NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|303291081|ref|XP_003064827|]
View 

uncharacterized protein MICPUCDRAFT_67802 [Micromonas pusilla CCMP1545]

Protein Classification

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
RecA-like_VPS4 cd19521
ATPase domain of vacuolar protein sorting-associated protein 4; Vacuolar protein ...
 135-305 8.51e-114

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: 331.44  E-value: 8.51e-114
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 303291081 135 KPDVKWDDVAGLTSAKEALKEAVILPVKFPQFFTGKRKAWSGFLLYGPPGTGKSFLAKAVATEADSTFFSISSSDLVSKW 214
Cdd:cd19521    1 KPNVKWEDVAGLEGAKEALKEAVILPVKFPHLFTGNRKPWSGILLYGPPGTGKSYLAKAVATEANSTFFSVSSSDLVSKW 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 303291081 215 MGESEKLVNQLFTMAREKSPSIIFIDEIDALCGARGEgGESEASRRIKTEILVQMQGVGNEAGRVLVLAATNTPYQLDQA 294
Cdd:cd19521   81 MGESEKLVKQLFAMARENKPSIIFIDEVDSLCGTRGE-GESEASRRIKTELLVQMNGVGNDSQGVLVLGATNIPWQLDSA 159

                        170
                 ....*....|.
gi 303291081 295 VRRRFDKRIYI 305
Cdd:cd19521  160 IRRRFEKRIYI 170
cell_div_CdvC super family cl49147
cell division protein CdvC;
12-444 1.76e-73

cell division protein CdvC;


The actual alignment was detected with superfamily member NF041006:

Pssm-ID: 468935 [Multi-domain]  Cd Length: 371  Bit Score: 235.40  E-value: 1.76e-73
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 303291081  12 EKAIALVKEAVERDKASEYAAAFKLYTSALDHFTVYLK-YEKNPMMQ---QTIKtkftEYLERAEELKKLmdaddaaadg 87
Cdd:NF041006   9 EMARKYAIAAVKADKEGRYEEAINNYKKAIEILTQIVRlYPDSPLRHayeQMIN----EYKKRIEVLEEL---------- 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 303291081  88 RTNPNASPELIKArpkdtkkggvgkggaEDDEMskmrgalggaIVTEKPDVKWDDVAGLTSAKEALKEAVILPVKFPQFF 167
Cdd:NF041006  75 VPAEPAGPDVEKE---------------SDEEL----------VVKEKPKVTFSDIVGLEDVKEALKEAIVYPSKRPDLF 129

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 303291081 168 TgkrKAW-SGFLLYGPPGTGKSFLAKAVATEADSTFFSISSSDLVSKWMGESEKLVNQLFTMAREKS-----PSIIFIDE 241
Cdd:NF041006 130 P---LGWpRGILLYGPPGCGKTMLAAAVANEIDSEFIHVDAASIMSKWLGEAEKNVAKIFKKAREKSkeegkPAIIFIDE 206

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 303291081 242 IDALCGARGE--GGESeasrRIKTEILVQMQGV--GNEAGRVLVLAATNTPYQLDQAVRRRFDKRIYIPLPDAPARAHMF 317
Cdd:NF041006 207 IDALLGVYSSevGGEV----RVRNQFLKEMDGLqdKSENYHVYVIGATNKPWRLDEPFLRRFQKRIYIPLPDREQRLELL 282

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 303291081 318 RVHVGETPHDlTDADFQSLGAQSEGFSGSDIDHVVkdvlyepvrktqEATHFktttgpdgderyvpcspgdpdaweRTLE 397
Cdd:NF041006 283 KYYTSKIKLE-NDVDLDELAEMTEGYTASDIRDIV------------QAAHM------------------------RVVK 325

                        410       420       430       440
                 ....*....|....*....|....*....|....*....|....*..
gi 303291081 398 QLAEDGLGErvhPPPISANDFRKVLARARPTVAAGDLEEHERFTREF 444
Cdd:NF041006 326 EMFEKGLGE---PRPITMEDFKEVLKIRKPSVNQEMLKAYEAWHEKF 369
 
Name Accession Description Interval E-value
RecA-like_VPS4 cd19521
ATPase domain of vacuolar protein sorting-associated protein 4; Vacuolar protein ...
 135-305 8.51e-114

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: 331.44  E-value: 8.51e-114
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 303291081 135 KPDVKWDDVAGLTSAKEALKEAVILPVKFPQFFTGKRKAWSGFLLYGPPGTGKSFLAKAVATEADSTFFSISSSDLVSKW 214
Cdd:cd19521    1 KPNVKWEDVAGLEGAKEALKEAVILPVKFPHLFTGNRKPWSGILLYGPPGTGKSYLAKAVATEANSTFFSVSSSDLVSKW 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 303291081 215 MGESEKLVNQLFTMAREKSPSIIFIDEIDALCGARGEgGESEASRRIKTEILVQMQGVGNEAGRVLVLAATNTPYQLDQA 294
Cdd:cd19521   81 MGESEKLVKQLFAMARENKPSIIFIDEVDSLCGTRGE-GESEASRRIKTELLVQMNGVGNDSQGVLVLGATNIPWQLDSA 159

                        170
                 ....*....|.
gi 303291081 295 VRRRFDKRIYI 305
Cdd:cd19521  160 IRRRFEKRIYI 170
RPT1 COG1222
ATP-dependent 26S proteasome regulatory subunit [Posttranslational modification, protein ...
 125-354 1.75e-82

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


Pssm-ID: 440835 [Multi-domain]  Cd Length: 326  Bit Score: 256.86  E-value: 1.75e-82
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 303291081 125 GALGGAIVTEKPDVKWDDVAGLTSAKEALKEAVILPVKFPQFFT--GKRkAWSGFLLYGPPGTGKSFLAKAVATEADSTF 202
Cdd:COG1222   62 TPRGTAVPAESPDVTFDDIGGLDEQIEEIREAVELPLKNPELFRkyGIE-PPKGVLLYGPPGTGKTLLAKAVAGELGAPF 140

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 303291081 203 FSISSSDLVSKWMGESEKLVNQLFTMAREKSPSIIFIDEIDALCGARGEGGESEASRRIKTEILVQMQGVgNEAGRVLVL 282
Cdd:COG1222  141 IRVRGSELVSKYIGEGARNVREVFELAREKAPSIIFIDEIDAIAARRTDDGTSGEVQRTVNQLLAELDGF-ESRGDVLII 219

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 303291081 283 AATNTPYQLDQAVRR--RFDKRIYIPLPDAPARAHMFRVHVGETPhDLTDADFQSLGAQSEGFSGSDIDHVVKD 354
Cdd:COG1222  220 AATNRPDLLDPALLRpgRFDRVIEVPLPDEEAREEILKIHLRDMP-LADDVDLDKLAKLTEGFSGADLKAIVTE 292
cell_div_CdvC NF041006
cell division protein CdvC;
12-444 1.76e-73

cell division protein CdvC;


Pssm-ID: 468935 [Multi-domain]  Cd Length: 371  Bit Score: 235.40  E-value: 1.76e-73
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 303291081  12 EKAIALVKEAVERDKASEYAAAFKLYTSALDHFTVYLK-YEKNPMMQ---QTIKtkftEYLERAEELKKLmdaddaaadg 87
Cdd:NF041006   9 EMARKYAIAAVKADKEGRYEEAINNYKKAIEILTQIVRlYPDSPLRHayeQMIN----EYKKRIEVLEEL---------- 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 303291081  88 RTNPNASPELIKArpkdtkkggvgkggaEDDEMskmrgalggaIVTEKPDVKWDDVAGLTSAKEALKEAVILPVKFPQFF 167
Cdd:NF041006  75 VPAEPAGPDVEKE---------------SDEEL----------VVKEKPKVTFSDIVGLEDVKEALKEAIVYPSKRPDLF 129

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 303291081 168 TgkrKAW-SGFLLYGPPGTGKSFLAKAVATEADSTFFSISSSDLVSKWMGESEKLVNQLFTMAREKS-----PSIIFIDE 241
Cdd:NF041006 130 P---LGWpRGILLYGPPGCGKTMLAAAVANEIDSEFIHVDAASIMSKWLGEAEKNVAKIFKKAREKSkeegkPAIIFIDE 206

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 303291081 242 IDALCGARGE--GGESeasrRIKTEILVQMQGV--GNEAGRVLVLAATNTPYQLDQAVRRRFDKRIYIPLPDAPARAHMF 317
Cdd:NF041006 207 IDALLGVYSSevGGEV----RVRNQFLKEMDGLqdKSENYHVYVIGATNKPWRLDEPFLRRFQKRIYIPLPDREQRLELL 282

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 303291081 318 RVHVGETPHDlTDADFQSLGAQSEGFSGSDIDHVVkdvlyepvrktqEATHFktttgpdgderyvpcspgdpdaweRTLE 397
Cdd:NF041006 283 KYYTSKIKLE-NDVDLDELAEMTEGYTASDIRDIV------------QAAHM------------------------RVVK 325

                        410       420       430       440
                 ....*....|....*....|....*....|....*....|....*..
gi 303291081 398 QLAEDGLGErvhPPPISANDFRKVLARARPTVAAGDLEEHERFTREF 444
Cdd:NF041006 326 EMFEKGLGE---PRPITMEDFKEVLKIRKPSVNQEMLKAYEAWHEKF 369
SpoVK COG0464
AAA+-type ATPase, SpoVK/Ycf46/Vps4 family [Cell wall/membrane/envelope biogenesis, Cell cycle ...
 8-361 8.56e-70

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: 226.72  E-value: 8.56e-70
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 303291081   8 IAIREKAIALVKEAVERDKASEYAAAFKLYTSALDHFTVYLKYEKNPMMQQTIKTKFTEYLERAEELKKLMDADDAAADG 87
Cdd:COG0464   31 LALAAALLLLLLLLLLLLLALLLVELLLLLLSGALAALLLLALLLLALLALLAALLSALELLLLGELLLLLLLLLLLLLL 110

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 303291081  88 RTNPNASPELIKARPKDTKKGGVGKGGAEDDemskmrgALGGAIVTEKPDVKWDDVAGLTSAKEALKEAVILPVKFPQFF 167
Cdd:COG0464  111 LLDLERALLELLRESAEALALAAPLVTYEDI-------GGLEEELLELREAILDDLGGLEEVKEELRELVALPLKRPELR 183

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 303291081 168 TGKRKAWS-GFLLYGPPGTGKSFLAKAVATEADSTFFSISSSDLVSKWMGESEKLVNQLFTMAREKSPSIIFIDEIDALC 246
Cdd:COG0464  184 EEYGLPPPrGLLLYGPPGTGKTLLARALAGELGLPLIEVDLSDLVSKYVGETEKNLREVFDKARGLAPCVLFIDEADALA 263

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 303291081 247 GARGEGGESeASRRIKTEILVQMQGVgneAGRVLVLAATNTPYQLDQAVRRRFDKRIYIPLPDAPARAHMFRVHVGETPH 326
Cdd:COG0464  264 GKRGEVGDG-VGRRVVNTLLTEMEEL---RSDVVVIAATNRPDLLDPALLRRFDEIIFFPLPDAEERLEIFRIHLRKRPL 339

                        330       340       350
                 ....*....|....*....|....*....|....*
gi 303291081 327 DlTDADFQSLGAQSEGFSGSDIDHVVKDVLYEPVR 361
Cdd:COG0464  340 D-EDVDLEELAEATEGLSGADIRNVVRRAALQALR 373
PRK03992 PRK03992
proteasome-activating nucleotidase; Provisional
 132-353 6.61e-61

proteasome-activating nucleotidase; Provisional


Pssm-ID: 179699 [Multi-domain]  Cd Length: 389  Bit Score: 203.14  E-value: 6.61e-61
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 303291081 132 VTEKPDVKWDDVAGLTSAKEALKEAVILPVKFPQFFtgkRK----AWSGFLLYGPPGTGKSFLAKAVATEADSTFFSISS 207
Cdd:PRK03992 122 VIESPNVTYEDIGGLEEQIREVREAVELPLKKPELF---EEvgiePPKGVLLYGPPGTGKTLLAKAVAHETNATFIRVVG 198

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 303291081 208 SDLVSKWMGESEKLVNQLFTMAREKSPSIIFIDEIDALCGAR---GEGGESEASRRIkTEILVQMQGVgNEAGRVLVLAA 284
Cdd:PRK03992 199 SELVQKFIGEGARLVRELFELAREKAPSIIFIDEIDAIAAKRtdsGTSGDREVQRTL-MQLLAEMDGF-DPRGNVKIIAA 276

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 303291081 285 TNTPYQLDQAVRR--RFDKRIYIPLPDAPARAHMFRVH-----VGEtphdltDADFQSLGAQSEGFSGSDIDHVVK 353
Cdd:PRK03992 277 TNRIDILDPAILRpgRFDRIIEVPLPDEEGRLEILKIHtrkmnLAD------DVDLEELAELTEGASGADLKAICT 346
CDC48 TIGR01243
AAA family ATPase, CDC48 subfamily; This subfamily of the AAA family ATPases includes two ...
 131-445 1.50e-59

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: 207.45  E-value: 1.50e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 303291081  131 IVTEKPDVKWDDVAGLTSAKEALKEAVILPVKFPQFFT--GKRKAwSGFLLYGPPGTGKSFLAKAVATEADSTFFSISSS 208
Cdd:TIGR01243 443 VLVEVPNVRWSDIGGLEEVKQELREAVEWPLKHPEIFEkmGIRPP-KGVLLFGPPGTGKTLLAKAVATESGANFIAVRGP 521

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 303291081  209 DLVSKWMGESEKLVNQLFTMAREKSPSIIFIDEIDALCGARGEGGESEASRRIKTEILVQMQGVgNEAGRVLVLAATNTP 288
Cdd:TIGR01243 522 EILSKWVGESEKAIREIFRKARQAAPAIIFFDEIDAIAPARGARFDTSVTDRIVNQLLTEMDGI-QELSNVVVIAATNRP 600

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 303291081  289 YQLDQAVRR--RFDKRIYIPLPDAPARAHMFRVHVGETPHDlTDADFQSLGAQSEGFSGSDIDHVVKDVLYEPVRKTQEA 366
Cdd:TIGR01243 601 DILDPALLRpgRFDRLILVPPPDEEARKEIFKIHTRSMPLA-EDVDLEELAEMTEGYTGADIEAVCREAAMAALRESIGS 679

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 303291081  367 ThfktttgpdgderyvpcspgdpdawerTLEQLaEDGLGERVHPPPISANDFRKVLARARPTVAAGDLEEHERFTREFG 445
Cdd:TIGR01243 680 P---------------------------AKEKL-EVGEEEFLKDLKVEMRHFLEALKKVKPSVSKEDMLRYERLAKELK 730
AAA pfam00004
ATPase family associated with various cellular activities (AAA); AAA family proteins often ...
 178-307 4.31e-57

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


Pssm-ID: 459627 [Multi-domain]  Cd Length: 130  Bit Score: 184.33  E-value: 4.31e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 303291081  178 LLYGPPGTGKSFLAKAVATEADSTFFSISSSDLVSKWMGESEKLVNQLFTMAREKSPSIIFIDEIDALCGARGEGGESEa 257
Cdd:pfam00004   2 LLYGPPGTGKTTLAKAVAKELGAPFIEISGSELVSKYVGESEKRLRELFEAAKKLAPCVIFIDEIDALAGSRGSGGDSE- 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 303291081  258 SRRIKTEILVQMQGVGNEAGRVLVLAATNTPYQLDQAVRRRFDKRIYIPL 307
Cdd:pfam00004  81 SRRVVNQLLTELDGFTSSNSKVIVIAATNRPDKLDPALLGRFDRIIEFPL 130
Vps4_C pfam09336
Vps4 C terminal oligomerization domain; This domain is found at the C terminal of ATPase ...
 381-445 3.98e-25

Vps4 C terminal oligomerization domain; This domain is found at the C terminal of ATPase proteins involved in vacuolar sorting. It forms an alpha helix structure and is required for oligomerization.


Pssm-ID: 462762 [Multi-domain]  Cd Length: 61  Bit Score: 97.57  E-value: 3.98e-25
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 303291081  381 YVPCSPGDPDAWERTLEQLAedglGERVHPPPISANDFRKVLARARPTVAAGDLEEHERFTREFG 445
Cdd:pfam09336   1 LTPCSPGDPGAIEMTWMDIP----SDKLLEPPVTMKDFLKALKSSRPTVSKEDLEKYEEFTKEFG 61
MIT_VPS4 cd02678
MIT: domain contained within Microtubule Interacting and Trafficking molecules. This ...
 11-76 9.52e-23

MIT: domain contained within Microtubule Interacting and Trafficking molecules. This sub-family of MIT domains is found in intracellular protein transport proteins of the AAA-ATPase family. The molecular function of the MIT domain is unclear.


Pssm-ID: 239141  Cd Length: 75  Bit Score: 91.17  E-value: 9.52e-23
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 303291081  11 REKAIALVKEAVERDKASEYAAAFKLYTSALDHFTVYLKYEKNPMMQQTIKTKFTEYLERAEELKK 76
Cdd:cd02678    3 LQKAIELVKKAIEEDNAGNYEEALRLYQHALEYFMHALKYEKNPKSKESIRAKCTEYLDRAEKLKE 68
AAA smart00382
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ...
 178-309 1.02e-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: 82.42  E-value: 1.02e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 303291081   178 LLYGPPGTGKSFLAKAVATEADST---FFSISSSDL--------------VSKWMGESEKLVNQLFTMAREKSPSIIFID 240
Cdd:smart00382   6 LIVGPPGSGKTTLARALARELGPPgggVIYIDGEDIleevldqllliivgGKKASGSGELRLRLALALARKLKPDVLILD 85

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 303291081   241 EIDALCGARGEGGESEASRRIKTEILVQMqgvgneaGRVLVLAATNTPYQLDQA-VRRRFDKRIYIPLPD 309
Cdd:smart00382  86 EITSLLDAEQEALLLLLEELRLLLLLKSE-------KNLTVILTTNDEKDLGPAlLRRRFDRRIVLLLIL 148
MIT smart00745
Microtubule Interacting and Trafficking molecule domain;
12-77 4.49e-14

Microtubule Interacting and Trafficking molecule domain;


Pssm-ID: 197854  Cd Length: 77  Bit Score: 66.95  E-value: 4.49e-14
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 303291081    12 EKAIALVKEAVERDKASEYAAAFKLYTSALDHFTVYLKYEKNPMMQQTIKTKFTEYLERAEELKKL 77
Cdd:smart00745   6 SKAKELISKALKADEAGNYEEALELYKKAIEYLLEGIKVESDSKRREALKAKAAEYLDRAEEIKKS 71
IS21_help_AAA NF038214
IS21-like element helper ATPase IstB; This protein family model resembles PF01695, but was ...
 178-242 3.71e-04

IS21-like element helper ATPase IstB; This protein family model resembles PF01695, but was built to hit full-length AAA+ ATPases of IS21 family IS (insertion sequence) elements.


Pssm-ID: 439516  Cd Length: 232  Bit Score: 41.69  E-value: 3.71e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 303291081 178 LLYGPPGTGKSFLAKAVATEA----DSTFFsISSSDLVSKWM-----GESEKLVNQLftmAReksPSIIFIDEI 242
Cdd:NF038214  94 LLLGPPGTGKTHLAIALGYAAcrqgYRVRF-TTAADLVEQLAqaradGRLGRLLRRL---AR---YDLLIIDEL 160
 
Name Accession Description Interval E-value
RecA-like_VPS4 cd19521
ATPase domain of vacuolar protein sorting-associated protein 4; Vacuolar protein ...
 135-305 8.51e-114

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: 331.44  E-value: 8.51e-114
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 303291081 135 KPDVKWDDVAGLTSAKEALKEAVILPVKFPQFFTGKRKAWSGFLLYGPPGTGKSFLAKAVATEADSTFFSISSSDLVSKW 214
Cdd:cd19521    1 KPNVKWEDVAGLEGAKEALKEAVILPVKFPHLFTGNRKPWSGILLYGPPGTGKSYLAKAVATEANSTFFSVSSSDLVSKW 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 303291081 215 MGESEKLVNQLFTMAREKSPSIIFIDEIDALCGARGEgGESEASRRIKTEILVQMQGVGNEAGRVLVLAATNTPYQLDQA 294
Cdd:cd19521   81 MGESEKLVKQLFAMARENKPSIIFIDEVDSLCGTRGE-GESEASRRIKTELLVQMNGVGNDSQGVLVLGATNIPWQLDSA 159

                        170
                 ....*....|.
gi 303291081 295 VRRRFDKRIYI 305
Cdd:cd19521  160 IRRRFEKRIYI 170
RecA-like_VPS4-like cd19509
ATPase domain of VPS4, ATAD1, K, KTNA1, Spastin, FIGL-1 and similar ATPase domains; This ...
 143-305 5.32e-86

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: 259.98  E-value: 5.32e-86
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 303291081 143 VAGLTSAKEALKEAVILPVKFPQFFTGKRKAWSGFLLYGPPGTGKSFLAKAVATEADSTFFSISSSDLVSKWMGESEKLV 222
Cdd:cd19509    1 IAGLDDAKEALKEAVILPSLRPDLFPGLRGPPRGILLYGPPGTGKTLLARAVASESGSTFFSISASSLVSKWVGESEKIV 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 303291081 223 NQLFTMAREKSPSIIFIDEIDALCGARGEgGESEASRRIKTEILVQMQGVGN-EAGRVLVLAATNTPYQLDQAVRRRFDK 301
Cdd:cd19509   81 RALFALARELQPSIIFIDEIDSLLSERGS-GEHEASRRVKTEFLVQMDGVLNkPEDRVLVLGATNRPWELDEAFLRRFEK 159


                 ....
gi 303291081 302 RIYI 305
Cdd:cd19509  160 RIYI 163
RPT1 COG1222
ATP-dependent 26S proteasome regulatory subunit [Posttranslational modification, protein ...
 125-354 1.75e-82

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


Pssm-ID: 440835 [Multi-domain]  Cd Length: 326  Bit Score: 256.86  E-value: 1.75e-82
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 303291081 125 GALGGAIVTEKPDVKWDDVAGLTSAKEALKEAVILPVKFPQFFT--GKRkAWSGFLLYGPPGTGKSFLAKAVATEADSTF 202
Cdd:COG1222   62 TPRGTAVPAESPDVTFDDIGGLDEQIEEIREAVELPLKNPELFRkyGIE-PPKGVLLYGPPGTGKTLLAKAVAGELGAPF 140

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 303291081 203 FSISSSDLVSKWMGESEKLVNQLFTMAREKSPSIIFIDEIDALCGARGEGGESEASRRIKTEILVQMQGVgNEAGRVLVL 282
Cdd:COG1222  141 IRVRGSELVSKYIGEGARNVREVFELAREKAPSIIFIDEIDAIAARRTDDGTSGEVQRTVNQLLAELDGF-ESRGDVLII 219

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 303291081 283 AATNTPYQLDQAVRR--RFDKRIYIPLPDAPARAHMFRVHVGETPhDLTDADFQSLGAQSEGFSGSDIDHVVKD 354
Cdd:COG1222  220 AATNRPDLLDPALLRpgRFDRVIEVPLPDEEAREEILKIHLRDMP-LADDVDLDKLAKLTEGFSGADLKAIVTE 292
RecA-like_KTNA1 cd19522
Katanin p60 ATPase-containing subunit A1; Katanin p60 ATPase-containing subunit A1 (KTNA1) is ...
 142-305 6.71e-76

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: 234.49  E-value: 6.71e-76
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 303291081 142 DVAGLTSAKEALKEAVILPVKFPQFFTGKRKAWSGFLLYGPPGTGKSFLAKAVATEADSTFFSISSSDLVSKWMGESEKL 221
Cdd:cd19522    1 DIADLEEAKKLLEEAVVLPMWMPEFFKGIRRPWKGVLMVGPPGTGKTLLAKAVATECGTTFFNVSSSTLTSKYRGESEKL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 303291081 222 VNQLFTMAREKSPSIIFIDEIDALCGARGEGGESEASRRIKTEILVQMQGVGNEAGR------VLVLAATNTPYQLDQAV 295
Cdd:cd19522   81 VRLLFEMARFYAPTTIFIDEIDSICSRRGTSEEHEASRRVKSELLVQMDGVGGASENddpskmVMVLAATNFPWDIDEAL 160

                        170
                 ....*....|
gi 303291081 296 RRRFDKRIYI 305
Cdd:cd19522  161 RRRLEKRIYI 170
cell_div_CdvC NF041006
cell division protein CdvC;
12-444 1.76e-73

cell division protein CdvC;


Pssm-ID: 468935 [Multi-domain]  Cd Length: 371  Bit Score: 235.40  E-value: 1.76e-73
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 303291081  12 EKAIALVKEAVERDKASEYAAAFKLYTSALDHFTVYLK-YEKNPMMQ---QTIKtkftEYLERAEELKKLmdaddaaadg 87
Cdd:NF041006   9 EMARKYAIAAVKADKEGRYEEAINNYKKAIEILTQIVRlYPDSPLRHayeQMIN----EYKKRIEVLEEL---------- 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 303291081  88 RTNPNASPELIKArpkdtkkggvgkggaEDDEMskmrgalggaIVTEKPDVKWDDVAGLTSAKEALKEAVILPVKFPQFF 167
Cdd:NF041006  75 VPAEPAGPDVEKE---------------SDEEL----------VVKEKPKVTFSDIVGLEDVKEALKEAIVYPSKRPDLF 129

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 303291081 168 TgkrKAW-SGFLLYGPPGTGKSFLAKAVATEADSTFFSISSSDLVSKWMGESEKLVNQLFTMAREKS-----PSIIFIDE 241
Cdd:NF041006 130 P---LGWpRGILLYGPPGCGKTMLAAAVANEIDSEFIHVDAASIMSKWLGEAEKNVAKIFKKAREKSkeegkPAIIFIDE 206

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 303291081 242 IDALCGARGE--GGESeasrRIKTEILVQMQGV--GNEAGRVLVLAATNTPYQLDQAVRRRFDKRIYIPLPDAPARAHMF 317
Cdd:NF041006 207 IDALLGVYSSevGGEV----RVRNQFLKEMDGLqdKSENYHVYVIGATNKPWRLDEPFLRRFQKRIYIPLPDREQRLELL 282

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 303291081 318 RVHVGETPHDlTDADFQSLGAQSEGFSGSDIDHVVkdvlyepvrktqEATHFktttgpdgderyvpcspgdpdaweRTLE 397
Cdd:NF041006 283 KYYTSKIKLE-NDVDLDELAEMTEGYTASDIRDIV------------QAAHM------------------------RVVK 325

                        410       420       430       440
                 ....*....|....*....|....*....|....*....|....*..
gi 303291081 398 QLAEDGLGErvhPPPISANDFRKVLARARPTVAAGDLEEHERFTREF 444
Cdd:NF041006 326 EMFEKGLGE---PRPITMEDFKEVLKIRKPSVNQEMLKAYEAWHEKF 369
SpoVK COG0464
AAA+-type ATPase, SpoVK/Ycf46/Vps4 family [Cell wall/membrane/envelope biogenesis, Cell cycle ...
 8-361 8.56e-70

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: 226.72  E-value: 8.56e-70
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 303291081   8 IAIREKAIALVKEAVERDKASEYAAAFKLYTSALDHFTVYLKYEKNPMMQQTIKTKFTEYLERAEELKKLMDADDAAADG 87
Cdd:COG0464   31 LALAAALLLLLLLLLLLLLALLLVELLLLLLSGALAALLLLALLLLALLALLAALLSALELLLLGELLLLLLLLLLLLLL 110

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 303291081  88 RTNPNASPELIKARPKDTKKGGVGKGGAEDDemskmrgALGGAIVTEKPDVKWDDVAGLTSAKEALKEAVILPVKFPQFF 167
Cdd:COG0464  111 LLDLERALLELLRESAEALALAAPLVTYEDI-------GGLEEELLELREAILDDLGGLEEVKEELRELVALPLKRPELR 183

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 303291081 168 TGKRKAWS-GFLLYGPPGTGKSFLAKAVATEADSTFFSISSSDLVSKWMGESEKLVNQLFTMAREKSPSIIFIDEIDALC 246
Cdd:COG0464  184 EEYGLPPPrGLLLYGPPGTGKTLLARALAGELGLPLIEVDLSDLVSKYVGETEKNLREVFDKARGLAPCVLFIDEADALA 263

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 303291081 247 GARGEGGESeASRRIKTEILVQMQGVgneAGRVLVLAATNTPYQLDQAVRRRFDKRIYIPLPDAPARAHMFRVHVGETPH 326
Cdd:COG0464  264 GKRGEVGDG-VGRRVVNTLLTEMEEL---RSDVVVIAATNRPDLLDPALLRRFDEIIFFPLPDAEERLEIFRIHLRKRPL 339

                        330       340       350
                 ....*....|....*....|....*....|....*
gi 303291081 327 DlTDADFQSLGAQSEGFSGSDIDHVVKDVLYEPVR 361
Cdd:COG0464  340 D-EDVDLEELAEATEGLSGADIRNVVRRAALQALR 373
RecA-like_Figl-1 cd19525
ATPase domain of Fidgetin-Like 1 (FIGL-1); FIGL-1 may participate in DNA repair in the nucleus; ...
 131-305 4.11e-68

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: 215.24  E-value: 4.11e-68
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 303291081 131 IVTEKPDVKWDDVAGLTSAKEALKEAVILPVKFPQFFTGKRKAWSGFLLYGPPGTGKSFLAKAVATEADSTFFSISSSDL 210
Cdd:cd19525   12 IMDHGPPINWADIAGLEFAKKTIKEIVVWPMLRPDIFTGLRGPPKGILLFGPPGTGKTLIGKCIASQSGATFFSISASSL 91

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 303291081 211 VSKWMGESEKLVNQLFTMAREKSPSIIFIDEIDALCGARGEgGESEASRRIKTEILVQMQGVGNEA-GRVLVLAATNTPY 289
Cdd:cd19525   92 TSKWVGEGEKMVRALFSVARCKQPAVIFIDEIDSLLSQRGE-GEHESSRRIKTEFLVQLDGATTSSeDRILVVGATNRPQ 170

                        170
                 ....*....|....*.
gi 303291081 290 QLDQAVRRRFDKRIYI 305
Cdd:cd19525  171 EIDEAARRRLVKRLYI 186
RecA-like_spastin cd19524
ATPase domain of spastin; Spastin is an ATP-dependent microtubule-severing protein involved in ...
 142-305 6.72e-64

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: 203.54  E-value: 6.72e-64
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 303291081 142 DVAGLTSAKEALKEAVILPVKFPQFFTGKRKAWSGFLLYGPPGTGKSFLAKAVATEADSTFFSISSSDLVSKWMGESEKL 221
Cdd:cd19524    1 DIAGQDLAKQALQEMVILPSLRPELFTGLRAPARGLLLFGPPGNGKTMLAKAVAAESNATFFNISAASLTSKYVGEGEKL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 303291081 222 VNQLFTMAREKSPSIIFIDEIDALCGARGEgGESEASRRIKTEILVQMQGV-GNEAGRVLVLAATNTPYQLDQAVRRRFD 300
Cdd:cd19524   81 VRALFAVARELQPSIIFIDEVDSLLSERSE-GEHEASRRLKTEFLIEFDGVqSNGDDRVLVMGATNRPQELDDAVLRRFT 159


                 ....*
gi 303291081 301 KRIYI 305
Cdd:cd19524  160 KRVYV 164
PRK03992 PRK03992
proteasome-activating nucleotidase; Provisional
 132-353 6.61e-61

proteasome-activating nucleotidase; Provisional


Pssm-ID: 179699 [Multi-domain]  Cd Length: 389  Bit Score: 203.14  E-value: 6.61e-61
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 303291081 132 VTEKPDVKWDDVAGLTSAKEALKEAVILPVKFPQFFtgkRK----AWSGFLLYGPPGTGKSFLAKAVATEADSTFFSISS 207
Cdd:PRK03992 122 VIESPNVTYEDIGGLEEQIREVREAVELPLKKPELF---EEvgiePPKGVLLYGPPGTGKTLLAKAVAHETNATFIRVVG 198

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 303291081 208 SDLVSKWMGESEKLVNQLFTMAREKSPSIIFIDEIDALCGAR---GEGGESEASRRIkTEILVQMQGVgNEAGRVLVLAA 284
Cdd:PRK03992 199 SELVQKFIGEGARLVRELFELAREKAPSIIFIDEIDAIAAKRtdsGTSGDREVQRTL-MQLLAEMDGF-DPRGNVKIIAA 276

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 303291081 285 TNTPYQLDQAVRR--RFDKRIYIPLPDAPARAHMFRVH-----VGEtphdltDADFQSLGAQSEGFSGSDIDHVVK 353
Cdd:PRK03992 277 TNRIDILDPAILRpgRFDRIIEVPLPDEEGRLEILKIHtrkmnLAD------DVDLEELAELTEGASGADLKAICT 346
CDC48 TIGR01243
AAA family ATPase, CDC48 subfamily; This subfamily of the AAA family ATPases includes two ...
 131-445 1.50e-59

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: 207.45  E-value: 1.50e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 303291081  131 IVTEKPDVKWDDVAGLTSAKEALKEAVILPVKFPQFFT--GKRKAwSGFLLYGPPGTGKSFLAKAVATEADSTFFSISSS 208
Cdd:TIGR01243 443 VLVEVPNVRWSDIGGLEEVKQELREAVEWPLKHPEIFEkmGIRPP-KGVLLFGPPGTGKTLLAKAVATESGANFIAVRGP 521

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 303291081  209 DLVSKWMGESEKLVNQLFTMAREKSPSIIFIDEIDALCGARGEGGESEASRRIKTEILVQMQGVgNEAGRVLVLAATNTP 288
Cdd:TIGR01243 522 EILSKWVGESEKAIREIFRKARQAAPAIIFFDEIDAIAPARGARFDTSVTDRIVNQLLTEMDGI-QELSNVVVIAATNRP 600

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 303291081  289 YQLDQAVRR--RFDKRIYIPLPDAPARAHMFRVHVGETPHDlTDADFQSLGAQSEGFSGSDIDHVVKDVLYEPVRKTQEA 366
Cdd:TIGR01243 601 DILDPALLRpgRFDRLILVPPPDEEARKEIFKIHTRSMPLA-EDVDLEELAEMTEGYTGADIEAVCREAAMAALRESIGS 679

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 303291081  367 ThfktttgpdgderyvpcspgdpdawerTLEQLaEDGLGERVHPPPISANDFRKVLARARPTVAAGDLEEHERFTREFG 445
Cdd:TIGR01243 680 P---------------------------AKEKL-EVGEEEFLKDLKVEMRHFLEALKKVKPSVSKEDMLRYERLAKELK 730
AAA pfam00004
ATPase family associated with various cellular activities (AAA); AAA family proteins often ...
 178-307 4.31e-57

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


Pssm-ID: 459627 [Multi-domain]  Cd Length: 130  Bit Score: 184.33  E-value: 4.31e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 303291081  178 LLYGPPGTGKSFLAKAVATEADSTFFSISSSDLVSKWMGESEKLVNQLFTMAREKSPSIIFIDEIDALCGARGEGGESEa 257
Cdd:pfam00004   2 LLYGPPGTGKTTLAKAVAKELGAPFIEISGSELVSKYVGESEKRLRELFEAAKKLAPCVIFIDEIDALAGSRGSGGDSE- 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 303291081  258 SRRIKTEILVQMQGVGNEAGRVLVLAATNTPYQLDQAVRRRFDKRIYIPL 307
Cdd:pfam00004  81 SRRVVNQLLTELDGFTSSNSKVIVIAATNRPDKLDPALLGRFDRIIEFPL 130
RecA-like_CDC48_r2-like cd19511
second of two ATPase domains of CDC48/p97, PEX1 and -6, VAT and NVL, and similar ATPase ...
 149-305 4.12e-56

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: 182.87  E-value: 4.12e-56
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 303291081 149 AKEALKEAVILPVKFPQFFT--GKRKAwSGFLLYGPPGTGKSFLAKAVATEADSTFFSISSSDLVSKWMGESEKLVNQLF 226
Cdd:cd19511    1 VKRELKEAVEWPLKHPDAFKrlGIRPP-KGVLLYGPPGCGKTLLAKALASEAGLNFISVKGPELFSKYVGESERAVREIF 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 303291081 227 TMAREKSPSIIFIDEIDALCGARGEGGESEASRRIKTEILVQMQGVgnEAGR-VLVLAATNTPYQLDQAVRR--RFDKRI 303
Cdd:cd19511   80 QKARQAAPCIIFFDEIDSLAPRRGQSDSSGVTDRVVSQLLTELDGI--ESLKgVVVIAATNRPDMIDPALLRpgRLDKLI 157


                 ..
gi 303291081 304 YI 305
Cdd:cd19511  158 YV 159
RecA-like_ATAD1 cd19520
ATPase domain of ATPase family AAA domain-containing protein 1 and similar ATPase domains; ...
 142-305 8.17e-52

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: 172.22  E-value: 8.17e-52
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 303291081 142 DVAGLTSAKEALKEAVILPVKFPQFFTGKR--KAWSGFLLYGPPGTGKSFLAKAVATEADSTFFSISSSDLVSKWMGESE 219
Cdd:cd19520    1 DIGGLDEVITELKELVILPLQRPELFDNSRllQPPKGVLLYGPPGCGKTMLAKATAKEAGARFINLQVSSLTDKWYGESQ 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 303291081 220 KLVNQLFTMAREKSPSIIFIDEIDALCGARgEGGESEASRRIKTEILVQMQGVGNEAG-RVLVLAATNTPYQLDQAVRRR 298
Cdd:cd19520   81 KLVAAVFSLASKLQPSIIFIDEIDSFLRQR-SSTDHEATAMMKAEFMSLWDGLSTDGNcRVIVMGATNRPQDLDEAILRR 159


                 ....*..
gi 303291081 299 FDKRIYI 305
Cdd:cd19520  160 MPKRFHI 166
FtsH_fam TIGR01241
ATP-dependent metalloprotease FtsH; HflB(FtsH) is a pleiotropic protein required for correct ...
 133-352 1.18e-51

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: 181.33  E-value: 1.18e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 303291081  133 TEKPDVKWDDVAGLTSAKEALKEAVILpVKFPQFFT--GKRKAwSGFLLYGPPGTGKSFLAKAVATEADSTFFSISSSDL 210
Cdd:TIGR01241  47 EEKPKVTFKDVAGIDEAKEELMEIVDF-LKNPSKFTklGAKIP-KGVLLVGPPGTGKTLLAKAVAGEAGVPFFSISGSDF 124

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 303291081  211 VSKWMGESEKLVNQLFTMAREKSPSIIFIDEIDALCGARGEGGESEASRRIKT--EILVQMQGVGNEAGrVLVLAATNTP 288
Cdd:TIGR01241 125 VEMFVGVGASRVRDLFEQAKKNAPCIIFIDEIDAVGRQRGAGLGGGNDEREQTlnQLLVEMDGFGTNTG-VIVIAATNRP 203

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 303291081  289 YQLDQAVRR--RFDKRIYIPLPDAPARAHMFRVHVGETPHDlTDADFQSLGAQSEGFSGSDIDHVV 352
Cdd:TIGR01241 204 DVLDPALLRpgRFDRQVVVDLPDIKGREEILKVHAKNKKLA-PDVDLKAVARRTPGFSGADLANLL 268
RecA-like_protease cd19481
proteases similar to RecA; RecA-like NTPases. This family includes the NTP binding domain of ...
 149-305 1.35e-51

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: 171.31  E-value: 1.35e-51
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 303291081 149 AKEALKEAVILPVKFPQFFTGKRKAWSGFLLYGPPGTGKSFLAKAVATEADSTFFSISSSDLVSKWMGESEKLVNQLFTM 228
Cdd:cd19481    1 LKASLREAVEAPRRGSRLRRYGLGLPKGILLYGPPGTGKTLLAKALAGELGLPLIVVKLSSLLSKYVGESEKNLRKIFER 80

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 303291081 229 AREKSPSIIFIDEIDALCGARGEGGESEASRRIKTEILVQMQGVgNEAGRVLVLAATNTPYQLDQAVRR--RFDKRIYI 305
Cdd:cd19481   81 ARRLAPCILFIDEIDAIGRKRDSSGESGELRRVLNQLLTELDGV-NSRSKVLVIAATNRPDLLDPALLRpgRFDEVIEF 158
RecA-like_CDC48_NLV2_r1-like cd19503
first of two ATPase domains of CDC48 and NLV2, and similar ATPase domains; CDC48 in yeast and ...
 142-305 2.06e-50

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: 168.24  E-value: 2.06e-50
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 303291081 142 DVAGLTSAKEALKEAVILPVKFPQFFTGKRKAW-SGFLLYGPPGTGKSFLAKAVATEADSTFFSISSSDLVSKWMGESEK 220
Cdd:cd19503    1 DIGGLDEQIASLKELIELPLKYPELFRALGLKPpRGVLLHGPPGTGKTLLARAVANEAGANFLSISGPSIVSKYLGESEK 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 303291081 221 LVNQLFTMAREKSPSIIFIDEIDALCGARGEGGEsEASRRIKTEILVQMQGVGNeAGRVLVLAATNTPYQLDQAVRR--R 298
Cdd:cd19503   81 NLREIFEEARSHAPSIIFIDEIDALAPKREEDQR-EVERRVVAQLLTLMDGMSS-RGKVVVIAATNRPDAIDPALRRpgR 158


                 ....*..
gi 303291081 299 FDKRIYI 305
Cdd:cd19503  159 FDREVEI 165
HflB COG0465
ATP-dependent Zn proteases [Posttranslational modification, protein turnover, chaperones];
120-348 3.88e-50

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


Pssm-ID: 440233 [Multi-domain]  Cd Length: 583  Bit Score: 179.08  E-value: 3.88e-50
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 303291081 120 MSKMRGALGGA----------IVTEKPDVKWDDVAGLTSAKEALKEAV-ILpvKFPQFFT--GKR--KawsGFLLYGPPG 184
Cdd:COG0465  111 MRRMQGGGGGAmsfgkskaklYDEDKPKVTFDDVAGVDEAKEELQEIVdFL--KDPEKFTrlGAKipK---GVLLVGPPG 185

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 303291081 185 TGKSFLAKAVATEADSTFFSISSSDLVSkwM----GESEklVNQLFTMAREKSPSIIFIDEIDALCGARG---EGGESEa 257
Cdd:COG0465  186 TGKTLLAKAVAGEAGVPFFSISGSDFVE--MfvgvGASR--VRDLFEQAKKNAPCIIFIDEIDAVGRQRGaglGGGHDE- 260

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 303291081 258 srRIKT--EILVQMQGVGNEAGrVLVLAATNTPYQLDQAVRR--RFDKRIYIPLPDAPARAHMFRVHVGETPHDlTDADF 333
Cdd:COG0465  261 --REQTlnQLLVEMDGFEGNEG-VIVIAATNRPDVLDPALLRpgRFDRQVVVDLPDVKGREAILKVHARKKPLA-PDVDL 336

                        250
                 ....*....|....*
gi 303291081 334 QSLGAQSEGFSGSDI 348
Cdd:COG0465  337 EVIARRTPGFSGADL 351
RecA-like_VCP_r2 cd19529
second of two ATPase domains of Valosin-containing protein-like ATPase (VAT) and similar ...
 149-305 5.17e-48

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: 161.89  E-value: 5.17e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 303291081 149 AKEALKEAVILPVKFPQFFTGKR-KAWSGFLLYGPPGTGKSFLAKAVATEADSTFFSISSSDLVSKWMGESEKLVNQLFT 227
Cdd:cd19529    1 VKQELKEAVEWPLLKPEVFKRLGiRPPKGILLYGPPGTGKTLLAKAVATESNANFISVKGPELLSKWVGESEKAIREIFR 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 303291081 228 MAREKSPSIIFIDEIDALCGARGEGGESEASRRIKTEILVQMQGVgNEAGRVLVLAATNTPYQLDQAVRR--RFDKRIYI 305
Cdd:cd19529   81 KARQVAPCVIFFDEIDSIAPRRGTTGDSGVTERVVNQLLTELDGL-EEMNGVVVIAATNRPDIIDPALLRagRFDRLIYI 159
RecA-like_PAN_like cd19502
proteasome activating nucleotidase PAN and related proteasome subunits; This subfamily ...
 140-303 6.56e-48

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: 162.12  E-value: 6.56e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 303291081 140 WDDVAGLTSAKEALKEAVILPVKFPQFFT--GKRKAwSGFLLYGPPGTGKSFLAKAVATEADSTFFSISSSDLVSKWMGE 217
Cdd:cd19502    2 YEDIGGLDEQIREIREVVELPLKHPELFEelGIEPP-KGVLLYGPPGTGKTLLAKAVANHTDATFIRVVGSELVQKYIGE 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 303291081 218 SEKLVNQLFTMAREKSPSIIFIDEIDALCGAR---GEGGESEAsRRIKTEILVQMQGVgNEAGRVLVLAATNTPYQLDQA 294
Cdd:cd19502   81 GARLVRELFEMAREKAPSIIFIDEIDAIGAKRfdsGTGGDREV-QRTMLELLNQLDGF-DPRGNIKVIMATNRPDILDPA 158

                        170
                 ....*....|.
gi 303291081 295 VRR--RFDKRI 303
Cdd:cd19502  159 LLRpgRFDRKI 169
RecA-like_FtsH cd19501
ATP-dependent zinc metalloprotease FtsH; FtsH ATPase is a processive, ATP-dependent zinc ...
 138-305 6.62e-48

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: 162.02  E-value: 6.62e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 303291081 138 VKWDDVAGLTSAKEALKEAVILpVKFPQFFT--GKRKAwSGFLLYGPPGTGKSFLAKAVATEADSTFFSISSSDLVSKWM 215
Cdd:cd19501    1 VTFKDVAGCEEAKEELKEVVEF-LKNPEKFTklGAKIP-KGVLLVGPPGTGKTLLAKAVAGEAGVPFFSISGSDFVEMFV 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 303291081 216 GESEKLVNQLFTMAREKSPSIIFIDEIDALCGARGEGGESEASRRIKT--EILVQMQGVGNEAGrVLVLAATNTPYQLDQ 293
Cdd:cd19501   79 GVGASRVRDLFEQAKKNAPCIVFIDEIDAVGRKRGAGLGGGHDEREQTlnQLLVEMDGFESNTG-VIVIAATNRPDVLDP 157

                        170
                 ....*....|....
gi 303291081 294 AVRR--RFDKRIYI 305
Cdd:cd19501  158 ALLRpgRFDRQVYV 171
CDC48 TIGR01243
AAA family ATPase, CDC48 subfamily; This subfamily of the AAA family ATPases includes two ...
 136-362 1.17e-47

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: 174.32  E-value: 1.17e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 303291081  136 PDVKWDDVAGLTSAKEALKEAVILPVKFPQFFtgKR---KAWSGFLLYGPPGTGKSFLAKAVATEADSTFFSISSSDLVS 212
Cdd:TIGR01243 173 PKVTYEDIGGLKEAKEKIREMVELPMKHPELF--EHlgiEPPKGVLLYGPPGTGKTLLAKAVANEAGAYFISINGPEIMS 250

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 303291081  213 KWMGESEKLVNQLFTMAREKSPSIIFIDEIDALCGARGEG-GESEasRRIKTEILVQMQGVgNEAGRVLVLAATNTPYQL 291
Cdd:TIGR01243 251 KYYGESEERLREIFKEAEENAPSIIFIDEIDAIAPKREEVtGEVE--KRVVAQLLTLMDGL-KGRGRVIVIGATNRPDAL 327

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 303291081  292 DQAVRR--RFDKRIYIPLPDAPARAHMFRVHVGETPHdLTDADFQSLGAQSEGFSGSDIDHVVKDVLYEPVRK 362
Cdd:TIGR01243 328 DPALRRpgRFDREIVIRVPDKRARKEILKVHTRNMPL-AEDVDLDKLAEVTHGFVGADLAALAKEAAMAALRR 399
COG1223 COG1223
Predicted ATPase, AAA+ superfamily [General function prediction only];
140-356 8.58e-44

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


Pssm-ID: 440836 [Multi-domain]  Cd Length: 246  Bit Score: 153.89  E-value: 8.58e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 303291081 140 WDDVAGLTSAKEALKEAVIlpvkfpqfFTGKRKAWSGF--------LLYGPPGTGKSFLAKAVATEADSTFFSISSSDLV 211
Cdd:COG1223    1 LDDVVGQEEAKKKLKLIIK--------ELRRRENLRKFglwpprkiLFYGPPGTGKTMLAEALAGELKLPLLTVRLDSLI 72

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 303291081 212 SKWMGESEKLVNQLFTMAREKsPSIIFIDEIDALCGARG---EGGEseaSRRIKTEILVQMqgvGNEAGRVLVLAATNTP 288
Cdd:COG1223   73 GSYLGETARNLRKLFDFARRA-PCVIFFDEFDAIAKDRGdqnDVGE---VKRVVNALLQEL---DGLPSGSVVIAATNHP 145

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 303291081 289 YQLDQAVRRRFDKRIYIPLPDAPARAHMFRVHVGETPHDLtDADFQSLGAQSEGFSGSDIDHVVKDVL 356
Cdd:COG1223  146 ELLDSALWRRFDEVIEFPLPDKEERKEILELNLKKFPLPF-ELDLKKLAKKLEGLSGADIEKVLKTAL 212
PTZ00454 PTZ00454
26S protease regulatory subunit 6B-like protein; Provisional
 132-362 5.20e-43

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


Pssm-ID: 240423 [Multi-domain]  Cd Length: 398  Bit Score: 156.08  E-value: 5.20e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 303291081 132 VTEKPDVKWDDVAGLTSAKEALKEAVILPVKFPQFF--TGKRKAwSGFLLYGPPGTGKSFLAKAVATEADSTFFSISSSD 209
Cdd:PTZ00454 136 MSEKPDVTYSDIGGLDIQKQEIREAVELPLTCPELYeqIGIDPP-RGVLLYGPPGTGKTMLAKAVAHHTTATFIRVVGSE 214

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 303291081 210 LVSKWMGESEKLVNQLFTMAREKSPSIIFIDEIDALCGAR--GEGGESEASRRIKTEILVQMQGVgNEAGRVLVLAATNT 287
Cdd:PTZ00454 215 FVQKYLGEGPRMVRDVFRLARENAPSIIFIDEVDSIATKRfdAQTGADREVQRILLELLNQMDGF-DQTTNVKVIMATNR 293

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 303291081 288 PYQLDQAVRR--RFDKRIYIPLPDAPARAHMFRVHVGETphDLT-DADFQSLGAQSEGFSGSDIDHVVKDVLYEPVRK 362
Cdd:PTZ00454 294 ADTLDPALLRpgRLDRKIEFPLPDRRQKRLIFQTITSKM--NLSeEVDLEDFVSRPEKISAADIAAICQEAGMQAVRK 369
RecA-like_CDC48_r2-like cd19528
second of two ATPase domains of CDC48 and similar ATPase domains; CDC48 in yeast and p97 or ...
 150-305 4.19e-42

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: 146.50  E-value: 4.19e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 303291081 150 KEALKEAVILPVKFPQFFTGKRKAWS-GFLLYGPPGTGKSFLAKAVATEADSTFFSISSSDLVSKWMGESEKLVNQLFTM 228
Cdd:cd19528    2 KRELQELVQYPVEHPDKFLKFGMTPSkGVLFYGPPGCGKTLLAKAIANECQANFISVKGPELLTMWFGESEANVRDIFDK 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 303291081 229 AREKSPSIIFIDEIDALCGARG--EGGESEASRRIKTEILVQMQGVgNEAGRVLVLAATNTPYQLDQAVRR--RFDKRIY 304
Cdd:cd19528   82 ARAAAPCVLFFDELDSIAKARGgnIGDAGGAADRVINQILTEMDGM-NTKKNVFIIGATNRPDIIDPAILRpgRLDQLIY 160


                 .
gi 303291081 305 I 305
Cdd:cd19528  161 I 161
RecA-like_CDC48_r1-like cd19519
first of two ATPase domains of CDC48 and similar ATPase domains; CDC48 in yeast and p97 or VCP ...
 142-306 5.64e-42

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: 146.43  E-value: 5.64e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 303291081 142 DVAGLTSAKEALKEAVILPVKFPQFFtgKR---KAWSGFLLYGPPGTGKSFLAKAVATEADSTFFSISSSDLVSKWMGES 218
Cdd:cd19519    1 DIGGCRKQLAQIREMVELPLRHPELF--KAigiKPPRGILLYGPPGTGKTLIARAVANETGAFFFLINGPEIMSKLAGES 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 303291081 219 EKLVNQLFTMAREKSPSIIFIDEIDALCGARgEGGESEASRRIKTEILVQMQGVgNEAGRVLVLAATNTPYQLDQAVRR- 297
Cdd:cd19519   79 ESNLRKAFEEAEKNAPAIIFIDEIDAIAPKR-EKTHGEVERRIVSQLLTLMDGL-KQRAHVIVMAATNRPNSIDPALRRf 156

                        170
                 ....*....|
gi 303291081 298 -RFDKRIYIP 306
Cdd:cd19519  157 gRFDREIDIG 166
RecA-like_fidgetin cd19523
ATPase domain of fidgetin; Fidgetin (FIGN) is a ATP-dependent microtubule severing protein. ...
 142-305 9.00e-41

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: 143.10  E-value: 9.00e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 303291081 142 DVAGLTSAKEALKEAVILPVKFPQFFTGKRKAWSGFLLYGPPGTGKSFLAKAVATEADSTFFSISSSDLVSKWMGESEKL 221
Cdd:cd19523    1 DIAGLGALKAAIKEEVLWPLLRPDAFSGLLRLPRSILLFGPRGTGKTLLGRCLASQLGATFLRLRGSTLVAKWAGEGEKI 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 303291081 222 VNQLFTMAREKSPSIIFIDEIDALCGARGEggESEASRRIKTEILVQMQGV-GNEAGRVLVLAATNTPYQLDQAVRRRFD 300
Cdd:cd19523   81 LQASFLAARCRQPSVLFISDLDALLSSQDD--EASPVGRLQVELLAQLDGVlGSGEDGVLVVCTTSKPEEIDESLRRYFS 158


                 ....*
gi 303291081 301 KRIYI 305
Cdd:cd19523  159 KRLLV 163
RecA-like_NVL_r1-like cd19518
first of two ATPase domains of NVL (nuclear VCP-like protein) and similar ATPase domains; NVL ...
 142-303 1.24e-39

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: 140.23  E-value: 1.24e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 303291081 142 DVAGLTSAKEALKEAVILPVKFPQFF--TGKRKAwSGFLLYGPPGTGKSFLAKAVATEADSTFFSISSSDLVSKWMGESE 219
Cdd:cd19518    1 DIGGMDSTLKELCELLIHPILPPEYFqhLGVEPP-RGVLLHGPPGCGKTMLANAIAGELKVPFLKISATEIVSGVSGESE 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 303291081 220 KLVNQLFTMAREKSPSIIFIDEIDALCGARgEGGESEASRRIKTEILVQMQGVGNE---AGRVLVLAATNTPYQLDQAVR 296
Cdd:cd19518   80 EKIRELFDQAISNAPCIVFIDEIDAITPKR-ESAQREMERRIVSQLLTCMDELNNEktaGGPVLVIGATNRPDSLDPALR 158


                 ....*....
gi 303291081 297 R--RFDKRI 303
Cdd:cd19518  159 RagRFDREI 167
PTZ00361 PTZ00361
26 proteosome regulatory subunit 4-like protein; Provisional
 132-348 2.26e-39

26 proteosome regulatory subunit 4-like protein; Provisional


Pssm-ID: 185575 [Multi-domain]  Cd Length: 438  Bit Score: 146.84  E-value: 2.26e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 303291081 132 VTEKPDVKWDDVAGLTSAKEALKEAVILPVKFPQFFTG-KRKAWSGFLLYGPPGTGKSFLAKAVATEADSTFFSISSSDL 210
Cdd:PTZ00361 174 VDKAPLESYADIGGLEQQIQEIKEAVELPLTHPELYDDiGIKPPKGVILYGPPGTGKTLLAKAVANETSATFLRVVGSEL 253

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 303291081 211 VSKWMGESEKLVNQLFTMAREKSPSIIFIDEIDALCGARGE---GGESEASRRIkTEILVQMQGVgNEAGRVLVLAATNT 287
Cdd:PTZ00361 254 IQKYLGDGPKLVRELFRVAEENAPSIVFIDEIDAIGTKRYDatsGGEKEIQRTM-LELLNQLDGF-DSRGDVKVIMATNR 331

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 303291081 288 PYQLDQAVRR--RFDKRIYIPLPDAPARAHMFRVHVGETPHDlTDADFQSLGAQSEGFSGSDI 348
Cdd:PTZ00361 332 IESLDPALIRpgRIDRKIEFPNPDEKTKRRIFEIHTSKMTLA-EDVDLEEFIMAKDELSGADI 393
hflB PRK10733
ATP-dependent zinc metalloprotease FtsH;
142-354 4.42e-39

ATP-dependent zinc metalloprotease FtsH;


Pssm-ID: 182683 [Multi-domain]  Cd Length: 644  Bit Score: 149.41  E-value: 4.42e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 303291081 142 DVAGLTSAKEALKEAVILPVKFPQFFTGKRKAWSGFLLYGPPGTGKSFLAKAVATEADSTFFSISSSDLVSKWMGESEKL 221
Cdd:PRK10733 153 DVAGCDEAKEEVAELVEYLREPSRFQKLGGKIPKGVLMVGPPGTGKTLLAKAIAGEAKVPFFTISGSDFVEMFVGVGASR 232

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 303291081 222 VNQLFTMAREKSPSIIFIDEIDALCGARGE--GGESEASRRIKTEILVQMQGV-GNEAgrVLVLAATNTPYQLDQAVRR- 297
Cdd:PRK10733 233 VRDMFEQAKKAAPCIIFIDEIDAVGRQRGAglGGGHDEREQTLNQMLVEMDGFeGNEG--IIVIAATNRPDVLDPALLRp 310

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 303291081 298 -RFDKRIYIPLPDAPARAHMFRVHVGETPHDlTDADFQSLGAQSEGFSGSDIDHVVKD 354
Cdd:PRK10733 311 gRFDRQVVVGLPDVRGREQILKVHMRRVPLA-PDIDAAIIARGTPGFSGADLANLVNE 367
RecA-like_NVL_r2-like cd19530
second of two ATPase domains of NVL (nuclear VCP-like protein) and similar ATPase domains; NVL ...
 146-305 1.17e-38

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: 137.23  E-value: 1.17e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 303291081 146 LTSAKEALKEAVILPVKFPQFFTG-KRKAWSGFLLYGPPGTGKSFLAKAVATEADSTFFSISSSDLVSKWMGESEKLVNQ 224
Cdd:cd19530    1 LDHVREELTMSILRPIKRPDIYKAlGIDLPTGVLLYGPPGCGKTLLAKAVANESGANFISVKGPELLNKYVGESERAVRQ 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 303291081 225 LFTMAREKSPSIIFIDEIDALCGARGeGGESEASRRIKTEILVQMQGVGNEAGrVLVLAATNTPYQLDQAVRR--RFDKR 302
Cdd:cd19530   81 VFQRARASAPCVIFFDEVDALVPKRG-DGGSWASERVVNQLLTEMDGLEERSN-VFVIAATNRPDIIDPAMLRpgRLDKT 158


                 ...
gi 303291081 303 IYI 305
Cdd:cd19530  159 LYV 161
ftsH CHL00176
cell division protein; Validated
 135-348 2.54e-38

cell division protein; Validated


Pssm-ID: 214386 [Multi-domain]  Cd Length: 638  Bit Score: 147.12  E-value: 2.54e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 303291081 135 KPDVKWDDVAGLTSAKEALKEAVILpVKFPQFFTGK-RKAWSGFLLYGPPGTGKSFLAKAVATEADSTFFSISSSDLVSK 213
Cdd:CHL00176 177 DTGITFRDIAGIEEAKEEFEEVVSF-LKKPERFTAVgAKIPKGVLLVGPPGTGKTLLAKAIAGEAEVPFFSISGSEFVEM 255

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 303291081 214 WMGESEKLVNQLFTMAREKSPSIIFIDEIDALCGARGE--GGESEASRRIKTEILVQMQGVGNEAGrVLVLAATNTPYQL 291
Cdd:CHL00176 256 FVGVGAARVRDLFKKAKENSPCIVFIDEIDAVGRQRGAgiGGGNDEREQTLNQLLTEMDGFKGNKG-VIVIAATNRVDIL 334

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 303291081 292 DQAVRR--RFDKRIYIPLPDAPARAHMFRVHVGETPHDLtDADFQSLGAQSEGFSGSDI 348
Cdd:CHL00176 335 DAALLRpgRFDRQITVSLPDREGRLDILKVHARNKKLSP-DVSLELIARRTPGFSGADL 392
RecA-like_PEX6_r2 cd19527
second of two ATPase domains of Peroxisomal biogenesis factor 6 (PEX6); PEX6(also known as ...
 150-305 7.67e-38

second of two ATPase domains of Peroxisomal biogenesis factor 6 (PEX6); PEX6(also known as Peroxin61)/PEX1 is a protein unfoldase; PEX6 and PEX1 form a heterohexameric Type-2 AAA-ATPase complex and are essential for peroxisome biogenesis as they are required for the import of folded proteins into the peroxisomal matrix. This subfamily represents the second ATPase domain of PEX6. This subfamily belongs to the RecA-like NTPase family which includes the NTP binding domain of F1 and V1 H(+)ATPases, DnaB and related helicases as well as bacterial RecA and related eukaryotic and archaeal recombinases. The RecA-like NTPase family also includes bacterial conjugation proteins and related DNA transfer proteins involved in type II and type IV secretion.


Pssm-ID: 410935 [Multi-domain]  Cd Length: 160  Bit Score: 135.33  E-value: 7.67e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 303291081 150 KEALKEAVILPVKFPQFFTGKRKAWSGFLLYGPPGTGKSFLAKAVATEADSTFFSISSSDLVSKWMGESEKLVNQLFTMA 229
Cdd:cd19527    2 KKEILDTIQLPLEHPELFSSGLRKRSGILLYGPPGTGKTLLAKAIATECSLNFLSVKGPELINMYIGESEANVREVFQKA 81

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 303291081 230 REKSPSIIFIDEIDALCGARGEGGESEASR-RIKTEILVQMQGVGNEAGRVLVLAATNTPYQLDQAVRR--RFDKRIYI 305
Cdd:cd19527   82 RDAKPCVIFFDELDSLAPSRGNSGDSGGVMdRVVSQLLAELDGMSSSGQDVFVIGATNRPDLLDPALLRpgRFDKLLYL 160
RecA-like_Yta7-like cd19517
ATPase domain of Saccharomyces cerevisiae Yta7 and similar ATPase domains; Saccharomyces ...
 142-304 3.17e-33

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: 123.00  E-value: 3.17e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 303291081 142 DVAGLTSAKEALKEAVILPVKFPQFFTG-KRKAWSGFLLYGPPGTGKSFLAKAVATEADS-----TFFSISSSDLVSKWM 215
Cdd:cd19517    1 DIGGLSHYINQLKEMVFFPLLYPEVFAKfKITPPRGVLFHGPPGTGKTLMARALAAECSKggqkvSFFMRKGADCLSKWV 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 303291081 216 GESEKLVNQLFTMAREKSPSIIFIDEIDALCGARGEGGESEASRRIKTeILVQMQGVGNEaGRVLVLAATNTPYQLDQAV 295
Cdd:cd19517   81 GEAERQLRLLFEEAYRMQPSIIFFDEIDGLAPVRSSKQEQIHASIVST-LLALMDGLDNR-GQVVVIGATNRPDALDPAL 158

                        170
                 ....*....|.
gi 303291081 296 RR--RFDKRIY 304
Cdd:cd19517  159 RRpgRFDREFY 169
RecA-like_PEX1_r2 cd19526
second of two ATPase domains of Peroxisomal biogenesis factor 1 (PEX1); PEX1(also known as ...
 149-304 5.05e-33

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: 122.15  E-value: 5.05e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 303291081 149 AKEALKEAVILPVKFPQFFTGKR-KAWSGFLLYGPPGTGKSFLAKAVATEADSTFFSISSSDLVSKWMGESEKLVNQLFT 227
Cdd:cd19526    1 VKKALEETIEWPSKYPKIFASSPlRLRSGILLYGPPGCGKTLLASAIASECGLNFISVKGPELLNKYIGASEQNVRDLFS 80

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 303291081 228 MAREKSPSIIFIDEIDALCGARGEgGESEASRRIKTEILVQMQGVGNEAGrVLVLAATNTPYQLDQAVRR--RFDKRIY 304
Cdd:cd19526   81 RAQSAKPCILFFDEFDSIAPKRGH-DSTGVTDRVVNQLLTQLDGVEGLDG-VYVLAATSRPDLIDPALLRpgRLDKLVY 157
AAA cd00009
The AAA+ (ATPases Associated with a wide variety of cellular Activities) superfamily ...
 144-307 2.31e-25

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: 101.07  E-value: 2.31e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 303291081 144 AGLTSAKEALKEAVilpvkfpqfftgKRKAWSGFLLYGPPGTGKSFLAKAVATEA---DSTFFSISSSDLVSKWMGESEK 220
Cdd:cd00009    1 VGQEEAIEALREAL------------ELPPPKNLLLYGPPGTGKTTLARAIANELfrpGAPFLYLNASDLLEGLVVAELF 68

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 303291081 221 ---LVNQLFTMAREKSPSIIFIDEIDALcgargeggeSEASRRIKTEILVQMQGVGNEAGRVLVLAATNTPY--QLDQAV 295
Cdd:cd00009   69 ghfLVRLLFELAEKAKPGVLFIDEIDSL---------SRGAQNALLRVLETLNDLRIDRENVRVIGATNRPLlgDLDRAL 139

                        170
                 ....*....|..
gi 303291081 296 RRRFDKRIYIPL 307
Cdd:cd00009  140 YDRLDIRIVIPL 151
Vps4_C pfam09336
Vps4 C terminal oligomerization domain; This domain is found at the C terminal of ATPase ...
 381-445 3.98e-25

Vps4 C terminal oligomerization domain; This domain is found at the C terminal of ATPase proteins involved in vacuolar sorting. It forms an alpha helix structure and is required for oligomerization.


Pssm-ID: 462762 [Multi-domain]  Cd Length: 61  Bit Score: 97.57  E-value: 3.98e-25
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 303291081  381 YVPCSPGDPDAWERTLEQLAedglGERVHPPPISANDFRKVLARARPTVAAGDLEEHERFTREFG 445
Cdd:pfam09336   1 LTPCSPGDPGAIEMTWMDIP----SDKLLEPPVTMKDFLKALKSSRPTVSKEDLEKYEEFTKEFG 61
MIT_VPS4 cd02678
MIT: domain contained within Microtubule Interacting and Trafficking molecules. This ...
 11-76 9.52e-23

MIT: domain contained within Microtubule Interacting and Trafficking molecules. This sub-family of MIT domains is found in intracellular protein transport proteins of the AAA-ATPase family. The molecular function of the MIT domain is unclear.


Pssm-ID: 239141  Cd Length: 75  Bit Score: 91.17  E-value: 9.52e-23
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 303291081  11 REKAIALVKEAVERDKASEYAAAFKLYTSALDHFTVYLKYEKNPMMQQTIKTKFTEYLERAEELKK 76
Cdd:cd02678    3 LQKAIELVKKAIEEDNAGNYEEALRLYQHALEYFMHALKYEKNPKSKESIRAKCTEYLDRAEKLKE 68
MIT pfam04212
MIT (microtubule interacting and transport) domain; The MIT domain forms an asymmetric ...
 12-76 6.57e-20

MIT (microtubule interacting and transport) domain; The MIT domain forms an asymmetric three-helix bundle and binds ESCRT-III (endosomal sorting complexes required for transport) substrates.


Pssm-ID: 461228  Cd Length: 66  Bit Score: 82.97  E-value: 6.57e-20
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 303291081   12 EKAIALVKEAVERDKASEYAAAFKLYTSALDHFTVYLKYEKNPMMQQTIKTKFTEYLERAEELKK 76
Cdd:pfam04212   2 SKALELVKKAVEEDNAGNYEEALELYKEALDYLLLALKETKNEERRELLRAKIAEYLERAEELKE 66
AAA smart00382
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ...
 178-309 1.02e-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: 82.42  E-value: 1.02e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 303291081   178 LLYGPPGTGKSFLAKAVATEADST---FFSISSSDL--------------VSKWMGESEKLVNQLFTMAREKSPSIIFID 240
Cdd:smart00382   6 LIVGPPGSGKTTLARALARELGPPgggVIYIDGEDIleevldqllliivgGKKASGSGELRLRLALALARKLKPDVLILD 85

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 303291081   241 EIDALCGARGEGGESEASRRIKTEILVQMqgvgneaGRVLVLAATNTPYQLDQA-VRRRFDKRIYIPLPD 309
Cdd:smart00382  86 EITSLLDAEQEALLLLLEELRLLLLLKSE-------KNLTVILTTNDEKDLGPAlLRRRFDRRIVLLLIL 148
MIT cd02656
MIT: domain contained within Microtubule Interacting and Trafficking molecules. The MIT domain ...
 12-77 3.07e-17

MIT: domain contained within Microtubule Interacting and Trafficking molecules. The MIT domain is found in sorting nexins, the nuclear thiol protease PalBH, the AAA protein spastin and archaebacterial proteins with similar domain architecture, vacuolar sorting proteins and others. The molecular function of the MIT domain is unclear.


Pssm-ID: 239121  Cd Length: 75  Bit Score: 75.81  E-value: 3.07e-17
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 303291081  12 EKAIALVKEAVERDKASEYAAAFKLYTSALDHFTVYLKYEKNPMMQQTIKTKFTEYLERAEELKKL 77
Cdd:cd02656    4 QQAKELIKQAVKEDEDGNYEEALELYKEALDYLLQALKAEKEPKLRKLLRKKVKEYLDRAEFLKEL 69
RecA-like_Ycf46-like cd19507
ATPase domain of Ycf46 and similar ATPase domains; Ycf46 may play a role in the regulation of ...
 142-305 2.16e-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: 2.16e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 303291081 142 DVAGLTSAKEALKeavilpvkfpqfftgKRK-AWS------------GFLLYGPPGTGKSFLAKAVATEADSTFFSISSS 208
Cdd:cd19507    1 DVGGLDNLKDWLK---------------KRKaAFSkqasayglptpkGLLLVGIQGTGKSLTAKAIAGVWQLPLLRLDMG 65

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 303291081 209 DLVSKWMGESEKLVNQLFTMAREKSPSIIFIDEIDALCGARGEGGESEASRRIKTEILVQMQgvgNEAGRVLVLAATNTP 288
Cdd:cd19507   66 RLFGGLVGESESRLRQMIQTAEAIAPCVLWIDEIEKGFSNADSKGDSGTSSRVLGTFLTWLQ---EKKKPVFVVATANNV 142

                        170
                 ....*....|....*....
gi 303291081 289 YQLDQAVRR--RFDKRIYI 305
Cdd:cd19507  143 QSLPPELLRkgRFDEIFFV 161
RecA-like_NSF-SEC18_r1-like cd19504
first of two ATPase domains of NSF and SEC18, and similar ATPase domains; ...
 176-305 2.20e-16

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: 76.76  E-value: 2.20e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 303291081 176 GFLLYGPPGTGKSFLAKAVATEADSTFFSI-SSSDLVSKWMGESEKLVNQLFTMAREK--------SPSIIFIDEIDALC 246
Cdd:cd19504   37 GILLYGPPGTGKTLMARQIGKMLNAREPKIvNGPEILNKYVGESEANIRKLFADAEEEqrrlgansGLHIIIFDEIDAIC 116

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 303291081 247 GARGE-GGESEASRRIKTEILVQMQGVgNEAGRVLVLAATNTPYQLDQAVRR--RFDKRIYI 305
Cdd:cd19504  117 KQRGSmAGSTGVHDTVVNQLLSKIDGV-EQLNNILVIGMTNRKDLIDEALLRpgRLEVQMEI 177
RecA-like_Pch2-like cd19508
ATPase domain of Pachytene checkpoint 2 (Pch2) and similar ATPase domains; Pch2 (known as ...
 178-305 8.61e-16

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: 75.56  E-value: 8.61e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 303291081 178 LLYGPPGTGKSFLAKAVA---------TEADSTFFSISSSDLVSKWMGESEKLVNQLFT----MAREKSPSI-IFIDEID 243
Cdd:cd19508   56 LLHGPPGTGKTSLCKALAqklsirlssRYRYGQLIEINSHSLFSKWFSESGKLVTKMFQkiqeLIDDKDALVfVLIDEVE 135

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 303291081 244 ALCGAR---GEGGESEASRRIKTEILVQMQGVgNEAGRVLVLAATNTPYQLDQAVRRRFDKRIYI 305
Cdd:cd19508  136 SLAAARsasSSGTEPSDAIRVVNAVLTQIDRI-KRYHNNVILLTSNLLEKIDVAFVDRADIKQYI 199
MIT_2 cd02684
MIT: domain contained within Microtubule Interacting and Trafficking molecules. This ...
 12-78 1.24e-15

MIT: domain contained within Microtubule Interacting and Trafficking molecules. This sub-family of MIT domains is found in proteins with an n-terminal serine/threonine kinase domain. The molecular function of the MIT domain is unclear.


Pssm-ID: 239147  Cd Length: 75  Bit Score: 71.39  E-value: 1.24e-15
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 303291081  12 EKAIALVKEAVERDKASEYAAAFKLYTSALDHFTVYLKYEKNPMMQQTIKTKFTEYLERAEELKKLM 78
Cdd:cd02684    4 EKAIALVVQAVKKDQRGDAAAALSLYCSALQYFVPALHYETDAQRKEALRQKVLQYVSRAEELKALI 70
ycf46 CHL00195
Ycf46; Provisional
 136-403 1.50e-15

Ycf46; Provisional


Pssm-ID: 177094 [Multi-domain]  Cd Length: 489  Bit Score: 78.52  E-value: 1.50e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 303291081 136 PDVKWDDVAGLTSAKEALKeavilpvKFPQFFTGKRKAWS-----GFLLYGPPGTGKSFLAKAVATEADSTFFSISSSDL 210
Cdd:CHL00195 223 VNEKISDIGGLDNLKDWLK-------KRSTSFSKQASNYGlptprGLLLVGIQGTGKSLTAKAIANDWQLPLLRLDVGKL 295

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 303291081 211 VSKWMGESEKLVNQLFTMAREKSPSIIFIDEID-ALCG--ARGEGGESeaSRRIKTEIlvqmQGVGNEAGRVLVLAATNT 287
Cdd:CHL00195 296 FGGIVGESESRMRQMIRIAEALSPCILWIDEIDkAFSNseSKGDSGTT--NRVLATFI----TWLSEKKSPVFVVATANN 369

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 303291081 288 PYQLDQAVRR--RFDKRIYIPLPDAPARAHMFRVHVGET-PHDLTDADFQSLGAQSEGFSGSDIDHVVKDVLYEPVRKTQ 364
Cdd:CHL00195 370 IDLLPLEILRkgRFDEIFFLDLPSLEEREKIFKIHLQKFrPKSWKKYDIKKLSKLSNKFSGAEIEQSIIEAMYIAFYEKR 449

                        250       260       270
                 ....*....|....*....|....*....|....*....
gi 303291081 365 EathFKTTTGPDGDERYVPCSPGDPDAWERtLEQLAEDG 403
Cdd:CHL00195 450 E---FTTDDILLALKQFIPLAQTEKEQIEA-LQNWASSG 484
MIT smart00745
Microtubule Interacting and Trafficking molecule domain;
12-77 4.49e-14

Microtubule Interacting and Trafficking molecule domain;


Pssm-ID: 197854  Cd Length: 77  Bit Score: 66.95  E-value: 4.49e-14
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 303291081    12 EKAIALVKEAVERDKASEYAAAFKLYTSALDHFTVYLKYEKNPMMQQTIKTKFTEYLERAEELKKL 77
Cdd:smart00745   6 SKAKELISKALKADEAGNYEEALELYKKAIEYLLEGIKVESDSKRREALKAKAAEYLDRAEEIKKS 71
RecA-like_BCS1 cd19510
Mitochondrial chaperone BCS1; Mitochondrial chaperone BCS1 is necessary for the assembly of ...
 153-305 6.54e-13

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: 66.22  E-value: 6.54e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 303291081 153 LKEAVILPVKFPQFFTGKRKAWS-GFLLYGPPGTGKSFLAKAVATEADSTFFSISSSDLVSkwmgeSEKLVNQLFTMARE 231
Cdd:cd19510    1 IIDDLKDFIKNEDWYNDRGIPYRrGYLLYGPPGTGKSSFIAALAGELDYDICDLNLSEVVL-----TDDRLNHLLNTAPK 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 303291081 232 KspSIIFIDEIDALCGARGEGGESEA-----SRRIKTEILVQMQGVGNEAGRVLVLaATNTPYQLDQAVRR--RFDKRIY 304
Cdd:cd19510   76 Q--SIILLEDIDAAFESREHNKKNPSaygglSRVTFSGLLNALDGVASSEERIVFM-TTNHIERLDPALIRpgRVDMKIY 152


                 .
gi 303291081 305 I 305
Cdd:cd19510  153 M 153
RecA-like_ATAD3-like cd19512
ATPase domains of ATPase AAA-domain protein 3A (ATAD3A), -3B, and -3C, and similar ATPase ...
 178-303 5.66e-12

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: 63.31  E-value: 5.66e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 303291081 178 LLYGPPGTGKSFLAKAVATEADSTFFSISSSDLVSkwMG-ESEKLVNQLFTMA-REKSPSIIFIDEIDALCGARGEGGES 255
Cdd:cd19512   26 LFYGPPGTGKTLFAKKLALHSGMDYAIMTGGDVAP--MGrEGVTAIHKVFDWAnTSRRGLLLFVDEADAFLRKRSTEKIS 103

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 303291081 256 EASRRIKTEILVQMqgvGNEAGRVLVLAATNTPYQLDQAVRRRFDKRI 303
Cdd:cd19512  104 EDLRAALNAFLYRT---GEQSNKFMLVLASNQPEQFDWAINDRIDEMV 148
RecA-like_IQCA1 cd19506
ATPase domain of IQ and AAA domain-containing protein 1 (IQCA1); IQCA1 (also known as dynein ...
 178-303 2.36e-09

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: 56.00  E-value: 2.36e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 303291081 178 LLYGPPGTGKSFLAKAVATEADSTFFSISSSDLVSKWMGES--EKLVNQLFTMAREKSPSIIFIDEIDALCGARGEGGES 255
Cdd:cd19506   30 LLAGPSGVGKKMLVHAICTETGANLFNLSPSNIAGKYPGKNglQMMLHLVLKVARQLQPSVIWIGDAEKTFYKKVPKTEK 109

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 303291081 256 EAS-RRIKTEILVQMQGVGNEaGRVLVLAATNTPYQLDQAVRRRFDKRI 303
Cdd:cd19506  110 QLDpKRLKKDLPKILKSLKPE-DRVLIVGTTSRPFEADLKSFCKVYNKI 157
MIT_SNX15 cd02677
MIT: domain contained within Microtubule Interacting and Trafficking molecules. This MIT ...
 12-74 9.62e-09

MIT: domain contained within Microtubule Interacting and Trafficking molecules. This MIT domain sub-family is found in sorting nexin 15 and related proteins. The molecular function of the MIT domain is unclear.


Pssm-ID: 239140  Cd Length: 75  Bit Score: 51.96  E-value: 9.62e-09
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 303291081  12 EKAIALVKEAVERDKASEYAAAFKLYTSALDHFTVYLKYEKNPMMQQTIKTKFTEYLERAEEL 74
Cdd:cd02677    4 EQAAELIRLALEKEEEGDYEAAFEFYRAGVDLLLKGVQGDSSPERREAVKRKIAEYLKRAEEI 66
AAA_5 pfam07728
AAA domain (dynein-related subfamily); This Pfam entry includes some of the AAA proteins not ...
 176-299 2.90e-08

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: 52.29  E-value: 2.90e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 303291081  176 GFLLYGPPGTGKSFLAK--AVATEADSTFF-----SISSSDLVSKW--MGESEKLVNQLFTMArEKSPSIIFIDEIDalc 246
Cdd:pfam07728   1 GVLLVGPPGTGKTELAErlAAALSNRPVFYvqltrDTTEEDLFGRRniDPGGASWVDGPLVRA-AREGEIAVLDEIN--- 76

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 303291081  247 gargeggeseasrRIKTEILVQMQGVGNEAGRVL---------------VLAATNTPYQ----LDQAVRRRF 299
Cdd:pfam07728  77 -------------RANPDVLNSLLSLLDERRLLLpdggelvkaapdgfrLIATMNPLDRglneLSPALRSRF 135
RecA-like_Ycf2 cd19505
ATPase domain of plant YCF2; Ycf2 is a chloroplast ATPase which has an essential function; ...
 176-305 1.27e-07

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: 51.22  E-value: 1.27e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 303291081 176 GFLLYGPPGTGKSFLAKAVATEADSTFFSISSSDLVSKW--------------MGESEKLVNQLFTMAREKSPSIIFIDE 241
Cdd:cd19505   14 GILLIGSIETGRSYLIKSLAANSYVPLIRISLNKLLYNKpdfgnddwidgmliLKESLHRLNLQFELAKAMSPCIIWIPN 93

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 303291081 242 IDALcGARGEGGESEASRRIKTEILV---QMQGVGNEAGRVLVLAATNTPYQLDQAV--RRRFDKRIYI 305
Cdd:cd19505   94 IHEL-NVNRSTQNLEEDPKLLLGLLLnylSRDFEKSSTRNILVIASTHIPQKVDPALiaPNRLDTCINI 161
PRK13342 PRK13342
recombination factor protein RarA; Reviewed
 177-242 1.02e-06

recombination factor protein RarA; Reviewed


Pssm-ID: 237355 [Multi-domain]  Cd Length: 413  Bit Score: 50.85  E-value: 1.02e-06
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 303291081 177 FLLYGPPGTGKSFLAKAVATEADSTFFSISSS-----DLvskwmgesEKLVNQLFTMAREKSPSIIFIDEI 242
Cdd:PRK13342  39 MILWGPPGTGKTTLARIIAGATDAPFEALSAVtsgvkDL--------REVIEEARQRRSAGRRTILFIDEI 101
MIT_1 cd02683
MIT: domain contained within Microtubule Interacting and Trafficking molecules. This ...
 12-76 1.08e-06

MIT: domain contained within Microtubule Interacting and Trafficking molecules. This sub-family of MIT domains is found in proteins with unknown function, co-occuring with an as yet undescribed domain. The molecular function of the MIT domain is unclear.


Pssm-ID: 239146  Cd Length: 77  Bit Score: 46.26  E-value: 1.08e-06
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 303291081  12 EKAIALVKEAVERDKASEYAAAFKLYTSALDHFTVYLKYEKNPMMQQTIKTKFTEYLERAEELKK 76
Cdd:cd02683    4 LAAKEVLKRAVELDQEGRFQEALVCYQEGIDLLMQVLKGTKDEAKKKNLRQKISEYMDRAEAIKK 68
AAA_2 pfam07724
AAA domain (Cdc48 subfamily); This Pfam entry includes some of the AAA proteins not detected ...
 177-243 2.66e-06

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: 47.19  E-value: 2.66e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 303291081  177 FLLYGPPGTGKSFLAKAVA----------TEADSTFFSISSSdlVSKWMGESEKLVN-----QLFTMAREKSPSIIFIDE 241
Cdd:pfam07724   6 FLFLGPTGVGKTELAKALAellfgderalIRIDMSEYMEEHS--VSRLIGAPPGYVGyeeggQLTEAVRRKPYSIVLIDE 83


                  ..
gi 303291081  242 ID 243
Cdd:pfam07724  84 IE 85
RarA COG2256
Replication-associated recombination protein RarA (DNA-dependent ATPase) [Replication, ...
 177-245 5.67e-06

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


Pssm-ID: 441857 [Multi-domain]  Cd Length: 439  Bit Score: 48.51  E-value: 5.67e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 303291081 177 FLLYGPPGTGKSFLAKAVATEADSTFFSISS-----SDLvskwmgesEKLVNQLFTMAREKSPSIIFIDEI--------D 243
Cdd:COG2256   52 MILWGPPGTGKTTLARLIANATDAEFVALSAvtsgvKDI--------REVIEEARERRAYGRRTILFVDEIhrfnkaqqD 123


                 ..
gi 303291081 244 AL 245
Cdd:COG2256  124 AL 125
T7SS_EccA TIGR03922
type VII secretion AAA-ATPase EccA; This model represents the AAA family ATPase, EccA, of the ...
 178-306 6.47e-06

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: 48.30  E-value: 6.47e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 303291081  178 LLYGPPGTGKSFLAKAVATE-------ADSTFFSISSSDLVSKWMGESEKLVNQLFTMAREKspsIIFIDEIDALCgARG 250
Cdd:TIGR03922 316 LFAGPPGTGKTTIARVVAKIycglgvlRKPLVREVSRADLIGQYIGESEAKTNEIIDSALGG---VLFLDEAYTLV-ETG 391

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 303291081  251 EGGESEASRRIKTEILVQMQgvgNEAGRVLVLAA-----TNTPYQLDQAVRRRFDKRIYIP 306
Cdd:TIGR03922 392 YGQKDPFGLEAIDTLLARME---NDRDRLVVIGAgyrkdLDKFLEVNEGLRSRFTRVIEFP 449
clpA PRK11034
ATP-dependent Clp protease ATP-binding subunit; Provisional
 178-301 8.03e-06

ATP-dependent Clp protease ATP-binding subunit; Provisional


Pssm-ID: 236828 [Multi-domain]  Cd Length: 758  Bit Score: 48.29  E-value: 8.03e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 303291081 178 LLYGPPGTGKSFLAKAVATE----------ADSTFFSISSSDLV--SKWMGESEKLVNQLFTMAREKSPSIIFIDEIDAL 245
Cdd:PRK11034 211 LLVGESGVGKTAIAEGLAWRivqgdvpevmADCTIYSLDIGSLLagTKYRGDFEKRFKALLKQLEQDTNSILFIDEIHTI 290

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 303291081 246 CGA-RGEGGESEASRRIKTEIlvqmqgvgnEAGRVLVLAAT-----NTPYQLDQAVRRRFDK 301
Cdd:PRK11034 291 IGAgAASGGQVDAANLIKPLL---------SSGKIRVIGSTtyqefSNIFEKDRALARRFQK 343
ruvB PRK00080
Holliday junction branch migration DNA helicase RuvB;
178-245 1.28e-04

Holliday junction branch migration DNA helicase RuvB;


Pssm-ID: 234619 [Multi-domain]  Cd Length: 328  Bit Score: 43.97  E-value: 1.28e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 303291081 178 LLYGPPGTGKSFLAKAVATEADSTFFSIS------SSDLVSkwmgeseklvnqLFTMAREKspSIIFIDEIDAL 245
Cdd:PRK00080  55 LLYGPPGLGKTTLANIIANEMGVNIRITSgpalekPGDLAA------------ILTNLEEG--DVLFIDEIHRL 114
DnaC COG1484
DNA replication protein DnaC [Replication, recombination and repair];
176-242 1.93e-04

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


Pssm-ID: 441093 [Multi-domain]  Cd Length: 242  Bit Score: 42.85  E-value: 1.93e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 303291081 176 GFLLYGPPGTGKSFLAKAVATEA-----DSTFFSIssSDLVSKWM-----GESEKLVNQLftmareKSPSIIFIDEI 242
Cdd:COG1484  101 NLILLGPPGTGKTHLAIALGHEAcragyRVRFTTA--PDLVNELKearadGRLERLLKRL------AKVDLLILDEL 169
PRK08116 PRK08116
hypothetical protein; Validated
 176-197 2.34e-04

hypothetical protein; Validated


Pssm-ID: 236153 [Multi-domain]  Cd Length: 268  Bit Score: 42.70  E-value: 2.34e-04
                         10        20
                 ....*....|....*....|..
gi 303291081 176 GFLLYGPPGTGKSFLAKAVATE 197
Cdd:PRK08116 116 GLLLWGSVGTGKTYLAACIANE 137
IS21_help_AAA NF038214
IS21-like element helper ATPase IstB; This protein family model resembles PF01695, but was ...
 178-242 3.71e-04

IS21-like element helper ATPase IstB; This protein family model resembles PF01695, but was built to hit full-length AAA+ ATPases of IS21 family IS (insertion sequence) elements.


Pssm-ID: 439516  Cd Length: 232  Bit Score: 41.69  E-value: 3.71e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 303291081 178 LLYGPPGTGKSFLAKAVATEA----DSTFFsISSSDLVSKWM-----GESEKLVNQLftmAReksPSIIFIDEI 242
Cdd:NF038214  94 LLLGPPGTGKTHLAIALGYAAcrqgYRVRF-TTAADLVEQLAqaradGRLGRLLRRL---AR---YDLLIIDEL 160
TIP49 pfam06068
TIP49 P-loop domain; This family consists of the C-terminal region of several eukaryotic and ...
 170-221 4.82e-04

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: 42.30  E-value: 4.82e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 303291081  170 KRKAWSGFLLYGPPGTGKSFLAKAVATE--ADSTFFSISSSDLVSKWMGESEKL 221
Cdd:pfam06068  46 GKIAGRAVLIAGPPGTGKTALAIAISKElgEDTPFTSISGSEVYSLEMKKTEAL 99
TIP49 COG1224
DNA helicase TIP49, TBP-interacting protein [Transcription];
176-221 6.34e-04

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


Pssm-ID: 440837 [Multi-domain]  Cd Length: 452  Bit Score: 41.88  E-value: 6.34e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*...
gi 303291081 176 GFLLYGPPGTGKSFLAKAVATE--ADSTFFSISSSDLVSKWMGESEKL 221
Cdd:COG1224   66 GILIVGPPGTGKTALAVAIARElgEDTPFVAISGSEIYSAELKKTEFL 113
RecA-like_HslU cd19498
ATP-dependent protease ATPase subunit HslU; HslU is a component of the ATP-dependent protease ...
 178-259 7.28e-04

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: 40.44  E-value: 7.28e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 303291081 178 LLYGPPGTGKSFLAKAVATEADSTFFSISSSDLVSkwMGESEKLVNqlfTMAREKSPSIIFIDEIDALCgARGEGGESEA 257
Cdd:cd19498   50 LMIGPTGVGKTEIARRLAKLAGAPFIKVEATKFTE--VGYVGRDVE---SIIRDLVEGIVFIDEIDKIA-KRGGSSGPDV 123


                 ..
gi 303291081 258 SR 259
Cdd:cd19498  124 SR 125
AAA_lid_3 pfam17862
AAA+ lid domain; This entry represents the alpha helical AAA+ lid domain that is found to the ...
 330-370 2.88e-03

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: 35.59  E-value: 2.88e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 303291081  330 DADFQSLGAQSEGFSGSDIDHVVKDVLYEPVRKTQEATHFK 370
Cdd:pfam17862   1 DVDLEELAERTEGFSGADLEALCREAALAALRRGLEAVTQE 41
44 PHA02544
clamp loader, small subunit; Provisional
 178-243 3.30e-03

clamp loader, small subunit; Provisional


Pssm-ID: 222866 [Multi-domain]  Cd Length: 316  Bit Score: 39.20  E-value: 3.30e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 303291081 178 LLYGP-PGTGKSFLAKAVATEADSTFFSISSSDlvskwmGESEKLVNQL--F--TMAREKSPSIIFIDEID 243
Cdd:PHA02544  46 LLHSPsPGTGKTTVAKALCNEVGAEVLFVNGSD------CRIDFVRNRLtrFasTVSLTGGGKVIIIDEFD 110
McrB COG1401
5-methylcytosine-specific restriction endonuclease McrBC, GTP-binding regulatory subunit McrB ...
 178-195 4.84e-03

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


Pssm-ID: 441011 [Multi-domain]  Cd Length: 477  Bit Score: 39.37  E-value: 4.84e-03
                         10
                 ....*....|....*...
gi 303291081 178 LLYGPPGTGKSFLAKAVA 195
Cdd:COG1401  225 ILAGPPGTGKTYLARRLA 242
RecA-like_superfamily cd01120
RecA-like_NTPases; RecA-like NTPases. This superfamily includes the NTP binding domain of F1 ...
 177-304 7.56e-03

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: 36.33  E-value: 7.56e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 303291081 177 FLLYGPPGTGKSFLAKAVATEA---DSTFFSISSSDlvskwmgeseKLVNQLFTMAREKSPSIIFIDEIDALCGARGEGG 253
Cdd:cd01120    1 ILITGPPGSGKTTLLLQFAEQAllsDEPVIFISFLD----------TILEAIEDLIEEKKLDIIIIDSLSSLARASQGDR 70

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 303291081 254 ESEASRRIKTEILVQMQgvgneaGRVLVLAATNTPYQLDQAVRRRFDKRIY 304
Cdd:cd01120   71 SSELLEDLAKLLRAARN------TGITVIATIHSDKFDIDRGGSSNDERLL 115
RecA-like_Lon cd19500
lon protease homolog 2 peroxisomal; Lon protease (also known as Lon peptidase) is an ...
 178-245 7.68e-03

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: 37.54  E-value: 7.68e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 303291081 178 LLYGPPGTGKSFLAKAVATEADSTFFSISSSDLVSkwmgESE--------------KLVnQLFTMAREKSPsIIFIDEID 243
Cdd:cd19500   41 CLVGPPGVGKTSLGKSIARALGRKFVRISLGGVRD----EAEirghrrtyvgampgRII-QALKKAGTNNP-VFLLDEID 114


                 ..
gi 303291081 244 AL 245
Cdd:cd19500  115 KI 116
RecA-like_ClpB_Hsp104-like cd19499
Chaperone protein ClpB/Hsp104 subfamily; Bacterial Caseinolytic peptidase B (ClpB) and ...
 177-243 8.09e-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: 37.16  E-value: 8.09e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 303291081 177 FLLYGPPGTGKSFLAKAVA-----TEADSTFFSISS-------SDLVSKWMG-----ESEKLVNQLftmaREKSPSIIFI 239
Cdd:cd19499   44 FLFLGPTGVGKTELAKALAellfgDEDNLIRIDMSEymekhsvSRLIGAPPGyvgytEGGQLTEAV----RRKPYSVVLL 119


                 ....
gi 303291081 240 DEID 243
Cdd:cd19499  120 DEIE 123
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH