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Conserved domains on  [gi|767959635|ref|XP_011517602|]
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ATP-dependent zinc metalloprotease YME1L1 isoform X1 [Homo sapiens]

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
Gene Ontology:  GO:0004176|GO:0004222|GO:0016020|GO:0005524
MEROPS:  M41
PubMed:  10788805|29097521|31988523|22498346|16966379|19656850
SCOP:  4001627

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
HflB COG0465
ATP-dependent Zn proteases [Posttranslational modification, protein turnover, chaperones];
299-734 0e+00

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


:

Pssm-ID: 440233 [Multi-domain]  Cd Length: 583  Bit Score: 699.87  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767959635 299 QMKNVTFEHVKGVEEAKQELQEVVEFLKNPQKFTILGGKLPKGILLVGPPGTGKTLLARAVAGEADVPFYYASGSEFDEM 378
Cdd:COG0465  135 DKPKVTFDDVAGVDEAKEELQEIVDFLKDPEKFTRLGAKIPKGVLLVGPPGTGKTLLAKAVAGEAGVPFFSISGSDFVEM 214

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767959635 379 FVGVGASRIRNLFREAKANAPCVIFIDELDSVGGKRIESPM--HPYSRQTINQLLAEMDGFKPNEGVIIIGATNFPEALD 456
Cdd:COG0465  215 FVGVGASRVRDLFEQAKKNAPCIIFIDEIDAVGRQRGAGLGggHDEREQTLNQLLVEMDGFEGNEGVIVIAATNRPDVLD 294

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767959635 457 NALIRPGRFDMQVTVPRPDVKGRTEILKWYLNKIKFDQSVDPEIIARGTVGFSGAELENLVNQAALKAAVDGKEMVTMKE 536
Cdd:COG0465  295 PALLRPGRFDRQVVVDLPDVKGREAILKVHARKKPLAPDVDLEVIARRTPGFSGADLANLVNEAALLAARRNKKAVTMED 374

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767959635 537 LEFSKDKILMGPERRSVEIDNKNKTITAYHESGHAIIAYYTKDAMPINKATIMPRGPTLGHVSLLPENDRWNETRAQLLA 616
Cdd:COG0465  375 FEEAIDRVIAGPERKSRVISEKEKKITAYHEAGHALVAALLPGADPVHKVTIIPRGRALGYTMQLPEEDRYLYTKEELLD 454

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767959635 617 QMDVSMGGRVAEELIFGtdHITTGASSDFDNATKIAKRMVTKFGMSEKLGVMTYSDTG-------------KLSPETQSA 683
Cdd:COG0465  455 RIAVLLGGRAAEELVFG--EVTTGASNDLERATKIARAMVTEYGMSEKLGPVAYGESEgevflgrdigqsrNYSEETARE 532

                        410       420       430       440       450
                 ....*....|....*....|....*....|....*....|....*....|.
gi 767959635 684 IEQEIRILLRDSYERAKHILKTHAKEHKNLAEALLTYETLDAKEIQIVLEG 734
Cdd:COG0465  533 IDEEVRRIIDEAYERAKEILTENRDKLDALAEALLEKETLDGEELEEILAG 583
 
Name Accession Description Interval E-value
HflB COG0465
ATP-dependent Zn proteases [Posttranslational modification, protein turnover, chaperones];
299-734 0e+00

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


Pssm-ID: 440233 [Multi-domain]  Cd Length: 583  Bit Score: 699.87  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767959635 299 QMKNVTFEHVKGVEEAKQELQEVVEFLKNPQKFTILGGKLPKGILLVGPPGTGKTLLARAVAGEADVPFYYASGSEFDEM 378
Cdd:COG0465  135 DKPKVTFDDVAGVDEAKEELQEIVDFLKDPEKFTRLGAKIPKGVLLVGPPGTGKTLLAKAVAGEAGVPFFSISGSDFVEM 214

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767959635 379 FVGVGASRIRNLFREAKANAPCVIFIDELDSVGGKRIESPM--HPYSRQTINQLLAEMDGFKPNEGVIIIGATNFPEALD 456
Cdd:COG0465  215 FVGVGASRVRDLFEQAKKNAPCIIFIDEIDAVGRQRGAGLGggHDEREQTLNQLLVEMDGFEGNEGVIVIAATNRPDVLD 294

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767959635 457 NALIRPGRFDMQVTVPRPDVKGRTEILKWYLNKIKFDQSVDPEIIARGTVGFSGAELENLVNQAALKAAVDGKEMVTMKE 536
Cdd:COG0465  295 PALLRPGRFDRQVVVDLPDVKGREAILKVHARKKPLAPDVDLEVIARRTPGFSGADLANLVNEAALLAARRNKKAVTMED 374

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767959635 537 LEFSKDKILMGPERRSVEIDNKNKTITAYHESGHAIIAYYTKDAMPINKATIMPRGPTLGHVSLLPENDRWNETRAQLLA 616
Cdd:COG0465  375 FEEAIDRVIAGPERKSRVISEKEKKITAYHEAGHALVAALLPGADPVHKVTIIPRGRALGYTMQLPEEDRYLYTKEELLD 454

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767959635 617 QMDVSMGGRVAEELIFGtdHITTGASSDFDNATKIAKRMVTKFGMSEKLGVMTYSDTG-------------KLSPETQSA 683
Cdd:COG0465  455 RIAVLLGGRAAEELVFG--EVTTGASNDLERATKIARAMVTEYGMSEKLGPVAYGESEgevflgrdigqsrNYSEETARE 532

                        410       420       430       440       450
                 ....*....|....*....|....*....|....*....|....*....|.
gi 767959635 684 IEQEIRILLRDSYERAKHILKTHAKEHKNLAEALLTYETLDAKEIQIVLEG 734
Cdd:COG0465  533 IDEEVRRIIDEAYERAKEILTENRDKLDALAEALLEKETLDGEELEEILAG 583
FtsH_fam TIGR01241
ATP-dependent metalloprotease FtsH; HflB(FtsH) is a pleiotropic protein required for correct ...
 300-733 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: 618.53  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767959635  300 MKNVTFEHVKGVEEAKQELQEVVEFLKNPQKFTILGGKLPKGILLVGPPGTGKTLLARAVAGEADVPFYYASGSEFDEMF 379
Cdd:TIGR01241  49 KPKVTFKDVAGIDEAKEELMEIVDFLKNPSKFTKLGAKIPKGVLLVGPPGTGKTLLAKAVAGEAGVPFFSISGSDFVEMF 128

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767959635  380 VGVGASRIRNLFREAKANAPCVIFIDELDSVGGKR--IESPMHPYSRQTINQLLAEMDGFKPNEGVIIIGATNFPEALDN 457
Cdd:TIGR01241 129 VGVGASRVRDLFEQAKKNAPCIIFIDEIDAVGRQRgaGLGGGNDEREQTLNQLLVEMDGFGTNTGVIVIAATNRPDVLDP 208

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767959635  458 ALIRPGRFDMQVTVPRPDVKGRTEILKWYLNKIKFDQSVDPEIIARGTVGFSGAELENLVNQAALKAAVDGKEMVTMKEL 537
Cdd:TIGR01241 209 ALLRPGRFDRQVVVDLPDIKGREEILKVHAKNKKLAPDVDLKAVARRTPGFSGADLANLLNEAALLAARKNKTEITMNDI 288

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767959635  538 EFSKDKILMGPERRSVEIDNKNKTITAYHESGHAIIAYYTKDAMPINKATIMPRGPTLGHVSLLPENDRWNETRAQLLAQ 617
Cdd:TIGR01241 289 EEAIDRVIAGPEKKSRVISEKEKKLVAYHEAGHALVGLLLKDADPVHKVTIIPRGQALGYTQFLPEEDKYLYTKSQLLAQ 368

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767959635  618 MDVSMGGRVAEELIFGtdHITTGASSDFDNATKIAKRMVTKFGMSEKLGVMTYSDTGK-------------LSPETQSAI 684
Cdd:TIGR01241 369 IAVLLGGRAAEEIIFG--EVTTGASNDIKQATNIARAMVTEWGMSDKLGPVAYGSDGGdvflgrgfakakeYSEETAREI 446

                         410       420       430       440
                  ....*....|....*....|....*....|....*....|....*....
gi 767959635  685 EQEIRILLRDSYERAKHILKTHAKEHKNLAEALLTYETLDAKEIQIVLE 733
Cdd:TIGR01241 447 DEEVKRIIEEAYKRAKQILTENRDELELLAKALLEKETITREEIKELLA 495
hflB PRK10733
ATP-dependent zinc metalloprotease FtsH;
299-740 4.18e-161

ATP-dependent zinc metalloprotease FtsH;


Pssm-ID: 182683 [Multi-domain]  Cd Length: 644  Bit Score: 480.30  E-value: 4.18e-161
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767959635 299 QMKNvTFEHVKGVEEAKQELQEVVEFLKNPQKFTILGGKLPKGILLVGPPGTGKTLLARAVAGEADVPFYYASGSEFDEM 378
Cdd:PRK10733 146 QIKT-TFADVAGCDEAKEEVAELVEYLREPSRFQKLGGKIPKGVLMVGPPGTGKTLLAKAIAGEAKVPFFTISGSDFVEM 224

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767959635 379 FVGVGASRIRNLFREAKANAPCVIFIDELDSVGGKRIES--PMHPYSRQTINQLLAEMDGFKPNEGVIIIGATNFPEALD 456
Cdd:PRK10733 225 FVGVGASRVRDMFEQAKKAAPCIIFIDEIDAVGRQRGAGlgGGHDEREQTLNQMLVEMDGFEGNEGIIVIAATNRPDVLD 304

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767959635 457 NALIRPGRFDMQVTVPRPDVKGRTEILKWYLNKIKFDQSVDPEIIARGTVGFSGAELENLVNQAALKAAVDGKEMVTMKE 536
Cdd:PRK10733 305 PALLRPGRFDRQVVVGLPDVRGREQILKVHMRRVPLAPDIDAAIIARGTPGFSGADLANLVNEAALFAARGNKRVVSMVE 384

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767959635 537 LEFSKDKILMGPERRSVEIDNKNKTITAYHESGHAIIAYYTKDAMPINKATIMPRGPTLGHVSLLPENDRWNETRAQLLA 616
Cdd:PRK10733 385 FEKAKDKIMMGAERRSMVMTEAQKESTAYHEAGHAIIGRLVPEHDPVHKVTIIPRGRALGVTFFLPEGDAISASRQKLES 464

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767959635 617 QMDVSMGGRVAEELIFGTDHITTGASSDFDNATKIAKRMVTKFGMSEKLGVMTYSD-------------TGKLSPETQSA 683
Cdd:PRK10733 465 QISTLYGGRLAEEIIYGPEHVSTGASNDIKVATNLARNMVTQWGFSEKLGPLLYAEeegevflgrsvakAKHMSDETARI 544

                        410       420       430       440       450
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 767959635 684 IEQEIRILLRDSYERAKHILKTHAKEHKNLAEALLTYETLDAKEIQIVLEGKklEVR 740
Cdd:PRK10733 545 IDQEVKALIERNYNRARQLLTDNMDILHAMKDALMKYETIDAPQIDDLMARR--DVR 599
RecA-like_FtsH cd19501
ATP-dependent zinc metalloprotease FtsH; FtsH ATPase is a processive, ATP-dependent zinc ...
 303-471 3.85e-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: 315.71  E-value: 3.85e-104
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767959635 303 VTFEHVKGVEEAKQELQEVVEFLKNPQKFTILGGKLPKGILLVGPPGTGKTLLARAVAGEADVPFYYASGSEFDEMFVGV 382
Cdd:cd19501    1 VTFKDVAGCEEAKEELKEVVEFLKNPEKFTKLGAKIPKGVLLVGPPGTGKTLLAKAVAGEAGVPFFSISGSDFVEMFVGV 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767959635 383 GASRIRNLFREAKANAPCVIFIDELDSVGGKR--IESPMHPYSRQTINQLLAEMDGFKPNEGVIIIGATNFPEALDNALI 460
Cdd:cd19501   81 GASRVRDLFEQAKKNAPCIVFIDEIDAVGRKRgaGLGGGHDEREQTLNQLLVEMDGFESNTGVIVIAATNRPDVLDPALL 160

                        170
                 ....*....|.
gi 767959635 461 RPGRFDMQVTV 471
Cdd:cd19501  161 RPGRFDRQVYV 171
Peptidase_M41 pfam01434
Peptidase family M41;
553-731 2.40e-86

Peptidase family M41;


Pssm-ID: 460210 [Multi-domain]  Cd Length: 190  Bit Score: 270.24  E-value: 2.40e-86
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767959635  553 VEIDNKNKTITAYHESGHAIIAYYTKDAMPINKATIMPRGPTLGHVSLLPENDRWNETRAQLLAQMDVSMGGRVAEELIF 632
Cdd:pfam01434   1 RVISEEEKKIVAYHEAGHALVGLLLPGADPVHKVTIIPRGQALGYTQFLPEEDKLLYTKEQLLARIAVLLGGRAAEELIF 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767959635  633 GtdHITTGASSDFDNATKIAKRMVTKFGMSEKLGVMTYSDTG-------------KLSPETQSAIEQEIRILLRDSYERA 699
Cdd:pfam01434  81 G--EVTTGASNDLEKATKIARQMVTEFGMSDKLGPVSLEESDgnvflgrgmgkrkPYSEETADIIDEEVKRLLEEAYERA 158

                         170       180       190
                  ....*....|....*....|....*....|..
gi 767959635  700 KHILKTHAKEHKNLAEALLTYETLDAKEIQIV 731
Cdd:pfam01434 159 KEILTEHRDELEALAEALLEKETLDAEEIREL 190
AAA smart00382
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ...
 339-475 6.25e-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: 81.27  E-value: 6.25e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767959635   339 PKGILLVGPPGTGKTLLARAVAGEADVP---FYYASGSEFDE--------------MFVGVGASRIRNLFREAKANAPCV 401
Cdd:smart00382   2 GEVILIVGPPGSGKTTLARALARELGPPgggVIYIDGEDILEevldqllliivggkKASGSGELRLRLALALARKLKPDV 81

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 767959635   402 IFIDELDSVGGKRIESPMhpysrqTINQLLAEMDGFKPNEGVIIIGATNFPEALDNALIRPgRFDMQVTVPRPD 475
Cdd:smart00382  82 LILDEITSLLDAEQEALL------LLLEELRLLLLLKSEKNLTVILTTNDEKDLGPALLRR-RFDRRIVLLLIL 148
 
Name Accession Description Interval E-value
HflB COG0465
ATP-dependent Zn proteases [Posttranslational modification, protein turnover, chaperones];
299-734 0e+00

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


Pssm-ID: 440233 [Multi-domain]  Cd Length: 583  Bit Score: 699.87  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767959635 299 QMKNVTFEHVKGVEEAKQELQEVVEFLKNPQKFTILGGKLPKGILLVGPPGTGKTLLARAVAGEADVPFYYASGSEFDEM 378
Cdd:COG0465  135 DKPKVTFDDVAGVDEAKEELQEIVDFLKDPEKFTRLGAKIPKGVLLVGPPGTGKTLLAKAVAGEAGVPFFSISGSDFVEM 214

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767959635 379 FVGVGASRIRNLFREAKANAPCVIFIDELDSVGGKRIESPM--HPYSRQTINQLLAEMDGFKPNEGVIIIGATNFPEALD 456
Cdd:COG0465  215 FVGVGASRVRDLFEQAKKNAPCIIFIDEIDAVGRQRGAGLGggHDEREQTLNQLLVEMDGFEGNEGVIVIAATNRPDVLD 294

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767959635 457 NALIRPGRFDMQVTVPRPDVKGRTEILKWYLNKIKFDQSVDPEIIARGTVGFSGAELENLVNQAALKAAVDGKEMVTMKE 536
Cdd:COG0465  295 PALLRPGRFDRQVVVDLPDVKGREAILKVHARKKPLAPDVDLEVIARRTPGFSGADLANLVNEAALLAARRNKKAVTMED 374

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767959635 537 LEFSKDKILMGPERRSVEIDNKNKTITAYHESGHAIIAYYTKDAMPINKATIMPRGPTLGHVSLLPENDRWNETRAQLLA 616
Cdd:COG0465  375 FEEAIDRVIAGPERKSRVISEKEKKITAYHEAGHALVAALLPGADPVHKVTIIPRGRALGYTMQLPEEDRYLYTKEELLD 454

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767959635 617 QMDVSMGGRVAEELIFGtdHITTGASSDFDNATKIAKRMVTKFGMSEKLGVMTYSDTG-------------KLSPETQSA 683
Cdd:COG0465  455 RIAVLLGGRAAEELVFG--EVTTGASNDLERATKIARAMVTEYGMSEKLGPVAYGESEgevflgrdigqsrNYSEETARE 532

                        410       420       430       440       450
                 ....*....|....*....|....*....|....*....|....*....|.
gi 767959635 684 IEQEIRILLRDSYERAKHILKTHAKEHKNLAEALLTYETLDAKEIQIVLEG 734
Cdd:COG0465  533 IDEEVRRIIDEAYERAKEILTENRDKLDALAEALLEKETLDGEELEEILAG 583
FtsH_fam TIGR01241
ATP-dependent metalloprotease FtsH; HflB(FtsH) is a pleiotropic protein required for correct ...
 300-733 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: 618.53  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767959635  300 MKNVTFEHVKGVEEAKQELQEVVEFLKNPQKFTILGGKLPKGILLVGPPGTGKTLLARAVAGEADVPFYYASGSEFDEMF 379
Cdd:TIGR01241  49 KPKVTFKDVAGIDEAKEELMEIVDFLKNPSKFTKLGAKIPKGVLLVGPPGTGKTLLAKAVAGEAGVPFFSISGSDFVEMF 128

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767959635  380 VGVGASRIRNLFREAKANAPCVIFIDELDSVGGKR--IESPMHPYSRQTINQLLAEMDGFKPNEGVIIIGATNFPEALDN 457
Cdd:TIGR01241 129 VGVGASRVRDLFEQAKKNAPCIIFIDEIDAVGRQRgaGLGGGNDEREQTLNQLLVEMDGFGTNTGVIVIAATNRPDVLDP 208

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767959635  458 ALIRPGRFDMQVTVPRPDVKGRTEILKWYLNKIKFDQSVDPEIIARGTVGFSGAELENLVNQAALKAAVDGKEMVTMKEL 537
Cdd:TIGR01241 209 ALLRPGRFDRQVVVDLPDIKGREEILKVHAKNKKLAPDVDLKAVARRTPGFSGADLANLLNEAALLAARKNKTEITMNDI 288

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767959635  538 EFSKDKILMGPERRSVEIDNKNKTITAYHESGHAIIAYYTKDAMPINKATIMPRGPTLGHVSLLPENDRWNETRAQLLAQ 617
Cdd:TIGR01241 289 EEAIDRVIAGPEKKSRVISEKEKKLVAYHEAGHALVGLLLKDADPVHKVTIIPRGQALGYTQFLPEEDKYLYTKSQLLAQ 368

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767959635  618 MDVSMGGRVAEELIFGtdHITTGASSDFDNATKIAKRMVTKFGMSEKLGVMTYSDTGK-------------LSPETQSAI 684
Cdd:TIGR01241 369 IAVLLGGRAAEEIIFG--EVTTGASNDIKQATNIARAMVTEWGMSDKLGPVAYGSDGGdvflgrgfakakeYSEETAREI 446

                         410       420       430       440
                  ....*....|....*....|....*....|....*....|....*....
gi 767959635  685 EQEIRILLRDSYERAKHILKTHAKEHKNLAEALLTYETLDAKEIQIVLE 733
Cdd:TIGR01241 447 DEEVKRIIEEAYKRAKQILTENRDELELLAKALLEKETITREEIKELLA 495
hflB PRK10733
ATP-dependent zinc metalloprotease FtsH;
299-740 4.18e-161

ATP-dependent zinc metalloprotease FtsH;


Pssm-ID: 182683 [Multi-domain]  Cd Length: 644  Bit Score: 480.30  E-value: 4.18e-161
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767959635 299 QMKNvTFEHVKGVEEAKQELQEVVEFLKNPQKFTILGGKLPKGILLVGPPGTGKTLLARAVAGEADVPFYYASGSEFDEM 378
Cdd:PRK10733 146 QIKT-TFADVAGCDEAKEEVAELVEYLREPSRFQKLGGKIPKGVLMVGPPGTGKTLLAKAIAGEAKVPFFTISGSDFVEM 224

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767959635 379 FVGVGASRIRNLFREAKANAPCVIFIDELDSVGGKRIES--PMHPYSRQTINQLLAEMDGFKPNEGVIIIGATNFPEALD 456
Cdd:PRK10733 225 FVGVGASRVRDMFEQAKKAAPCIIFIDEIDAVGRQRGAGlgGGHDEREQTLNQMLVEMDGFEGNEGIIVIAATNRPDVLD 304

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767959635 457 NALIRPGRFDMQVTVPRPDVKGRTEILKWYLNKIKFDQSVDPEIIARGTVGFSGAELENLVNQAALKAAVDGKEMVTMKE 536
Cdd:PRK10733 305 PALLRPGRFDRQVVVGLPDVRGREQILKVHMRRVPLAPDIDAAIIARGTPGFSGADLANLVNEAALFAARGNKRVVSMVE 384

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767959635 537 LEFSKDKILMGPERRSVEIDNKNKTITAYHESGHAIIAYYTKDAMPINKATIMPRGPTLGHVSLLPENDRWNETRAQLLA 616
Cdd:PRK10733 385 FEKAKDKIMMGAERRSMVMTEAQKESTAYHEAGHAIIGRLVPEHDPVHKVTIIPRGRALGVTFFLPEGDAISASRQKLES 464

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767959635 617 QMDVSMGGRVAEELIFGTDHITTGASSDFDNATKIAKRMVTKFGMSEKLGVMTYSD-------------TGKLSPETQSA 683
Cdd:PRK10733 465 QISTLYGGRLAEEIIYGPEHVSTGASNDIKVATNLARNMVTQWGFSEKLGPLLYAEeegevflgrsvakAKHMSDETARI 544

                        410       420       430       440       450
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 767959635 684 IEQEIRILLRDSYERAKHILKTHAKEHKNLAEALLTYETLDAKEIQIVLEGKklEVR 740
Cdd:PRK10733 545 IDQEVKALIERNYNRARQLLTDNMDILHAMKDALMKYETIDAPQIDDLMARR--DVR 599
ftsH CHL00176
cell division protein; Validated
 301-733 7.03e-161

cell division protein; Validated


Pssm-ID: 214386 [Multi-domain]  Cd Length: 638  Bit Score: 479.55  E-value: 7.03e-161
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767959635 301 KNVTFEHVKGVEEAKQELQEVVEFLKNPQKFTILGGKLPKGILLVGPPGTGKTLLARAVAGEADVPFYYASGSEFDEMFV 380
Cdd:CHL00176 178 TGITFRDIAGIEEAKEEFEEVVSFLKKPERFTAVGAKIPKGVLLVGPPGTGKTLLAKAIAGEAEVPFFSISGSEFVEMFV 257

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767959635 381 GVGASRIRNLFREAKANAPCVIFIDELDSVG---GKRIESPMHPySRQTINQLLAEMDGFKPNEGVIIIGATNFPEALDN 457
Cdd:CHL00176 258 GVGAARVRDLFKKAKENSPCIVFIDEIDAVGrqrGAGIGGGNDE-REQTLNQLLTEMDGFKGNKGVIVIAATNRVDILDA 336

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767959635 458 ALIRPGRFDMQVTVPRPDVKGRTEILKWYLNKIKFDQSVDPEIIARGTVGFSGAELENLVNQAALKAAVDGKEMVTMKEL 537
Cdd:CHL00176 337 ALLRPGRFDRQITVSLPDREGRLDILKVHARNKKLSPDVSLELIARRTPGFSGADLANLLNEAAILTARRKKATITMKEI 416

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767959635 538 EFSKDKILMGPERRSVEiDNKNKTITAYHESGHAIIAYYTKDAMPINKATIMPRGPTLGHVSLLPENDRWNETRAQLLAQ 617
Cdd:CHL00176 417 DTAIDRVIAGLEGTPLE-DSKNKRLIAYHEVGHAIVGTLLPNHDPVQKVTLIPRGQAKGLTWFTPEEDQSLVSRSQILAR 495

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767959635 618 MDVSMGGRVAEELIFGTDHITTGASSDFDNATKIAKRMVTKFGMSeKLGVMTYSDTG--------------KLSPETQSA 683
Cdd:CHL00176 496 IVGALGGRAAEEVVFGSTEVTTGASNDLQQVTNLARQMVTRFGMS-SIGPISLESNNstdpflgrfmqrnsEYSEEIADK 574

                        410       420       430       440       450
                 ....*....|....*....|....*....|....*....|....*....|
gi 767959635 684 IEQEIRILLRDSYERAKHILKTHAKEHKNLAEALLTYETLDAKEIQIVLE 733
Cdd:CHL00176 575 IDMEVRSILHTCYQYAYQILKDNRVLIDLLVELLLQKETIDGDEFREIVN 624
RPT1 COG1222
ATP-dependent 26S proteasome regulatory subunit [Posttranslational modification, protein ...
 302-550 1.23e-105

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


Pssm-ID: 440835 [Multi-domain]  Cd Length: 326  Bit Score: 325.81  E-value: 1.23e-105
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767959635 302 NVTFEHVKGVEEAKQELQEVVE-FLKNPQKFTILGGKLPKGILLVGPPGTGKTLLARAVAGEADVPFYYASGSEFDEMFV 380
Cdd:COG1222   74 DVTFDDIGGLDEQIEEIREAVElPLKNPELFRKYGIEPPKGVLLYGPPGTGKTLLAKAVAGELGAPFIRVRGSELVSKYI 153

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767959635 381 GVGASRIRNLFREAKANAPCVIFIDELDSVGGKRIESPMHPYSRQTINQLLAEMDGFKPNEGVIIIGATNFPEALDNALI 460
Cdd:COG1222  154 GEGARNVREVFELAREKAPSIIFIDEIDAIAARRTDDGTSGEVQRTVNQLLAELDGFESRGDVLIIAATNRPDLLDPALL 233

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767959635 461 RPGRFDMQVTVPRPDVKGRTEILKWYLNKIKFDQSVDPEIIARGTVGFSGAELENLVNQAALKAAVDGKEMVTMKELEFS 540
Cdd:COG1222  234 RPGRFDRVIEVPLPDEEAREEILKIHLRDMPLADDVDLDKLAKLTEGFSGADLKAIVTEAGMFAIREGRDTVTMEDLEKA 313

                        250
                 ....*....|
gi 767959635 541 KDKILMGPER 550
Cdd:COG1222  314 IEKVKKKTET 323
RecA-like_FtsH cd19501
ATP-dependent zinc metalloprotease FtsH; FtsH ATPase is a processive, ATP-dependent zinc ...
 303-471 3.85e-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: 315.71  E-value: 3.85e-104
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767959635 303 VTFEHVKGVEEAKQELQEVVEFLKNPQKFTILGGKLPKGILLVGPPGTGKTLLARAVAGEADVPFYYASGSEFDEMFVGV 382
Cdd:cd19501    1 VTFKDVAGCEEAKEELKEVVEFLKNPEKFTKLGAKIPKGVLLVGPPGTGKTLLAKAVAGEAGVPFFSISGSDFVEMFVGV 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767959635 383 GASRIRNLFREAKANAPCVIFIDELDSVGGKR--IESPMHPYSRQTINQLLAEMDGFKPNEGVIIIGATNFPEALDNALI 460
Cdd:cd19501   81 GASRVRDLFEQAKKNAPCIVFIDEIDAVGRKRgaGLGGGHDEREQTLNQLLVEMDGFESNTGVIVIAATNRPDVLDPALL 160

                        170
                 ....*....|.
gi 767959635 461 RPGRFDMQVTV 471
Cdd:cd19501  161 RPGRFDRQVYV 171
Peptidase_M41 pfam01434
Peptidase family M41;
553-731 2.40e-86

Peptidase family M41;


Pssm-ID: 460210 [Multi-domain]  Cd Length: 190  Bit Score: 270.24  E-value: 2.40e-86
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767959635  553 VEIDNKNKTITAYHESGHAIIAYYTKDAMPINKATIMPRGPTLGHVSLLPENDRWNETRAQLLAQMDVSMGGRVAEELIF 632
Cdd:pfam01434   1 RVISEEEKKIVAYHEAGHALVGLLLPGADPVHKVTIIPRGQALGYTQFLPEEDKLLYTKEQLLARIAVLLGGRAAEELIF 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767959635  633 GtdHITTGASSDFDNATKIAKRMVTKFGMSEKLGVMTYSDTG-------------KLSPETQSAIEQEIRILLRDSYERA 699
Cdd:pfam01434  81 G--EVTTGASNDLEKATKIARQMVTEFGMSDKLGPVSLEESDgnvflgrgmgkrkPYSEETADIIDEEVKRLLEEAYERA 158

                         170       180       190
                  ....*....|....*....|....*....|..
gi 767959635  700 KHILKTHAKEHKNLAEALLTYETLDAKEIQIV 731
Cdd:pfam01434 159 KEILTEHRDELEALAEALLEKETLDAEEIREL 190
PRK03992 PRK03992
proteasome-activating nucleotidase; Provisional
 302-554 2.74e-81

proteasome-activating nucleotidase; Provisional


Pssm-ID: 179699 [Multi-domain]  Cd Length: 389  Bit Score: 264.39  E-value: 2.74e-81
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767959635 302 NVTFEHVKGVEEAKQELQEVVEF-LKNPQKFTILGGKLPKGILLVGPPGTGKTLLARAVAGEADVPFYYASGSEFDEMFV 380
Cdd:PRK03992 127 NVTYEDIGGLEEQIREVREAVELpLKKPELFEEVGIEPPKGVLLYGPPGTGKTLLAKAVAHETNATFIRVVGSELVQKFI 206

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767959635 381 GVGASRIRNLFREAKANAPCVIFIDELDSVGGKRIESpMHPYSRQ---TINQLLAEMDGFKPNEGVIIIGATNFPEALDN 457
Cdd:PRK03992 207 GEGARLVRELFELAREKAPSIIFIDEIDAIAAKRTDS-GTSGDREvqrTLMQLLAEMDGFDPRGNVKIIAATNRIDILDP 285

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767959635 458 ALIRPGRFDMQVTVPRPDVKGRTEILKWYLNKIKFDQSVDPEIIARGTVGFSGAELENLVNQAALKAAVDGKEMVTMKEL 537
Cdd:PRK03992 286 AILRPGRFDRIIEVPLPDEEGRLEILKIHTRKMNLADDVDLEELAELTEGASGADLKAICTEAGMFAIRDDRTEVTMEDF 365

                        250
                 ....*....|....*..
gi 767959635 538 EFSKDKILMGPERRSVE 554
Cdd:PRK03992 366 LKAIEKVMGKEEKDSME 382
SpoVK COG0464
AAA+-type ATPase, SpoVK/Ycf46/Vps4 family [Cell wall/membrane/envelope biogenesis, Cell cycle ...
 305-538 8.65e-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: 250.21  E-value: 8.65e-76
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767959635 305 FEHVKGVEEAKQELQEVVE-FLKNPQKFTILGGKLPKGILLVGPPGTGKTLLARAVAGEADVPFYYASGSEFDEMFVGVG 383
Cdd:COG0464  156 LDDLGGLEEVKEELRELVAlPLKRPELREEYGLPPPRGLLLYGPPGTGKTLLARALAGELGLPLIEVDLSDLVSKYVGET 235

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767959635 384 ASRIRNLFREAKANAPCVIFIDELDSVGGKRiESPMHPYSRQTINQLLAEMDGFkpNEGVIIIGATNFPEALDNALIRpg 463
Cdd:COG0464  236 EKNLREVFDKARGLAPCVLFIDEADALAGKR-GEVGDGVGRRVVNTLLTEMEEL--RSDVVVIAATNRPDLLDPALLR-- 310

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 767959635 464 RFDMQVTVPRPDVKGRTEILKWYLNKIKFDQSVDPEIIARGTVGFSGAELENLVNQAALKAAVDGKEMVTMKELE 538
Cdd:COG0464  311 RFDEIIFFPLPDAEERLEIFRIHLRKRPLDEDVDLEELAEATEGLSGADIRNVVRRAALQALRLGREPVTTEDLL 385
26Sp45 TIGR01242
26S proteasome subunit P45 family; Many proteins may score above the trusted cutoff because an ...
 302-545 4.72e-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: 238.93  E-value: 4.72e-72
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767959635  302 NVTFEHVKGVEEAKQELQEVVEF-LKNPQKFTILGGKLPKGILLVGPPGTGKTLLARAVAGEADVPFYYASGSEFDEMFV 380
Cdd:TIGR01242 118 NVSYEDIGGLEEQIREIREAVELpLKHPELFEEVGIEPPKGVLLYGPPGTGKTLLAKAVAHETNATFIRVVGSELVRKYI 197

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767959635  381 GVGASRIRNLFREAKANAPCVIFIDELDSVGGKRIESPM--HPYSRQTINQLLAEMDGFKPNEGVIIIGATNFPEALDNA 458
Cdd:TIGR01242 198 GEGARLVREIFELAKEKAPSIIFIDEIDAIAAKRTDSGTsgDREVQRTLMQLLAELDGFDPRGNVKVIAATNRPDILDPA 277

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767959635  459 LIRPGRFDMQVTVPRPDVKGRTEILKWYLNKIKFDQSVDPEIIARGTVGFSGAELENLVNQAALKAAVDGKEMVTMKELE 538
Cdd:TIGR01242 278 LLRPGRFDRIIEVPLPDFEGRLEILKIHTRKMKLAEDVDLEAIAKMTEGASGADLKAICTEAGMFAIREERDYVTMDDFI 357


                  ....*..
gi 767959635  539 FSKDKIL 545
Cdd:TIGR01242 358 KAVEKVL 364
COG1223 COG1223
Predicted ATPase, AAA+ superfamily [General function prediction only];
305-538 1.74e-64

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


Pssm-ID: 440836 [Multi-domain]  Cd Length: 246  Bit Score: 214.75  E-value: 1.74e-64
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767959635 305 FEHVKGVEEAKQELQEVVEFLK---NPQKFtilGGKLPKGILLVGPPGTGKTLLARAVAGEADVPFYYASGSEFDEMFVG 381
Cdd:COG1223    1 LDDVVGQEEAKKKLKLIIKELRrreNLRKF---GLWPPRKILFYGPPGTGKTMLAEALAGELKLPLLTVRLDSLIGSYLG 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767959635 382 VGASRIRNLFREAKaNAPCVIFIDELDSVGGKRIESPMHPYSRQTINQLLAEMDGFkpNEGVIIIGATNFPEALDNALIR 461
Cdd:COG1223   78 ETARNLRKLFDFAR-RAPCVIFFDEFDAIAKDRGDQNDVGEVKRVVNALLQELDGL--PSGSVVIAATNHPELLDSALWR 154

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 767959635 462 pgRFDMQVTVPRPDVKGRTEILKWYLNKIKFDQSVDPEIIARGTVGFSGAELENLVNQAALKAAVDGKEMVTMKELE 538
Cdd:COG1223  155 --RFDEVIEFPLPDKEERKEILELNLKKFPLPFELDLKKLAKKLEGLSGADIEKVLKTALKKAILEDREKVTKEDLE 229
CDC48 TIGR01243
AAA family ATPase, CDC48 subfamily; This subfamily of the AAA family ATPases includes two ...
 298-545 6.45e-63

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


Pssm-ID: 273521 [Multi-domain]  Cd Length: 733  Bit Score: 224.02  E-value: 6.45e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767959635  298 VQMKNVTFEHVKGVEEAKQELQEVVEF-LKNPQKFTILGGKLPKGILLVGPPGTGKTLLARAVAGEADVPFYYASGSEFD 376
Cdd:TIGR01243 445 VEVPNVRWSDIGGLEEVKQELREAVEWpLKHPEIFEKMGIRPPKGVLLFGPPGTGKTLLAKAVATESGANFIAVRGPEIL 524

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767959635  377 EMFVGVGASRIRNLFREAKANAPCVIFIDELDSVGGKRIESPMHPYSRQTINQLLAEMDGFKPNEGVIIIGATNFPEALD 456
Cdd:TIGR01243 525 SKWVGESEKAIREIFRKARQAAPAIIFFDEIDAIAPARGARFDTSVTDRIVNQLLTEMDGIQELSNVVVIAATNRPDILD 604

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767959635  457 NALIRPGRFDMQVTVPRPDVKGRTEILKWYLNKIKFDQSVDPEIIARGTVGFSGAELENLVNQAALKAAVDGKEMVTMKE 536
Cdd:TIGR01243 605 PALLRPGRFDRLILVPPPDEEARKEIFKIHTRSMPLAEDVDLEELAEMTEGYTGADIEAVCREAAMAALRESIGSPAKEK 684


                  ....*....
gi 767959635  537 LEFSKDKIL 545
Cdd:TIGR01243 685 LEVGEEEFL 693
RecA-like_protease cd19481
proteases similar to RecA; RecA-like NTPases. This family includes the NTP binding domain of ...
 314-471 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: 202.90  E-value: 2.11e-61
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767959635 314 AKQELQEVVEFLKNPQKFTILGGKLPKGILLVGPPGTGKTLLARAVAGEADVPFYYASGSEFDEMFVGVGASRIRNLFRE 393
Cdd:cd19481    1 LKASLREAVEAPRRGSRLRRYGLGLPKGILLYGPPGTGKTLLAKALAGELGLPLIVVKLSSLLSKYVGESEKNLRKIFER 80

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 767959635 394 AKANAPCVIFIDELDSVGGKRIESPMHPYSRQTINQLLAEMDGFKPNEGVIIIGATNFPEALDNALIRPGRFDMQVTV 471
Cdd:cd19481   81 ARRLAPCILFIDEIDAIGRKRDSSGESGELRRVLNQLLTELDGVNSRSKVLVIAATNRPDLLDPALLRPGRFDEVIEF 158
RecA-like_PAN_like cd19502
proteasome activating nucleotidase PAN and related proteasome subunits; This subfamily ...
 304-471 2.94e-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: 192.55  E-value: 2.94e-57
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767959635 304 TFEHVKGVEEAKQELQEVVEF-LKNPQKFTILGGKLPKGILLVGPPGTGKTLLARAVAGEADVPFYYASGSEFDEMFVGV 382
Cdd:cd19502    1 TYEDIGGLDEQIREIREVVELpLKHPELFEELGIEPPKGVLLYGPPGTGKTLLAKAVANHTDATFIRVVGSELVQKYIGE 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767959635 383 GASRIRNLFREAKANAPCVIFIDELDSVGGKRIESPMHPYS--RQTINQLLAEMDGFKPNEGVIIIGATNFPEALDNALI 460
Cdd:cd19502   81 GARLVRELFEMAREKAPSIIFIDEIDAIGAKRFDSGTGGDRevQRTMLELLNQLDGFDPRGNIKVIMATNRPDILDPALL 160

                        170
                 ....*....|.
gi 767959635 461 RPGRFDMQVTV 471
Cdd:cd19502  161 RPGRFDRKIEF 171
CDC48 TIGR01243
AAA family ATPase, CDC48 subfamily; This subfamily of the AAA family ATPases includes two ...
 303-524 1.11e-56

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: 206.30  E-value: 1.11e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767959635  303 VTFEHVKGVEEAKQELQEVVEF-LKNPQKFTILGGKLPKGILLVGPPGTGKTLLARAVAGEADVPFYYASGSEFDEMFVG 381
Cdd:TIGR01243 175 VTYEDIGGLKEAKEKIREMVELpMKHPELFEHLGIEPPKGVLLYGPPGTGKTLLAKAVANEAGAYFISINGPEIMSKYYG 254

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767959635  382 VGASRIRNLFREAKANAPCVIFIDELDSVGGKRiESPMHPYSRQTINQLLAEMDGFKPNEGVIIIGATNFPEALDNALIR 461
Cdd:TIGR01243 255 ESEERLREIFKEAEENAPSIIFIDEIDAIAPKR-EEVTGEVEKRVVAQLLTLMDGLKGRGRVIVIGATNRPDALDPALRR 333

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 767959635  462 PGRFDMQVTVPRPDVKGRTEILKWYLNKIKFDQSVDPEIIARGTVGFSGAELENLVNQAALKA 524
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 ...
 314-466 3.50e-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: 183.64  E-value: 3.50e-54
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767959635 314 AKQELQEVVEF-LKNPQKFTILGGKLPKGILLVGPPGTGKTLLARAVAGEADVPFYYASGSEFDEMFVGVGASRIRNLFR 392
Cdd:cd19511    1 VKRELKEAVEWpLKHPDAFKRLGIRPPKGVLLYGPPGCGKTLLAKALASEAGLNFISVKGPELFSKYVGESERAVREIFQ 80

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 767959635 393 EAKANAPCVIFIDELDSVGGKRIESPMHPYSRQTINQLLAEMDGFKPNEGVIIIGATNFPEALDNALIRPGRFD 466
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 ...
 308-469 4.47e-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: 180.95  E-value: 4.47e-53
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767959635 308 VKGVEEAKQELQEVVEF-LKNPQKFTILGGKLPKGILLVGPPGTGKTLLARAVAGEADVPFYYASGSEFDEMFVGVGASR 386
Cdd:cd19503    2 IGGLDEQIASLKELIELpLKYPELFRALGLKPPRGVLLHGPPGTGKTLLARAVANEAGANFLSISGPSIVSKYLGESEKN 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767959635 387 IRNLFREAKANAPCVIFIDELDSVGGKRiESPMHPYSRQTINQLLAEMDGFKPNEGVIIIGATNFPEALDNALIRPGRFD 466
Cdd:cd19503   82 LREIFEEARSHAPSIIFIDEIDALAPKR-EEDQREVERRVVAQLLTLMDGMSSRGKVVVIAATNRPDAIDPALRRPGRFD 160


                 ...
gi 767959635 467 MQV 469
Cdd:cd19503  161 REV 163
AAA pfam00004
ATPase family associated with various cellular activities (AAA); AAA family proteins often ...
 342-473 5.93e-51

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


Pssm-ID: 459627 [Multi-domain]  Cd Length: 130  Bit Score: 173.55  E-value: 5.93e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767959635  342 ILLVGPPGTGKTLLARAVAGEADVPFYYASGSEFDEMFVGVGASRIRNLFREAKANAPCVIFIDELDSVGGKRiESPMHP 421
Cdd:pfam00004   1 LLLYGPPGTGKTTLAKAVAKELGAPFIEISGSELVSKYVGESEKRLRELFEAAKKLAPCVIFIDEIDALAGSR-GSGGDS 79

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 767959635  422 YSRQTINQLLAEMDGFKPNEG-VIIIGATNFPEALDNALIrpGRFDMQVTVPR 473
Cdd:pfam00004  80 ESRRVVNQLLTELDGFTSSNSkVIVIAATNRPDKLDPALL--GRFDRIIEFPL 130
RecA-like_VCP_r2 cd19529
second of two ATPase domains of Valosin-containing protein-like ATPase (VAT) and similar ...
 314-471 6.54e-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: 174.61  E-value: 6.54e-51
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767959635 314 AKQELQEVVEF-LKNPQKFTILGGKLPKGILLVGPPGTGKTLLARAVAGEADVPFYYASGSEFDEMFVGVGASRIRNLFR 392
Cdd:cd19529    1 VKQELKEAVEWpLLKPEVFKRLGIRPPKGILLYGPPGTGKTLLAKAVATESNANFISVKGPELLSKWVGESEKAIREIFR 80

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 767959635 393 EAKANAPCVIFIDELDSVGGKRIESPMHPYSRQTINQLLAEMDGFKPNEGVIIIGATNFPEALDNALIRPGRFDMQVTV 471
Cdd:cd19529   81 KARQVAPCVIFFDEIDSIAPRRGTTGDSGVTERVVNQLLTELDGLEEMNGVVVIAATNRPDIIDPALLRAGRFDRLIYI 159
RecA-like_CDC48_r1-like cd19519
first of two ATPase domains of CDC48 and similar ATPase domains; CDC48 in yeast and p97 or VCP ...
 308-472 1.74e-48

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


Pssm-ID: 410927 [Multi-domain]  Cd Length: 166  Bit Score: 168.38  E-value: 1.74e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767959635 308 VKGVEEAKQELQEVVEF-LKNPQKFTILGGKLPKGILLVGPPGTGKTLLARAVAGEADVPFYYASGSEFDEMFVGVGASR 386
Cdd:cd19519    2 IGGCRKQLAQIREMVELpLRHPELFKAIGIKPPRGILLYGPPGTGKTLIARAVANETGAFFFLINGPEIMSKLAGESESN 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767959635 387 IRNLFREAKANAPCVIFIDELDSVGGKRiESPMHPYSRQTINQLLAEMDGFKPNEGVIIIGATNFPEALDNALIRPGRFD 466
Cdd:cd19519   82 LRKAFEEAEKNAPAIIFIDEIDAIAPKR-EKTHGEVERRIVSQLLTLMDGLKQRAHVIVMAATNRPNSIDPALRRFGRFD 160


                 ....*.
gi 767959635 467 MQVTVP 472
Cdd:cd19519  161 REIDIG 166
PTZ00361 PTZ00361
26 proteosome regulatory subunit 4-like protein; Provisional
 291-545 7.82e-48

26 proteosome regulatory subunit 4-like protein; Provisional


Pssm-ID: 185575 [Multi-domain]  Cd Length: 438  Bit Score: 175.34  E-value: 7.82e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767959635 291 LDSAVDP-VQMKNV------TFEHVKGVEEAKQELQEVVEF-LKNPQKFTILGGKLPKGILLVGPPGTGKTLLARAVAGE 362
Cdd:PTZ00361 161 LLDEVDPlVSVMKVdkapleSYADIGGLEQQIQEIKEAVELpLTHPELYDDIGIKPPKGVILYGPPGTGKTLLAKAVANE 240

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767959635 363 ADVPFYYASGSEFDEMFVGVGASRIRNLFREAKANAPCVIFIDELDSVGGKRIE--SPMHPYSRQTINQLLAEMDGFKPN 440
Cdd:PTZ00361 241 TSATFLRVVGSELIQKYLGDGPKLVRELFRVAEENAPSIVFIDEIDAIGTKRYDatSGGEKEIQRTMLELLNQLDGFDSR 320

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767959635 441 EGVIIIGATNFPEALDNALIRPGRFDMQVTVPRPDVKGRTEILKWYLNKIKFDQSVDPEIIARGTVGFSGAELENLVNQA 520
Cdd:PTZ00361 321 GDVKVIMATNRIESLDPALIRPGRIDRKIEFPNPDEKTKRRIFEIHTSKMTLAEDVDLEEFIMAKDELSGADIKAICTEA 400

                        250       260
                 ....*....|....*....|....*
gi 767959635 521 ALKAAVDGKEMVTMKELEFSKDKIL 545
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 ...
 307-469 1.32e-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: 160.65  E-value: 1.32e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767959635 307 HVKGVEEAKQELQEVVEFLK-NPQKFTILGGKLPKGILLVGPPGTGKTLLARAVAGEADVPFYYASGSEFDEMFVGVGAS 385
Cdd:cd19518    1 DIGGMDSTLKELCELLIHPIlPPEYFQHLGVEPPRGVLLHGPPGCGKTMLANAIAGELKVPFLKISATEIVSGVSGESEE 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767959635 386 RIRNLFREAKANAPCVIFIDELDSVGGKRiESPMHPYSRQTINQLLAEMDGFKPNE----GVIIIGATNFPEALDNALIR 461
Cdd:cd19518   81 KIRELFDQAISNAPCIVFIDEIDAITPKR-ESAQREMERRIVSQLLTCMDELNNEKtaggPVLVIGATNRPDSLDPALRR 159


                 ....*...
gi 767959635 462 PGRFDMQV 469
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 ...
 315-471 4.72e-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: 4.72e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767959635 315 KQELQEVVEF-LKNPQKFTILGGKLPKGILLVGPPGTGKTLLARAVAGEADVPFYYASGSEFDEMFVGVGASRIRNLFRE 393
Cdd:cd19528    2 KRELQELVQYpVEHPDKFLKFGMTPSKGVLFYGPPGCGKTLLAKAIANECQANFISVKGPELLTMWFGESEANVRDIFDK 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767959635 394 AKANAPCVIFIDELDSVGGKRIESPMHP--YSRQTINQLLAEMDGFKPNEGVIIIGATNFPEALDNALIRPGRFDMQVTV 471
Cdd:cd19528   82 ARAAAPCVLFFDELDSIAKARGGNIGDAggAADRVINQILTEMDGMNTKKNVFIIGATNRPDIIDPAILRPGRLDQLIYI 161
PTZ00454 PTZ00454
26S protease regulatory subunit 6B-like protein; Provisional
 292-538 2.11e-44

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


Pssm-ID: 240423 [Multi-domain]  Cd Length: 398  Bit Score: 164.55  E-value: 2.11e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767959635 292 DSAVDPVQMK---NVTFEHVKGVEEAKQELQEVVEF-LKNPQKFTILGGKLPKGILLVGPPGTGKTLLARAVAGEADVPF 367
Cdd:PTZ00454 128 DSSIQLLQMSekpDVTYSDIGGLDIQKQEIREAVELpLTCPELYEQIGIDPPRGVLLYGPPGTGKTMLAKAVAHHTTATF 207

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767959635 368 YYASGSEFDEMFVGVGASRIRNLFREAKANAPCVIFIDELDSVGGKRIESpmhpysrQT---------INQLLAEMDGFK 438
Cdd:PTZ00454 208 IRVVGSEFVQKYLGEGPRMVRDVFRLARENAPSIIFIDEVDSIATKRFDA-------QTgadrevqriLLELLNQMDGFD 280

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767959635 439 PNEGVIIIGATNFPEALDNALIRPGRFDMQVTVPRPDVKGRTEILKWYLNKIKFDQSVDPEIIARGTVGFSGAELENLVN 518
Cdd:PTZ00454 281 QTTNVKVIMATNRADTLDPALLRPGRLDRKIEFPLPDRRQKRLIFQTITSKMNLSEEVDLEDFVSRPEKISAADIAAICQ 360

                        250       260
                 ....*....|....*....|
gi 767959635 519 QAALKAAVDGKEMVTMKELE 538
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 ...
 311-471 2.12e-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: 148.40  E-value: 2.12e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767959635 311 VEEAKQELQ-EVVEFLKNPQKFTILGGKLPKGILLVGPPGTGKTLLARAVAGEADVPFYYASGSEFDEMFVGVGASRIRN 389
Cdd:cd19530    1 LDHVREELTmSILRPIKRPDIYKALGIDLPTGVLLYGPPGCGKTLLAKAVANESGANFISVKGPELLNKYVGESERAVRQ 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767959635 390 LFREAKANAPCVIFIDELDSVGGKRIESPMHPYSRqTINQLLAEMDGFKPNEGVIIIGATNFPEALDNALIRPGRFDMQV 469
Cdd:cd19530   81 VFQRARASAPCVIFFDEVDALVPKRGDGGSWASER-VVNQLLTEMDGLEERSNVFVIAATNRPDIIDPAMLRPGRLDKTL 159


                 ..
gi 767959635 470 TV 471
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 ...
 308-465 1.48e-40

ATPase domain of VPS4, ATAD1, K, KTNA1, Spastin, FIGL-1 and similar ATPase domains; This subfamily includes the ATPase domains of vacuolar protein sorting-associated protein 4 (VPS4), ATPase family AAA domain-containing protein 1 (ATAD1, also known as Thorase), Katanin p60 ATPase-containing subunit A1 (KTNA1), Spastin, and Fidgetin-Like 1 (FIGL-1). This subfamily belongs to the RecA-like NTPase family which includes the NTP binding domain of F1 and V1 H(+)ATPases, DnaB and related helicases as well as bacterial RecA and related eukaryotic and archaeal recombinases. The RecA-like NTPase family also includes bacterial conjugation proteins and related DNA transfer proteins involved in type II and type IV secretion.


Pssm-ID: 410917 [Multi-domain]  Cd Length: 163  Bit Score: 145.96  E-value: 1.48e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767959635 308 VKGVEEAKQELQEVVEF-LKNPQKFTiLGGKLPKGILLVGPPGTGKTLLARAVAGEADVPFYYASGSEFDEMFVGVGASR 386
Cdd:cd19509    1 IAGLDDAKEALKEAVILpSLRPDLFP-GLRGPPRGILLYGPPGTGKTLLARAVASESGSTFFSISASSLVSKWVGESEKI 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767959635 387 IRNLFREAKANAPCVIFIDELDSVGGKRIESPmHPYSRQTINQLLAEMDGF--KPNEGVIIIGATNFPEALDNALIRpgR 464
Cdd:cd19509   80 VRALFALARELQPSIIFIDEIDSLLSERGSGE-HEASRRVKTEFLVQMDGVlnKPEDRVLVLGATNRPWELDEAFLR--R 156


                 .
gi 767959635 465 F 465
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 ...
 314-469 2.15e-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: 2.15e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767959635 314 AKQELQEVVEF-LKNPQKFTILGGKLPKGILLVGPPGTGKTLLARAVAGEADVPFYYASGSEFDEMFVGVGASRIRNLFR 392
Cdd:cd19526    1 VKKALEETIEWpSKYPKIFASSPLRLRSGILLYGPPGCGKTLLASAIASECGLNFISVKGPELLNKYIGASEQNVRDLFS 80

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 767959635 393 EAKANAPCVIFIDELDSVGGKRIESPMHPYSRqTINQLLAEMDGFKPNEGVIIIGATNFPEALDNALIRPGRFDMQV 469
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 ...
 315-466 1.50e-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: 134.95  E-value: 1.50e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767959635 315 KQELQEVVEF-LKNPQKFTiLGGKLPKGILLVGPPGTGKTLLARAVAGEADVPFYYASGSEFDEMFVGVGASRIRNLFRE 393
Cdd:cd19527    2 KKEILDTIQLpLEHPELFS-SGLRKRSGILLYGPPGTGKTLLAKAIATECSLNFLSVKGPELINMYIGESEANVREVFQK 80

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 767959635 394 AKANAPCVIFIDELDSVGGKRIES-PMHPYSRQTINQLLAEMDGF-KPNEGVIIIGATNFPEALDNALIRPGRFD 466
Cdd:cd19527   81 ARDAKPCVIFFDELDSLAPSRGNSgDSGGVMDRVVSQLLAELDGMsSSGQDVFVIGATNRPDLLDPALLRPGRFD 155
RecA-like_VPS4 cd19521
ATPase domain of vacuolar protein sorting-associated protein 4; Vacuolar protein ...
 302-471 1.53e-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: 132.29  E-value: 1.53e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767959635 302 NVTFEHVKGVEEAKQELQEVVEF-LKNPQKFTilGGKLP-KGILLVGPPGTGKTLLARAVAGEADVPFYYASGSEFDEMF 379
Cdd:cd19521    3 NVKWEDVAGLEGAKEALKEAVILpVKFPHLFT--GNRKPwSGILLYGPPGTGKSYLAKAVATEANSTFFSVSSSDLVSKW 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767959635 380 VGVGASRIRNLFREAKANAPCVIFIDELDSVGGKRIESPMHPySRQTINQLLAEMDGF-KPNEGVIIIGATNFPEALDNA 458
Cdd:cd19521   81 MGESEKLVKQLFAMARENKPSIIFIDEVDSLCGTRGEGESEA-SRRIKTELLVQMNGVgNDSQGVLVLGATNIPWQLDSA 159

                        170
                 ....*....|...
gi 767959635 459 LIRpgRFDMQVTV 471
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; ...
 303-461 1.62e-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: 127.03  E-value: 1.62e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767959635 303 VTFEHVKGVEEAKQELQEVVEF-LKNPQKFTILGGKlPKGILLVGPPGTGKTLLARAVAGEADVPFYYASGSEFDEMFVG 381
Cdd:cd19525   19 INWADIAGLEFAKKTIKEIVVWpMLRPDIFTGLRGP-PKGILLFGPPGTGKTLIGKCIASQSGATFFSISASSLTSKWVG 97

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767959635 382 VGASRIRNLFREAKANAPCVIFIDELDSVGGKRIESPmHPYSRQTINQLLAEMDGFK--PNEGVIIIGATNFPEALDNAL 459
Cdd:cd19525   98 EGEKMVRALFSVARCKQPAVIFIDEIDSLLSQRGEGE-HESSRRIKTEFLVQLDGATtsSEDRILVVGATNRPQEIDEAA 176


                 ..
gi 767959635 460 IR 461
Cdd:cd19525  177 RR 178
pup_AAA TIGR03689
proteasome ATPase; In the Actinobacteria, as shown for Mycobacterium tuberculosis, some ...
 302-488 1.71e-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: 132.53  E-value: 1.71e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767959635  302 NVTFEHVKGVEEAKQELQEVVE--FLkNPQKFTILGGKLPKGILLVGPPGTGKTLLARAVA--------GEADVPFYYAS 371
Cdd:TIGR03689 178 DVTYADIGGLGSQIEQIRDAVElpFL-HPELYREYGLKPPKGVLLYGPPGCGKTLIAKAVAnslaarigAEGGGKSYFLN 256

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767959635  372 --GSEFDEMFVGVGASRIRNLFREAKANA----PCVIFIDELDSV---GGKRIESPMHpysrQTI-NQLLAEMDGFKPNE 441
Cdd:TIGR03689 257 ikGPELLNKYVGETERQIRLIFQRAREKAsegrPVIVFFDEMDSLfrtRGSGVSSDVE----TTVvPQLLAEIDGVESLD 332

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 767959635  442 GVIIIGATNFPEALDNALIRPGRFDMQVTVPRPDVKGRTEILKWYLN 488
Cdd:TIGR03689 333 NVIVIGASNREDMIDPAILRPGRLDVKIRIERPDAEAAADIFAKYLT 379
RecA-like_KTNA1 cd19522
Katanin p60 ATPase-containing subunit A1; Katanin p60 ATPase-containing subunit A1 (KTNA1) is ...
 308-461 7.55e-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: 7.55e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767959635 308 VKGVEEAKQELQE-VVEFLKNPQKFTilGGKLP-KGILLVGPPGTGKTLLARAVAGEADVPFYYASGSEFDEMFVGVGAS 385
Cdd:cd19522    2 IADLEEAKKLLEEaVVLPMWMPEFFK--GIRRPwKGVLMVGPPGTGKTLLAKAVATECGTTFFNVSSSTLTSKYRGESEK 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767959635 386 RIRNLFREAKANAPCVIFIDELDSVGGKRIESPMHPYSRQTINQLLAEMDGF-------KPNEGVIIIGATNFPEALDNA 458
Cdd:cd19522   80 LVRLLFEMARFYAPTTIFIDEIDSICSRRGTSEEHEASRRVKSELLVQMDGVggasendDPSKMVMVLAATNFPWDIDEA 159


                 ...
gi 767959635 459 LIR 461
Cdd:cd19522  160 LRR 162
RecA-like_spastin cd19524
ATPase domain of spastin; Spastin is an ATP-dependent microtubule-severing protein involved in ...
 308-471 3.17e-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: 119.95  E-value: 3.17e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767959635 308 VKGVEEAKQELQEVVEF-LKNPQKFTILGGKlPKGILLVGPPGTGKTLLARAVAGEADVPFYYASGSEFDEMFVGVGASR 386
Cdd:cd19524    2 IAGQDLAKQALQEMVILpSLRPELFTGLRAP-ARGLLLFGPPGNGKTMLAKAVAAESNATFFNISAASLTSKYVGEGEKL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767959635 387 IRNLFREAKANAPCVIFIDELDSVGGKRIESPmHPYSRQTINQLLAEMDGFK--PNEGVIIIGATNFPEALDNALIRpgR 464
Cdd:cd19524   81 VRALFAVARELQPSIIFIDEVDSLLSERSEGE-HEASRRLKTEFLIEFDGVQsnGDDRVLVMGATNRPQELDDAVLR--R 157


                 ....*..
gi 767959635 465 FDMQVTV 471
Cdd:cd19524  158 FTKRVYV 164
RecA-like_Yta7-like cd19517
ATPase domain of Saccharomyces cerevisiae Yta7 and similar ATPase domains; Saccharomyces ...
 308-466 3.27e-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: 119.92  E-value: 3.27e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767959635 308 VKGVEEAKQELQEVVEF-LKNPQKFTILGGKLPKGILLVGPPGTGKTLLARAVA-----GEADVPFYYASGSEFDEMFVG 381
Cdd:cd19517    2 IGGLSHYINQLKEMVFFpLLYPEVFAKFKITPPRGVLFHGPPGTGKTLMARALAaecskGGQKVSFFMRKGADCLSKWVG 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767959635 382 VGASRIRNLFREAKANAPCVIFIDELDSVGGKRiESPMHPYSRQTINQLLAEMDGFKPNEGVIIIGATNFPEALDNALIR 461
Cdd:cd19517   82 EAERQLRLLFEEAYRMQPSIIFFDEIDGLAPVR-SSKQEQIHASIVSTLLALMDGLDNRGQVVVIGATNRPDALDPALRR 160


                 ....*
gi 767959635 462 PGRFD 466
Cdd:cd19517  161 PGRFD 165
RecA-like_ATAD1 cd19520
ATPase domain of ATPase family AAA domain-containing protein 1 and similar ATPase domains; ...
 310-465 1.25e-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: 1.25e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767959635 310 GVEEAKQELQEVVEF-LKNPQKFTilGGKL---PKGILLVGPPGTGKTLLARAVAGEADVPFYYASGSEFDEMFVGVGAS 385
Cdd:cd19520    4 GLDEVITELKELVILpLQRPELFD--NSRLlqpPKGVLLYGPPGCGKTMLAKATAKEAGARFINLQVSSLTDKWYGESQK 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767959635 386 RIRNLFREAKANAPCVIFIDELDSVGGKRiESPMHPYSRQTINQLLAEMDGF--KPNEGVIIIGATNFPEALDNALIR-- 461
Cdd:cd19520   82 LVAAVFSLASKLQPSIIFIDEIDSFLRQR-SSTDHEATAMMKAEFMSLWDGLstDGNCRVIVMGATNRPQDLDEAILRrm 160


                 ....
gi 767959635 462 PGRF 465
Cdd:cd19520  161 PKRF 164
AAA cd00009
The AAA+ (ATPases Associated with a wide variety of cellular Activities) superfamily ...
 309-472 5.49e-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: 104.15  E-value: 5.49e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767959635 309 KGVEEAKQELQEVVEFLKnpqkftilggklPKGILLVGPPGTGKTLLARAVAGEA---DVPFYYASGSEFDEMFVG---V 382
Cdd:cd00009    1 VGQEEAIEALREALELPP------------PKNLLLYGPPGTGKTTLARAIANELfrpGAPFLYLNASDLLEGLVVaelF 68

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767959635 383 GASRIRNLFREAKANAPCVIFIDELDSVGGKRIEspmhpysrQTINQLLAEMDGFKPNEGVIIIGATNFPEALDNALIRP 462
Cdd:cd00009   69 GHFLVRLLFELAEKAKPGVLFIDEIDSLSRGAQN--------ALLRVLETLNDLRIDRENVRVIGATNRPLLGDLDRALY 140

                        170
                 ....*....|
gi 767959635 463 GRFDMQVTVP 472
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; ...
 334-471 5.86e-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: 102.18  E-value: 5.86e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767959635 334 LGGKLPKGILLVGPPGTGKTLLARAV-----AGEADVpfyyASGSEFDEMFVGVGASRIRNLFREAKANAPC-------- 400
Cdd:cd19504   30 LGCKHVKGILLYGPPGTGKTLMARQIgkmlnAREPKI----VNGPEILNKYVGESEANIRKLFADAEEEQRRlgansglh 105

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 767959635 401 VIFIDELDSV----GGKRIESPMHPysrQTINQLLAEMDGFKPNEGVIIIGATNFPEALDNALIRPGRFDMQVTV 471
Cdd:cd19504  106 IIIFDEIDAIckqrGSMAGSTGVHD---TVVNQLLSKIDGVEQLNNILVIGMTNRKDLIDEALLRPGRLEVQMEI 177
RecA-like_BCS1 cd19510
Mitochondrial chaperone BCS1; Mitochondrial chaperone BCS1 is necessary for the assembly of ...
 318-471 9.04e-21

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


Pssm-ID: 410918 [Multi-domain]  Cd Length: 153  Bit Score: 89.33  E-value: 9.04e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767959635 318 LQEVVEFLKNPQKFTILGGKLPKGILLVGPPGTGKTLLARAVAGEADVPFYYASGSEfdemfVGVGASRIRNLFREAKAN 397
Cdd:cd19510    2 IDDLKDFIKNEDWYNDRGIPYRRGYLLYGPPGTGKSSFIAALAGELDYDICDLNLSE-----VVLTDDRLNHLLNTAPKQ 76

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 767959635 398 ApcVIFIDELDSVGGKRIESPMHPY-----SRQTINQLLAEMDGFKPNEGVIIIGATNFPEALDNALIRPGRFDMQVTV 471
Cdd:cd19510   77 S--IILLEDIDAAFESREHNKKNPSaygglSRVTFSGLLNALDGVASSEERIVFMTTNHIERLDPALIRPGRVDMKIYM 153
RecA-like_fidgetin cd19523
ATPase domain of fidgetin; Fidgetin (FIGN) is a ATP-dependent microtubule severing protein. ...
 308-461 4.78e-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: 4.78e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767959635 308 VKGVEEAKQELQ-EVVEFLKNPQKFTILGgKLPKGILLVGPPGTGKTLLARAVAGEADVPFYYASGSEFDEMFVGVGASR 386
Cdd:cd19523    2 IAGLGALKAAIKeEVLWPLLRPDAFSGLL-RLPRSILLFGPRGTGKTLLGRCLASQLGATFLRLRGSTLVAKWAGEGEKI 80

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 767959635 387 IRNLFREAKANAPCVIFIDELDSVGGKRIESPmHPYSRQTInQLLAEMDGF--KPNEGVIIIGATNFPEALDNALIR 461
Cdd:cd19523   81 LQASFLAARCRQPSVLFISDLDALLSSQDDEA-SPVGRLQV-ELLAQLDGVlgSGEDGVLVVCTTSKPEEIDESLRR 155
ycf46 CHL00195
Ycf46; Provisional
 302-547 1.16e-18

Ycf46; Provisional


Pssm-ID: 177094 [Multi-domain]  Cd Length: 489  Bit Score: 89.69  E-value: 1.16e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767959635 302 NVTFEHVKGVEEAKQELQEVVE-FLKNPQKFtilGGKLPKGILLVGPPGTGKTLLARAVAGEADVPFYYAsgsEFDEMF- 379
Cdd:CHL00195 224 NEKISDIGGLDNLKDWLKKRSTsFSKQASNY---GLPTPRGLLLVGIQGTGKSLTAKAIANDWQLPLLRL---DVGKLFg 297

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767959635 380 --VGVGASRIRNLFREAKANAPCVIFIDELDsvggkRIESPMHPYSRQ-TINQLLAEM-----DGFKPnegVIIIGATNF 451
Cdd:CHL00195 298 giVGESESRMRQMIRIAEALSPCILWIDEID-----KAFSNSESKGDSgTTNRVLATFitwlsEKKSP---VFVVATANN 369

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767959635 452 PEALDNALIRPGRFDMQVTVPRPDVKGRTEILKWYLNKIKFD--QSVDPEIIARGTVGFSGAELENLVNQaALKAAVDGK 529
Cdd:CHL00195 370 IDLLPLEILRKGRFDEIFFLDLPSLEEREKIFKIHLQKFRPKswKKYDIKKLSKLSNKFSGAEIEQSIIE-AMYIAFYEK 448

                        250
                 ....*....|....*...
gi 767959635 530 EmvtmkelEFSKDKILMG 547
Cdd:CHL00195 449 R-------EFTTDDILLA 459
AAA smart00382
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ...
 339-475 6.25e-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: 81.27  E-value: 6.25e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767959635   339 PKGILLVGPPGTGKTLLARAVAGEADVP---FYYASGSEFDE--------------MFVGVGASRIRNLFREAKANAPCV 401
Cdd:smart00382   2 GEVILIVGPPGSGKTTLARALARELGPPgggVIYIDGEDILEevldqllliivggkKASGSGELRLRLALALARKLKPDV 81

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 767959635   402 IFIDELDSVGGKRIESPMhpysrqTINQLLAEMDGFKPNEGVIIIGATNFPEALDNALIRPgRFDMQVTVPRPD 475
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 ...
 338-466 4.54e-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: 76.25  E-value: 4.54e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767959635 338 LPKGILLVGPPGTGKTLLARAVAGEADVPFYYASGSEFDEMFVGVGASRIRNLFREAKANAPCVIFIDELDSVGGKRIES 417
Cdd:cd19507   30 TPKGLLLVGIQGTGKSLTAKAIAGVWQLPLLRLDMGRLFGGLVGESESRLRQMIQTAEAIAPCVLWIDEIEKGFSNADSK 109

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 767959635 418 PMHPYSRQTINQLLAEM-DGFKPnegVIIIGATNFPEALDNALIRPGRFD 466
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; ...
 334-466 3.12e-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: 62.39  E-value: 3.12e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767959635 334 LGGKLPKGILLVGPPGTGKTLLARAVAGEADVPFYYASGSEF--------------DEMFVGVGASRIRNLFREAKANAP 399
Cdd:cd19505    7 LGLSPSKGILLIGSIETGRSYLIKSLAANSYVPLIRISLNKLlynkpdfgnddwidGMLILKESLHRLNLQFELAKAMSP 86

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 767959635 400 CVIFID---ELDS--VGGKRIESPMhpYSRQTINQLLAEMDGFKPNEGVIIIGATNFPEALDNALIRPGRFD 466
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 ...
 340-469 7.18e-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: 57.92  E-value: 7.18e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767959635 340 KGILLVGPPGTGKTLLARAVAGEADVPFYYASGSEFDEMFVGvGASRIRNLFREA-KANAPCVIFIDELDSVGGKRIESP 418
Cdd:cd19512   23 RNILFYGPPGTGKTLFAKKLALHSGMDYAIMTGGDVAPMGRE-GVTAIHKVFDWAnTSRRGLLLFVDEADAFLRKRSTEK 101

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 767959635 419 MHPYSRQTINQLLAEMdGFKPNEGVIIIgATNFPEALDNALirPGRFDMQV 469
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 ...
 495-538 4.08e-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: 52.54  E-value: 4.08e-09
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 767959635  495 SVDPEIIARGTVGFSGAELENLVNQAALKAAVDGKEMVTMKELE 538
Cdd:pfam17862   1 DVDLEELAERTEGFSGADLEALCREAALAALRRGLEAVTQEDLE 44
PRK13342 PRK13342
recombination factor protein RarA; Reviewed
 333-406 7.84e-09

recombination factor protein RarA; Reviewed


Pssm-ID: 237355 [Multi-domain]  Cd Length: 413  Bit Score: 58.56  E-value: 7.84e-09
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 767959635 333 ILGGKLPKgILLVGPPGTGKTLLARAVAGEADVPFYYASGSefdemFVGVgaSRIRNLFREAKANA----PCVIFIDE 406
Cdd:PRK13342  31 IEAGRLSS-MILWGPPGTGKTTLARIIAGATDAPFEALSAV-----TSGV--KDLREVIEEARQRRsagrRTILFIDE 100
TIP49 COG1224
DNA helicase TIP49, TBP-interacting protein [Transcription];
310-375 1.28e-08

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


Pssm-ID: 440837 [Multi-domain]  Cd Length: 452  Bit Score: 58.06  E-value: 1.28e-08
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 767959635 310 GVEEAKQELQEVVEFLKNpqkftilgGKLP-KGILLVGPPGTGKTLLARAVAGE--ADVPFYYASGSEF 375
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 ...
 338-413 4.09e-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: 53.92  E-value: 4.09e-08
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 767959635 338 LPKGILLVGPPGTGKTLLARAVAGEADVPFYYASGSEFDEM-FVGVGA-SRIRNLfreakanAPCVIFIDELDSVGGK 413
Cdd:cd19498   45 TPKNILMIGPTGVGKTEIARRLAKLAGAPFIKVEATKFTEVgYVGRDVeSIIRDL-------VEGIVFIDEIDKIAKR 115
RecA-like_Lon cd19500
lon protease homolog 2 peroxisomal; Lon protease (also known as Lon peptidase) is an ...
 310-411 8.58e-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: 8.58e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767959635 310 GVEEAKQELQE--VVEFLKNPQKFTILggklpkgiLLVGPPGTGKTLLARAVAGEADVPFYYAS-GSEFDE--------M 378
Cdd:cd19500   14 GLEDVKERILEylAVRKLKGSMKGPIL--------CLVGPPGVGKTSLGKSIARALGRKFVRISlGGVRDEaeirghrrT 85

                         90       100       110
                 ....*....|....*....|....*....|...
gi 767959635 379 FVGVGASRIRNLFREAKANAPcVIFIDELDSVG 411
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 ...
 297-413 3.45e-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: 52.22  E-value: 3.45e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767959635 297 PVQMKNVTFEHVKGVEEAKQELQEVV----EFLKNPQKFTILGGKLPKG-ILLVGPPGTGKTLLARAVAGEADVPFYYAS 371
Cdd:cd19497    3 PKEIKEHLDKYVIGQERAKKVLSVAVynhyKRIRNNLKQKDDDVELEKSnILLIGPTGSGKTLLAQTLAKILDVPFAIAD 82

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 767959635 372 GSEFDEM-FVG--VgASRIRNLFREAKANAP----CVIFIDELDSVGGK 413
Cdd:cd19497   83 ATTLTEAgYVGedV-ENILLKLLQAADYDVEraqrGIVYIDEIDKIARK 130
RarA COG2256
Replication-associated recombination protein RarA (DNA-dependent ATPase) [Replication, ...
 333-406 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 767959635 333 ILGGKLPKgILLVGPPGTGKTLLARAVAGEADVPFYYASGsefdemfVGVGASRIRNLFREAKANA----PCVIFIDE 406
Cdd:COG2256   44 IEAGRLSS-MILWGPPGTGKTTLARLIANATDAEFVALSA-------VTSGVKDIREVIEEARERRaygrRTILFVDE 113
T7SS_EccA TIGR03922
type VII secretion AAA-ATPase EccA; This model represents the AAA family ATPase, EccA, of the ...
 310-527 5.85e-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: 5.85e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767959635  310 GVEEAKQElqevVEFLKNPQKFTIL----GGKLP---KGILLVGPPGTGKTLLARAVAgeadvpfyyasgsefdEMFVGV 382
Cdd:TIGR03922 280 GLERVKRQ----VAALKSSTAMALAraerGLPVAqtsNHMLFAGPPGTGKTTIARVVA----------------KIYCGL 339

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767959635  383 GASR---IRNLFR-----------EAKANAPC------VIFIDELDSVGGKRIESPmHPYSRQTINQLLAEMDGFKPNEG 442
Cdd:TIGR03922 340 GVLRkplVREVSRadligqyigesEAKTNEIIdsalggVLFLDEAYTLVETGYGQK-DPFGLEAIDTLLARMENDRDRLV 418

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767959635  443 VIIIGatnFPEALDNAL-IRPGrfdmqvtvprpdVKGRteilkwYLNKIKFDQSVDPEIIARGTVgfSGAELENLVNQAA 521
Cdd:TIGR03922 419 VIGAG---YRKDLDKFLeVNEG------------LRSR------FTRVIEFPSYSPDELVEIARR--MATERDSVLDDAA 475


                  ....*.
gi 767959635  522 LKAAVD 527
Cdd:TIGR03922 476 ADALLE 481
TIP49 pfam06068
TIP49 P-loop domain; This family consists of the C-terminal region of several eukaryotic and ...
 290-375 5.94e-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: 52.31  E-value: 5.94e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767959635  290 GLDSAVDPVQMKnvtfEHVKGVEEAKQELQEVVEFLKNPQkftiLGGKlpkGILLVGPPGTGKTLLARAVAGE--ADVPF 367
Cdd:pfam06068  12 GLDEDGEARYVS----GGLVGQEKAREAAGVIVEMIKEGK----IAGR---AVLIAGPPGTGKTALAIAISKElgEDTPF 80


                  ....*...
gi 767959635  368 YYASGSEF 375
Cdd:pfam06068  81 TSISGSEV 88
PRK04195 PRK04195
replication factor C large subunit; Provisional
 304-413 6.31e-07

replication factor C large subunit; Provisional


Pssm-ID: 235250 [Multi-domain]  Cd Length: 482  Bit Score: 52.62  E-value: 6.31e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767959635 304 TFEHVKGVEEAKQELQEVVEflknpqkfTILGGKLPKGILLVGPPGTGKTLLARAVAGEADVPFYYASGSEF---DEM-- 378
Cdd:PRK04195  12 TLSDVVGNEKAKEQLREWIE--------SWLKGKPKKALLLYGPPGVGKTSLAHALANDYGWEVIELNASDQrtaDVIer 83

                         90       100       110
                 ....*....|....*....|....*....|....*
gi 767959635 379 FVGvGASRIRNLFREAKAnapcVIFIDELDSVGGK 413
Cdd:PRK04195  84 VAG-EAATSGSLFGARRK----LILLDEVDGIHGN 113
AAA_5 pfam07728
AAA domain (dynein-related subfamily); This Pfam entry includes some of the AAA proteins not ...
 341-465 1.20e-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: 1.20e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767959635  341 GILLVGPPGTGKTLLARAVAG--EADVPFYYA--SGSEFDEMF-----VGVGASRIRNLFREAkANAPCVIFIDELDSVG 411
Cdd:pfam07728   1 GVLLVGPPGTGKTELAERLAAalSNRPVFYVQltRDTTEEDLFgrrniDPGGASWVDGPLVRA-AREGEIAVLDEINRAN 79

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 767959635  412 GKRIESpmhpysrqtINQLLAE-----MDGF----KPNEGVIIIGATNFPEA----LDNALIRpgRF 465
Cdd:pfam07728  80 PDVLNS---------LLSLLDErrlllPDGGelvkAAPDGFRLIATMNPLDRglneLSPALRS--RF 135
RecA-like_Pch2-like cd19508
ATPase domain of Pachytene checkpoint 2 (Pch2) and similar ATPase domains; Pch2 (known as ...
 342-460 5.66e-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: 5.66e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767959635 342 ILLVGPPGTGKTLLARAVAGEADV--PFYYASG--------SEFDEMFvGVGASRIRNLFR------EAKANAPCVIfID 405
Cdd:cd19508   55 VLLHGPPGTGKTSLCKALAQKLSIrlSSRYRYGqlieinshSLFSKWF-SESGKLVTKMFQkiqeliDDKDALVFVL-ID 132

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 767959635 406 ELDSVGGKRIESPMHPYSRQTI---NQLLAEMDGFKPNEGVIIIGATNFPEALDNALI 460
Cdd:cd19508  133 EVESLAAARSASSSGTEPSDAIrvvNAVLTQIDRIKRYHNNVILLTSNLLEKIDVAFV 190
CDC6 COG1474
Cdc6-related protein, AAA superfamily ATPase [Replication, recombination and repair];
317-456 6.43e-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: 6.43e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767959635 317 ELQEVVEFLKnpqkfTILGGKLPKGILLVGPPGTGKTLLARAV-------AGEADVPFYYA------SGSEF-------D 376
Cdd:COG1474   34 EIEELASALR-----PALRGERPSNVLIYGPTGTGKTAVAKYVleeleeeAEERGVDVRVVyvncrqASTRYrvlsrilE 108

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767959635 377 EMFV-------GVGASRIRNLFREA--KANAPCVIFIDELDSVGGKRIESPMHPYSRqtinqLLAEMDGFKpnegVIIIG 447
Cdd:COG1474  109 ELGSgedipstGLSTDELFDRLYEAldERDGVLVVVLDEIDYLVDDEGDDLLYQLLR-----ANEELEGAR----VGVIG 179

                        170
                 ....*....|..
gi 767959635 448 ATN---FPEALD 456
Cdd:COG1474  180 ISNdleFLENLD 191
RecA-like_superfamily cd01120
RecA-like_NTPases; RecA-like NTPases. This superfamily includes the NTP binding domain of F1 ...
 342-458 1.39e-05

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


Pssm-ID: 410865 [Multi-domain]  Cd Length: 119  Bit Score: 44.80  E-value: 1.39e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767959635 342 ILLVGPPGTGKTLLARAVAGEA---DVPFYYASgsefdemFVGVGASRIRnlfREAKANAPCVIFIDELDSVGGKRIesp 418
Cdd:cd01120    1 ILITGPPGSGKTTLLLQFAEQAllsDEPVIFIS-------FLDTILEAIE---DLIEEKKLDIIIIDSLSSLARASQ--- 67

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 767959635 419 mhPYSRQTINQLLAEMDGFKPNEGVIIIgATNFPEALDNA 458
Cdd:cd01120   68 --GDRSSELLEDLAKLLRAARNTGITVI-ATIHSDKFDID 104
DnaX COG2812
DNA polymerase III, gamma/tau subunits [Replication, recombination and repair];
304-360 4.26e-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: 4.26e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 767959635 304 TFEHVKGveeakQElqEVVEFLKNpqkfTILGGKLPKGILLVGPPGTGKTLLARAVA 360
Cdd:COG2812    8 TFDDVVG-----QE--HVVRTLKN----ALASGRLAHAYLFTGPRGVGKTTLARILA 53
clpX PRK05342
ATP-dependent Clp protease ATP-binding subunit ClpX;
342-367 4.28e-05

ATP-dependent Clp protease ATP-binding subunit ClpX;


Pssm-ID: 235422 [Multi-domain]  Cd Length: 412  Bit Score: 46.69  E-value: 4.28e-05
                         10        20
                 ....*....|....*....|....*.
gi 767959635 342 ILLVGPPGTGKTLLARAVAGEADVPF 367
Cdd:PRK05342 111 ILLIGPTGSGKTLLAQTLARILDVPF 136
NACHT COG5635
Predicted NTPase, NACHT family domain [Signal transduction mechanisms];
319-444 6.29e-05

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


Pssm-ID: 444362 [Multi-domain]  Cd Length: 935  Bit Score: 46.72  E-value: 6.29e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767959635 319 QEVVEFLKNPQKFTILGGKLPKgILLVGPPGTGKTLLARAVA---------GEADVPFY-----YASGSEFDEM---FVG 381
Cdd:COG5635  161 LNLLERIESLKRLELLEAKKKR-LLILGEPGSGKTTLLRYLAlelaeryldAEDPIPILielrdLAEEASLEDLlaeALE 239

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 767959635 382 VGASRIRNLFREAKANAPCVIFIDELDsvggkriESPMHPYSRQTINQLLAEMDGFKPNEGVI 444
Cdd:COG5635  240 KRGGEPEDALERLLRNGRLLLLLDGLD-------EVPDEADRDEVLNQLRRFLERYPKARVII 295
ClpX COG1219
ATP-dependent protease Clp, ATPase subunit ClpX [Posttranslational modification, protein ...
 342-367 6.56e-05

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


Pssm-ID: 440832 [Multi-domain]  Cd Length: 409  Bit Score: 45.81  E-value: 6.56e-05
                         10        20
                 ....*....|....*....|....*.
gi 767959635 342 ILLVGPPGTGKTLLARAVAGEADVPF 367
Cdd:COG1219  112 ILLIGPTGSGKTLLAQTLARILDVPF 137
HolB COG0470
DNA polymerase III, delta prime subunit [Replication, recombination and repair];
312-360 1.75e-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: 1.75e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*....
gi 767959635 312 EEAKQELQEVVEflknpqkftilGGKLPKGILLVGPPGTGKTLLARAVA 360
Cdd:COG0470    2 EEAWEQLLAAAE-----------SGRLPHALLLHGPPGIGKTTLALALA 39
MoxR COG0714
MoxR-like ATPase [General function prediction only]; MoxR-like ATPase is part of the Pathway ...
 342-367 1.94e-04

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


Pssm-ID: 440478 [Multi-domain]  Cd Length: 292  Bit Score: 44.00  E-value: 1.94e-04
                         10        20
                 ....*....|....*....|....*.
gi 767959635 342 ILLVGPPGTGKTLLARAVAGEADVPF 367
Cdd:COG0714   34 LLLEGVPGVGKTTLAKALARALGLPF 59
ABC_ATPase cd00267
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ...
 317-461 3.24e-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: 3.24e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767959635 317 ELQEVVEFLKNPQKFTILGGKLPKG--ILLVGPPGTGKTLLARAVAGEADVPfyyaSGS-EFDEmfVGVGASRIRNLFRE 393
Cdd:cd00267    1 EIENLSFRYGGRTALDNVSLTLKAGeiVALVGPNGSGKSTLLRAIAGLLKPT----SGEiLIDG--KDIAKLPLEELRRR 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767959635 394 -------------------AKANAPCVIFIDELDsvggkrieSPMHPYSRQTINQLLAEMdgfkPNEGVIIIGATNFPEA 454
Cdd:cd00267   75 igyvpqlsggqrqrvalarALLLNPDLLLLDEPT--------SGLDPASRERLLELLREL----AEEGRTVIIVTHDPEL 142


                 ....*..
gi 767959635 455 LDNALIR 461
Cdd:cd00267  143 AELAADR 149
DnaA COG0593
Chromosomal replication initiation ATPase DnaA [Replication, recombination and repair];
342-565 3.64e-04

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


Pssm-ID: 440358 [Multi-domain]  Cd Length: 303  Bit Score: 43.26  E-value: 3.64e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767959635 342 ILLVGPPGTGKTLLARAVAGEA-----DVPFYYASGSEFDEMFVGVGASRIRNLFREAKANAPCVIfIDELDSVGGKrie 416
Cdd:COG0593   37 LFLYGGVGLGKTHLLHAIGNEAlennpGARVVYLTAEEFTNDFINAIRNNTIEEFKEKYRSVDVLL-IDDIQFLAGK--- 112

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767959635 417 spmhpYSRQ-----TINQLLAemdgfkpNEGVIIIGATNFPEALDNAL--IRpGRFDM--QVTVPRPDVKGRTEILKwyl 487
Cdd:COG0593  113 -----EATQeeffhTFNALRE-------AGKQIVLTSDRPPKELPGLEerLR-SRLEWglVVDIQPPDLETRIAILR--- 176

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767959635 488 NKIKFDQ-SVDPEI---IARgTVGFSGAELENLVNQAALKAAVDGKEmVTmkeLEFSKD--KILMGPERRSVEIDNKNKT 561
Cdd:COG0593  177 KKAADRGlELPDEVleyLAR-RIERNVRELEGALNRLDAYALLTGRP-IT---LELAREvlKDLLRAQKKEITIEDIQKA 251


                 ....
gi 767959635 562 ITAY 565
Cdd:COG0593  252 VAEY 255
KaiC-like cd01124
Circadian Clock Protein KaiC; KaiC is a circadian clock protein, most studied in cyanobacteria. ...
 333-434 4.13e-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: 4.13e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767959635 333 ILGGKLPKG--ILLVGPPGTGKTLLARAvageadvpfYYASGSEFDE--MFVGVGaSRIRNLFREAKAnapcvIFIDELD 408
Cdd:cd01124   11 LLGGGIPKGsvTLLTGGPGTGKTLFGLQ---------FLYAGAKNGEpgLFFTFE-ESPERLLRNAKS-----FGWDFDE 75

                         90       100
                 ....*....|....*....|....*....
gi 767959635 409 SVGGKRI---ESPMHPYSRQTINQLLAEM 434
Cdd:cd01124   76 MEDEGKLiivDAPPTEAGRFSLDELLSRI 104
TIGR02928 TIGR02928
orc1/cdc6 family replication initiation protein; Members of this protein family are found ...
 316-456 4.22e-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: 4.22e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767959635  316 QELQEVVEFLKnpqkfTILGGKLPKGILLVGPPGTGKTLLARAV-------AGEADVPFYYA------------------ 370
Cdd:TIGR02928  22 EQIEELAKALR-----PILRGSRPSNVFIYGKTGTGKTAVTKYVmkeleeaAEDRDVRVVTVyvncqildtlyqvlvela 96

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767959635  371 ---SGSEFDEMFVGVGASRI-RNLFREAKANAPCVIFI-DELDSVGGKRIESPMhpysrqtinQLL-AEMDGFKPNEGVI 444
Cdd:TIGR02928  97 nqlRGSGEEVPTTGLSTSEVfRRLYKELNERGDSLIIVlDEIDYLVGDDDDLLY---------QLSrARSNGDLDNAKVG 167

                         170
                  ....*....|....*
gi 767959635  445 IIGATN---FPEALD 456
Cdd:TIGR02928 168 VIGISNdlkFRENLD 182
ruvB PRK00080
Holliday junction branch migration DNA helicase RuvB;
342-406 4.59e-04

Holliday junction branch migration DNA helicase RuvB;


Pssm-ID: 234619 [Multi-domain]  Cd Length: 328  Bit Score: 43.20  E-value: 4.59e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 767959635 342 ILLVGPPGTGKTLLARAVAGEADVPFYYASGSEFDEmfvgvgASRIRNLFREAKANApcVIFIDE 406
Cdd:PRK00080  54 VLLYGPPGLGKTTLANIIANEMGVNIRITSGPALEK------PGDLAAILTNLEEGD--VLFIDE 110
44 PHA02544
clamp loader, small subunit; Provisional
 336-411 6.22e-04

clamp loader, small subunit; Provisional


Pssm-ID: 222866 [Multi-domain]  Cd Length: 316  Bit Score: 42.67  E-value: 6.22e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767959635 336 GKLPKGILLVGPPGTGKTLLARAVAGEADVPFYYASGSEfdemfvgvgaSRIRNLFREAKANA--------PCVIFIDEL 407
Cdd:PHA02544  40 GRIPNMLLHSPSPGTGKTTVAKALCNEVGAEVLFVNGSD----------CRIDFVRNRLTRFAstvsltggGKVIIIDEF 109


                 ....
gi 767959635 408 DSVG 411
Cdd:PHA02544 110 DRLG 113
RAD55 COG0467
RecA-superfamily ATPase, KaiC/GvpD/RAD55 family [Signal transduction mechanisms];
333-356 6.30e-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: 6.30e-04
                         10        20
                 ....*....|....*....|....*.
gi 767959635 333 ILGGKLPKG--ILLVGPPGTGKTLLA 356
Cdd:COG0467   12 LLGGGLPRGssTLLSGPPGTGKTTLA 37
YifB COG0606
Predicted Mg-chelatase, contains ChlI-like and ATPase domains, YifB family [Posttranslational ...
 342-361 7.84e-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: 7.84e-04
                         10        20
                 ....*....|....*....|
gi 767959635 342 ILLVGPPGTGKTLLARAVAG 361
Cdd:COG0606  214 LLMIGPPGSGKTMLARRLPG 233
AAA_22 pfam13401
AAA domain;
342-455 1.02e-03

AAA domain;


Pssm-ID: 379165 [Multi-domain]  Cd Length: 129  Bit Score: 39.63  E-value: 1.02e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767959635  342 ILLVGPPGTGKTLLAR-----AVAGEADVPFYYASGS----EFDEMFV---------GVGASRIRNLFREA--KANAPCV 401
Cdd:pfam13401   8 LVLTGESGTGKTTLLRrlleqLPEVRDSVVFVDLPSGtspkDLLRALLralglplsgRLSKEELLAALQQLllALAVAVV 87

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 767959635  402 IFIDELDSVggkriespmhpySRQTINQLLAEMDGFKPNEGVIIIGATNFPEAL 455
Cdd:pfam13401  88 LIIDEAQHL------------SLEALEELRDLLNLSSKLLQLILVGTPELRELL 129
McrB COG1401
5-methylcytosine-specific restriction endonuclease McrBC, GTP-binding regulatory subunit McrB ...
 337-407 1.06e-03

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


Pssm-ID: 441011 [Multi-domain]  Cd Length: 477  Bit Score: 42.06  E-value: 1.06e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767959635 337 KLPKGILLVGPPGTGKT----LLARAVAGEAD-----VPFY--YasgseFDEMFVG------------VGASRIRNLFRE 393
Cdd:COG1401  219 KTKKNVILAGPPGTGKTylarRLAEALGGEDNgriefVQFHpsW-----SYEDFLLgyrpsldegkyePTPGIFLRFCLK 293

                         90
                 ....*....|....*.
gi 767959635 394 AKAN--APCVIFIDEL 407
Cdd:COG1401  294 AEKNpdKPYVLIIDEI 309
RecA-like_ClpB_Hsp104-like cd19499
Chaperone protein ClpB/Hsp104 subfamily; Bacterial Caseinolytic peptidase B (ClpB) and ...
 305-408 1.53e-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: 1.53e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767959635 305 FEHVKGVEEAKQELQEVVEF----LKNPQKftilggklPKG-ILLVGPPGTGKTLLARAVAGeadvpFYYASG------- 372
Cdd:cd19499   10 HERVVGQDEAVKAVSDAIRRaragLSDPNR--------PIGsFLFLGPTGVGKTELAKALAE-----LLFGDEdnlirid 76

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 767959635 373 -SEFDEMFVG----------VGASRIRNLFREAKANAPCVIFIDELD 408
Cdd:cd19499   77 mSEYMEKHSVsrligappgyVGYTEGGQLTEAVRRKPYSVVLLDEIE 123
AAA_2 pfam07724
AAA domain (Cdc48 subfamily); This Pfam entry includes some of the AAA proteins not detected ...
 339-408 2.08e-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: 39.49  E-value: 2.08e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767959635  339 PKG-ILLVGPPGTGKTLLARAVAGEADV---PFYYASGSEFDE-----MFVG-----VGASRIRNLFREAKANAPCVIFI 404
Cdd:pfam07724   2 PIGsFLFLGPTGVGKTELAKALAELLFGderALIRIDMSEYMEehsvsRLIGappgyVGYEEGGQLTEAVRRKPYSIVLI 81


                  ....
gi 767959635  405 DELD 408
Cdd:pfam07724  82 DEIE 85
PRK08116 PRK08116
hypothetical protein; Validated
 300-362 2.35e-03

hypothetical protein; Validated


Pssm-ID: 236153 [Multi-domain]  Cd Length: 268  Bit Score: 40.39  E-value: 2.35e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 767959635 300 MKNVTFEHVKGVEEAKQELQEVVEFLKNpqkFTILGGKlPKGILLVGPPGTGKTLLARAVAGE 362
Cdd:PRK08116  79 FRNSTFENFLFDKGSEKAYKIARKYVKK---FEEMKKE-NVGLLLWGSVGTGKTYLAACIANE 137
rfc PRK00440
replication factor C small subunit; Reviewed
 304-409 3.71e-03

replication factor C small subunit; Reviewed


Pssm-ID: 234763 [Multi-domain]  Cd Length: 319  Bit Score: 40.24  E-value: 3.71e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767959635 304 TFEHVKGVEEAKQELQEVVEflknpqkftilGGKLPKgILLVGPPGTGKT----LLARAVAGEadvpfYY--------AS 371
Cdd:PRK00440  15 TLDEIVGQEEIVERLKSYVK-----------EKNMPH-LLFAGPPGTGKTtaalALARELYGE-----DWrenflelnAS 77

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 767959635 372 gsefDEMFVGVGASRIRNLFREAKAN-APC-VIFIDELDS 409
Cdd:PRK00440  78 ----DERGIDVIRNKIKEFARTAPVGgAPFkIIFLDEADN 113
Mg_chelatase pfam01078
Magnesium chelatase, subunit ChlI; Magnesium-chelatase is a three-component enzyme that ...
 342-361 4.03e-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: 4.03e-03
                          10        20
                  ....*....|....*....|
gi 767959635  342 ILLVGPPGTGKTLLARAVAG 361
Cdd:pfam01078  25 LLMIGPPGSGKTMLAKRLPG 44
RuvB_N pfam05496
Holliday junction DNA helicase RuvB P-loop domain; The RuvB protein makes up part of the ...
 342-372 4.26e-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: 4.26e-03
                          10        20        30
                  ....*....|....*....|....*....|.
gi 767959635  342 ILLVGPPGTGKTLLARAVAGEADVPFYYASG 372
Cdd:pfam05496  36 VLLYGPPGLGKTTLANIIANEMGVNIRITSG 66
RuvB COG2255
Holliday junction resolvasome RuvABC, ATP-dependent DNA helicase subunit RuvB [Replication, ...
 342-372 4.51e-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: 4.51e-03
                         10        20        30
                 ....*....|....*....|....*....|.
gi 767959635 342 ILLVGPPGTGKTLLARAVAGEADVPFYYASG 372
Cdd:COG2255   57 VLLYGPPGLGKTTLAHIIANEMGVNIRITSG 87
ruvB TIGR00635
Holliday junction DNA helicase, RuvB subunit; All proteins in this family for which functions ...
 304-467 5.10e-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: 39.59  E-value: 5.10e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767959635  304 TFEHVKGVEEAKQELQEVVEFLKNPQKftilggkLPKGILLVGPPGTGKTLLARAVAGEADVPFYYASGSEFDEmfvgvg 383
Cdd:TIGR00635   2 LLAEFIGQEKVKEQLQLFIEAAKMRQE-------ALDHLLLYGPPGLGKTTLAHIIANEMGVNLKITSGPALEK------ 68

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767959635  384 ASRIRNLFREAKANApcVIFIDELdsvggkriespmHPYSRQTINQLLAEMDGFK--------PNEGVI--------IIG 447
Cdd:TIGR00635  69 PGDLAAILTNLEEGD--VLFIDEI------------HRLSPAVEELLYPAMEDFRldivigkgPSARSVrldlppftLVG 134

                         170       180
                  ....*....|....*....|
gi 767959635  448 ATNFPEALDNALIrpGRFDM 467
Cdd:TIGR00635 135 ATTRAGMLTSPLR--DRFGI 152
RecA-like_IQCA1 cd19506
ATPase domain of IQ and AAA domain-containing protein 1 (IQCA1); IQCA1 (also known as dynein ...
 338-452 6.38e-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: 37.89  E-value: 6.38e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767959635 338 LPKGILLVGPPGTGKTLLARAVAGEADVPFYYASGSEFDEMFVGVGASR--IRNLFREAKANAPCVIFIDELDSVGGKRI 415
Cdd:cd19506   25 LVKSLLLAGPSGVGKKMLVHAICTETGANLFNLSPSNIAGKYPGKNGLQmmLHLVLKVARQLQPSVIWIGDAEKTFYKKV 104

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 767959635 416 ---ESPMHPYS-RQTINQLLAEMdgfKPNEGVIIIGATNFP 452
Cdd:cd19506  105 pktEKQLDPKRlKKDLPKILKSL---KPEDRVLIVGTTSRP 142
ExeA COG3267
Type II secretory pathway ATPase component GspA/ExeA/MshM [Intracellular trafficking, ...
 342-406 7.00e-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: 7.00e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767959635 342 ILLVGPPGTGKTLLARAVAGE-------ADVPFYYASGSEFDEMF---VGVGASRI----------RNLFREAKANAPCV 401
Cdd:COG3267   46 VVLTGEVGTGKTTLLRRLLERlpddvkvAYIPNPQLSPAELLRAIadeLGLEPKGAskadllrqlqEFLLELAAAGRRVV 125


                 ....*
gi 767959635 402 IFIDE 406
Cdd:COG3267  126 LIIDE 130
DnaC COG1484
DNA replication protein DnaC [Replication, recombination and repair];
340-407 8.08e-03

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


Pssm-ID: 441093 [Multi-domain]  Cd Length: 242  Bit Score: 38.61  E-value: 8.08e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 767959635 340 KGILLVGPPGTGKTLLARAVAGEA-----DVPFYYASgSEFDEMfvgVGASRIRNLFREAK--ANAPCVIfIDEL 407
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.
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