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Conserved domains on  [gi|359718987|ref|NP_001240795|]
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ATP-dependent zinc metalloprotease YME1L1 isoform 4 [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

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];
242-677 0e+00

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


:

Pssm-ID: 440233 [Multi-domain]  Cd Length: 583  Bit Score: 697.94  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359718987 242 QMKNVTFEHVKGVEEAKQELQEVVEFLKNPQKFTILGGKLPKGILLVGPPGTGKTLLARAVAGEADVPFYYASGSEFDEM 321
Cdd:COG0465  135 DKPKVTFDDVAGVDEAKEELQEIVDFLKDPEKFTRLGAKIPKGVLLVGPPGTGKTLLAKAVAGEAGVPFFSISGSDFVEM 214
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359718987 322 FVGVGASRIRNLFREAKANAPCVIFIDELDSVGGKRIESPM--HPYSRQTINQLLAEMDGFKPNEGVIIIGATNFPEALD 399
Cdd:COG0465  215 FVGVGASRVRDLFEQAKKNAPCIIFIDEIDAVGRQRGAGLGggHDEREQTLNQLLVEMDGFEGNEGVIVIAATNRPDVLD 294
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359718987 400 NALIRPGRFDMQVTVPRPDVKGRTEILKWYLNKIKFDQSVDPEIIARGTVGFSGAELENLVNQAALKAAVDGKEMVTMKE 479
Cdd:COG0465  295 PALLRPGRFDRQVVVDLPDVKGREAILKVHARKKPLAPDVDLEVIARRTPGFSGADLANLVNEAALLAARRNKKAVTMED 374
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359718987 480 LEFSKDKILMGPERRSVEIDNKNKTITAYHESGHAIIAYYTKDAMPINKATIMPRGPTLGHVSLLPENDRWNETRAQLLA 559
Cdd:COG0465  375 FEEAIDRVIAGPERKSRVISEKEKKITAYHEAGHALVAALLPGADPVHKVTIIPRGRALGYTMQLPEEDRYLYTKEELLD 454
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359718987 560 QMDVSMGGRVAEELIFGtdHITTGASSDFDNATKIAKRMVTKFGMSEKLGVMTYSDTG-------------KLSPETQSA 626
Cdd:COG0465  455 RIAVLLGGRAAEELVFG--EVTTGASNDLERATKIARAMVTEYGMSEKLGPVAYGESEgevflgrdigqsrNYSEETARE 532
                        410       420       430       440       450
                 ....*....|....*....|....*....|....*....|....*....|.
gi 359718987 627 IEQEIRILLRDSYERAKHILKTHAKEHKNLAEALLTYETLDAKEIQIVLEG 677
Cdd:COG0465  533 IDEEVRRIIDEAYERAKEILTENRDKLDALAEALLEKETLDGEELEEILAG 583
 
Name Accession Description Interval E-value
HflB COG0465
ATP-dependent Zn proteases [Posttranslational modification, protein turnover, chaperones];
242-677 0e+00

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


Pssm-ID: 440233 [Multi-domain]  Cd Length: 583  Bit Score: 697.94  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359718987 242 QMKNVTFEHVKGVEEAKQELQEVVEFLKNPQKFTILGGKLPKGILLVGPPGTGKTLLARAVAGEADVPFYYASGSEFDEM 321
Cdd:COG0465  135 DKPKVTFDDVAGVDEAKEELQEIVDFLKDPEKFTRLGAKIPKGVLLVGPPGTGKTLLAKAVAGEAGVPFFSISGSDFVEM 214
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359718987 322 FVGVGASRIRNLFREAKANAPCVIFIDELDSVGGKRIESPM--HPYSRQTINQLLAEMDGFKPNEGVIIIGATNFPEALD 399
Cdd:COG0465  215 FVGVGASRVRDLFEQAKKNAPCIIFIDEIDAVGRQRGAGLGggHDEREQTLNQLLVEMDGFEGNEGVIVIAATNRPDVLD 294
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359718987 400 NALIRPGRFDMQVTVPRPDVKGRTEILKWYLNKIKFDQSVDPEIIARGTVGFSGAELENLVNQAALKAAVDGKEMVTMKE 479
Cdd:COG0465  295 PALLRPGRFDRQVVVDLPDVKGREAILKVHARKKPLAPDVDLEVIARRTPGFSGADLANLVNEAALLAARRNKKAVTMED 374
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359718987 480 LEFSKDKILMGPERRSVEIDNKNKTITAYHESGHAIIAYYTKDAMPINKATIMPRGPTLGHVSLLPENDRWNETRAQLLA 559
Cdd:COG0465  375 FEEAIDRVIAGPERKSRVISEKEKKITAYHEAGHALVAALLPGADPVHKVTIIPRGRALGYTMQLPEEDRYLYTKEELLD 454
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359718987 560 QMDVSMGGRVAEELIFGtdHITTGASSDFDNATKIAKRMVTKFGMSEKLGVMTYSDTG-------------KLSPETQSA 626
Cdd:COG0465  455 RIAVLLGGRAAEELVFG--EVTTGASNDLERATKIARAMVTEYGMSEKLGPVAYGESEgevflgrdigqsrNYSEETARE 532
                        410       420       430       440       450
                 ....*....|....*....|....*....|....*....|....*....|.
gi 359718987 627 IEQEIRILLRDSYERAKHILKTHAKEHKNLAEALLTYETLDAKEIQIVLEG 677
Cdd:COG0465  533 IDEEVRRIIDEAYERAKEILTENRDKLDALAEALLEKETLDGEELEEILAG 583
FtsH_fam TIGR01241
ATP-dependent metalloprotease FtsH; HflB(FtsH) is a pleiotropic protein required for correct ...
243-676 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: 616.61  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359718987  243 MKNVTFEHVKGVEEAKQELQEVVEFLKNPQKFTILGGKLPKGILLVGPPGTGKTLLARAVAGEADVPFYYASGSEFDEMF 322
Cdd:TIGR01241  49 KPKVTFKDVAGIDEAKEELMEIVDFLKNPSKFTKLGAKIPKGVLLVGPPGTGKTLLAKAVAGEAGVPFFSISGSDFVEMF 128
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359718987  323 VGVGASRIRNLFREAKANAPCVIFIDELDSVGGKR--IESPMHPYSRQTINQLLAEMDGFKPNEGVIIIGATNFPEALDN 400
Cdd:TIGR01241 129 VGVGASRVRDLFEQAKKNAPCIIFIDEIDAVGRQRgaGLGGGNDEREQTLNQLLVEMDGFGTNTGVIVIAATNRPDVLDP 208
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359718987  401 ALIRPGRFDMQVTVPRPDVKGRTEILKWYLNKIKFDQSVDPEIIARGTVGFSGAELENLVNQAALKAAVDGKEMVTMKEL 480
Cdd:TIGR01241 209 ALLRPGRFDRQVVVDLPDIKGREEILKVHAKNKKLAPDVDLKAVARRTPGFSGADLANLLNEAALLAARKNKTEITMNDI 288
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359718987  481 EFSKDKILMGPERRSVEIDNKNKTITAYHESGHAIIAYYTKDAMPINKATIMPRGPTLGHVSLLPENDRWNETRAQLLAQ 560
Cdd:TIGR01241 289 EEAIDRVIAGPEKKSRVISEKEKKLVAYHEAGHALVGLLLKDADPVHKVTIIPRGQALGYTQFLPEEDKYLYTKSQLLAQ 368
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359718987  561 MDVSMGGRVAEELIFGtdHITTGASSDFDNATKIAKRMVTKFGMSEKLGVMTYSDTGK-------------LSPETQSAI 627
Cdd:TIGR01241 369 IAVLLGGRAAEEIIFG--EVTTGASNDIKQATNIARAMVTEWGMSDKLGPVAYGSDGGdvflgrgfakakeYSEETAREI 446
                         410       420       430       440
                  ....*....|....*....|....*....|....*....|....*....
gi 359718987  628 EQEIRILLRDSYERAKHILKTHAKEHKNLAEALLTYETLDAKEIQIVLE 676
Cdd:TIGR01241 447 DEEVKRIIEEAYKRAKQILTENRDELELLAKALLEKETITREEIKELLA 495
hflB PRK10733
ATP-dependent zinc metalloprotease FtsH;
242-683 1.54e-161

ATP-dependent zinc metalloprotease FtsH;


Pssm-ID: 182683 [Multi-domain]  Cd Length: 644  Bit Score: 479.53  E-value: 1.54e-161
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359718987 242 QMKNvTFEHVKGVEEAKQELQEVVEFLKNPQKFTILGGKLPKGILLVGPPGTGKTLLARAVAGEADVPFYYASGSEFDEM 321
Cdd:PRK10733 146 QIKT-TFADVAGCDEAKEEVAELVEYLREPSRFQKLGGKIPKGVLMVGPPGTGKTLLAKAIAGEAKVPFFTISGSDFVEM 224
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359718987 322 FVGVGASRIRNLFREAKANAPCVIFIDELDSVGGKRIES--PMHPYSRQTINQLLAEMDGFKPNEGVIIIGATNFPEALD 399
Cdd:PRK10733 225 FVGVGASRVRDMFEQAKKAAPCIIFIDEIDAVGRQRGAGlgGGHDEREQTLNQMLVEMDGFEGNEGIIVIAATNRPDVLD 304
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359718987 400 NALIRPGRFDMQVTVPRPDVKGRTEILKWYLNKIKFDQSVDPEIIARGTVGFSGAELENLVNQAALKAAVDGKEMVTMKE 479
Cdd:PRK10733 305 PALLRPGRFDRQVVVGLPDVRGREQILKVHMRRVPLAPDIDAAIIARGTPGFSGADLANLVNEAALFAARGNKRVVSMVE 384
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359718987 480 LEFSKDKILMGPERRSVEIDNKNKTITAYHESGHAIIAYYTKDAMPINKATIMPRGPTLGHVSLLPENDRWNETRAQLLA 559
Cdd:PRK10733 385 FEKAKDKIMMGAERRSMVMTEAQKESTAYHEAGHAIIGRLVPEHDPVHKVTIIPRGRALGVTFFLPEGDAISASRQKLES 464
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359718987 560 QMDVSMGGRVAEELIFGTDHITTGASSDFDNATKIAKRMVTKFGMSEKLGVMTYSD-------------TGKLSPETQSA 626
Cdd:PRK10733 465 QISTLYGGRLAEEIIYGPEHVSTGASNDIKVATNLARNMVTQWGFSEKLGPLLYAEeegevflgrsvakAKHMSDETARI 544
                        410       420       430       440       450
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 359718987 627 IEQEIRILLRDSYERAKHILKTHAKEHKNLAEALLTYETLDAKEIQIVLEGKklEVR 683
Cdd:PRK10733 545 IDQEVKALIERNYNRARQLLTDNMDILHAMKDALMKYETIDAPQIDDLMARR--DVR 599
RecA-like_FtsH cd19501
ATP-dependent zinc metalloprotease FtsH; FtsH ATPase is a processive, ATP-dependent zinc ...
246-414 1.97e-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: 314.94  E-value: 1.97e-104
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359718987 246 VTFEHVKGVEEAKQELQEVVEFLKNPQKFTILGGKLPKGILLVGPPGTGKTLLARAVAGEADVPFYYASGSEFDEMFVGV 325
Cdd:cd19501    1 VTFKDVAGCEEAKEELKEVVEFLKNPEKFTKLGAKIPKGVLLVGPPGTGKTLLAKAVAGEAGVPFFSISGSDFVEMFVGV 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359718987 326 GASRIRNLFREAKANAPCVIFIDELDSVGGKR--IESPMHPYSRQTINQLLAEMDGFKPNEGVIIIGATNFPEALDNALI 403
Cdd:cd19501   81 GASRVRDLFEQAKKNAPCIVFIDEIDAVGRKRgaGLGGGHDEREQTLNQLLVEMDGFESNTGVIVIAATNRPDVLDPALL 160
                        170
                 ....*....|.
gi 359718987 404 RPGRFDMQVTV 414
Cdd:cd19501  161 RPGRFDRQVYV 171
Peptidase_M41 pfam01434
Peptidase family M41;
496-674 2.10e-86

Peptidase family M41;


Pssm-ID: 460210 [Multi-domain]  Cd Length: 190  Bit Score: 269.09  E-value: 2.10e-86
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359718987  496 VEIDNKNKTITAYHESGHAIIAYYTKDAMPINKATIMPRGPTLGHVSLLPENDRWNETRAQLLAQMDVSMGGRVAEELIF 575
Cdd:pfam01434   1 RVISEEEKKIVAYHEAGHALVGLLLPGADPVHKVTIIPRGQALGYTQFLPEEDKLLYTKEQLLARIAVLLGGRAAEELIF 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359718987  576 GtdHITTGASSDFDNATKIAKRMVTKFGMSEKLGVMTYSDTG-------------KLSPETQSAIEQEIRILLRDSYERA 642
Cdd:pfam01434  81 G--EVTTGASNDLEKATKIARQMVTEFGMSDKLGPVSLEESDgnvflgrgmgkrkPYSEETADIIDEEVKRLLEEAYERA 158
                         170       180       190
                  ....*....|....*....|....*....|..
gi 359718987  643 KHILKTHAKEHKNLAEALLTYETLDAKEIQIV 674
Cdd:pfam01434 159 KEILTEHRDELEALAEALLEKETLDAEEIREL 190
AAA smart00382
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ...
282-418 7.54e-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: 80.88  E-value: 7.54e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359718987   282 PKGILLVGPPGTGKTLLARAVAGEADVP---FYYASGSEFDE--------------MFVGVGASRIRNLFREAKANAPCV 344
Cdd:smart00382   2 GEVILIVGPPGSGKTTLARALARELGPPgggVIYIDGEDILEevldqllliivggkKASGSGELRLRLALALARKLKPDV 81
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 359718987   345 IFIDELDSVGGKRIESPMhpysrqTINQLLAEMDGFKPNEGVIIIGATNFPEALDNALIRPgRFDMQVTVPRPD 418
Cdd:smart00382  82 LILDEITSLLDAEQEALL------LLLEELRLLLLLKSEKNLTVILTTNDEKDLGPALLRR-RFDRRIVLLLIL 148
 
Name Accession Description Interval E-value
HflB COG0465
ATP-dependent Zn proteases [Posttranslational modification, protein turnover, chaperones];
242-677 0e+00

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


Pssm-ID: 440233 [Multi-domain]  Cd Length: 583  Bit Score: 697.94  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359718987 242 QMKNVTFEHVKGVEEAKQELQEVVEFLKNPQKFTILGGKLPKGILLVGPPGTGKTLLARAVAGEADVPFYYASGSEFDEM 321
Cdd:COG0465  135 DKPKVTFDDVAGVDEAKEELQEIVDFLKDPEKFTRLGAKIPKGVLLVGPPGTGKTLLAKAVAGEAGVPFFSISGSDFVEM 214
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359718987 322 FVGVGASRIRNLFREAKANAPCVIFIDELDSVGGKRIESPM--HPYSRQTINQLLAEMDGFKPNEGVIIIGATNFPEALD 399
Cdd:COG0465  215 FVGVGASRVRDLFEQAKKNAPCIIFIDEIDAVGRQRGAGLGggHDEREQTLNQLLVEMDGFEGNEGVIVIAATNRPDVLD 294
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359718987 400 NALIRPGRFDMQVTVPRPDVKGRTEILKWYLNKIKFDQSVDPEIIARGTVGFSGAELENLVNQAALKAAVDGKEMVTMKE 479
Cdd:COG0465  295 PALLRPGRFDRQVVVDLPDVKGREAILKVHARKKPLAPDVDLEVIARRTPGFSGADLANLVNEAALLAARRNKKAVTMED 374
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359718987 480 LEFSKDKILMGPERRSVEIDNKNKTITAYHESGHAIIAYYTKDAMPINKATIMPRGPTLGHVSLLPENDRWNETRAQLLA 559
Cdd:COG0465  375 FEEAIDRVIAGPERKSRVISEKEKKITAYHEAGHALVAALLPGADPVHKVTIIPRGRALGYTMQLPEEDRYLYTKEELLD 454
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359718987 560 QMDVSMGGRVAEELIFGtdHITTGASSDFDNATKIAKRMVTKFGMSEKLGVMTYSDTG-------------KLSPETQSA 626
Cdd:COG0465  455 RIAVLLGGRAAEELVFG--EVTTGASNDLERATKIARAMVTEYGMSEKLGPVAYGESEgevflgrdigqsrNYSEETARE 532
                        410       420       430       440       450
                 ....*....|....*....|....*....|....*....|....*....|.
gi 359718987 627 IEQEIRILLRDSYERAKHILKTHAKEHKNLAEALLTYETLDAKEIQIVLEG 677
Cdd:COG0465  533 IDEEVRRIIDEAYERAKEILTENRDKLDALAEALLEKETLDGEELEEILAG 583
FtsH_fam TIGR01241
ATP-dependent metalloprotease FtsH; HflB(FtsH) is a pleiotropic protein required for correct ...
243-676 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: 616.61  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359718987  243 MKNVTFEHVKGVEEAKQELQEVVEFLKNPQKFTILGGKLPKGILLVGPPGTGKTLLARAVAGEADVPFYYASGSEFDEMF 322
Cdd:TIGR01241  49 KPKVTFKDVAGIDEAKEELMEIVDFLKNPSKFTKLGAKIPKGVLLVGPPGTGKTLLAKAVAGEAGVPFFSISGSDFVEMF 128
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359718987  323 VGVGASRIRNLFREAKANAPCVIFIDELDSVGGKR--IESPMHPYSRQTINQLLAEMDGFKPNEGVIIIGATNFPEALDN 400
Cdd:TIGR01241 129 VGVGASRVRDLFEQAKKNAPCIIFIDEIDAVGRQRgaGLGGGNDEREQTLNQLLVEMDGFGTNTGVIVIAATNRPDVLDP 208
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359718987  401 ALIRPGRFDMQVTVPRPDVKGRTEILKWYLNKIKFDQSVDPEIIARGTVGFSGAELENLVNQAALKAAVDGKEMVTMKEL 480
Cdd:TIGR01241 209 ALLRPGRFDRQVVVDLPDIKGREEILKVHAKNKKLAPDVDLKAVARRTPGFSGADLANLLNEAALLAARKNKTEITMNDI 288
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359718987  481 EFSKDKILMGPERRSVEIDNKNKTITAYHESGHAIIAYYTKDAMPINKATIMPRGPTLGHVSLLPENDRWNETRAQLLAQ 560
Cdd:TIGR01241 289 EEAIDRVIAGPEKKSRVISEKEKKLVAYHEAGHALVGLLLKDADPVHKVTIIPRGQALGYTQFLPEEDKYLYTKSQLLAQ 368
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359718987  561 MDVSMGGRVAEELIFGtdHITTGASSDFDNATKIAKRMVTKFGMSEKLGVMTYSDTGK-------------LSPETQSAI 627
Cdd:TIGR01241 369 IAVLLGGRAAEEIIFG--EVTTGASNDIKQATNIARAMVTEWGMSDKLGPVAYGSDGGdvflgrgfakakeYSEETAREI 446
                         410       420       430       440
                  ....*....|....*....|....*....|....*....|....*....
gi 359718987  628 EQEIRILLRDSYERAKHILKTHAKEHKNLAEALLTYETLDAKEIQIVLE 676
Cdd:TIGR01241 447 DEEVKRIIEEAYKRAKQILTENRDELELLAKALLEKETITREEIKELLA 495
hflB PRK10733
ATP-dependent zinc metalloprotease FtsH;
242-683 1.54e-161

ATP-dependent zinc metalloprotease FtsH;


Pssm-ID: 182683 [Multi-domain]  Cd Length: 644  Bit Score: 479.53  E-value: 1.54e-161
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359718987 242 QMKNvTFEHVKGVEEAKQELQEVVEFLKNPQKFTILGGKLPKGILLVGPPGTGKTLLARAVAGEADVPFYYASGSEFDEM 321
Cdd:PRK10733 146 QIKT-TFADVAGCDEAKEEVAELVEYLREPSRFQKLGGKIPKGVLMVGPPGTGKTLLAKAIAGEAKVPFFTISGSDFVEM 224
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359718987 322 FVGVGASRIRNLFREAKANAPCVIFIDELDSVGGKRIES--PMHPYSRQTINQLLAEMDGFKPNEGVIIIGATNFPEALD 399
Cdd:PRK10733 225 FVGVGASRVRDMFEQAKKAAPCIIFIDEIDAVGRQRGAGlgGGHDEREQTLNQMLVEMDGFEGNEGIIVIAATNRPDVLD 304
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359718987 400 NALIRPGRFDMQVTVPRPDVKGRTEILKWYLNKIKFDQSVDPEIIARGTVGFSGAELENLVNQAALKAAVDGKEMVTMKE 479
Cdd:PRK10733 305 PALLRPGRFDRQVVVGLPDVRGREQILKVHMRRVPLAPDIDAAIIARGTPGFSGADLANLVNEAALFAARGNKRVVSMVE 384
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359718987 480 LEFSKDKILMGPERRSVEIDNKNKTITAYHESGHAIIAYYTKDAMPINKATIMPRGPTLGHVSLLPENDRWNETRAQLLA 559
Cdd:PRK10733 385 FEKAKDKIMMGAERRSMVMTEAQKESTAYHEAGHAIIGRLVPEHDPVHKVTIIPRGRALGVTFFLPEGDAISASRQKLES 464
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359718987 560 QMDVSMGGRVAEELIFGTDHITTGASSDFDNATKIAKRMVTKFGMSEKLGVMTYSD-------------TGKLSPETQSA 626
Cdd:PRK10733 465 QISTLYGGRLAEEIIYGPEHVSTGASNDIKVATNLARNMVTQWGFSEKLGPLLYAEeegevflgrsvakAKHMSDETARI 544
                        410       420       430       440       450
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 359718987 627 IEQEIRILLRDSYERAKHILKTHAKEHKNLAEALLTYETLDAKEIQIVLEGKklEVR 683
Cdd:PRK10733 545 IDQEVKALIERNYNRARQLLTDNMDILHAMKDALMKYETIDAPQIDDLMARR--DVR 599
ftsH CHL00176
cell division protein; Validated
244-676 1.58e-161

cell division protein; Validated


Pssm-ID: 214386 [Multi-domain]  Cd Length: 638  Bit Score: 479.16  E-value: 1.58e-161
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359718987 244 KNVTFEHVKGVEEAKQELQEVVEFLKNPQKFTILGGKLPKGILLVGPPGTGKTLLARAVAGEADVPFYYASGSEFDEMFV 323
Cdd:CHL00176 178 TGITFRDIAGIEEAKEEFEEVVSFLKKPERFTAVGAKIPKGVLLVGPPGTGKTLLAKAIAGEAEVPFFSISGSEFVEMFV 257
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359718987 324 GVGASRIRNLFREAKANAPCVIFIDELDSVG---GKRIESPMHPySRQTINQLLAEMDGFKPNEGVIIIGATNFPEALDN 400
Cdd:CHL00176 258 GVGAARVRDLFKKAKENSPCIVFIDEIDAVGrqrGAGIGGGNDE-REQTLNQLLTEMDGFKGNKGVIVIAATNRVDILDA 336
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359718987 401 ALIRPGRFDMQVTVPRPDVKGRTEILKWYLNKIKFDQSVDPEIIARGTVGFSGAELENLVNQAALKAAVDGKEMVTMKEL 480
Cdd:CHL00176 337 ALLRPGRFDRQITVSLPDREGRLDILKVHARNKKLSPDVSLELIARRTPGFSGADLANLLNEAAILTARRKKATITMKEI 416
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359718987 481 EFSKDKILMGPERRSVEiDNKNKTITAYHESGHAIIAYYTKDAMPINKATIMPRGPTLGHVSLLPENDRWNETRAQLLAQ 560
Cdd:CHL00176 417 DTAIDRVIAGLEGTPLE-DSKNKRLIAYHEVGHAIVGTLLPNHDPVQKVTLIPRGQAKGLTWFTPEEDQSLVSRSQILAR 495
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359718987 561 MDVSMGGRVAEELIFGTDHITTGASSDFDNATKIAKRMVTKFGMSeKLGVMTYSDTG--------------KLSPETQSA 626
Cdd:CHL00176 496 IVGALGGRAAEEVVFGSTEVTTGASNDLQQVTNLARQMVTRFGMS-SIGPISLESNNstdpflgrfmqrnsEYSEEIADK 574
                        410       420       430       440       450
                 ....*....|....*....|....*....|....*....|....*....|
gi 359718987 627 IEQEIRILLRDSYERAKHILKTHAKEHKNLAEALLTYETLDAKEIQIVLE 676
Cdd:CHL00176 575 IDMEVRSILHTCYQYAYQILKDNRVLIDLLVELLLQKETIDGDEFREIVN 624
RPT1 COG1222
ATP-dependent 26S proteasome regulatory subunit [Posttranslational modification, protein ...
245-493 8.47e-106

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


Pssm-ID: 440835 [Multi-domain]  Cd Length: 326  Bit Score: 324.65  E-value: 8.47e-106
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359718987 245 NVTFEHVKGVEEAKQELQEVVE-FLKNPQKFTILGGKLPKGILLVGPPGTGKTLLARAVAGEADVPFYYASGSEFDEMFV 323
Cdd:COG1222   74 DVTFDDIGGLDEQIEEIREAVElPLKNPELFRKYGIEPPKGVLLYGPPGTGKTLLAKAVAGELGAPFIRVRGSELVSKYI 153
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359718987 324 GVGASRIRNLFREAKANAPCVIFIDELDSVGGKRIESPMHPYSRQTINQLLAEMDGFKPNEGVIIIGATNFPEALDNALI 403
Cdd:COG1222  154 GEGARNVREVFELAREKAPSIIFIDEIDAIAARRTDDGTSGEVQRTVNQLLAELDGFESRGDVLIIAATNRPDLLDPALL 233
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359718987 404 RPGRFDMQVTVPRPDVKGRTEILKWYLNKIKFDQSVDPEIIARGTVGFSGAELENLVNQAALKAAVDGKEMVTMKELEFS 483
Cdd:COG1222  234 RPGRFDRVIEVPLPDEEAREEILKIHLRDMPLADDVDLDKLAKLTEGFSGADLKAIVTEAGMFAIREGRDTVTMEDLEKA 313
                        250
                 ....*....|
gi 359718987 484 KDKILMGPER 493
Cdd:COG1222  314 IEKVKKKTET 323
RecA-like_FtsH cd19501
ATP-dependent zinc metalloprotease FtsH; FtsH ATPase is a processive, ATP-dependent zinc ...
246-414 1.97e-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: 314.94  E-value: 1.97e-104
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359718987 246 VTFEHVKGVEEAKQELQEVVEFLKNPQKFTILGGKLPKGILLVGPPGTGKTLLARAVAGEADVPFYYASGSEFDEMFVGV 325
Cdd:cd19501    1 VTFKDVAGCEEAKEELKEVVEFLKNPEKFTKLGAKIPKGVLLVGPPGTGKTLLAKAVAGEAGVPFFSISGSDFVEMFVGV 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359718987 326 GASRIRNLFREAKANAPCVIFIDELDSVGGKR--IESPMHPYSRQTINQLLAEMDGFKPNEGVIIIGATNFPEALDNALI 403
Cdd:cd19501   81 GASRVRDLFEQAKKNAPCIVFIDEIDAVGRKRgaGLGGGHDEREQTLNQLLVEMDGFESNTGVIVIAATNRPDVLDPALL 160
                        170
                 ....*....|.
gi 359718987 404 RPGRFDMQVTV 414
Cdd:cd19501  161 RPGRFDRQVYV 171
Peptidase_M41 pfam01434
Peptidase family M41;
496-674 2.10e-86

Peptidase family M41;


Pssm-ID: 460210 [Multi-domain]  Cd Length: 190  Bit Score: 269.09  E-value: 2.10e-86
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359718987  496 VEIDNKNKTITAYHESGHAIIAYYTKDAMPINKATIMPRGPTLGHVSLLPENDRWNETRAQLLAQMDVSMGGRVAEELIF 575
Cdd:pfam01434   1 RVISEEEKKIVAYHEAGHALVGLLLPGADPVHKVTIIPRGQALGYTQFLPEEDKLLYTKEQLLARIAVLLGGRAAEELIF 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359718987  576 GtdHITTGASSDFDNATKIAKRMVTKFGMSEKLGVMTYSDTG-------------KLSPETQSAIEQEIRILLRDSYERA 642
Cdd:pfam01434  81 G--EVTTGASNDLEKATKIARQMVTEFGMSDKLGPVSLEESDgnvflgrgmgkrkPYSEETADIIDEEVKRLLEEAYERA 158
                         170       180       190
                  ....*....|....*....|....*....|..
gi 359718987  643 KHILKTHAKEHKNLAEALLTYETLDAKEIQIV 674
Cdd:pfam01434 159 KEILTEHRDELEALAEALLEKETLDAEEIREL 190
PRK03992 PRK03992
proteasome-activating nucleotidase; Provisional
245-497 1.48e-81

proteasome-activating nucleotidase; Provisional


Pssm-ID: 179699 [Multi-domain]  Cd Length: 389  Bit Score: 263.62  E-value: 1.48e-81
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359718987 245 NVTFEHVKGVEEAKQELQEVVEF-LKNPQKFTILGGKLPKGILLVGPPGTGKTLLARAVAGEADVPFYYASGSEFDEMFV 323
Cdd:PRK03992 127 NVTYEDIGGLEEQIREVREAVELpLKKPELFEEVGIEPPKGVLLYGPPGTGKTLLAKAVAHETNATFIRVVGSELVQKFI 206
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359718987 324 GVGASRIRNLFREAKANAPCVIFIDELDSVGGKRIESpMHPYSRQ---TINQLLAEMDGFKPNEGVIIIGATNFPEALDN 400
Cdd:PRK03992 207 GEGARLVRELFELAREKAPSIIFIDEIDAIAAKRTDS-GTSGDREvqrTLMQLLAEMDGFDPRGNVKIIAATNRIDILDP 285
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359718987 401 ALIRPGRFDMQVTVPRPDVKGRTEILKWYLNKIKFDQSVDPEIIARGTVGFSGAELENLVNQAALKAAVDGKEMVTMKEL 480
Cdd:PRK03992 286 AILRPGRFDRIIEVPLPDEEGRLEILKIHTRKMNLADDVDLEELAELTEGASGADLKAICTEAGMFAIRDDRTEVTMEDF 365
                        250
                 ....*....|....*..
gi 359718987 481 EFSKDKILMGPERRSVE 497
Cdd:PRK03992 366 LKAIEKVMGKEEKDSME 382
SpoVK COG0464
AAA+-type ATPase, SpoVK/Ycf46/Vps4 family [Cell wall/membrane/envelope biogenesis, Cell cycle ...
248-481 1.46e-75

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: 248.29  E-value: 1.46e-75
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359718987 248 FEHVKGVEEAKQELQEVVE-FLKNPQKFTILGGKLPKGILLVGPPGTGKTLLARAVAGEADVPFYYASGSEFDEMFVGVG 326
Cdd:COG0464  156 LDDLGGLEEVKEELRELVAlPLKRPELREEYGLPPPRGLLLYGPPGTGKTLLARALAGELGLPLIEVDLSDLVSKYVGET 235
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359718987 327 ASRIRNLFREAKANAPCVIFIDELDSVGGKRiESPMHPYSRQTINQLLAEMDGFkpNEGVIIIGATNFPEALDNALIRpg 406
Cdd:COG0464  236 EKNLREVFDKARGLAPCVLFIDEADALAGKR-GEVGDGVGRRVVNTLLTEMEEL--RSDVVVIAATNRPDLLDPALLR-- 310
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 359718987 407 RFDMQVTVPRPDVKGRTEILKWYLNKIKFDQSVDPEIIARGTVGFSGAELENLVNQAALKAAVDGKEMVTMKELE 481
Cdd:COG0464  311 RFDEIIFFPLPDAEERLEIFRIHLRKRPLDEDVDLEELAEATEGLSGADIRNVVRRAALQALRLGREPVTTEDLL 385
26Sp45 TIGR01242
26S proteasome subunit P45 family; Many proteins may score above the trusted cutoff because an ...
245-488 2.67e-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: 238.55  E-value: 2.67e-72
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359718987  245 NVTFEHVKGVEEAKQELQEVVEF-LKNPQKFTILGGKLPKGILLVGPPGTGKTLLARAVAGEADVPFYYASGSEFDEMFV 323
Cdd:TIGR01242 118 NVSYEDIGGLEEQIREIREAVELpLKHPELFEEVGIEPPKGVLLYGPPGTGKTLLAKAVAHETNATFIRVVGSELVRKYI 197
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359718987  324 GVGASRIRNLFREAKANAPCVIFIDELDSVGGKRIESPM--HPYSRQTINQLLAEMDGFKPNEGVIIIGATNFPEALDNA 401
Cdd:TIGR01242 198 GEGARLVREIFELAKEKAPSIIFIDEIDAIAAKRTDSGTsgDREVQRTLMQLLAELDGFDPRGNVKVIAATNRPDILDPA 277
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359718987  402 LIRPGRFDMQVTVPRPDVKGRTEILKWYLNKIKFDQSVDPEIIARGTVGFSGAELENLVNQAALKAAVDGKEMVTMKELE 481
Cdd:TIGR01242 278 LLRPGRFDRIIEVPLPDFEGRLEILKIHTRKMKLAEDVDLEAIAKMTEGASGADLKAICTEAGMFAIREERDYVTMDDFI 357

                  ....*..
gi 359718987  482 FSKDKIL 488
Cdd:TIGR01242 358 KAVEKVL 364
COG1223 COG1223
Predicted ATPase, AAA+ superfamily [General function prediction only];
248-481 1.33e-64

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


Pssm-ID: 440836 [Multi-domain]  Cd Length: 246  Bit Score: 213.98  E-value: 1.33e-64
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359718987 248 FEHVKGVEEAKQELQEVVEFLK---NPQKFtilGGKLPKGILLVGPPGTGKTLLARAVAGEADVPFYYASGSEFDEMFVG 324
Cdd:COG1223    1 LDDVVGQEEAKKKLKLIIKELRrreNLRKF---GLWPPRKILFYGPPGTGKTMLAEALAGELKLPLLTVRLDSLIGSYLG 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359718987 325 VGASRIRNLFREAKaNAPCVIFIDELDSVGGKRIESPMHPYSRQTINQLLAEMDGFkpNEGVIIIGATNFPEALDNALIR 404
Cdd:COG1223   78 ETARNLRKLFDFAR-RAPCVIFFDEFDAIAKDRGDQNDVGEVKRVVNALLQELDGL--PSGSVVIAATNHPELLDSALWR 154
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 359718987 405 pgRFDMQVTVPRPDVKGRTEILKWYLNKIKFDQSVDPEIIARGTVGFSGAELENLVNQAALKAAVDGKEMVTMKELE 481
Cdd:COG1223  155 --RFDEVIEFPLPDKEERKEILELNLKKFPLPFELDLKKLAKKLEGLSGADIEKVLKTALKKAILEDREKVTKEDLE 229
CDC48 TIGR01243
AAA family ATPase, CDC48 subfamily; This subfamily of the AAA family ATPases includes two ...
241-488 4.66e-63

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


Pssm-ID: 273521 [Multi-domain]  Cd Length: 733  Bit Score: 223.25  E-value: 4.66e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359718987  241 VQMKNVTFEHVKGVEEAKQELQEVVEF-LKNPQKFTILGGKLPKGILLVGPPGTGKTLLARAVAGEADVPFYYASGSEFD 319
Cdd:TIGR01243 445 VEVPNVRWSDIGGLEEVKQELREAVEWpLKHPEIFEKMGIRPPKGVLLFGPPGTGKTLLAKAVATESGANFIAVRGPEIL 524
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359718987  320 EMFVGVGASRIRNLFREAKANAPCVIFIDELDSVGGKRIESPMHPYSRQTINQLLAEMDGFKPNEGVIIIGATNFPEALD 399
Cdd:TIGR01243 525 SKWVGESEKAIREIFRKARQAAPAIIFFDEIDAIAPARGARFDTSVTDRIVNQLLTEMDGIQELSNVVVIAATNRPDILD 604
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359718987  400 NALIRPGRFDMQVTVPRPDVKGRTEILKWYLNKIKFDQSVDPEIIARGTVGFSGAELENLVNQAALKAAVDGKEMVTMKE 479
Cdd:TIGR01243 605 PALLRPGRFDRLILVPPPDEEARKEIFKIHTRSMPLAEDVDLEELAEMTEGYTGADIEAVCREAAMAALRESIGSPAKEK 684

                  ....*....
gi 359718987  480 LEFSKDKIL 488
Cdd:TIGR01243 685 LEVGEEEFL 693
RecA-like_protease cd19481
proteases similar to RecA; RecA-like NTPases. This family includes the NTP binding domain of ...
257-414 1.26e-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: 202.51  E-value: 1.26e-61
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359718987 257 AKQELQEVVEFLKNPQKFTILGGKLPKGILLVGPPGTGKTLLARAVAGEADVPFYYASGSEFDEMFVGVGASRIRNLFRE 336
Cdd:cd19481    1 LKASLREAVEAPRRGSRLRRYGLGLPKGILLYGPPGTGKTLLAKALAGELGLPLIVVKLSSLLSKYVGESEKNLRKIFER 80
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 359718987 337 AKANAPCVIFIDELDSVGGKRIESPMHPYSRQTINQLLAEMDGFKPNEGVIIIGATNFPEALDNALIRPGRFDMQVTV 414
Cdd:cd19481   81 ARRLAPCILFIDEIDAIGRKRDSSGESGELRRVLNQLLTELDGVNSRSKVLVIAATNRPDLLDPALLRPGRFDEVIEF 158
RecA-like_PAN_like cd19502
proteasome activating nucleotidase PAN and related proteasome subunits; This subfamily ...
247-414 1.64e-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: 192.17  E-value: 1.64e-57
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359718987 247 TFEHVKGVEEAKQELQEVVEF-LKNPQKFTILGGKLPKGILLVGPPGTGKTLLARAVAGEADVPFYYASGSEFDEMFVGV 325
Cdd:cd19502    1 TYEDIGGLDEQIREIREVVELpLKHPELFEELGIEPPKGVLLYGPPGTGKTLLAKAVANHTDATFIRVVGSELVQKYIGE 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359718987 326 GASRIRNLFREAKANAPCVIFIDELDSVGGKRIESPMHPYS--RQTINQLLAEMDGFKPNEGVIIIGATNFPEALDNALI 403
Cdd:cd19502   81 GARLVRELFEMAREKAPSIIFIDEIDAIGAKRFDSGTGGDRevQRTMLELLNQLDGFDPRGNIKVIMATNRPDILDPALL 160
                        170
                 ....*....|.
gi 359718987 404 RPGRFDMQVTV 414
Cdd:cd19502  161 RPGRFDRKIEF 171
CDC48 TIGR01243
AAA family ATPase, CDC48 subfamily; This subfamily of the AAA family ATPases includes two ...
246-467 9.18e-57

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


Pssm-ID: 273521 [Multi-domain]  Cd Length: 733  Bit Score: 205.53  E-value: 9.18e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359718987  246 VTFEHVKGVEEAKQELQEVVEF-LKNPQKFTILGGKLPKGILLVGPPGTGKTLLARAVAGEADVPFYYASGSEFDEMFVG 324
Cdd:TIGR01243 175 VTYEDIGGLKEAKEKIREMVELpMKHPELFEHLGIEPPKGVLLYGPPGTGKTLLAKAVANEAGAYFISINGPEIMSKYYG 254
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359718987  325 VGASRIRNLFREAKANAPCVIFIDELDSVGGKRiESPMHPYSRQTINQLLAEMDGFKPNEGVIIIGATNFPEALDNALIR 404
Cdd:TIGR01243 255 ESEERLREIFKEAEENAPSIIFIDEIDAIAPKR-EEVTGEVEKRVVAQLLTLMDGLKGRGRVIVIGATNRPDALDPALRR 333
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 359718987  405 PGRFDMQVTVPRPDVKGRTEILKWYLNKIKFDQSVDPEIIARGTVGFSGAELENLVNQAALKA 467
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 ...
257-409 2.13e-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: 183.25  E-value: 2.13e-54
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359718987 257 AKQELQEVVEF-LKNPQKFTILGGKLPKGILLVGPPGTGKTLLARAVAGEADVPFYYASGSEFDEMFVGVGASRIRNLFR 335
Cdd:cd19511    1 VKRELKEAVEWpLKHPDAFKRLGIRPPKGVLLYGPPGCGKTLLAKALASEAGLNFISVKGPELFSKYVGESERAVREIFQ 80
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 359718987 336 EAKANAPCVIFIDELDSVGGKRIESPMHPYSRQTINQLLAEMDGFKPNEGVIIIGATNFPEALDNALIRPGRFD 409
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 ...
251-412 3.46e-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: 180.18  E-value: 3.46e-53
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359718987 251 VKGVEEAKQELQEVVEF-LKNPQKFTILGGKLPKGILLVGPPGTGKTLLARAVAGEADVPFYYASGSEFDEMFVGVGASR 329
Cdd:cd19503    2 IGGLDEQIASLKELIELpLKYPELFRALGLKPPRGVLLHGPPGTGKTLLARAVANEAGANFLSISGPSIVSKYLGESEKN 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359718987 330 IRNLFREAKANAPCVIFIDELDSVGGKRiESPMHPYSRQTINQLLAEMDGFKPNEGVIIIGATNFPEALDNALIRPGRFD 409
Cdd:cd19503   82 LREIFEEARSHAPSIIFIDEIDALAPKR-EEDQREVERRVVAQLLTLMDGMSSRGKVVVIAATNRPDAIDPALRRPGRFD 160

                 ...
gi 359718987 410 MQV 412
Cdd:cd19503  161 REV 163
AAA pfam00004
ATPase family associated with various cellular activities (AAA); AAA family proteins often ...
285-416 3.14e-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: 3.14e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359718987  285 ILLVGPPGTGKTLLARAVAGEADVPFYYASGSEFDEMFVGVGASRIRNLFREAKANAPCVIFIDELDSVGGKRiESPMHP 364
Cdd:pfam00004   1 LLLYGPPGTGKTTLAKAVAKELGAPFIEISGSELVSKYVGESEKRLRELFEAAKKLAPCVIFIDEIDALAGSR-GSGGDS 79
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 359718987  365 YSRQTINQLLAEMDGFKPNEG-VIIIGATNFPEALDNALIrpGRFDMQVTVPR 416
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 ...
257-414 5.13e-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: 174.22  E-value: 5.13e-51
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359718987 257 AKQELQEVVEF-LKNPQKFTILGGKLPKGILLVGPPGTGKTLLARAVAGEADVPFYYASGSEFDEMFVGVGASRIRNLFR 335
Cdd:cd19529    1 VKQELKEAVEWpLLKPEVFKRLGIRPPKGILLYGPPGTGKTLLAKAVATESNANFISVKGPELLSKWVGESEKAIREIFR 80
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 359718987 336 EAKANAPCVIFIDELDSVGGKRIESPMHPYSRQTINQLLAEMDGFKPNEGVIIIGATNFPEALDNALIRPGRFDMQVTV 414
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 ...
251-415 1.06e-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: 1.06e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359718987 251 VKGVEEAKQELQEVVEF-LKNPQKFTILGGKLPKGILLVGPPGTGKTLLARAVAGEADVPFYYASGSEFDEMFVGVGASR 329
Cdd:cd19519    2 IGGCRKQLAQIREMVELpLRHPELFKAIGIKPPRGILLYGPPGTGKTLIARAVANETGAFFFLINGPEIMSKLAGESESN 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359718987 330 IRNLFREAKANAPCVIFIDELDSVGGKRiESPMHPYSRQTINQLLAEMDGFKPNEGVIIIGATNFPEALDNALIRPGRFD 409
Cdd:cd19519   82 LRKAFEEAEKNAPAIIFIDEIDAIAPKR-EKTHGEVERRIVSQLLTLMDGLKQRAHVIVMAATNRPNSIDPALRRFGRFD 160

                 ....*.
gi 359718987 410 MQVTVP 415
Cdd:cd19519  161 REIDIG 166
PTZ00361 PTZ00361
26 proteosome regulatory subunit 4-like protein; Provisional
234-488 5.60e-48

26 proteosome regulatory subunit 4-like protein; Provisional


Pssm-ID: 185575 [Multi-domain]  Cd Length: 438  Bit Score: 174.96  E-value: 5.60e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359718987 234 LDSAVDP-VQMKNV------TFEHVKGVEEAKQELQEVVEF-LKNPQKFTILGGKLPKGILLVGPPGTGKTLLARAVAGE 305
Cdd:PTZ00361 161 LLDEVDPlVSVMKVdkapleSYADIGGLEQQIQEIKEAVELpLTHPELYDDIGIKPPKGVILYGPPGTGKTLLAKAVANE 240
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359718987 306 ADVPFYYASGSEFDEMFVGVGASRIRNLFREAKANAPCVIFIDELDSVGGKRIE--SPMHPYSRQTINQLLAEMDGFKPN 383
Cdd:PTZ00361 241 TSATFLRVVGSELIQKYLGDGPKLVRELFRVAEENAPSIVFIDEIDAIGTKRYDatSGGEKEIQRTMLELLNQLDGFDSR 320
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359718987 384 EGVIIIGATNFPEALDNALIRPGRFDMQVTVPRPDVKGRTEILKWYLNKIKFDQSVDPEIIARGTVGFSGAELENLVNQA 463
Cdd:PTZ00361 321 GDVKVIMATNRIESLDPALIRPGRIDRKIEFPNPDEKTKRRIFEIHTSKMTLAEDVDLEEFIMAKDELSGADIKAICTEA 400
                        250       260
                 ....*....|....*....|....*
gi 359718987 464 ALKAAVDGKEMVTMKELEFSKDKIL 488
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 ...
250-412 8.66e-46

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: 160.26  E-value: 8.66e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359718987 250 HVKGVEEAKQELQEVVEFLK-NPQKFTILGGKLPKGILLVGPPGTGKTLLARAVAGEADVPFYYASGSEFDEMFVGVGAS 328
Cdd:cd19518    1 DIGGMDSTLKELCELLIHPIlPPEYFQHLGVEPPRGVLLHGPPGCGKTMLANAIAGELKVPFLKISATEIVSGVSGESEE 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359718987 329 RIRNLFREAKANAPCVIFIDELDSVGGKRiESPMHPYSRQTINQLLAEMDGFKPNE----GVIIIGATNFPEALDNALIR 404
Cdd:cd19518   81 KIRELFDQAISNAPCIVFIDEIDAITPKR-ESAQREMERRIVSQLLTCMDELNNEKtaggPVLVIGATNRPDSLDPALRR 159

                 ....*...
gi 359718987 405 PGRFDMQV 412
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 ...
258-414 3.04e-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: 3.04e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359718987 258 KQELQEVVEF-LKNPQKFTILGGKLPKGILLVGPPGTGKTLLARAVAGEADVPFYYASGSEFDEMFVGVGASRIRNLFRE 336
Cdd:cd19528    2 KRELQELVQYpVEHPDKFLKFGMTPSKGVLFYGPPGCGKTLLAKAIANECQANFISVKGPELLTMWFGESEANVRDIFDK 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359718987 337 AKANAPCVIFIDELDSVGGKRIESPMHP--YSRQTINQLLAEMDGFKPNEGVIIIGATNFPEALDNALIRPGRFDMQVTV 414
Cdd:cd19528   82 ARAAAPCVLFFDELDSIAKARGGNIGDAggAADRVINQILTEMDGMNTKKNVFIIGATNRPDIIDPAILRPGRLDQLIYI 161
PTZ00454 PTZ00454
26S protease regulatory subunit 6B-like protein; Provisional
235-481 1.87e-44

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


Pssm-ID: 240423 [Multi-domain]  Cd Length: 398  Bit Score: 164.17  E-value: 1.87e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359718987 235 DSAVDPVQMK---NVTFEHVKGVEEAKQELQEVVEF-LKNPQKFTILGGKLPKGILLVGPPGTGKTLLARAVAGEADVPF 310
Cdd:PTZ00454 128 DSSIQLLQMSekpDVTYSDIGGLDIQKQEIREAVELpLTCPELYEQIGIDPPRGVLLYGPPGTGKTMLAKAVAHHTTATF 207
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359718987 311 YYASGSEFDEMFVGVGASRIRNLFREAKANAPCVIFIDELDSVGGKRIESpmhpysrQT---------INQLLAEMDGFK 381
Cdd:PTZ00454 208 IRVVGSEFVQKYLGEGPRMVRDVFRLARENAPSIIFIDEVDSIATKRFDA-------QTgadrevqriLLELLNQMDGFD 280
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359718987 382 PNEGVIIIGATNFPEALDNALIRPGRFDMQVTVPRPDVKGRTEILKWYLNKIKFDQSVDPEIIARGTVGFSGAELENLVN 461
Cdd:PTZ00454 281 QTTNVKVIMATNRADTLDPALLRPGRLDRKIEFPLPDRRQKRLIFQTITSKMNLSEEVDLEDFVSRPEKISAADIAAICQ 360
                        250       260
                 ....*....|....*....|
gi 359718987 462 QAALKAAVDGKEMVTMKELE 481
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 ...
254-414 1.89e-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: 148.02  E-value: 1.89e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359718987 254 VEEAKQELQ-EVVEFLKNPQKFTILGGKLPKGILLVGPPGTGKTLLARAVAGEADVPFYYASGSEFDEMFVGVGASRIRN 332
Cdd:cd19530    1 LDHVREELTmSILRPIKRPDIYKALGIDLPTGVLLYGPPGCGKTLLAKAVANESGANFISVKGPELLNKYVGESERAVRQ 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359718987 333 LFREAKANAPCVIFIDELDSVGGKRIESPMHPYSRqTINQLLAEMDGFKPNEGVIIIGATNFPEALDNALIRPGRFDMQV 412
Cdd:cd19530   81 VFQRARASAPCVIFFDEVDALVPKRGDGGSWASER-VVNQLLTEMDGLEERSNVFVIAATNRPDIIDPAMLRPGRLDKTL 159

                 ..
gi 359718987 413 TV 414
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 ...
251-408 9.77e-41

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


Pssm-ID: 410917 [Multi-domain]  Cd Length: 163  Bit Score: 146.34  E-value: 9.77e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359718987 251 VKGVEEAKQELQEVVEF-LKNPQKFTiLGGKLPKGILLVGPPGTGKTLLARAVAGEADVPFYYASGSEFDEMFVGVGASR 329
Cdd:cd19509    1 IAGLDDAKEALKEAVILpSLRPDLFP-GLRGPPRGILLYGPPGTGKTLLARAVASESGSTFFSISASSLVSKWVGESEKI 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359718987 330 IRNLFREAKANAPCVIFIDELDSVGGKRIESPmHPYSRQTINQLLAEMDGF--KPNEGVIIIGATNFPEALDNALIRpgR 407
Cdd:cd19509   80 VRALFALARELQPSIIFIDEIDSLLSERGSGE-HEASRRVKTEFLVQMDGVlnKPEDRVLVLGATNRPWELDEAFLR--R 156

                 .
gi 359718987 408 F 408
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 ...
257-412 1.81e-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: 136.79  E-value: 1.81e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359718987 257 AKQELQEVVEF-LKNPQKFTILGGKLPKGILLVGPPGTGKTLLARAVAGEADVPFYYASGSEFDEMFVGVGASRIRNLFR 335
Cdd:cd19526    1 VKKALEETIEWpSKYPKIFASSPLRLRSGILLYGPPGCGKTLLASAIASECGLNFISVKGPELLNKYIGASEQNVRDLFS 80
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 359718987 336 EAKANAPCVIFIDELDSVGGKRIESPMHPYSRqTINQLLAEMDGFKPNEGVIIIGATNFPEALDNALIRPGRFDMQV 412
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 ...
258-409 1.17e-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: 1.17e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359718987 258 KQELQEVVEF-LKNPQKFTiLGGKLPKGILLVGPPGTGKTLLARAVAGEADVPFYYASGSEFDEMFVGVGASRIRNLFRE 336
Cdd:cd19527    2 KKEILDTIQLpLEHPELFS-SGLRKRSGILLYGPPGTGKTLLAKAIATECSLNFLSVKGPELINMYIGESEANVREVFQK 80
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 359718987 337 AKANAPCVIFIDELDSVGGKRIES-PMHPYSRQTINQLLAEMDGF-KPNEGVIIIGATNFPEALDNALIRPGRFD 409
Cdd:cd19527   81 ARDAKPCVIFFDELDSLAPSRGNSgDSGGVMDRVVSQLLAELDGMsSSGQDVFVIGATNRPDLLDPALLRPGRFD 155
RecA-like_VPS4 cd19521
ATPase domain of vacuolar protein sorting-associated protein 4; Vacuolar protein ...
245-414 1.13e-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: 1.13e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359718987 245 NVTFEHVKGVEEAKQELQEVVEF-LKNPQKFTilGGKLP-KGILLVGPPGTGKTLLARAVAGEADVPFYYASGSEFDEMF 322
Cdd:cd19521    3 NVKWEDVAGLEGAKEALKEAVILpVKFPHLFT--GNRKPwSGILLYGPPGTGKSYLAKAVATEANSTFFSVSSSDLVSKW 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359718987 323 VGVGASRIRNLFREAKANAPCVIFIDELDSVGGKRIESPMHPySRQTINQLLAEMDGF-KPNEGVIIIGATNFPEALDNA 401
Cdd:cd19521   81 MGESEKLVKQLFAMARENKPSIIFIDEVDSLCGTRGEGESEA-SRRIKTELLVQMNGVgNDSQGVLVLGATNIPWQLDSA 159
                        170
                 ....*....|...
gi 359718987 402 LIRpgRFDMQVTV 414
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; ...
246-404 1.41e-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: 1.41e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359718987 246 VTFEHVKGVEEAKQELQEVVEF-LKNPQKFTILGGKlPKGILLVGPPGTGKTLLARAVAGEADVPFYYASGSEFDEMFVG 324
Cdd:cd19525   19 INWADIAGLEFAKKTIKEIVVWpMLRPDIFTGLRGP-PKGILLFGPPGTGKTLIGKCIASQSGATFFSISASSLTSKWVG 97
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359718987 325 VGASRIRNLFREAKANAPCVIFIDELDSVGGKRIESPmHPYSRQTINQLLAEMDGFK--PNEGVIIIGATNFPEALDNAL 402
Cdd:cd19525   98 EGEKMVRALFSVARCKQPAVIFIDEIDSLLSQRGEGE-HESSRRIKTEFLVQLDGATtsSEDRILVVGATNRPQEIDEAA 176

                 ..
gi 359718987 403 IR 404
Cdd:cd19525  177 RR 178
pup_AAA TIGR03689
proteasome ATPase; In the Actinobacteria, as shown for Mycobacterium tuberculosis, some ...
245-431 3.35e-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: 130.98  E-value: 3.35e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359718987  245 NVTFEHVKGVEEAKQELQEVVE--FLkNPQKFTILGGKLPKGILLVGPPGTGKTLLARAVA--------GEADVPFYYAS 314
Cdd:TIGR03689 178 DVTYADIGGLGSQIEQIRDAVElpFL-HPELYREYGLKPPKGVLLYGPPGCGKTLIAKAVAnslaarigAEGGGKSYFLN 256
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359718987  315 --GSEFDEMFVGVGASRIRNLFREAKANA----PCVIFIDELDSV---GGKRIESPMHpysrQTI-NQLLAEMDGFKPNE 384
Cdd:TIGR03689 257 ikGPELLNKYVGETERQIRLIFQRAREKAsegrPVIVFFDEMDSLfrtRGSGVSSDVE----TTVvPQLLAEIDGVESLD 332
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 359718987  385 GVIIIGATNFPEALDNALIRPGRFDMQVTVPRPDVKGRTEILKWYLN 431
Cdd:TIGR03689 333 NVIVIGASNREDMIDPAILRPGRLDVKIRIERPDAEAAADIFAKYLT 379
RecA-like_KTNA1 cd19522
Katanin p60 ATPase-containing subunit A1; Katanin p60 ATPase-containing subunit A1 (KTNA1) is ...
251-404 6.49e-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: 6.49e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359718987 251 VKGVEEAKQELQE-VVEFLKNPQKFTilGGKLP-KGILLVGPPGTGKTLLARAVAGEADVPFYYASGSEFDEMFVGVGAS 328
Cdd:cd19522    2 IADLEEAKKLLEEaVVLPMWMPEFFK--GIRRPwKGVLMVGPPGTGKTLLAKAVATECGTTFFNVSSSTLTSKYRGESEK 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359718987 329 RIRNLFREAKANAPCVIFIDELDSVGGKRIESPMHPYSRQTINQLLAEMDGF-------KPNEGVIIIGATNFPEALDNA 401
Cdd:cd19522   80 LVRLLFEMARFYAPTTIFIDEIDSICSRRGTSEEHEASRRVKSELLVQMDGVggasendDPSKMVMVLAATNFPWDIDEA 159

                 ...
gi 359718987 402 LIR 404
Cdd:cd19522  160 LRR 162
RecA-like_Yta7-like cd19517
ATPase domain of Saccharomyces cerevisiae Yta7 and similar ATPase domains; Saccharomyces ...
251-409 2.75e-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: 2.75e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359718987 251 VKGVEEAKQELQEVVEF-LKNPQKFTILGGKLPKGILLVGPPGTGKTLLARAVA-----GEADVPFYYASGSEFDEMFVG 324
Cdd:cd19517    2 IGGLSHYINQLKEMVFFpLLYPEVFAKFKITPPRGVLFHGPPGTGKTLMARALAaecskGGQKVSFFMRKGADCLSKWVG 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359718987 325 VGASRIRNLFREAKANAPCVIFIDELDSVGGKRiESPMHPYSRQTINQLLAEMDGFKPNEGVIIIGATNFPEALDNALIR 404
Cdd:cd19517   82 EAERQLRLLFEEAYRMQPSIIFFDEIDGLAPVR-SSKQEQIHASIVSTLLALMDGLDNRGQVVVIGATNRPDALDPALRR 160

                 ....*
gi 359718987 405 PGRFD 409
Cdd:cd19517  161 PGRFD 165
RecA-like_spastin cd19524
ATPase domain of spastin; Spastin is an ATP-dependent microtubule-severing protein involved in ...
251-414 3.91e-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: 119.18  E-value: 3.91e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359718987 251 VKGVEEAKQELQEVVEF-LKNPQKFTILGGKlPKGILLVGPPGTGKTLLARAVAGEADVPFYYASGSEFDEMFVGVGASR 329
Cdd:cd19524    2 IAGQDLAKQALQEMVILpSLRPELFTGLRAP-ARGLLLFGPPGNGKTMLAKAVAAESNATFFNISAASLTSKYVGEGEKL 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359718987 330 IRNLFREAKANAPCVIFIDELDSVGGKRIESPmHPYSRQTINQLLAEMDGFK--PNEGVIIIGATNFPEALDNALIRpgR 407
Cdd:cd19524   81 VRALFAVARELQPSIIFIDEVDSLLSERSEGE-HEASRRLKTEFLIEFDGVQsnGDDRVLVMGATNRPQELDDAVLR--R 157

                 ....*..
gi 359718987 408 FDMQVTV 414
Cdd:cd19524  158 FTKRVYV 164
RecA-like_ATAD1 cd19520
ATPase domain of ATPase family AAA domain-containing protein 1 and similar ATPase domains; ...
253-408 9.97e-29

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: 9.97e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359718987 253 GVEEAKQELQEVVEF-LKNPQKFTilGGKL---PKGILLVGPPGTGKTLLARAVAGEADVPFYYASGSEFDEMFVGVGAS 328
Cdd:cd19520    4 GLDEVITELKELVILpLQRPELFD--NSRLlqpPKGVLLYGPPGCGKTMLAKATAKEAGARFINLQVSSLTDKWYGESQK 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359718987 329 RIRNLFREAKANAPCVIFIDELDSVGGKRiESPMHPYSRQTINQLLAEMDGF--KPNEGVIIIGATNFPEALDNALIR-- 404
Cdd:cd19520   82 LVAAVFSLASKLQPSIIFIDEIDSFLRQR-SSTDHEATAMMKAEFMSLWDGLstDGNCRVIVMGATNRPQDLDEAILRrm 160

                 ....
gi 359718987 405 PGRF 408
Cdd:cd19520  161 PKRF 164
AAA cd00009
The AAA+ (ATPases Associated with a wide variety of cellular Activities) superfamily ...
252-415 5.69e-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: 5.69e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359718987 252 KGVEEAKQELQEVVEFLKnpqkftilggklPKGILLVGPPGTGKTLLARAVAGEA---DVPFYYASGSEFDEMFVG---V 325
Cdd:cd00009    1 VGQEEAIEALREALELPP------------PKNLLLYGPPGTGKTTLARAIANELfrpGAPFLYLNASDLLEGLVVaelF 68
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359718987 326 GASRIRNLFREAKANAPCVIFIDELDSVGGKRIEspmhpysrQTINQLLAEMDGFKPNEGVIIIGATNFPEALDNALIRP 405
Cdd:cd00009   69 GHFLVRLLFELAEKAKPGVLFIDEIDSLSRGAQN--------ALLRVLETLNDLRIDRENVRVIGATNRPLLGDLDRALY 140
                        170
                 ....*....|
gi 359718987 406 GRFDMQVTVP 415
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; ...
277-414 6.55e-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: 6.55e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359718987 277 LGGKLPKGILLVGPPGTGKTLLARAV-----AGEADVpfyyASGSEFDEMFVGVGASRIRNLFREAKANAPC-------- 343
Cdd:cd19504   30 LGCKHVKGILLYGPPGTGKTLMARQIgkmlnAREPKI----VNGPEILNKYVGESEANIRKLFADAEEEQRRlgansglh 105
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 359718987 344 VIFIDELDSV----GGKRIESPMHPysrQTINQLLAEMDGFKPNEGVIIIGATNFPEALDNALIRPGRFDMQVTV 414
Cdd:cd19504  106 IIIFDEIDAIckqrGSMAGSTGVHD---TVVNQLLSKIDGVEQLNNILVIGMTNRKDLIDEALLRPGRLEVQMEI 177
RecA-like_BCS1 cd19510
Mitochondrial chaperone BCS1; Mitochondrial chaperone BCS1 is necessary for the assembly of ...
261-414 8.01e-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: 8.01e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359718987 261 LQEVVEFLKNPQKFTILGGKLPKGILLVGPPGTGKTLLARAVAGEADVPFYYASGSEfdemfVGVGASRIRNLFREAKAN 340
Cdd:cd19510    2 IDDLKDFIKNEDWYNDRGIPYRRGYLLYGPPGTGKSSFIAALAGELDYDICDLNLSE-----VVLTDDRLNHLLNTAPKQ 76
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 359718987 341 ApcVIFIDELDSVGGKRIESPMHPY-----SRQTINQLLAEMDGFKPNEGVIIIGATNFPEALDNALIRPGRFDMQVTV 414
Cdd:cd19510   77 S--IILLEDIDAAFESREHNKKNPSaygglSRVTFSGLLNALDGVASSEERIVFMTTNHIERLDPALIRPGRVDMKIYM 153
RecA-like_fidgetin cd19523
ATPase domain of fidgetin; Fidgetin (FIGN) is a ATP-dependent microtubule severing protein. ...
251-404 4.36e-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: 4.36e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359718987 251 VKGVEEAKQELQ-EVVEFLKNPQKFTILGgKLPKGILLVGPPGTGKTLLARAVAGEADVPFYYASGSEFDEMFVGVGASR 329
Cdd:cd19523    2 IAGLGALKAAIKeEVLWPLLRPDAFSGLL-RLPRSILLFGPRGTGKTLLGRCLASQLGATFLRLRGSTLVAKWAGEGEKI 80
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 359718987 330 IRNLFREAKANAPCVIFIDELDSVGGKRIESPmHPYSRQTInQLLAEMDGF--KPNEGVIIIGATNFPEALDNALIR 404
Cdd:cd19523   81 LQASFLAARCRQPSVLFISDLDALLSSQDDEA-SPVGRLQV-ELLAQLDGVlgSGEDGVLVVCTTSKPEEIDESLRR 155
ycf46 CHL00195
Ycf46; Provisional
245-490 8.13e-19

Ycf46; Provisional


Pssm-ID: 177094 [Multi-domain]  Cd Length: 489  Bit Score: 90.08  E-value: 8.13e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359718987 245 NVTFEHVKGVEEAKQELQEVVE-FLKNPQKFtilGGKLPKGILLVGPPGTGKTLLARAVAGEADVPFYYAsgsEFDEMF- 322
Cdd:CHL00195 224 NEKISDIGGLDNLKDWLKKRSTsFSKQASNY---GLPTPRGLLLVGIQGTGKSLTAKAIANDWQLPLLRL---DVGKLFg 297
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359718987 323 --VGVGASRIRNLFREAKANAPCVIFIDELDsvggkRIESPMHPYSRQ-TINQLLAEM-----DGFKPnegVIIIGATNF 394
Cdd:CHL00195 298 giVGESESRMRQMIRIAEALSPCILWIDEID-----KAFSNSESKGDSgTTNRVLATFitwlsEKKSP---VFVVATANN 369
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359718987 395 PEALDNALIRPGRFDMQVTVPRPDVKGRTEILKWYLNKIKFD--QSVDPEIIARGTVGFSGAELENLVNQaALKAAVDGK 472
Cdd:CHL00195 370 IDLLPLEILRKGRFDEIFFLDLPSLEEREKIFKIHLQKFRPKswKKYDIKKLSKLSNKFSGAEIEQSIIE-AMYIAFYEK 448
                        250
                 ....*....|....*...
gi 359718987 473 EmvtmkelEFSKDKILMG 490
Cdd:CHL00195 449 R-------EFTTDDILLA 459
AAA smart00382
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ...
282-418 7.54e-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: 80.88  E-value: 7.54e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359718987   282 PKGILLVGPPGTGKTLLARAVAGEADVP---FYYASGSEFDE--------------MFVGVGASRIRNLFREAKANAPCV 344
Cdd:smart00382   2 GEVILIVGPPGSGKTTLARALARELGPPgggVIYIDGEDILEevldqllliivggkKASGSGELRLRLALALARKLKPDV 81
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 359718987   345 IFIDELDSVGGKRIESPMhpysrqTINQLLAEMDGFKPNEGVIIIGATNFPEALDNALIRPgRFDMQVTVPRPD 418
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 ...
281-409 3.79e-16

ATPase domain of Ycf46 and similar ATPase domains; Ycf46 may play a role in the regulation of photosynthesis in cyanobacteria, especially in CO2 uptake and utilization. This subfamily belongs to the RecA-like NTPase family which includes the NTP binding domain of F1 and V1 H(+)ATPases, DnaB and related helicases as well as bacterial RecA and related eukaryotic and archaeal recombinases. The RecA-like NTPase family also includes bacterial conjugation proteins and related DNA transfer proteins involved in type II and type IV secretion.


Pssm-ID: 410915 [Multi-domain]  Cd Length: 161  Bit Score: 76.25  E-value: 3.79e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359718987 281 LPKGILLVGPPGTGKTLLARAVAGEADVPFYYASGSEFDEMFVGVGASRIRNLFREAKANAPCVIFIDELDSVGGKRIES 360
Cdd:cd19507   30 TPKGLLLVGIQGTGKSLTAKAIAGVWQLPLLRLDMGRLFGGLVGESESRLRQMIQTAEAIAPCVLWIDEIEKGFSNADSK 109
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 359718987 361 PMHPYSRQTINQLLAEM-DGFKPnegVIIIGATNFPEALDNALIRPGRFD 409
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; ...
277-409 1.97e-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: 62.78  E-value: 1.97e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359718987 277 LGGKLPKGILLVGPPGTGKTLLARAVAGEADVPFYYASGSEF--------------DEMFVGVGASRIRNLFREAKANAP 342
Cdd:cd19505    7 LGLSPSKGILLIGSIETGRSYLIKSLAANSYVPLIRISLNKLlynkpdfgnddwidGMLILKESLHRLNLQFELAKAMSP 86
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 359718987 343 CVIF---IDELDS--VGGKRIESPMhpYSRQTINQLLAEMDGFKPNEGVIIIGATNFPEALDNALIRPGRFD 409
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 ...
283-412 6.49e-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: 6.49e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359718987 283 KGILLVGPPGTGKTLLARAVAGEADVPFYYASGSEFDEMFVGvGASRIRNLFREA-KANAPCVIFIDELDSVGGKRIESP 361
Cdd:cd19512   23 RNILFYGPPGTGKTLFAKKLALHSGMDYAIMTGGDVAPMGRE-GVTAIHKVFDWAnTSRRGLLLFVDEADAFLRKRSTEK 101
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 359718987 362 MHPYSRQTINQLLAEMdGFKPNEGVIIIgATNFPEALDNALirPGRFDMQV 412
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 ...
438-481 4.81e-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: 52.16  E-value: 4.81e-09
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 359718987  438 SVDPEIIARGTVGFSGAELENLVNQAALKAAVDGKEMVTMKELE 481
Cdd:pfam17862   1 DVDLEELAERTEGFSGADLEALCREAALAALRRGLEAVTQEDLE 44
PRK13342 PRK13342
recombination factor protein RarA; Reviewed
276-349 8.26e-09

recombination factor protein RarA; Reviewed


Pssm-ID: 237355 [Multi-domain]  Cd Length: 413  Bit Score: 58.17  E-value: 8.26e-09
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 359718987 276 ILGGKLPKgILLVGPPGTGKTLLARAVAGEADVPFYYASGSefdemFVGVgaSRIRNLFREAKANA----PCVIFIDE 349
Cdd:PRK13342  31 IEAGRLSS-MILWGPPGTGKTTLARIIAGATDAPFEALSAV-----TSGV--KDLREVIEEARQRRsagrRTILFIDE 100
TIP49 COG1224
DNA helicase TIP49, TBP-interacting protein [Transcription];
253-318 1.28e-08

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


Pssm-ID: 440837 [Multi-domain]  Cd Length: 452  Bit Score: 57.67  E-value: 1.28e-08
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 359718987 253 GVEEAKQELQEVVEFLKNpqkftilgGKLP-KGILLVGPPGTGKTLLARAVAGE--ADVPFYYASGSEF 318
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 ...
281-356 4.45e-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: 53.54  E-value: 4.45e-08
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 359718987 281 LPKGILLVGPPGTGKTLLARAVAGEADVPFYYASGSEFDEM-FVGVGA-SRIRNLfreakanAPCVIFIDELDSVGGK 356
Cdd:cd19498   45 TPKNILMIGPTGVGKTEIARRLAKLAGAPFIKVEATKFTEVgYVGRDVeSIIRDL-------VEGIVFIDEIDKIAKR 115
RecA-like_Lon cd19500
lon protease homolog 2 peroxisomal; Lon protease (also known as Lon peptidase) is an ...
253-354 7.73e-08

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


Pssm-ID: 410908 [Multi-domain]  Cd Length: 182  Bit Score: 52.95  E-value: 7.73e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359718987 253 GVEEAKQELQE--VVEFLKNPQKFTILggklpkgiLLVGPPGTGKTLLARAVAGEADVPFYYAS-GSEFDE--------M 321
Cdd:cd19500   14 GLEDVKERILEylAVRKLKGSMKGPIL--------CLVGPPGVGKTSLGKSIARALGRKFVRISlGGVRDEaeirghrrT 85
                         90       100       110
                 ....*....|....*....|....*....|...
gi 359718987 322 FVGVGASRIRNLFREAKANAPcVIFIDELDSVG 354
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 ...
240-356 3.68e-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: 51.83  E-value: 3.68e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359718987 240 PVQMKNVTFEHVKGVEEAKQELQEVV----EFLKNPQKFTILGGKLPKG-ILLVGPPGTGKTLLARAVAGEADVPFYYAS 314
Cdd:cd19497    3 PKEIKEHLDKYVIGQERAKKVLSVAVynhyKRIRNNLKQKDDDVELEKSnILLIGPTGSGKTLLAQTLAKILDVPFAIAD 82
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 359718987 315 GSEFDEM-FVG--VgASRIRNLFREAKANAP----CVIFIDELDSVGGK 356
Cdd:cd19497   83 ATTLTEAgYVGedV-ENILLKLLQAADYDVEraqrGIVYIDEIDKIARK 130
RarA COG2256
Replication-associated recombination protein RarA (DNA-dependent ATPase) [Replication, ...
276-349 3.76e-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: 3.76e-07
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 359718987 276 ILGGKLPKgILLVGPPGTGKTLLARAVAGEADVPFYYASGsefdemfVGVGASRIRNLFREAKANA----PCVIFIDE 349
Cdd:COG2256   44 IEAGRLSS-MILWGPPGTGKTTLARLIANATDAEFVALSA-------VTSGVKDIREVIEEARERRaygrRTILFVDE 113
PRK04195 PRK04195
replication factor C large subunit; Provisional
247-356 5.75e-07

replication factor C large subunit; Provisional


Pssm-ID: 235250 [Multi-domain]  Cd Length: 482  Bit Score: 52.62  E-value: 5.75e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359718987 247 TFEHVKGVEEAKQELQEVVEflknpqkfTILGGKLPKGILLVGPPGTGKTLLARAVAGEADVPFYYASGSEF---DEM-- 321
Cdd:PRK04195  12 TLSDVVGNEKAKEQLREWIE--------SWLKGKPKKALLLYGPPGVGKTSLAHALANDYGWEVIELNASDQrtaDVIer 83
                         90       100       110
                 ....*....|....*....|....*....|....*
gi 359718987 322 FVGvGASRIRNLFREAKAnapcVIFIDELDSVGGK 356
Cdd:PRK04195  84 VAG-EAATSGSLFGARRK----LILLDEVDGIHGN 113
TIP49 pfam06068
TIP49 P-loop domain; This family consists of the C-terminal region of several eukaryotic and ...
233-318 6.21e-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: 51.93  E-value: 6.21e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359718987  233 GLDSAVDPVQMKnvtfEHVKGVEEAKQELQEVVEFLKNPQkftiLGGKlpkGILLVGPPGTGKTLLARAVAGE--ADVPF 310
Cdd:pfam06068  12 GLDEDGEARYVS----GGLVGQEKAREAAGVIVEMIKEGK----IAGR---AVLIAGPPGTGKTALAIAISKElgEDTPF 80

                  ....*...
gi 359718987  311 YYASGSEF 318
Cdd:pfam06068  81 TSISGSEV 88
T7SS_EccA TIGR03922
type VII secretion AAA-ATPase EccA; This model represents the AAA family ATPase, EccA, of the ...
253-470 7.78e-07

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


Pssm-ID: 188437 [Multi-domain]  Cd Length: 557  Bit Score: 52.15  E-value: 7.78e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359718987  253 GVEEAKQElqevVEFLKNPQKFTIL----GGKLP---KGILLVGPPGTGKTLLARAVAgeadvpfyyasgsefdEMFVGV 325
Cdd:TIGR03922 280 GLERVKRQ----VAALKSSTAMALAraerGLPVAqtsNHMLFAGPPGTGKTTIARVVA----------------KIYCGL 339
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359718987  326 GASR---IRNLFR-----------EAKANAPC------VIFIDELDSVGGKRIESPmHPYSRQTINQLLAEMDGFKPNEG 385
Cdd:TIGR03922 340 GVLRkplVREVSRadligqyigesEAKTNEIIdsalggVLFLDEAYTLVETGYGQK-DPFGLEAIDTLLARMENDRDRLV 418
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359718987  386 VIIIGatnFPEALDNAL-IRPGrfdmqvtvprpdVKGRteilkwYLNKIKFDQSVDPEIIARGTVgfSGAELENLVNQAA 464
Cdd:TIGR03922 419 VIGAG---YRKDLDKFLeVNEG------------LRSR------FTRVIEFPSYSPDELVEIARR--MATERDSVLDDAA 475

                  ....*.
gi 359718987  465 LKAAVD 470
Cdd:TIGR03922 476 ADALLE 481
AAA_5 pfam07728
AAA domain (dynein-related subfamily); This Pfam entry includes some of the AAA proteins not ...
284-408 1.21e-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: 48.06  E-value: 1.21e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359718987  284 GILLVGPPGTGKTLLARAVAG--EADVPFYYA--SGSEFDEMF-----VGVGASRIRNLFREAkANAPCVIFIDELDSVG 354
Cdd:pfam07728   1 GVLLVGPPGTGKTELAERLAAalSNRPVFYVQltRDTTEEDLFgrrniDPGGASWVDGPLVRA-AREGEIAVLDEINRAN 79
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 359718987  355 GKRIESpmhpysrqtINQLLAE-----MDGF----KPNEGVIIIGATNFPEA----LDNALIRpgRF 408
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 ...
285-403 5.29e-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: 5.29e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359718987 285 ILLVGPPGTGKTLLARAVAGEADV--PFYYASG--------SEFDEMFvGVGASRIRNLFR------EAKANAPCVIfID 348
Cdd:cd19508   55 VLLHGPPGTGKTSLCKALAQKLSIrlSSRYRYGqlieinshSLFSKWF-SESGKLVTKMFQkiqeliDDKDALVFVL-ID 132
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 359718987 349 ELDSVGGKRIESPMHPYSRQTI---NQLLAEMDGFKPNEGVIIIGATNFPEALDNALI 403
Cdd:cd19508  133 EVESLAAARSASSSGTEPSDAIrvvNAVLTQIDRIKRYHNNVILLTSNLLEKIDVAFV 190
CDC6 COG1474
Cdc6-related protein, AAA superfamily ATPase [Replication, recombination and repair];
260-399 8.42e-06

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


Pssm-ID: 441083 [Multi-domain]  Cd Length: 389  Bit Score: 48.69  E-value: 8.42e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359718987 260 ELQEVVEFLKnpqkfTILGGKLPKGILLVGPPGTGKTLLARAV-------AGEADVPFYYA------SGSEF-------D 319
Cdd:COG1474   34 EIEELASALR-----PALRGERPSNVLIYGPTGTGKTAVAKYVleeleeeAEERGVDVRVVyvncrqASTRYrvlsrilE 108
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359718987 320 EMFV-------GVGASRIRNLFREA--KANAPCVIFIDELDSVGGKRIESPMHPYSRqtinqLLAEMDGFKpnegVIIIG 390
Cdd:COG1474  109 ELGSgedipstGLSTDELFDRLYEAldERDGVLVVVLDEIDYLVDDEGDDLLYQLLR-----ANEELEGAR----VGVIG 179
                        170
                 ....*....|..
gi 359718987 391 ATN---FPEALD 399
Cdd:COG1474  180 ISNdleFLENLD 191
RecA-like_superfamily cd01120
RecA-like_NTPases; RecA-like NTPases. This superfamily includes the NTP binding domain of F1 ...
285-401 1.40e-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: 1.40e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359718987 285 ILLVGPPGTGKTLLARAVAGEA---DVPFYYASgsefdemFVGVGASRIRnlfREAKANAPCVIFIDELDSVGGKRIesp 361
Cdd:cd01120    1 ILITGPPGSGKTTLLLQFAEQAllsDEPVIFIS-------FLDTILEAIE---DLIEEKKLDIIIIDSLSSLARASQ--- 67
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 359718987 362 mhPYSRQTINQLLAEMDGFKPNEGVIIIgATNFPEALDNA 401
Cdd:cd01120   68 --GDRSSELLEDLAKLLRAARNTGITVI-ATIHSDKFDID 104
clpX PRK05342
ATP-dependent Clp protease ATP-binding subunit ClpX;
285-310 4.20e-05

ATP-dependent Clp protease ATP-binding subunit ClpX;


Pssm-ID: 235422 [Multi-domain]  Cd Length: 412  Bit Score: 46.31  E-value: 4.20e-05
                         10        20
                 ....*....|....*....|....*.
gi 359718987 285 ILLVGPPGTGKTLLARAVAGEADVPF 310
Cdd:PRK05342 111 ILLIGPTGSGKTLLAQTLARILDVPF 136
DnaX COG2812
DNA polymerase III, gamma/tau subunits [Replication, recombination and repair];
247-303 4.50e-05

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


Pssm-ID: 442061 [Multi-domain]  Cd Length: 340  Bit Score: 45.95  E-value: 4.50e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 359718987 247 TFEHVKGveeakQElqEVVEFLKNpqkfTILGGKLPKGILLVGPPGTGKTLLARAVA 303
Cdd:COG2812    8 TFDDVVG-----QE--HVVRTLKN----ALASGRLAHAYLFTGPRGVGKTTLARILA 53
ClpX COG1219
ATP-dependent protease Clp, ATPase subunit ClpX [Posttranslational modification, protein ...
285-310 6.12e-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: 6.12e-05
                         10        20
                 ....*....|....*....|....*.
gi 359718987 285 ILLVGPPGTGKTLLARAVAGEADVPF 310
Cdd:COG1219  112 ILLIGPTGSGKTLLAQTLARILDVPF 137
NACHT COG5635
Predicted NTPase, NACHT family domain [Signal transduction mechanisms];
262-387 1.01e-04

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


Pssm-ID: 444362 [Multi-domain]  Cd Length: 935  Bit Score: 45.57  E-value: 1.01e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359718987 262 QEVVEFLKNPQKFTILGGKLPKgILLVGPPGTGKTLLARAVA---------GEADVPFY-----YASGSEFDEM---FVG 324
Cdd:COG5635  161 LNLLERIESLKRLELLEAKKKR-LLILGEPGSGKTTLLRYLAlelaeryldAEDPIPILielrdLAEEASLEDLlaeALE 239
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 359718987 325 VGASRIRNLFREAKANAPCVIFIDELDsvggkriESPMHPYSRQTINQLLAEMDGFKPNEGVI 387
Cdd:COG5635  240 KRGGEPEDALERLLRNGRLLLLLDGLD-------EVPDEADRDEVLNQLRRFLERYPKARVII 295
HolB COG0470
DNA polymerase III, delta prime subunit [Replication, recombination and repair];
255-303 1.76e-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: 1.76e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*....
gi 359718987 255 EEAKQELQEVVEflknpqkftilGGKLPKGILLVGPPGTGKTLLARAVA 303
Cdd:COG0470    2 EEAWEQLLAAAE-----------SGRLPHALLLHGPPGIGKTTLALALA 39
MoxR COG0714
MoxR-like ATPase [General function prediction only]; MoxR-like ATPase is part of the Pathway ...
285-310 2.10e-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: 43.62  E-value: 2.10e-04
                         10        20
                 ....*....|....*....|....*.
gi 359718987 285 ILLVGPPGTGKTLLARAVAGEADVPF 310
Cdd:COG0714   34 LLLEGVPGVGKTTLAKALARALGLPF 59
ABC_ATPase cd00267
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ...
260-404 3.72e-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: 41.46  E-value: 3.72e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359718987 260 ELQEVVEFLKNPQKFTILGGKLPKG--ILLVGPPGTGKTLLARAVAGEADVPfyyaSGS-EFDEmfVGVGASRIRNLFRE 336
Cdd:cd00267    1 EIENLSFRYGGRTALDNVSLTLKAGeiVALVGPNGSGKSTLLRAIAGLLKPT----SGEiLIDG--KDIAKLPLEELRRR 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359718987 337 -------------------AKANAPCVIFIDELDsvggkrieSPMHPYSRQTINQLLAEMdgfkPNEGVIIIGATNFPEA 397
Cdd:cd00267   75 igyvpqlsggqrqrvalarALLLNPDLLLLDEPT--------SGLDPASRERLLELLREL----AEEGRTVIIVTHDPEL 142

                 ....*..
gi 359718987 398 LDNALIR 404
Cdd:cd00267  143 AELAADR 149
KaiC-like cd01124
Circadian Clock Protein KaiC; KaiC is a circadian clock protein, most studied in cyanobacteria. ...
276-377 3.75e-04

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


Pssm-ID: 410869 [Multi-domain]  Cd Length: 222  Bit Score: 42.64  E-value: 3.75e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359718987 276 ILGGKLPKG--ILLVGPPGTGKTLLARAvageadvpfYYASGSEFDE--MFVGVGaSRIRNLFREAKAnapcvIFIDELD 351
Cdd:cd01124   11 LLGGGIPKGsvTLLTGGPGTGKTLFGLQ---------FLYAGAKNGEpgLFFTFE-ESPERLLRNAKS-----FGWDFDE 75
                         90       100
                 ....*....|....*....|....*....
gi 359718987 352 SVGGKRI---ESPMHPYSRQTINQLLAEM 377
Cdd:cd01124   76 MEDEGKLiivDAPPTEAGRFSLDELLSRI 104
DnaA COG0593
Chromosomal replication initiation ATPase DnaA [Replication, recombination and repair];
285-508 4.45e-04

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


Pssm-ID: 440358 [Multi-domain]  Cd Length: 303  Bit Score: 42.87  E-value: 4.45e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359718987 285 ILLVGPPGTGKTLLARAVAGEA-----DVPFYYASGSEFDEMFVGVGASRIRNLFREAKANAPCVIfIDELDSVGGKrie 359
Cdd:COG0593   37 LFLYGGVGLGKTHLLHAIGNEAlennpGARVVYLTAEEFTNDFINAIRNNTIEEFKEKYRSVDVLL-IDDIQFLAGK--- 112
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359718987 360 spmhpYSRQ-----TINQLLAemdgfkpNEGVIIIGATNFPEALDNAL--IRpGRFDM--QVTVPRPDVKGRTEILKwyl 430
Cdd:COG0593  113 -----EATQeeffhTFNALRE-------AGKQIVLTSDRPPKELPGLEerLR-SRLEWglVVDIQPPDLETRIAILR--- 176
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359718987 431 NKIKFDQ-SVDPEI---IARgTVGFSGAELENLVNQAALKAAVDGKEmVTmkeLEFSKD--KILMGPERRSVEIDNKNKT 504
Cdd:COG0593  177 KKAADRGlELPDEVleyLAR-RIERNVRELEGALNRLDAYALLTGRP-IT---LELAREvlKDLLRAQKKEITIEDIQKA 251

                 ....
gi 359718987 505 ITAY 508
Cdd:COG0593  252 VAEY 255
ruvB PRK00080
Holliday junction branch migration DNA helicase RuvB;
285-349 4.45e-04

Holliday junction branch migration DNA helicase RuvB;


Pssm-ID: 234619 [Multi-domain]  Cd Length: 328  Bit Score: 42.81  E-value: 4.45e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 359718987 285 ILLVGPPGTGKTLLARAVAGEADVPFYYASGSEFDEmfvgvgASRIRNLFREAKANApcVIFIDE 349
Cdd:PRK00080  54 VLLYGPPGLGKTTLANIIANEMGVNIRITSGPALEK------PGDLAAILTNLEEGD--VLFIDE 110
TIGR02928 TIGR02928
orc1/cdc6 family replication initiation protein; Members of this protein family are found ...
259-399 5.27e-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: 43.01  E-value: 5.27e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359718987  259 QELQEVVEFLKnpqkfTILGGKLPKGILLVGPPGTGKTLLARAV-------AGEADVPFYYA------------------ 313
Cdd:TIGR02928  22 EQIEELAKALR-----PILRGSRPSNVFIYGKTGTGKTAVTKYVmkeleeaAEDRDVRVVTVyvncqildtlyqvlvela 96
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359718987  314 ---SGSEFDEMFVGVGASRI-RNLFREAKANAPCVIFI-DELDSVGGKRIESPMhpysrqtinQLL-AEMDGFKPNEGVI 387
Cdd:TIGR02928  97 nqlRGSGEEVPTTGLSTSEVfRRLYKELNERGDSLIIVlDEIDYLVGDDDDLLY---------QLSrARSNGDLDNAKVG 167
                         170
                  ....*....|....*
gi 359718987  388 IIGATN---FPEALD 399
Cdd:TIGR02928 168 VIGISNdlkFRENLD 182
44 PHA02544
clamp loader, small subunit; Provisional
279-354 5.29e-04

clamp loader, small subunit; Provisional


Pssm-ID: 222866 [Multi-domain]  Cd Length: 316  Bit Score: 42.67  E-value: 5.29e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359718987 279 GKLPKGILLVGPPGTGKTLLARAVAGEADVPFYYASGSEfdemfvgvgaSRIRNLFREAKANA--------PCVIFIDEL 350
Cdd:PHA02544  40 GRIPNMLLHSPSPGTGKTTVAKALCNEVGAEVLFVNGSD----------CRIDFVRNRLTRFAstvsltggGKVIIIDEF 109

                 ....
gi 359718987 351 DSVG 354
Cdd:PHA02544 110 DRLG 113
RAD55 COG0467
RecA-superfamily ATPase, KaiC/GvpD/RAD55 family [Signal transduction mechanisms];
276-299 5.67e-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: 5.67e-04
                         10        20
                 ....*....|....*....|....*.
gi 359718987 276 ILGGKLPKG--ILLVGPPGTGKTLLA 299
Cdd:COG0467   12 LLGGGLPRGssTLLSGPPGTGKTTLA 37
YifB COG0606
Predicted Mg-chelatase, contains ChlI-like and ATPase domains, YifB family [Posttranslational ...
285-304 7.32e-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: 7.32e-04
                         10        20
                 ....*....|....*....|
gi 359718987 285 ILLVGPPGTGKTLLARAVAG 304
Cdd:COG0606  214 LLMIGPPGSGKTMLARRLPG 233
McrB COG1401
5-methylcytosine-specific restriction endonuclease McrBC, GTP-binding regulatory subunit McrB ...
280-350 1.03e-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: 1.03e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359718987 280 KLPKGILLVGPPGTGKT----LLARAVAGEAD-----VPFY--YasgseFDEMFVG------------VGASRIRNLFRE 336
Cdd:COG1401  219 KTKKNVILAGPPGTGKTylarRLAEALGGEDNgriefVQFHpsW-----SYEDFLLgyrpsldegkyePTPGIFLRFCLK 293
                         90
                 ....*....|....*.
gi 359718987 337 AKAN--APCVIFIDEL 350
Cdd:COG1401  294 AEKNpdKPYVLIIDEI 309
AAA_22 pfam13401
AAA domain;
285-398 1.22e-03

AAA domain;


Pssm-ID: 379165 [Multi-domain]  Cd Length: 129  Bit Score: 39.25  E-value: 1.22e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359718987  285 ILLVGPPGTGKTLLAR-----AVAGEADVPFYYASGS----EFDEMFV---------GVGASRIRNLFREA--KANAPCV 344
Cdd:pfam13401   8 LVLTGESGTGKTTLLRrlleqLPEVRDSVVFVDLPSGtspkDLLRALLralglplsgRLSKEELLAALQQLllALAVAVV 87
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 359718987  345 IFIDELDSVggkriespmhpySRQTINQLLAEMDGFKPNEGVIIIGATNFPEAL 398
Cdd:pfam13401  88 LIIDEAQHL------------SLEALEELRDLLNLSSKLLQLILVGTPELRELL 129
RecA-like_ClpB_Hsp104-like cd19499
Chaperone protein ClpB/Hsp104 subfamily; Bacterial Caseinolytic peptidase B (ClpB) and ...
248-351 1.37e-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: 1.37e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359718987 248 FEHVKGVEEAKQELQEVVEF----LKNPQKftilggklPKG-ILLVGPPGTGKTLLARAVAGeadvpFYYASG------- 315
Cdd:cd19499   10 HERVVGQDEAVKAVSDAIRRaragLSDPNR--------PIGsFLFLGPTGVGKTELAKALAE-----LLFGDEdnlirid 76
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 359718987 316 -SEFDEMFVG----------VGASRIRNLFREAKANAPCVIFIDELD 351
Cdd:cd19499   77 mSEYMEKHSVsrligappgyVGYTEGGQLTEAVRRKPYSVVLLDEIE 123
PRK08116 PRK08116
hypothetical protein; Validated
243-305 1.97e-03

hypothetical protein; Validated


Pssm-ID: 236153 [Multi-domain]  Cd Length: 268  Bit Score: 40.77  E-value: 1.97e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 359718987 243 MKNVTFEHVKGVEEAKQELQEVVEFLKNpqkFTILGGKlPKGILLVGPPGTGKTLLARAVAGE 305
Cdd:PRK08116  79 FRNSTFENFLFDKGSEKAYKIARKYVKK---FEEMKKE-NVGLLLWGSVGTGKTYLAACIANE 137
AAA_2 pfam07724
AAA domain (Cdc48 subfamily); This Pfam entry includes some of the AAA proteins not detected ...
282-351 2.01e-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: 2.01e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359718987  282 PKG-ILLVGPPGTGKTLLARAVAGEADV---PFYYASGSEFDE-----MFVG-----VGASRIRNLFREAKANAPCVIFI 347
Cdd:pfam07724   2 PIGsFLFLGPTGVGKTELAKALAELLFGderALIRIDMSEYMEehsvsRLIGappgyVGYEEGGQLTEAVRRKPYSIVLI 81

                  ....
gi 359718987  348 DELD 351
Cdd:pfam07724  82 DEIE 85
Mg_chelatase pfam01078
Magnesium chelatase, subunit ChlI; Magnesium-chelatase is a three-component enzyme that ...
285-304 3.70e-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: 3.70e-03
                          10        20
                  ....*....|....*....|
gi 359718987  285 ILLVGPPGTGKTLLARAVAG 304
Cdd:pfam01078  25 LLMIGPPGSGKTMLAKRLPG 44
rfc PRK00440
replication factor C small subunit; Reviewed
247-352 3.84e-03

replication factor C small subunit; Reviewed


Pssm-ID: 234763 [Multi-domain]  Cd Length: 319  Bit Score: 39.86  E-value: 3.84e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359718987 247 TFEHVKGVEEAKQELQEVVEflknpqkftilGGKLPKgILLVGPPGTGKT----LLARAVAGEadvpfYY--------AS 314
Cdd:PRK00440  15 TLDEIVGQEEIVERLKSYVK-----------EKNMPH-LLFAGPPGTGKTtaalALARELYGE-----DWrenflelnAS 77
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 359718987 315 gsefDEMFVGVGASRIRNLFREAKAN-APC-VIFIDELDS 352
Cdd:PRK00440  78 ----DERGIDVIRNKIKEFARTAPVGgAPFkIIFLDEADN 113
RuvB_N pfam05496
Holliday junction DNA helicase RuvB P-loop domain; The RuvB protein makes up part of the ...
285-315 4.15e-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: 4.15e-03
                          10        20        30
                  ....*....|....*....|....*....|.
gi 359718987  285 ILLVGPPGTGKTLLARAVAGEADVPFYYASG 315
Cdd:pfam05496  36 VLLYGPPGLGKTTLANIIANEMGVNIRITSG 66
RuvB COG2255
Holliday junction resolvasome RuvABC, ATP-dependent DNA helicase subunit RuvB [Replication, ...
285-315 4.62e-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: 39.68  E-value: 4.62e-03
                         10        20        30
                 ....*....|....*....|....*....|.
gi 359718987 285 ILLVGPPGTGKTLLARAVAGEADVPFYYASG 315
Cdd:COG2255   57 VLLYGPPGLGKTTLAHIIANEMGVNIRITSG 87
ruvB TIGR00635
Holliday junction DNA helicase, RuvB subunit; All proteins in this family for which functions ...
247-410 5.13e-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: 5.13e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359718987  247 TFEHVKGVEEAKQELQEVVEFLKNPQKftilggkLPKGILLVGPPGTGKTLLARAVAGEADVPFYYASGSEFDEmfvgvg 326
Cdd:TIGR00635   2 LLAEFIGQEKVKEQLQLFIEAAKMRQE-------ALDHLLLYGPPGLGKTTLAHIIANEMGVNLKITSGPALEK------ 68
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359718987  327 ASRIRNLFREAKANApcVIFIDELdsvggkriespmHPYSRQTINQLLAEMDGFK--------PNEGVI--------IIG 390
Cdd:TIGR00635  69 PGDLAAILTNLEEGD--VLFIDEI------------HRLSPAVEELLYPAMEDFRldivigkgPSARSVrldlppftLVG 134
                         170       180
                  ....*....|....*....|
gi 359718987  391 ATNFPEALDNALIrpGRFDM 410
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 ...
281-395 5.61e-03

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


Pssm-ID: 410914 [Multi-domain]  Cd Length: 160  Bit Score: 38.28  E-value: 5.61e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359718987 281 LPKGILLVGPPGTGKTLLARAVAGEADVPFYYASGSEFDEMFVGVGASR--IRNLFREAKANAPCVIFIDELDSVGGKRI 358
Cdd:cd19506   25 LVKSLLLAGPSGVGKKMLVHAICTETGANLFNLSPSNIAGKYPGKNGLQmmLHLVLKVARQLQPSVIWIGDAEKTFYKKV 104
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 359718987 359 ---ESPMHPYS-RQTINQLLAEMdgfKPNEGVIIIGATNFP 395
Cdd:cd19506  105 pktEKQLDPKRlKKDLPKILKSL---KPEDRVLIVGTTSRP 142
ExeA COG3267
Type II secretory pathway ATPase component GspA/ExeA/MshM [Intracellular trafficking, ...
285-349 7.95e-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: 38.62  E-value: 7.95e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359718987 285 ILLVGPPGTGKTLLARAVAGE-------ADVPFYYASGSEFDEMF---VGVGASRI----------RNLFREAKANAPCV 344
Cdd:COG3267   46 VVLTGEVGTGKTTLLRRLLERlpddvkvAYIPNPQLSPAELLRAIadeLGLEPKGAskadllrqlqEFLLELAAAGRRVV 125

                 ....*
gi 359718987 345 IFIDE 349
Cdd:COG3267  126 LIIDE 130
DnaC COG1484
DNA replication protein DnaC [Replication, recombination and repair];
283-350 8.48e-03

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


Pssm-ID: 441093 [Multi-domain]  Cd Length: 242  Bit Score: 38.61  E-value: 8.48e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 359718987 283 KGILLVGPPGTGKTLLARAVAGEA-----DVPFYYASgSEFDEMfvgVGASRIRNLFREAK--ANAPCVIfIDEL 350
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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