFDRLIYI 159
AAA pfam00004
ATPase family associated with various cellular activities (AAA); AAA family proteins often ...
 375-506 3.75e-51

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


Pssm-ID: 459627 [Multi-domain]  Cd Length: 130  Bit Score: 174.70  E-value: 3.75e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46397258   375 ILLVGPPGTGKTLLARAVAGEADVPFYYASGSEFDEMFVGVGASRIRNLFREAKANAPCVIFIDELDSVGGKRiESPMHP 454
Cdd:pfam00004   1 LLLYGPPGTGKTTLAKAVAKELGAPFIEISGSELVSKYVGESEKRLRELFEAAKKLAPCVIFIDEIDALAGSR-GSGGDS 79

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 46397258   455 YSRQTINQLLAEMDGFKPNEG-VIIIGATNFPEALDNALIrpGRFDMQVTVPR 506
Cdd:pfam00004  80 ESRRVVNQLLTELDGFTSSNSkVIVIAATNRPDKLDPALL--GRFDRIIEFPL 130
RecA-like_CDC48_r1-like cd19519
first of two ATPase domains of CDC48 and similar ATPase domains; CDC48 in yeast and p97 or VCP ...
 341-505 8.19e-49

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


Pssm-ID: 410927 [Multi-domain]  Cd Length: 166  Bit Score: 169.54  E-value: 8.19e-49
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46397258 341 VKGVEEAKQELQEVVEF-LKNPQKFTILGGKLPKGILLVGPPGTGKTLLARAVAGEADVPFYYASGSEFDEMFVGVGASR 419
Cdd:cd19519   2 IGGCRKQLAQIREMVELpLRHPELFKAIGIKPPRGILLYGPPGTGKTLIARAVANETGAFFFLINGPEIMSKLAGESESN 81

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46397258 420 IRNLFREAKANAPCVIFIDELDSVGGKRiESPMHPYSRQTINQLLAEMDGFKPNEGVIIIGATNFPEALDNALIRPGRFD 499
Cdd:cd19519  82 LRKAFEEAEKNAPAIIFIDEIDAIAPKR-EKTHGEVERRIVSQLLTLMDGLKQRAHVIVMAATNRPNSIDPALRRFGRFD 160


                ....*.
gi 46397258 500 MQVTVP 505
Cdd:cd19519 161 REIDIG 166
PTZ00361 PTZ00361
26 proteosome regulatory subunit 4-like protein; Provisional
 324-578 3.95e-48

26 proteosome regulatory subunit 4-like protein; Provisional


Pssm-ID: 185575 [Multi-domain]  Cd Length: 438  Bit Score: 176.50  E-value: 3.95e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46397258  324 LDSAVDP-VQMKNV------TFEHVKGVEEAKQELQEVVEF-LKNPQKFTILGGKLPKGILLVGPPGTGKTLLARAVAGE 395
Cdd:PTZ00361 161 LLDEVDPlVSVMKVdkapleSYADIGGLEQQIQEIKEAVELpLTHPELYDDIGIKPPKGVILYGPPGTGKTLLAKAVANE 240

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46397258  396 ADVPFYYASGSEFDEMFVGVGASRIRNLFREAKANAPCVIFIDELDSVGGKRIE--SPMHPYSRQTINQLLAEMDGFKPN 473
Cdd:PTZ00361 241 TSATFLRVVGSELIQKYLGDGPKLVRELFRVAEENAPSIVFIDEIDAIGTKRYDatSGGEKEIQRTMLELLNQLDGFDSR 320

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46397258  474 EGVIIIGATNFPEALDNALIRPGRFDMQVTVPRPDVKGRTEILKWYLNKIKFDQSVDPEIIARGTVGFSGAELENLVNQA 553
Cdd:PTZ00361 321 GDVKVIMATNRIESLDPALIRPGRIDRKIEFPNPDEKTKRRIFEIHTSKMTLAEDVDLEEFIMAKDELSGADIKAICTEA 400

                        250       260
                 ....*....|....*....|....*
gi 46397258  554 ALKAAVDGKEMVTMKELEFSKDKIL 578
Cdd:PTZ00361 401 GLLALRERRMKVTQADFRKAKEKVL 425
RecA-like_NVL_r1-like cd19518
first of two ATPase domains of NVL (nuclear VCP-like protein) and similar ATPase domains; NVL ...
 340-502 1.13e-45

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: 161.03  E-value: 1.13e-45
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46397258 340 HVKGVEEAKQELQEVVEFLK-NPQKFTILGGKLPKGILLVGPPGTGKTLLARAVAGEADVPFYYASGSEFDEMFVGVGAS 418
Cdd:cd19518   1 DIGGMDSTLKELCELLIHPIlPPEYFQHLGVEPPRGVLLHGPPGCGKTMLANAIAGELKVPFLKISATEIVSGVSGESEE 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46397258 419 RIRNLFREAKANAPCVIFIDELDSVGGKRiESPMHPYSRQTINQLLAEMDGFKPNE----GVIIIGATNFPEALDNALIR 494
Cdd:cd19518  81 KIRELFDQAISNAPCIVFIDEIDAITPKR-ESAQREMERRIVSQLLTCMDELNNEKtaggPVLVIGATNRPDSLDPALRR 159


                ....*...
gi 46397258 495 PGRFDMQV 502
Cdd:cd19518 160 AGRFDREI 167
RecA-like_CDC48_r2-like cd19528
second of two ATPase domains of CDC48 and similar ATPase domains; CDC48 in yeast and p97 or ...
 348-504 5.76e-45

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: 158.83  E-value: 5.76e-45
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46397258 348 KQELQEVVEF-LKNPQKFTILGGKLPKGILLVGPPGTGKTLLARAVAGEADVPFYYASGSEFDEMFVGVGASRIRNLFRE 426
Cdd:cd19528   2 KRELQELVQYpVEHPDKFLKFGMTPSKGVLFYGPPGCGKTLLAKAIANECQANFISVKGPELLTMWFGESEANVRDIFDK 81

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46397258 427 AKANAPCVIFIDELDSVGGKRIESPMHP--YSRQTINQLLAEMDGFKPNEGVIIIGATNFPEALDNALIRPGRFDMQVTV 504
Cdd:cd19528  82 ARAAAPCVLFFDELDSIAKARGGNIGDAggAADRVINQILTEMDGMNTKKNVFIIGATNRPDIIDPAILRPGRLDQLIYI 161
PTZ00454 PTZ00454
26S protease regulatory subunit 6B-like protein; Provisional
 325-571 1.83e-44

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


Pssm-ID: 240423 [Multi-domain]  Cd Length: 398  Bit Score: 164.94  E-value: 1.83e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46397258  325 DSAVDPVQMK---NVTFEHVKGVEEAKQELQEVVEF-LKNPQKFTILGGKLPKGILLVGPPGTGKTLLARAVAGEADVPF 400
Cdd:PTZ00454 128 DSSIQLLQMSekpDVTYSDIGGLDIQKQEIREAVELpLTCPELYEQIGIDPPRGVLLYGPPGTGKTMLAKAVAHHTTATF 207

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46397258  401 YYASGSEFDEMFVGVGASRIRNLFREAKANAPCVIFIDELDSVGGKRIESpmhpysrQT---------INQLLAEMDGFK 471
Cdd:PTZ00454 208 IRVVGSEFVQKYLGEGPRMVRDVFRLARENAPSIIFIDEVDSIATKRFDA-------QTgadrevqriLLELLNQMDGFD 280

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46397258  472 PNEGVIIIGATNFPEALDNALIRPGRFDMQVTVPRPDVKGRTEILKWYLNKIKFDQSVDPEIIARGTVGFSGAELENLVN 551
Cdd:PTZ00454 281 QTTNVKVIMATNRADTLDPALLRPGRLDRKIEFPLPDRRQKRLIFQTITSKMNLSEEVDLEDFVSRPEKISAADIAAICQ 360

                        250       260
                 ....*....|....*....|
gi 46397258  552 QAALKAAVDGKEMVTMKELE 571
Cdd:PTZ00454 361 EAGMQAVRKNRYVILPKDFE 380
RecA-like_NVL_r2-like cd19530
second of two ATPase domains of NVL (nuclear VCP-like protein) and similar ATPase domains; NVL ...
 344-504 1.71e-41

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: 148.79  E-value: 1.71e-41
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46397258 344 VEEAKQELQ-EVVEFLKNPQKFTILGGKLPKGILLVGPPGTGKTLLARAVAGEADVPFYYASGSEFDEMFVGVGASRIRN 422
Cdd:cd19530   1 LDHVREELTmSILRPIKRPDIYKALGIDLPTGVLLYGPPGCGKTLLAKAVANESGANFISVKGPELLNKYVGESERAVRQ 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46397258 423 LFREAKANAPCVIFIDELDSVGGKRIESPMHPYSRqTINQLLAEMDGFKPNEGVIIIGATNFPEALDNALIRPGRFDMQV 502
Cdd:cd19530  81 VFQRARASAPCVIFFDEVDALVPKRGDGGSWASER-VVNQLLTEMDGLEERSNVFVIAATNRPDIIDPAMLRPGRLDKTL 159


                ..
gi 46397258 503 TV 504
Cdd:cd19530 160 YV 161
RecA-like_VPS4-like cd19509
ATPase domain of VPS4, ATAD1, K, KTNA1, Spastin, FIGL-1 and similar ATPase domains; This ...
 341-498 1.21e-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: 146.73  E-value: 1.21e-40
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46397258 341 VKGVEEAKQELQEVVEF-LKNPQKFTiLGGKLPKGILLVGPPGTGKTLLARAVAGEADVPFYYASGSEFDEMFVGVGASR 419
Cdd:cd19509   1 IAGLDDAKEALKEAVILpSLRPDLFP-GLRGPPRGILLYGPPGTGKTLLARAVASESGSTFFSISASSLVSKWVGESEKI 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46397258 420 IRNLFREAKANAPCVIFIDELDSVGGKRIESPmHPYSRQTINQLLAEMDGF--KPNEGVIIIGATNFPEALDNALIRpgR 497
Cdd:cd19509  80 VRALFALARELQPSIIFIDEIDSLLSERGSGE-HEASRRVKTEFLVQMDGVlnKPEDRVLVLGATNRPWELDEAFLR--R 156


                .
gi 46397258 498 F 498
Cdd:cd19509 157 F 157
RecA-like_PEX1_r2 cd19526
second of two ATPase domains of Peroxisomal biogenesis factor 1 (PEX1); PEX1(also known as ...
 347-502 2.29e-37

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: 137.17  E-value: 2.29e-37
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46397258 347 AKQELQEVVEF-LKNPQKFTILGGKLPKGILLVGPPGTGKTLLARAVAGEADVPFYYASGSEFDEMFVGVGASRIRNLFR 425
Cdd:cd19526   1 VKKALEETIEWpSKYPKIFASSPLRLRSGILLYGPPGCGKTLLASAIASECGLNFISVKGPELLNKYIGASEQNVRDLFS 80

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 46397258 426 EAKANAPCVIFIDELDSVGGKRIESPMHPYSRqTINQLLAEMDGFKPNEGVIIIGATNFPEALDNALIRPGRFDMQV 502
Cdd:cd19526  81 RAQSAKPCILFFDEFDSIAPKRGHDSTGVTDR-VVNQLLTQLDGVEGLDGVYVLAATSRPDLIDPALLRPGRLDKLV 156
RecA-like_PEX6_r2 cd19527
second of two ATPase domains of Peroxisomal biogenesis factor 6 (PEX6); PEX6(also known as ...
 348-499 1.05e-36

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: 135.33  E-value: 1.05e-36
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46397258 348 KQELQEVVEF-LKNPQKFTiLGGKLPKGILLVGPPGTGKTLLARAVAGEADVPFYYASGSEFDEMFVGVGASRIRNLFRE 426
Cdd:cd19527   2 KKEILDTIQLpLEHPELFS-SGLRKRSGILLYGPPGTGKTLLAKAIATECSLNFLSVKGPELINMYIGESEANVREVFQK 80

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 46397258 427 AKANAPCVIFIDELDSVGGKRIES-PMHPYSRQTINQLLAEMDGF-KPNEGVIIIGATNFPEALDNALIRPGRFD 499
Cdd:cd19527  81 ARDAKPCVIFFDELDSLAPSRGNSgDSGGVMDRVVSQLLAELDGMsSSGQDVFVIGATNRPDLLDPALLRPGRFD 155
RecA-like_VPS4 cd19521
ATPase domain of vacuolar protein sorting-associated protein 4; Vacuolar protein ...
 335-504 1.03e-35

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: 133.06  E-value: 1.03e-35
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46397258 335 NVTFEHVKGVEEAKQELQEVVEF-LKNPQKFTilGGKLP-KGILLVGPPGTGKTLLARAVAGEADVPFYYASGSEFDEMF 412
Cdd:cd19521   3 NVKWEDVAGLEGAKEALKEAVILpVKFPHLFT--GNRKPwSGILLYGPPGTGKSYLAKAVATEANSTFFSVSSSDLVSKW 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46397258 413 VGVGASRIRNLFREAKANAPCVIFIDELDSVGGKRIESPMHPySRQTINQLLAEMDGF-KPNEGVIIIGATNFPEALDNA 491
Cdd:cd19521  81 MGESEKLVKQLFAMARENKPSIIFIDEVDSLCGTRGEGESEA-SRRIKTELLVQMNGVgNDSQGVLVLGATNIPWQLDSA 159

                       170
                ....*....|...
gi 46397258 492 LIRpgRFDMQVTV 504
Cdd:cd19521 160 IRR--RFEKRIYI 170
RecA-like_Figl-1 cd19525
ATPase domain of Fidgetin-Like 1 (FIGL-1); FIGL-1 may participate in DNA repair in the nucleus; ...
 336-494 1.10e-33

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


Pssm-ID: 410933 [Multi-domain]  Cd Length: 186  Bit Score: 127.80  E-value: 1.10e-33
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46397258 336 VTFEHVKGVEEAKQELQEVVEF-LKNPQKFTILGGKlPKGILLVGPPGTGKTLLARAVAGEADVPFYYASGSEFDEMFVG 414
Cdd:cd19525  19 INWADIAGLEFAKKTIKEIVVWpMLRPDIFTGLRGP-PKGILLFGPPGTGKTLIGKCIASQSGATFFSISASSLTSKWVG 97

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46397258 415 VGASRIRNLFREAKANAPCVIFIDELDSVGGKRIESPmHPYSRQTINQLLAEMDGFK--PNEGVIIIGATNFPEALDNAL 492
Cdd:cd19525  98 EGEKMVRALFSVARCKQPAVIFIDEIDSLLSQRGEGE-HESSRRIKTEFLVQLDGATtsSEDRILVVGATNRPQEIDEAA 176


                ..
gi 46397258 493 IR 494
Cdd:cd19525 177 RR 178
pup_AAA TIGR03689
proteasome ATPase; In the Actinobacteria, as shown for Mycobacterium tuberculosis, some ...
 335-521 1.14e-32

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


Pssm-ID: 200312 [Multi-domain]  Cd Length: 512  Bit Score: 132.91  E-value: 1.14e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46397258   335 NVTFEHVKGVEEAKQELQEVVE--FLkNPQKFTILGGKLPKGILLVGPPGTGKTLLARAVA--------GEADVPFYYAS 404
Cdd:TIGR03689 178 DVTYADIGGLGSQIEQIRDAVElpFL-HPELYREYGLKPPKGVLLYGPPGCGKTLIAKAVAnslaarigAEGGGKSYFLN 256

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46397258   405 --GSEFDEMFVGVGASRIRNLFREAKANA----PCVIFIDELDSV---GGKRIESPMHpysrQTI-NQLLAEMDGFKPNE 474
Cdd:TIGR03689 257 ikGPELLNKYVGETERQIRLIFQRAREKAsegrPVIVFFDEMDSLfrtRGSGVSSDVE----TTVvPQLLAEIDGVESLD 332

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 46397258   475 GVIIIGATNFPEALDNALIRPGRFDMQVTVPRPDVKGRTEILKWYLN 521
Cdd:TIGR03689 333 NVIVIGASNREDMIDPAILRPGRLDVKIRIERPDAEAAADIFAKYLT 379
RecA-like_KTNA1 cd19522
Katanin p60 ATPase-containing subunit A1; Katanin p60 ATPase-containing subunit A1 (KTNA1) is ...
 341-494 8.06e-32

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


Pssm-ID: 410930 [Multi-domain]  Cd Length: 170  Bit Score: 121.63  E-value: 8.06e-32
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46397258 341 VKGVEEAKQELQE-VVEFLKNPQKFTilGGKLP-KGILLVGPPGTGKTLLARAVAGEADVPFYYASGSEFDEMFVGVGAS 418
Cdd:cd19522   2 IADLEEAKKLLEEaVVLPMWMPEFFK--GIRRPwKGVLMVGPPGTGKTLLAKAVATECGTTFFNVSSSTLTSKYRGESEK 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46397258 419 RIRNLFREAKANAPCVIFIDELDSVGGKRIESPMHPYSRQTINQLLAEMDGF-------KPNEGVIIIGATNFPEALDNA 491
Cdd:cd19522  80 LVRLLFEMARFYAPTTIFIDEIDSICSRRGTSEEHEASRRVKSELLVQMDGVggasendDPSKMVMVLAATNFPWDIDEA 159


                ...
gi 46397258 492 LIR 494
Cdd:cd19522 160 LRR 162
RecA-like_spastin cd19524
ATPase domain of spastin; Spastin is an ATP-dependent microtubule-severing protein involved in ...
 341-504 1.73e-31

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


Pssm-ID: 410932 [Multi-domain]  Cd Length: 164  Bit Score: 120.72  E-value: 1.73e-31
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46397258 341 VKGVEEAKQELQEVVEF-LKNPQKFTILGGKlPKGILLVGPPGTGKTLLARAVAGEADVPFYYASGSEFDEMFVGVGASR 419
Cdd:cd19524   2 IAGQDLAKQALQEMVILpSLRPELFTGLRAP-ARGLLLFGPPGNGKTMLAKAVAAESNATFFNISAASLTSKYVGEGEKL 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46397258 420 IRNLFREAKANAPCVIFIDELDSVGGKRIESPmHPYSRQTINQLLAEMDGFK--PNEGVIIIGATNFPEALDNALIRpgR 497
Cdd:cd19524  81 VRALFAVARELQPSIIFIDEVDSLLSERSEGE-HEASRRLKTEFLIEFDGVQsnGDDRVLVMGATNRPQELDDAVLR--R 157


                ....*..
gi 46397258 498 FDMQVTV 504
Cdd:cd19524 158 FTKRVYV 164
RecA-like_Yta7-like cd19517
ATPase domain of Saccharomyces cerevisiae Yta7 and similar ATPase domains; Saccharomyces ...
 341-499 2.87e-31

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: 120.31  E-value: 2.87e-31
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46397258 341 VKGVEEAKQELQEVVEF-LKNPQKFTILGGKLPKGILLVGPPGTGKTLLARAVA-----GEADVPFYYASGSEFDEMFVG 414
Cdd:cd19517   2 IGGLSHYINQLKEMVFFpLLYPEVFAKFKITPPRGVLFHGPPGTGKTLMARALAaecskGGQKVSFFMRKGADCLSKWVG 81

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46397258 415 VGASRIRNLFREAKANAPCVIFIDELDSVGGKRiESPMHPYSRQTINQLLAEMDGFKPNEGVIIIGATNFPEALDNALIR 494
Cdd:cd19517  82 EAERQLRLLFEEAYRMQPSIIFFDEIDGLAPVR-SSKQEQIHASIVSTLLALMDGLDNRGQVVVIGATNRPDALDPALRR 160


                ....*
gi 46397258 495 PGRFD 499
Cdd:cd19517 161 PGRFD 165
RecA-like_ATAD1 cd19520
ATPase domain of ATPase family AAA domain-containing protein 1 and similar ATPase domains; ...
 343-498 1.07e-28

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: 112.52  E-value: 1.07e-28
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46397258 343 GVEEAKQELQEVVEF-LKNPQKFTilGGKL---PKGILLVGPPGTGKTLLARAVAGEADVPFYYASGSEFDEMFVGVGAS 418
Cdd:cd19520   4 GLDEVITELKELVILpLQRPELFD--NSRLlqpPKGVLLYGPPGCGKTMLAKATAKEAGARFINLQVSSLTDKWYGESQK 81

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46397258 419 RIRNLFREAKANAPCVIFIDELDSVGGKRiESPMHPYSRQTINQLLAEMDGF--KPNEGVIIIGATNFPEALDNALIR-- 494
Cdd:cd19520  82 LVAAVFSLASKLQPSIIFIDEIDSFLRQR-SSTDHEATAMMKAEFMSLWDGLstDGNCRVIVMGATNRPQDLDEAILRrm 160


                ....
gi 46397258 495 PGRF 498
Cdd:cd19520 161 PKRF 164
AAA cd00009
The AAA+ (ATPases Associated with a wide variety of cellular Activities) superfamily ...
 342-505 3.32e-26

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


Pssm-ID: 99707 [Multi-domain]  Cd Length: 151  Bit Score: 104.92  E-value: 3.32e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46397258 342 KGVEEAKQELQEVVEFLKnpqkftilggklPKGILLVGPPGTGKTLLARAVAGEA---DVPFYYASGSEFDEMFVG---V 415
Cdd:cd00009   1 VGQEEAIEALREALELPP------------PKNLLLYGPPGTGKTTLARAIANELfrpGAPFLYLNASDLLEGLVVaelF 68

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46397258 416 GASRIRNLFREAKANAPCVIFIDELDSVGGKRIEspmhpysrQTINQLLAEMDGFKPNEGVIIIGATNFPEALDNALIRP 495
Cdd:cd00009  69 GHFLVRLLFELAEKAKPGVLFIDEIDSLSRGAQN--------ALLRVLETLNDLRIDRENVRVIGATNRPLLGDLDRALY 140

                       170
                ....*....|
gi 46397258 496 GRFDMQVTVP 505
Cdd:cd00009 141 DRLDIRIVIP 150
RecA-like_NSF-SEC18_r1-like cd19504
first of two ATPase domains of NSF and SEC18, and similar ATPase domains; ...
 367-504 3.73e-25

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: 102.95  E-value: 3.73e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46397258 367 LGGKLPKGILLVGPPGTGKTLLARAV-----AGEADVpfyyASGSEFDEMFVGVGASRIRNLFREAKANAPC-------- 433
Cdd:cd19504  30 LGCKHVKGILLYGPPGTGKTLMARQIgkmlnAREPKI----VNGPEILNKYVGESEANIRKLFADAEEEQRRlgansglh 105

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 46397258 434 VIFIDELDSV----GGKRIESPMHPysrQTINQLLAEMDGFKPNEGVIIIGATNFPEALDNALIRPGRFDMQVTV 504
Cdd:cd19504 106 IIIFDEIDAIckqrGSMAGSTGVHD---TVVNQLLSKIDGVEQLNNILVIGMTNRKDLIDEALLRPGRLEVQMEI 177
RecA-like_BCS1 cd19510
Mitochondrial chaperone BCS1; Mitochondrial chaperone BCS1 is necessary for the assembly of ...
 351-504 1.05e-20

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: 89.33  E-value: 1.05e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46397258 351 LQEVVEFLKNPQKFTILGGKLPKGILLVGPPGTGKTLLARAVAGEADVPFYYASGSEfdemfVGVGASRIRNLFREAKAN 430
Cdd:cd19510   2 IDDLKDFIKNEDWYNDRGIPYRRGYLLYGPPGTGKSSFIAALAGELDYDICDLNLSE-----VVLTDDRLNHLLNTAPKQ 76

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 46397258 431 ApcVIFIDELDSVGGKRIESPMHPY-----SRQTINQLLAEMDGFKPNEGVIIIGATNFPEALDNALIRPGRFDMQVTV 504
Cdd:cd19510  77 S--IILLEDIDAAFESREHNKKNPSaygglSRVTFSGLLNALDGVASSEERIVFMTTNHIERLDPALIRPGRVDMKIYM 153
RecA-like_fidgetin cd19523
ATPase domain of fidgetin; Fidgetin (FIGN) is a ATP-dependent microtubule severing protein. ...
 341-494 5.03e-19

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: 84.94  E-value: 5.03e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46397258 341 VKGVEEAKQELQ-EVVEFLKNPQKFTILGgKLPKGILLVGPPGTGKTLLARAVAGEADVPFYYASGSEFDEMFVGVGASR 419
Cdd:cd19523   2 IAGLGALKAAIKeEVLWPLLRPDAFSGLL-RLPRSILLFGPRGTGKTLLGRCLASQLGATFLRLRGSTLVAKWAGEGEKI 80

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 46397258 420 IRNLFREAKANAPCVIFIDELDSVGGKRIESPmHPYSRQTInQLLAEMDGF--KPNEGVIIIGATNFPEALDNALIR 494
Cdd:cd19523  81 LQASFLAARCRQPSVLFISDLDALLSSQDDEA-SPVGRLQV-ELLAQLDGVlgSGEDGVLVVCTTSKPEEIDESLRR 155
ycf46 CHL00195
Ycf46; Provisional
 335-580 9.90e-19

Ycf46; Provisional


Pssm-ID: 177094 [Multi-domain]  Cd Length: 489  Bit Score: 90.08  E-value: 9.90e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46397258  335 NVTFEHVKGVEEAKQELQEVVE-FLKNPQKFtilGGKLPKGILLVGPPGTGKTLLARAVAGEADVPFYYAsgsEFDEMF- 412
Cdd:CHL00195 224 NEKISDIGGLDNLKDWLKKRSTsFSKQASNY---GLPTPRGLLLVGIQGTGKSLTAKAIANDWQLPLLRL---DVGKLFg 297

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46397258  413 --VGVGASRIRNLFREAKANAPCVIFIDELDsvggkRIESPMHPYSRQ-TINQLLAEM-----DGFKPnegVIIIGATNF 484
Cdd:CHL00195 298 giVGESESRMRQMIRIAEALSPCILWIDEID-----KAFSNSESKGDSgTTNRVLATFitwlsEKKSP---VFVVATANN 369

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46397258  485 PEALDNALIRPGRFDMQVTVPRPDVKGRTEILKWYLNKIKFD--QSVDPEIIARGTVGFSGAELENLVNQaALKAAVDGK 562
Cdd:CHL00195 370 IDLLPLEILRKGRFDEIFFLDLPSLEEREKIFKIHLQKFRPKswKKYDIKKLSKLSNKFSGAEIEQSIIE-AMYIAFYEK 448

                        250
                 ....*....|....*...
gi 46397258  563 EmvtmkelEFSKDKILMG 580
Cdd:CHL00195 449 R-------EFTTDDILLA 459
AAA smart00382
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ...
 372-508 4.17e-18

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


Pssm-ID: 214640 [Multi-domain]  Cd Length: 148  Bit Score: 81.65  E-value: 4.17e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46397258    372 PKGILLVGPPGTGKTLLARAVAGEADVP---FYYASGSEFDE--------------MFVGVGASRIRNLFREAKANAPCV 434
Cdd:smart00382   2 GEVILIVGPPGSGKTTLARALARELGPPgggVIYIDGEDILEevldqllliivggkKASGSGELRLRLALALARKLKPDV 81

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 46397258    435 IFIDELDSVGGKRIESPMhpysrqTINQLLAEMDGFKPNEGVIIIGATNFPEALDNALIRPgRFDMQVTVPRPD 508
Cdd:smart00382  82 LILDEITSLLDAEQEALL------LLLEELRLLLLLKSEKNLTVILTTNDEKDLGPALLRR-RFDRRIVLLLIL 148
RecA-like_Ycf46-like cd19507
ATPase domain of Ycf46 and similar ATPase domains; Ycf46 may play a role in the regulation of ...
 371-499 3.79e-16

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: 76.64  E-value: 3.79e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46397258 371 LPKGILLVGPPGTGKTLLARAVAGEADVPFYYASGSEFDEMFVGVGASRIRNLFREAKANAPCVIFIDELDSVGGKRIES 450
Cdd:cd19507  30 TPKGLLLVGIQGTGKSLTAKAIAGVWQLPLLRLDMGRLFGGLVGESESRLRQMIQTAEAIAPCVLWIDEIEKGFSNADSK 109

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|
gi 46397258 451 PMHPYSRQTINQLLAEM-DGFKPnegVIIIGATNFPEALDNALIRPGRFD 499
Cdd:cd19507 110 GDSGTSSRVLGTFLTWLqEKKKP---VFVVATANNVQSLPPELLRKGRFD 156
RecA-like_Ycf2 cd19505
ATPase domain of plant YCF2; Ycf2 is a chloroplast ATPase which has an essential function; ...
 367-499 3.90e-11

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: 62.01  E-value: 3.90e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46397258 367 LGGKLPKGILLVGPPGTGKTLLARAVAGEADVPFYYASGSEF--------------DEMFVGVGASRIRNLFREAKANAP 432
Cdd:cd19505   7 LGLSPSKGILLIGSIETGRSYLIKSLAANSYVPLIRISLNKLlynkpdfgnddwidGMLILKESLHRLNLQFELAKAMSP 86

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 46397258 433 CVIF---IDELDS--VGGKRIESPMhpYSRQTINQLLAEMDGFKPNEGVIIIGATNFPEALDNALIRPGRFD 499
Cdd:cd19505  87 CIIWipnIHELNVnrSTQNLEEDPK--LLLGLLLNYLSRDFEKSSTRNILVIASTHIPQKVDPALIAPNRLD 156
RecA-like_ATAD3-like cd19512
ATPase domains of ATPase AAA-domain protein 3A (ATAD3A), -3B, and -3C, and similar ATPase ...
 373-502 5.87e-10

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: 58.31  E-value: 5.87e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46397258 373 KGILLVGPPGTGKTLLARAVAGEADVPFYYASGSEFDEMFVGvGASRIRNLFREA-KANAPCVIFIDELDSVGGKRIESP 451
Cdd:cd19512  23 RNILFYGPPGTGKTLFAKKLALHSGMDYAIMTGGDVAPMGRE-GVTAIHKVFDWAnTSRRGLLLFVDEADAFLRKRSTEK 101

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|.
gi 46397258 452 MHPYSRQTINQLLAEMdGFKPNEGVIIIgATNFPEALDNALirPGRFDMQV 502
Cdd:cd19512 102 ISEDLRAALNAFLYRT-GEQSNKFMLVL-ASNQPEQFDWAI--NDRIDEMV 148
AAA_lid_3 pfam17862
AAA+ lid domain; This entry represents the alpha helical AAA+ lid domain that is found to the ...
 528-571 3.90e-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: 52.93  E-value: 3.90e-09
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 46397258   528 SVDPEIIARGTVGFSGAELENLVNQAALKAAVDGKEMVTMKELE 571
Cdd:pfam17862   1 DVDLEELAERTEGFSGADLEALCREAALAALRRGLEAVTQEDLE 44
PRK13342 PRK13342
recombination factor protein RarA; Reviewed
 366-439 8.33e-09

recombination factor protein RarA; Reviewed


Pssm-ID: 237355 [Multi-domain]  Cd Length: 413  Bit Score: 58.56  E-value: 8.33e-09
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 46397258  366 ILGGKLPKgILLVGPPGTGKTLLARAVAGEADVPFYYASGSefdemFVGVgaSRIRNLFREAKANA----PCVIFIDE 439
Cdd:PRK13342  31 IEAGRLSS-MILWGPPGTGKTTLARIIAGATDAPFEALSAV-----TSGV--KDLREVIEEARQRRsagrRTILFIDE 100
TIP49 COG1224
DNA helicase TIP49, TBP-interacting protein [Transcription];
343-408 9.31e-09

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


Pssm-ID: 440837 [Multi-domain]  Cd Length: 452  Bit Score: 58.44  E-value: 9.31e-09
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 46397258 343 GVEEAKQELQEVVEFLKNpqkftilgGKLP-KGILLVGPPGTGKTLLARAVAGE--ADVPFYYASGSEF 408
Cdd:COG1224  42 GQVEAREAAGIVVKMIKE--------GKMAgKGILIVGPPGTGKTALAVAIARElgEDTPFVAISGSEI 102
RecA-like_HslU cd19498
ATP-dependent protease ATPase subunit HslU; HslU is a component of the ATP-dependent protease ...
 371-446 3.15e-08

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: 54.31  E-value: 3.15e-08
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 46397258 371 LPKGILLVGPPGTGKTLLARAVAGEADVPFYYASGSEFDEM-FVGVGA-SRIRNLfreakanAPCVIFIDELDSVGGK 446
Cdd:cd19498  45 TPKNILMIGPTGVGKTEIARRLAKLAGAPFIKVEATKFTEVgYVGRDVeSIIRDL-------VEGIVFIDEIDKIAKR 115
RecA-like_Lon cd19500
lon protease homolog 2 peroxisomal; Lon protease (also known as Lon peptidase) is an ...
 343-444 7.98e-08

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


Pssm-ID: 410908 [Multi-domain]  Cd Length: 182  Bit Score: 52.95  E-value: 7.98e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46397258 343 GVEEAKQELQE--VVEFLKNPQKFTILggklpkgiLLVGPPGTGKTLLARAVAGEADVPFYYAS-GSEFDE--------M 411
Cdd:cd19500  14 GLEDVKERILEylAVRKLKGSMKGPIL--------CLVGPPGVGKTSLGKSIARALGRKFVRISlGGVRDEaeirghrrT 85

                        90       100       110
                ....*....|....*....|....*....|...
gi 46397258 412 FVGVGASRIRNLFREAKANAPcVIFIDELDSVG 444
Cdd:cd19500  86 YVGAMPGRIIQALKKAGTNNP-VFLLDEIDKIG 117
RecA-like_ClpX cd19497
ATP-dependent Clp protease ATP-binding subunit ClpX; ClpX is a component of the ATP-dependent ...
 330-446 2.60e-07

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: 52.60  E-value: 2.60e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46397258 330 PVQMKNVTFEHVKGVEEAKQELQEVV----EFLKNPQKFTILGGKLPKG-ILLVGPPGTGKTLLARAVAGEADVPFYYAS 404
Cdd:cd19497   3 PKEIKEHLDKYVIGQERAKKVLSVAVynhyKRIRNNLKQKDDDVELEKSnILLIGPTGSGKTLLAQTLAKILDVPFAIAD 82

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*....
gi 46397258 405 GSEFDEM-FVG--VgASRIRNLFREAKANAP----CVIFIDELDSVGGK 446
Cdd:cd19497  83 ATTLTEAgYVGedV-ENILLKLLQAADYDVEraqrGIVYIDEIDKIARK 130
RarA COG2256
Replication-associated recombination protein RarA (DNA-dependent ATPase) [Replication, ...
 366-439 3.65e-07

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


Pssm-ID: 441857 [Multi-domain]  Cd Length: 439  Bit Score: 53.14  E-value: 3.65e-07
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 46397258 366 ILGGKLPKgILLVGPPGTGKTLLARAVAGEADVPFYYASGsefdemfVGVGASRIRNLFREAKANA----PCVIFIDE 439
Cdd:COG2256  44 IEAGRLSS-MILWGPPGTGKTTLARLIANATDAEFVALSA-------VTSGVKDIREVIEEARERRaygrRTILFVDE 113
TIP49 pfam06068
TIP49 P-loop domain; This family consists of the C-terminal region of several eukaryotic and ...
 323-408 4.79e-07

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: 52.70  E-value: 4.79e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46397258   323 GLDSAVDPVQMKnvtfEHVKGVEEAKQELQEVVEFLKNPQkftiLGGKlpkGILLVGPPGTGKTLLARAVAGE--ADVPF 400
Cdd:pfam06068  12 GLDEDGEARYVS----GGLVGQEKAREAAGVIVEMIKEGK----IAGR---AVLIAGPPGTGKTALAIAISKElgEDTPF 80


                  ....*...
gi 46397258   401 YYASGSEF 408
Cdd:pfam06068  81 TSISGSEV 88
PRK04195 PRK04195
replication factor C large subunit; Provisional
 337-446 5.07e-07

replication factor C large subunit; Provisional


Pssm-ID: 235250 [Multi-domain]  Cd Length: 482  Bit Score: 53.00  E-value: 5.07e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46397258  337 TFEHVKGVEEAKQELQEVVEflknpqkfTILGGKLPKGILLVGPPGTGKTLLARAVAGEADVPFYYASGSEF---DEM-- 411
Cdd:PRK04195  12 TLSDVVGNEKAKEQLREWIE--------SWLKGKPKKALLLYGPPGVGKTSLAHALANDYGWEVIELNASDQrtaDVIer 83

                         90       100       110
                 ....*....|....*....|....*....|....*
gi 46397258  412 FVGvGASRIRNLFREAKAnapcVIFIDELDSVGGK 446
Cdd:PRK04195  84 VAG-EAATSGSLFGARRK----LILLDEVDGIHGN 113
T7SS_EccA TIGR03922
type VII secretion AAA-ATPase EccA; This model represents the AAA family ATPase, EccA, of the ...
 343-560 6.21e-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: 52.92  E-value: 6.21e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46397258   343 GVEEAKQElqevVEFLKNPQKFTIL----GGKLP---KGILLVGPPGTGKTLLARAVAgeadvpfyyasgsefdEMFVGV 415
Cdd:TIGR03922 280 GLERVKRQ----VAALKSSTAMALAraerGLPVAqtsNHMLFAGPPGTGKTTIARVVA----------------KIYCGL 339

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46397258   416 GASR---IRNLFR-----------EAKANAPC------VIFIDELDSVGGKRIESPmHPYSRQTINQLLAEMDGFKPNEG 475
Cdd:TIGR03922 340 GVLRkplVREVSRadligqyigesEAKTNEIIdsalggVLFLDEAYTLVETGYGQK-DPFGLEAIDTLLARMENDRDRLV 418

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46397258   476 VIIIGatnFPEALDNAL-IRPGrfdmqvtvprpdVKGRteilkwYLNKIKFDQSVDPEIIARGTVgfSGAELENLVNQAA 554
Cdd:TIGR03922 419 VIGAG---YRKDLDKFLeVNEG------------LRSR------FTRVIEFPSYSPDELVEIARR--MATERDSVLDDAA 475


                  ....*.
gi 46397258   555 LKAAVD 560
Cdd:TIGR03922 476 ADALLE 481
AAA_5 pfam07728
AAA domain (dynein-related subfamily); This Pfam entry includes some of the AAA proteins not ...
 374-498 1.24e-06

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


Pssm-ID: 400191 [Multi-domain]  Cd Length: 135  Bit Score: 48.44  E-value: 1.24e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46397258   374 GILLVGPPGTGKTLLARAVAG--EADVPFYYA--SGSEFDEMF-----VGVGASRIRNLFREAkANAPCVIFIDELDSVG 444
Cdd:pfam07728   1 GVLLVGPPGTGKTELAERLAAalSNRPVFYVQltRDTTEEDLFgrrniDPGGASWVDGPLVRA-AREGEIAVLDEINRAN 79

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 46397258   445 GKRIESpmhpysrqtINQLLAE-----MDGF----KPNEGVIIIGATNFPEA----LDNALIRpgRF 498
Cdd:pfam07728  80 PDVLNS---------LLSLLDErrlllPDGGelvkAAPDGFRLIATMNPLDRglneLSPALRS--RF 135
CDC6 COG1474
Cdc6-related protein, AAA superfamily ATPase [Replication, recombination and repair];
350-489 6.40e-06

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


Pssm-ID: 441083 [Multi-domain]  Cd Length: 389  Bit Score: 49.08  E-value: 6.40e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46397258 350 ELQEVVEFLKnpqkfTILGGKLPKGILLVGPPGTGKTLLARAV-------AGEADVPFYYA------SGSEF-------D 409
Cdd:COG1474  34 EIEELASALR-----PALRGERPSNVLIYGPTGTGKTAVAKYVleeleeeAEERGVDVRVVyvncrqASTRYrvlsrilE 108

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46397258 410 EMFV-------GVGASRIRNLFREA--KANAPCVIFIDELDSVGGKRIESPMHPYSRqtinqLLAEMDGFKpnegVIIIG 480
Cdd:COG1474 109 ELGSgedipstGLSTDELFDRLYEAldERDGVLVVVLDEIDYLVDDEGDDLLYQLLR-----ANEELEGAR----VGVIG 179

                       170
                ....*....|..
gi 46397258 481 ATN---FPEALD 489
Cdd:COG1474 180 ISNdleFLENLD 191
RecA-like_Pch2-like cd19508
ATPase domain of Pachytene checkpoint 2 (Pch2) and similar ATPase domains; Pch2 (known as ...
 375-493 6.42e-06

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


Pssm-ID: 410916 [Multi-domain]  Cd Length: 199  Bit Score: 47.83  E-value: 6.42e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46397258 375 ILLVGPPGTGKTLLARAVAGEADV--PFYYASG--------SEFDEMFvGVGASRIRNLFR------EAKANAPCVIfID 438
Cdd:cd19508  55 VLLHGPPGTGKTSLCKALAQKLSIrlSSRYRYGqlieinshSLFSKWF-SESGKLVTKMFQkiqeliDDKDALVFVL-ID 132

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 46397258 439 ELDSVGGKRIESPMHPYSRQTI---NQLLAEMDGFKPNEGVIIIGATNFPEALDNALI 493
Cdd:cd19508 133 EVESLAAARSASSSGTEPSDAIrvvNAVLTQIDRIKRYHNNVILLTSNLLEKIDVAFV 190
RecA-like_superfamily cd01120
RecA-like_NTPases; RecA-like NTPases. This superfamily includes the NTP binding domain of F1 ...
 375-491 1.21e-05

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


Pssm-ID: 410865 [Multi-domain]  Cd Length: 119  Bit Score: 45.19  E-value: 1.21e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46397258 375 ILLVGPPGTGKTLLARAVAGEA---DVPFYYASgsefdemFVGVGASRIRnlfREAKANAPCVIFIDELDSVGGKRIesp 451
Cdd:cd01120   1 ILITGPPGSGKTTLLLQFAEQAllsDEPVIFIS-------FLDTILEAIE---DLIEEKKLDIIIIDSLSSLARASQ--- 67

                        90       100       110       120
                ....*....|....*....|....*....|....*....|
gi 46397258 452 mhPYSRQTINQLLAEMDGFKPNEGVIIIgATNFPEALDNA 491
Cdd:cd01120  68 --GDRSSELLEDLAKLLRAARNTGITVI-ATIHSDKFDID 104
clpX PRK05342
ATP-dependent Clp protease ATP-binding subunit ClpX;
375-400 3.97e-05

ATP-dependent Clp protease ATP-binding subunit ClpX;


Pssm-ID: 235422 [Multi-domain]  Cd Length: 412  Bit Score: 46.69  E-value: 3.97e-05
                         10        20
                 ....*....|....*....|....*.
gi 46397258  375 ILLVGPPGTGKTLLARAVAGEADVPF 400
Cdd:PRK05342 111 ILLIGPTGSGKTLLAQTLARILDVPF 136
DnaX COG2812
DNA polymerase III, gamma/tau subunits [Replication, recombination and repair];
337-393 4.38e-05

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


Pssm-ID: 442061 [Multi-domain]  Cd Length: 340  Bit Score: 46.34  E-value: 4.38e-05
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 46397258 337 TFEHVKGveeakQElqEVVEFLKNpqkfTILGGKLPKGILLVGPPGTGKTLLARAVA 393
Cdd:COG2812   8 TFDDVVG-----QE--HVVRTLKN----ALASGRLAHAYLFTGPRGVGKTTLARILA 53
ClpX COG1219
ATP-dependent protease Clp, ATPase subunit ClpX [Posttranslational modification, protein ...
 375-400 6.09e-05

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


Pssm-ID: 440832 [Multi-domain]  Cd Length: 409  Bit Score: 46.19  E-value: 6.09e-05
                        10        20
                ....*....|....*....|....*.
gi 46397258 375 ILLVGPPGTGKTLLARAVAGEADVPF 400
Cdd:COG1219 112 ILLIGPTGSGKTLLAQTLARILDVPF 137
NACHT COG5635
Predicted NTPase, NACHT family domain [Signal transduction mechanisms];
352-477 7.90e-05

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


Pssm-ID: 444362 [Multi-domain]  Cd Length: 935  Bit Score: 46.34  E-value: 7.90e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46397258 352 QEVVEFLKNPQKFTILGGKLPKgILLVGPPGTGKTLLARAVA---------GEADVPFY-----YASGSEFDEM---FVG 414
Cdd:COG5635 161 LNLLERIESLKRLELLEAKKKR-LLILGEPGSGKTTLLRYLAlelaeryldAEDPIPILielrdLAEEASLEDLlaeALE 239

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 46397258 415 VGASRIRNLFREAKANAPCVIFIDELDsvggkriESPMHPYSRQTINQLLAEMDGFKPNEGVI 477
Cdd:COG5635 240 KRGGEPEDALERLLRNGRLLLLLDGLD-------EVPDEADRDEVLNQLRRFLERYPKARVII 295
MoxR COG0714
MoxR-like ATPase [General function prediction only]; MoxR-like ATPase is part of the Pathway ...
 375-400 1.79e-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: 44.39  E-value: 1.79e-04
                        10        20
                ....*....|....*....|....*.
gi 46397258 375 ILLVGPPGTGKTLLARAVAGEADVPF 400
Cdd:COG0714  34 LLLEGVPGVGKTTLAKALARALGLPF 59
HolB COG0470
DNA polymerase III, delta prime subunit [Replication, recombination and repair];
345-393 1.85e-04

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


Pssm-ID: 440238 [Multi-domain]  Cd Length: 289  Bit Score: 44.20  E-value: 1.85e-04
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*....
gi 46397258 345 EEAKQELQEVVEflknpqkftilGGKLPKGILLVGPPGTGKTLLARAVA 393
Cdd:COG0470   2 EEAWEQLLAAAE-----------SGRLPHALLLHGPPGIGKTTLALALA 39
ABC_ATPase cd00267
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ...
 350-494 3.28e-04

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


Pssm-ID: 213179 [Multi-domain]  Cd Length: 157  Bit Score: 41.85  E-value: 3.28e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46397258 350 ELQEVVEFLKNPQKFTILGGKLPKG--ILLVGPPGTGKTLLARAVAGEADVPfyyaSGS-EFDEmfVGVGASRIRNLFRE 426
Cdd:cd00267   1 EIENLSFRYGGRTALDNVSLTLKAGeiVALVGPNGSGKSTLLRAIAGLLKPT----SGEiLIDG--KDIAKLPLEELRRR 74

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46397258 427 -------------------AKANAPCVIFIDELDsvggkrieSPMHPYSRQTINQLLAEMdgfkPNEGVIIIGATNFPEA 487
Cdd:cd00267  75 igyvpqlsggqrqrvalarALLLNPDLLLLDEPT--------SGLDPASRERLLELLREL----AEEGRTVIIVTHDPEL 142


                ....*..
gi 46397258 488 LDNALIR 494
Cdd:cd00267 143 AELAADR 149
KaiC-like cd01124
Circadian Clock Protein KaiC; KaiC is a circadian clock protein, most studied in cyanobacteria. ...
 366-467 3.43e-04

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: 42.64  E-value: 3.43e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46397258 366 ILGGKLPKG--ILLVGPPGTGKTLLARAvageadvpfYYASGSEFDE--MFVGVGaSRIRNLFREAKAnapcvIFIDELD 441
Cdd:cd01124  11 LLGGGIPKGsvTLLTGGPGTGKTLFGLQ---------FLYAGAKNGEpgLFFTFE-ESPERLLRNAKS-----FGWDFDE 75

                        90       100
                ....*....|....*....|....*....
gi 46397258 442 SVGGKRI---ESPMHPYSRQTINQLLAEM 467
Cdd:cd01124  76 MEDEGKLiivDAPPTEAGRFSLDELLSRI 104
DnaA COG0593
Chromosomal replication initiation ATPase DnaA [Replication, recombination and repair];
375-598 3.55e-04

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


Pssm-ID: 440358 [Multi-domain]  Cd Length: 303  Bit Score: 43.26  E-value: 3.55e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46397258 375 ILLVGPPGTGKTLLARAVAGEA-----DVPFYYASGSEFDEMFVGVGASRIRNLFREAKANAPCVIfIDELDSVGGKrie 449
Cdd:COG0593  37 LFLYGGVGLGKTHLLHAIGNEAlennpGARVVYLTAEEFTNDFINAIRNNTIEEFKEKYRSVDVLL-IDDIQFLAGK--- 112

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46397258 450 spmhpYSRQ-----TINQLLAemdgfkpNEGVIIIGATNFPEALDNAL--IRpGRFDM--QVTVPRPDVKGRTEILKwyl 520
Cdd:COG0593 113 -----EATQeeffhTFNALRE-------AGKQIVLTSDRPPKELPGLEerLR-SRLEWglVVDIQPPDLETRIAILR--- 176

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46397258 521 NKIKFDQ-SVDPEI---IARgTVGFSGAELENLVNQAALKAAVDGKEmVTmkeLEFSKD--KILMGPERRSVEIDNKNKT 594
Cdd:COG0593 177 KKAADRGlELPDEVleyLAR-RIERNVRELEGALNRLDAYALLTGRP-IT---LELAREvlKDLLRAQKKEITIEDIQKA 251


                ....
gi 46397258 595 ITAY 598
Cdd:COG0593 252 VAEY 255
TIGR02928 TIGR02928
orc1/cdc6 family replication initiation protein; Members of this protein family are found ...
 349-489 3.81e-04

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: 43.39  E-value: 3.81e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46397258   349 QELQEVVEFLKnpqkfTILGGKLPKGILLVGPPGTGKTLLARAV-------AGEADVPFYYA------------------ 403
Cdd:TIGR02928  22 EQIEELAKALR-----PILRGSRPSNVFIYGKTGTGKTAVTKYVmkeleeaAEDRDVRVVTVyvncqildtlyqvlvela 96

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46397258   404 ---SGSEFDEMFVGVGASRI-RNLFREAKANAPCVIFI-DELDSVGGKRIESPMhpysrqtinQLL-AEMDGFKPNEGVI 477
Cdd:TIGR02928  97 nqlRGSGEEVPTTGLSTSEVfRRLYKELNERGDSLIIVlDEIDYLVGDDDDLLY---------QLSrARSNGDLDNAKVG 167

                         170
                  ....*....|....*
gi 46397258   478 IIGATN---FPEALD 489
Cdd:TIGR02928 168 VIGISNdlkFRENLD 182
ruvB PRK00080
Holliday junction branch migration DNA helicase RuvB;
375-439 4.32e-04

Holliday junction branch migration DNA helicase RuvB;


Pssm-ID: 234619 [Multi-domain]  Cd Length: 328  Bit Score: 43.20  E-value: 4.32e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 46397258  375 ILLVGPPGTGKTLLARAVAGEADVPFYYASGSEFDEmfvgvgASRIRNLFREAKANApcVIFIDE 439
Cdd:PRK00080  54 VLLYGPPGLGKTTLANIIANEMGVNIRITSGPALEK------PGDLAAILTNLEEGD--VLFIDE 110
44 PHA02544
clamp loader, small subunit; Provisional
 369-444 6.01e-04

clamp loader, small subunit; Provisional


Pssm-ID: 222866 [Multi-domain]  Cd Length: 316  Bit Score: 42.67  E-value: 6.01e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46397258  369 GKLPKGILLVGPPGTGKTLLARAVAGEADVPFYYASGSEfdemfvgvgaSRIRNLFREAKANA--------PCVIFIDEL 440
Cdd:PHA02544  40 GRIPNMLLHSPSPGTGKTTVAKALCNEVGAEVLFVNGSD----------CRIDFVRNRLTRFAstvsltggGKVIIIDEF 109


                 ....
gi 46397258  441 DSVG 444
Cdd:PHA02544 110 DRLG 113
RAD55 COG0467
RecA-superfamily ATPase, KaiC/GvpD/RAD55 family [Signal transduction mechanisms];
366-389 6.06e-04

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


Pssm-ID: 440235 [Multi-domain]  Cd Length: 221  Bit Score: 41.82  E-value: 6.06e-04
                        10        20
                ....*....|....*....|....*.
gi 46397258 366 ILGGKLPKG--ILLVGPPGTGKTLLA 389
Cdd:COG0467  12 LLGGGLPRGssTLLSGPPGTGKTTLA 37
YifB COG0606
Predicted Mg-chelatase, contains ChlI-like and ATPase domains, YifB family [Posttranslational ...
 375-394 8.28e-04

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: 42.72  E-value: 8.28e-04
                        10        20
                ....*....|....*....|
gi 46397258 375 ILLVGPPGTGKTLLARAVAG 394
Cdd:COG0606 214 LLMIGPPGSGKTMLARRLPG 233
McrB COG1401
5-methylcytosine-specific restriction endonuclease McrBC, GTP-binding regulatory subunit McrB ...
 370-440 9.58e-04

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


Pssm-ID: 441011 [Multi-domain]  Cd Length: 477  Bit Score: 42.45  E-value: 9.58e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46397258 370 KLPKGILLVGPPGTGKT----LLARAVAGEAD-----VPFY--YasgseFDEMFVG------------VGASRIRNLFRE 426
Cdd:COG1401 219 KTKKNVILAGPPGTGKTylarRLAEALGGEDNgriefVQFHpsW-----SYEDFLLgyrpsldegkyePTPGIFLRFCLK 293

                        90
                ....*....|....*.
gi 46397258 427 AKAN--APCVIFIDEL 440
Cdd:COG1401 294 AEKNpdKPYVLIIDEI 309
AAA_22 pfam13401
AAA domain;
375-488 1.06e-03

AAA domain;


Pssm-ID: 379165 [Multi-domain]  Cd Length: 129  Bit Score: 39.63  E-value: 1.06e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46397258   375 ILLVGPPGTGKTLLAR-----AVAGEADVPFYYASGS----EFDEMFV---------GVGASRIRNLFREA--KANAPCV 434
Cdd:pfam13401   8 LVLTGESGTGKTTLLRrlleqLPEVRDSVVFVDLPSGtspkDLLRALLralglplsgRLSKEELLAALQQLllALAVAVV 87

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 46397258   435 IFIDELDSVggkriespmhpySRQTINQLLAEMDGFKPNEGVIIIGATNFPEAL 488
Cdd:pfam13401  88 LIIDEAQHL------------SLEALEELRDLLNLSSKLLQLILVGTPELRELL 129
RecA-like_ClpB_Hsp104-like cd19499
Chaperone protein ClpB/Hsp104 subfamily; Bacterial Caseinolytic peptidase B (ClpB) and ...
 338-441 1.34e-03

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


Pssm-ID: 410907 [Multi-domain]  Cd Length: 178  Bit Score: 40.24  E-value: 1.34e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46397258 338 FEHVKGVEEAKQELQEVVEF----LKNPQKftilggklPKG-ILLVGPPGTGKTLLARAVAGeadvpFYYASG------- 405
Cdd:cd19499  10 HERVVGQDEAVKAVSDAIRRaragLSDPNR--------PIGsFLFLGPTGVGKTELAKALAE-----LLFGDEdnlirid 76

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*..
gi 46397258 406 -SEFDEMFVG----------VGASRIRNLFREAKANAPCVIFIDELD 441
Cdd:cd19499  77 mSEYMEKHSVsrligappgyVGYTEGGQLTEAVRRKPYSVVLLDEIE 123
AAA_2 pfam07724
AAA domain (Cdc48 subfamily); This Pfam entry includes some of the AAA proteins not detected ...
 372-441 1.69e-03

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


Pssm-ID: 400187 [Multi-domain]  Cd Length: 168  Bit Score: 39.87  E-value: 1.69e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46397258   372 PKG-ILLVGPPGTGKTLLARAVAGEADV---PFYYASGSEFDE-----MFVG-----VGASRIRNLFREAKANAPCVIFI 437
Cdd:pfam07724   2 PIGsFLFLGPTGVGKTELAKALAELLFGderALIRIDMSEYMEehsvsRLIGappgyVGYEEGGQLTEAVRRKPYSIVLI 81


                  ....
gi 46397258   438 DELD 441
Cdd:pfam07724  82 DEIE 85
PRK08116 PRK08116
hypothetical protein; Validated
 333-395 2.28e-03

hypothetical protein; Validated


Pssm-ID: 236153 [Multi-domain]  Cd Length: 268  Bit Score: 40.77  E-value: 2.28e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 46397258  333 MKNVTFEHVKGVEEAKQELQEVVEFLKNpqkFTILGGKlPKGILLVGPPGTGKTLLARAVAGE 395
Cdd:PRK08116  79 FRNSTFENFLFDKGSEKAYKIARKYVKK---FEEMKKE-NVGLLLWGSVGTGKTYLAACIANE 137
rfc PRK00440
replication factor C small subunit; Reviewed
 337-442 3.49e-03

replication factor C small subunit; Reviewed


Pssm-ID: 234763 [Multi-domain]  Cd Length: 319  Bit Score: 40.24  E-value: 3.49e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46397258  337 TFEHVKGVEEAKQELQEVVEflknpqkftilGGKLPKgILLVGPPGTGKT----LLARAVAGEadvpfYY--------AS 404
Cdd:PRK00440  15 TLDEIVGQEEIVERLKSYVK-----------EKNMPH-LLFAGPPGTGKTtaalALARELYGE-----DWrenflelnAS 77

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 46397258  405 gsefDEMFVGVGASRIRNLFREAKAN-APC-VIFIDELDS 442
Cdd:PRK00440  78 ----DERGIDVIRNKIKEFARTAPVGgAPFkIIFLDEADN 113
ruvB TIGR00635
Holliday junction DNA helicase, RuvB subunit; All proteins in this family for which functions ...
 337-500 3.71e-03

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


Pssm-ID: 129721 [Multi-domain]  Cd Length: 305  Bit Score: 39.98  E-value: 3.71e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46397258   337 TFEHVKGVEEAKQELQEVVEFLKNPQKftilggkLPKGILLVGPPGTGKTLLARAVAGEADVPFYYASGSEFDEmfvgvg 416
Cdd:TIGR00635   2 LLAEFIGQEKVKEQLQLFIEAAKMRQE-------ALDHLLLYGPPGLGKTTLAHIIANEMGVNLKITSGPALEK------ 68

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46397258   417 ASRIRNLFREAKANApcVIFIDELdsvggkriespmHPYSRQTINQLLAEMDGFK--------PNEGVI--------IIG 480
Cdd:TIGR00635  69 PGDLAAILTNLEEGD--VLFIDEI------------HRLSPAVEELLYPAMEDFRldivigkgPSARSVrldlppftLVG 134

                         170       180
                  ....*....|....*....|
gi 46397258   481 ATNFPEALDNALIrpGRFDM 500
Cdd:TIGR00635 135 ATTRAGMLTSPLR--DRFGI 152
Mg_chelatase pfam01078
Magnesium chelatase, subunit ChlI; Magnesium-chelatase is a three-component enzyme that ...
 375-394 4.24e-03

Magnesium chelatase, subunit ChlI; Magnesium-chelatase is a three-component enzyme that catalyzes the insertion of Mg2+ into protoporphyrin IX. This is the first unique step in the synthesis of (bacterio)chlorophyll. Due to this, it is thought that Mg-chelatase has an important role in channelling inter- mediates into the (bacterio)chlorophyll branch in response to conditions suitable for photosynthetic growth. ChlI and BchD have molecular weight between 38-42 kDa.


Pssm-ID: 426032 [Multi-domain]  Cd Length: 207  Bit Score: 39.44  E-value: 4.24e-03
                          10        20
                  ....*....|....*....|
gi 46397258   375 ILLVGPPGTGKTLLARAVAG 394
Cdd:pfam01078  25 LLMIGPPGSGKTMLAKRLPG 44
RuvB_N pfam05496
Holliday junction DNA helicase RuvB P-loop domain; The RuvB protein makes up part of the ...
 375-405 4.43e-03

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


Pssm-ID: 398900 [Multi-domain]  Cd Length: 159  Bit Score: 38.64  E-value: 4.43e-03
                          10        20        30
                  ....*....|....*....|....*....|.
gi 46397258   375 ILLVGPPGTGKTLLARAVAGEADVPFYYASG 405
Cdd:pfam05496  36 VLLYGPPGLGKTTLANIIANEMGVNIRITSG 66
RuvB COG2255
Holliday junction resolvasome RuvABC, ATP-dependent DNA helicase subunit RuvB [Replication, ...
 375-405 4.55e-03

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


Pssm-ID: 441856 [Multi-domain]  Cd Length: 337  Bit Score: 40.06  E-value: 4.55e-03
                        10        20        30
                ....*....|....*....|....*....|.
gi 46397258 375 ILLVGPPGTGKTLLARAVAGEADVPFYYASG 405
Cdd:COG2255  57 VLLYGPPGLGKTTLAHIIANEMGVNIRITSG 87
RecA-like_IQCA1 cd19506
ATPase domain of IQ and AAA domain-containing protein 1 (IQCA1); IQCA1 (also known as dynein ...
 371-485 5.77e-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: 38.28  E-value: 5.77e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46397258 371 LPKGILLVGPPGTGKTLLARAVAGEADVPFYYASGSEFDEMFVGVGASR--IRNLFREAKANAPCVIFIDELDSVGGKRI 448
Cdd:cd19506  25 LVKSLLLAGPSGVGKKMLVHAICTETGANLFNLSPSNIAGKYPGKNGLQmmLHLVLKVARQLQPSVIWIGDAEKTFYKKV 104

                        90       100       110       120
                ....*....|....*....|....*....|....*....|.
gi 46397258 449 ---ESPMHPYS-RQTINQLLAEMdgfKPNEGVIIIGATNFP 485
Cdd:cd19506 105 pktEKQLDPKRlKKDLPKILKSL---KPEDRVLIVGTTSRP 142
ExeA COG3267
Type II secretory pathway ATPase component GspA/ExeA/MshM [Intracellular trafficking, ...
 375-439 7.64e-03

Type II secretory pathway ATPase component GspA/ExeA/MshM [Intracellular trafficking, secretion, and vesicular transport, Extracellular structures];


Pssm-ID: 442498 [Multi-domain]  Cd Length: 261  Bit Score: 39.00  E-value: 7.64e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46397258 375 ILLVGPPGTGKTLLARAVAGE-------ADVPFYYASGSEFDEMF---VGVGASRI----------RNLFREAKANAPCV 434
Cdd:COG3267  46 VVLTGEVGTGKTTLLRRLLERlpddvkvAYIPNPQLSPAELLRAIadeLGLEPKGAskadllrqlqEFLLELAAAGRRVV 125


                ....*
gi 46397258 435 IFIDE 439
Cdd:COG3267 126 LIIDE 130
DnaC COG1484
DNA replication protein DnaC [Replication, recombination and repair];
373-440 8.59e-03

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


Pssm-ID: 441093 [Multi-domain]  Cd Length: 242  Bit Score: 38.61  E-value: 8.59e-03
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 46397258 373 KGILLVGPPGTGKTLLARAVAGEA-----DVPFYYASgSEFDEMfvgVGASRIRNLFREAK--ANAPCVIfIDEL 440
Cdd:COG1484 100 ENLILLGPPGTGKTHLAIALGHEAcragyRVRFTTAP-DLVNEL---KEARADGRLERLLKrlAKVDLLI-LDEL 169
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH