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Conserved domains on  [gi|302675238|ref|XP_003027303|]
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26S proteasome subunit P45 [Schizophyllum commune H4-8]

Protein Classification

26S proteasome regulatory subunit 4( domain architecture ID 11488438)

26S proteasome regulatory subunit 4 is a component of the 26S proteasome, a multiprotein complex involved in the ATP-dependent degradation of ubiquitinated proteins

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PTZ00361 PTZ00361
26 proteosome regulatory subunit 4-like protein; Provisional
 1-446 0e+00

26 proteosome regulatory subunit 4-like protein; Provisional


:

Pssm-ID: 185575 [Multi-domain]  Cd Length: 438  Bit Score: 792.05  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302675238   1 MGNAASGLGQGGPPNPNQDKDKKekdqkkkWEPPLPTRVG-KKKRKGPATASKLPPVYPTTRCRLKLLKMERIKDYLLME 79
Cdd:PTZ00361   1 MGNAQGQGNNQKDKNKKKEKKKK-------ESPPPPHEIKrKKKRKGPDAASKLPKVTPNTKCRLRLLKLERIKDYLLLE 73

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302675238  80 EEFIQNQERLKPetREEKNEEDRSKVDDLRGSPMAVGTMEEIVDDDHAIISTSSGPEFYVSIMSYVDKDLLEPGCQVLLH 159
Cdd:PTZ00361  74 EEFITNQEAQKP--AQEKNEAELKKVDDLRGSPLSVGTLEEIIDENHAIVSSSVGPEYYVNILSFVDKEQLEPGCSVLLH 151

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302675238 160 HKTQSIVGVLQDDADPMVSVMKLDKAPTESYADIGGLEQQIQEIKESVELPLTHPELYEEMGIKPPKGVILYGVPGTGKT 239
Cdd:PTZ00361 152 NKTHSVVGILLDEVDPLVSVMKVDKAPLESYADIGGLEQQIQEIKEAVELPLTHPELYDDIGIKPPKGVILYGPPGTGKT 231

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302675238 240 LLAKAVANQTSATFLRIVGSELIQKYLGDGPKLVRELFRVAEEHAPSIVFIDEIDAVGTKRYDSTSGGEREIQRTMLELL 319
Cdd:PTZ00361 232 LLAKAVANETSATFLRVVGSELIQKYLGDGPKLVRELFRVAEENAPSIVFIDEIDAIGTKRYDATSGGEKEIQRTMLELL 311

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302675238 320 NQLDGFDTRGDVKVIMATNKIESLDPALIRPGRIDRKIEFPLPDVKTKRHIFRLHTSRMNLSEDVDLEEFVMTKDDLSGA 399
Cdd:PTZ00361 312 NQLDGFDSRGDVKVIMATNRIESLDPALIRPGRIDRKIEFPNPDEKTKRRIFEIHTSKMTLAEDVDLEEFIMAKDELSGA 391

                        410       420       430       440
                 ....*....|....*....|....*....|....*....|....*..
gi 302675238 400 DIKAVCTEAGLLALRERRMRVTKADFTSAREKVLYRKNEGTPEGLYL 446
Cdd:PTZ00361 392 DIKAICTEAGLLALRERRMKVTQADFRKAKEKVLYRKKGNIPEGLYL 438
 
Name Accession Description Interval E-value
PTZ00361 PTZ00361
26 proteosome regulatory subunit 4-like protein; Provisional
 1-446 0e+00

26 proteosome regulatory subunit 4-like protein; Provisional


Pssm-ID: 185575 [Multi-domain]  Cd Length: 438  Bit Score: 792.05  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302675238   1 MGNAASGLGQGGPPNPNQDKDKKekdqkkkWEPPLPTRVG-KKKRKGPATASKLPPVYPTTRCRLKLLKMERIKDYLLME 79
Cdd:PTZ00361   1 MGNAQGQGNNQKDKNKKKEKKKK-------ESPPPPHEIKrKKKRKGPDAASKLPKVTPNTKCRLRLLKLERIKDYLLLE 73

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302675238  80 EEFIQNQERLKPetREEKNEEDRSKVDDLRGSPMAVGTMEEIVDDDHAIISTSSGPEFYVSIMSYVDKDLLEPGCQVLLH 159
Cdd:PTZ00361  74 EEFITNQEAQKP--AQEKNEAELKKVDDLRGSPLSVGTLEEIIDENHAIVSSSVGPEYYVNILSFVDKEQLEPGCSVLLH 151

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302675238 160 HKTQSIVGVLQDDADPMVSVMKLDKAPTESYADIGGLEQQIQEIKESVELPLTHPELYEEMGIKPPKGVILYGVPGTGKT 239
Cdd:PTZ00361 152 NKTHSVVGILLDEVDPLVSVMKVDKAPLESYADIGGLEQQIQEIKEAVELPLTHPELYDDIGIKPPKGVILYGPPGTGKT 231

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302675238 240 LLAKAVANQTSATFLRIVGSELIQKYLGDGPKLVRELFRVAEEHAPSIVFIDEIDAVGTKRYDSTSGGEREIQRTMLELL 319
Cdd:PTZ00361 232 LLAKAVANETSATFLRVVGSELIQKYLGDGPKLVRELFRVAEENAPSIVFIDEIDAIGTKRYDATSGGEKEIQRTMLELL 311

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302675238 320 NQLDGFDTRGDVKVIMATNKIESLDPALIRPGRIDRKIEFPLPDVKTKRHIFRLHTSRMNLSEDVDLEEFVMTKDDLSGA 399
Cdd:PTZ00361 312 NQLDGFDSRGDVKVIMATNRIESLDPALIRPGRIDRKIEFPNPDEKTKRRIFEIHTSKMTLAEDVDLEEFIMAKDELSGA 391

                        410       420       430       440
                 ....*....|....*....|....*....|....*....|....*..
gi 302675238 400 DIKAVCTEAGLLALRERRMRVTKADFTSAREKVLYRKNEGTPEGLYL 446
Cdd:PTZ00361 392 DIKAICTEAGLLALRERRMKVTQADFRKAKEKVLYRKKGNIPEGLYL 438
RPT1 COG1222
ATP-dependent 26S proteasome regulatory subunit [Posttranslational modification, protein ...
 170-441 1.08e-131

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


Pssm-ID: 440835 [Multi-domain]  Cd Length: 326  Bit Score: 382.82  E-value: 1.08e-131
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302675238 170 QDDADPMVSVMKLDKAPTESYADIGGLEQQIQEIKESVELPLTHPELYEEMGIKPPKGVILYGVPGTGKTLLAKAVANQT 249
Cdd:COG1222   57 QKRLGTPRGTAVPAESPDVTFDDIGGLDEQIEEIREAVELPLKNPELFRKYGIEPPKGVLLYGPPGTGKTLLAKAVAGEL 136

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302675238 250 SATFLRIVGSELIQKYLGDGPKLVRELFRVAEEHAPSIVFIDEIDAVGTKRYDSTSGGerEIQRTMLELLNQLDGFDTRG 329
Cdd:COG1222  137 GAPFIRVRGSELVSKYIGEGARNVREVFELAREKAPSIIFIDEIDAIAARRTDDGTSG--EVQRTVNQLLAELDGFESRG 214

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302675238 330 DVKVIMATNKIESLDPALIRPGRIDRKIEFPLPDVKTKRHIFRLHTSRMNLSEDVDLEEFVMTKDDLSGADIKAVCTEAG 409
Cdd:COG1222  215 DVLIIAATNRPDLLDPALLRPGRFDRVIEVPLPDEEAREEILKIHLRDMPLADDVDLDKLAKLTEGFSGADLKAIVTEAG 294

                        250       260       270
                 ....*....|....*....|....*....|..
gi 302675238 410 LLALRERRMRVTKADFTSAREKVLYRKNEGTP 441
Cdd:COG1222  295 MFAIREGRDTVTMEDLEKAIEKVKKKTETATN 326
RecA-like_PAN_like cd19502
proteasome activating nucleotidase PAN and related proteasome subunits; This subfamily ...
 189-359 7.35e-113

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: 328.91  E-value: 7.35e-113
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302675238 189 SYADIGGLEQQIQEIKESVELPLTHPELYEEMGIKPPKGVILYGVPGTGKTLLAKAVANQTSATFLRIVGSELIQKYLGD 268
Cdd:cd19502    1 TYEDIGGLDEQIREIREVVELPLKHPELFEELGIEPPKGVLLYGPPGTGKTLLAKAVANHTDATFIRVVGSELVQKYIGE 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302675238 269 GPKLVRELFRVAEEHAPSIVFIDEIDAVGTKRYDSTSGGEREIQRTMLELLNQLDGFDTRGDVKVIMATNKIESLDPALI 348
Cdd:cd19502   81 GARLVRELFEMAREKAPSIIFIDEIDAIGAKRFDSGTGGDREVQRTMLELLNQLDGFDPRGNIKVIMATNRPDILDPALL 160

                        170
                 ....*....|.
gi 302675238 349 RPGRIDRKIEF 359
Cdd:cd19502  161 RPGRFDRKIEF 171
FtsH_fam TIGR01241
ATP-dependent metalloprotease FtsH; HflB(FtsH) is a pleiotropic protein required for correct ...
 180-434 2.38e-80

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: 256.83  E-value: 2.38e-80
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302675238  180 MKLDKAPTESYADIGGLEQQIQEIKESVELpLTHPELYEEMGIKPPKGVILYGVPGTGKTLLAKAVANQTSATFLRIVGS 259
Cdd:TIGR01241  44 LLNEEKPKVTFKDVAGIDEAKEELMEIVDF-LKNPSKFTKLGAKIPKGVLLVGPPGTGKTLLAKAVAGEAGVPFFSISGS 122

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302675238  260 ELIQKYLGDGPKLVRELFRVAEEHAPSIVFIDEIDAVGTKRYDSTSGGEREIQRTMLELLNQLDGFDTRGDVKVIMATNK 339
Cdd:TIGR01241 123 DFVEMFVGVGASRVRDLFEQAKKNAPCIIFIDEIDAVGRQRGAGLGGGNDEREQTLNQLLVEMDGFGTNTGVIVIAATNR 202

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302675238  340 IESLDPALIRPGRIDRKIEFPLPDVKTKRHIFRLHTSRMNLSEDVDLEEFVMTKDDLSGADIKAVCTEAGLLALRERRMR 419
Cdd:TIGR01241 203 PDVLDPALLRPGRFDRQVVVDLPDIKGREEILKVHAKNKKLAPDVDLKAVARRTPGFSGADLANLLNEAALLAARKNKTE 282

                         250
                  ....*....|....*
gi 302675238  420 VTKADFTSAREKVLY 434
Cdd:TIGR01241 283 ITMNDIEEAIDRVIA 297
AAA pfam00004
ATPase family associated with various cellular activities (AAA); AAA family proteins often ...
 228-361 7.61e-51

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


Pssm-ID: 459627 [Multi-domain]  Cd Length: 130  Bit Score: 168.16  E-value: 7.61e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302675238  228 VILYGVPGTGKTLLAKAVANQTSATFLRIVGSELIQKYLGDGPKLVRELFRVAEEHAPSIVFIDEIDAVGTKRYdstSGG 307
Cdd:pfam00004   1 LLLYGPPGTGKTTLAKAVAKELGAPFIEISGSELVSKYVGESEKRLRELFEAAKKLAPCVIFIDEIDALAGSRG---SGG 77

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 302675238  308 EREIQRTMLELLNQLDGFDTR-GDVKVIMATNKIESLDPALIrpGRIDRKIEFPL 361
Cdd:pfam00004  78 DSESRRVVNQLLTELDGFTSSnSKVIVIAATNRPDKLDPALL--GRFDRIIEFPL 130
AAA smart00382
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ...
 224-363 1.16e-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: 1.16e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302675238   224 PPKGVILYGVPGTGKTLLAKAVANQ---TSATFLRIVGSEL--------------IQKYLGDGPKLVRELFRVAEEHAPS 286
Cdd:smart00382   1 PGEVILIVGPPGSGKTTLARALARElgpPGGGVIYIDGEDIleevldqllliivgGKKASGSGELRLRLALALARKLKPD 80

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 302675238   287 IVFIDEIDAVGTKrydstsggEREIQRTMLELLNQLDGFDTRGDVKVIMATNKIESLDPALIRPgRIDRKIEFPLPD 363
Cdd:smart00382  81 VLILDEITSLLDA--------EQEALLLLLEELRLLLLLKSEKNLTVILTTNDEKDLGPALLRR-RFDRRIVLLLIL 148
 
Name Accession Description Interval E-value
PTZ00361 PTZ00361
26 proteosome regulatory subunit 4-like protein; Provisional
 1-446 0e+00

26 proteosome regulatory subunit 4-like protein; Provisional


Pssm-ID: 185575 [Multi-domain]  Cd Length: 438  Bit Score: 792.05  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302675238   1 MGNAASGLGQGGPPNPNQDKDKKekdqkkkWEPPLPTRVG-KKKRKGPATASKLPPVYPTTRCRLKLLKMERIKDYLLME 79
Cdd:PTZ00361   1 MGNAQGQGNNQKDKNKKKEKKKK-------ESPPPPHEIKrKKKRKGPDAASKLPKVTPNTKCRLRLLKLERIKDYLLLE 73

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302675238  80 EEFIQNQERLKPetREEKNEEDRSKVDDLRGSPMAVGTMEEIVDDDHAIISTSSGPEFYVSIMSYVDKDLLEPGCQVLLH 159
Cdd:PTZ00361  74 EEFITNQEAQKP--AQEKNEAELKKVDDLRGSPLSVGTLEEIIDENHAIVSSSVGPEYYVNILSFVDKEQLEPGCSVLLH 151

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302675238 160 HKTQSIVGVLQDDADPMVSVMKLDKAPTESYADIGGLEQQIQEIKESVELPLTHPELYEEMGIKPPKGVILYGVPGTGKT 239
Cdd:PTZ00361 152 NKTHSVVGILLDEVDPLVSVMKVDKAPLESYADIGGLEQQIQEIKEAVELPLTHPELYDDIGIKPPKGVILYGPPGTGKT 231

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302675238 240 LLAKAVANQTSATFLRIVGSELIQKYLGDGPKLVRELFRVAEEHAPSIVFIDEIDAVGTKRYDSTSGGEREIQRTMLELL 319
Cdd:PTZ00361 232 LLAKAVANETSATFLRVVGSELIQKYLGDGPKLVRELFRVAEENAPSIVFIDEIDAIGTKRYDATSGGEKEIQRTMLELL 311

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302675238 320 NQLDGFDTRGDVKVIMATNKIESLDPALIRPGRIDRKIEFPLPDVKTKRHIFRLHTSRMNLSEDVDLEEFVMTKDDLSGA 399
Cdd:PTZ00361 312 NQLDGFDSRGDVKVIMATNRIESLDPALIRPGRIDRKIEFPNPDEKTKRRIFEIHTSKMTLAEDVDLEEFIMAKDELSGA 391

                        410       420       430       440
                 ....*....|....*....|....*....|....*....|....*..
gi 302675238 400 DIKAVCTEAGLLALRERRMRVTKADFTSAREKVLYRKNEGTPEGLYL 446
Cdd:PTZ00361 392 DIKAICTEAGLLALRERRMKVTQADFRKAKEKVLYRKKGNIPEGLYL 438
PRK03992 PRK03992
proteasome-activating nucleotidase; Provisional
 68-442 1.39e-177

proteasome-activating nucleotidase; Provisional


Pssm-ID: 179699 [Multi-domain]  Cd Length: 389  Bit Score: 501.67  E-value: 1.39e-177
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302675238  68 KMERIKDYLLMEEEFIQNQERLKPETREEKNEEDR------SKVDDLRGSPMAVGTMEEIVDDDHAIISTSSGPEFYVSI 141
Cdd:PRK03992   2 RLEALEERNSELEEQIRQLELKLRDLEAENEKLERelerlkSELEKLKSPPLIVATVLEVLDDGRVVVKSSGGPQFLVNV 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302675238 142 MSYVDKDLLEPGCQVLLHHKTQSIVGVLQDDADPMVSVMKLDKAPTESYADIGGLEQQIQEIKESVELPLTHPELYEEMG 221
Cdd:PRK03992  82 SPFIDREKLKPGARVALNQQSLAIVEVLPSEKDPRVQAMEVIESPNVTYEDIGGLEEQIREVREAVELPLKKPELFEEVG 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302675238 222 IKPPKGVILYGVPGTGKTLLAKAVANQTSATFLRIVGSELIQKYLGDGPKLVRELFRVAEEHAPSIVFIDEIDAVGTKRY 301
Cdd:PRK03992 162 IEPPKGVLLYGPPGTGKTLLAKAVAHETNATFIRVVGSELVQKFIGEGARLVRELFELAREKAPSIIFIDEIDAIAAKRT 241

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302675238 302 DSTSGGEREIQRTMLELLNQLDGFDTRGDVKVIMATNKIESLDPALIRPGRIDRKIEFPLPDVKTKRHIFRLHTSRMNLS 381
Cdd:PRK03992 242 DSGTSGDREVQRTLMQLLAEMDGFDPRGNVKIIAATNRIDILDPAILRPGRFDRIIEVPLPDEEGRLEILKIHTRKMNLA 321

                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 302675238 382 EDVDLEEFVMTKDDLSGADIKAVCTEAGLLALRERRMRVTKADFTSAREKVLYRKNEGTPE 442
Cdd:PRK03992 322 DDVDLEELAELTEGASGADLKAICTEAGMFAIRDDRTEVTMEDFLKAIEKVMGKEEKDSME 382
PTZ00454 PTZ00454
26S protease regulatory subunit 6B-like protein; Provisional
 64-440 8.94e-159

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


Pssm-ID: 240423 [Multi-domain]  Cd Length: 398  Bit Score: 454.22  E-value: 8.94e-159
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302675238  64 LKLLKMERIKDYLLMEEEFIqnqerlKPETREEKNEEDRSK--VDDLRGSPMAVGTMEEIVDDDHAIISTSSGPEFYVSI 141
Cdd:PTZ00454  22 EKLKELEKELEFLDIQEEYI------KEEQKNLKRELIRAKeeVKRIQSVPLVIGQFLEMIDSNYGIVSSTSGSNYYVRI 95

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302675238 142 MSYVDKDLLEPGCQVLLHHKTQSIVGVLQDDADPMVSVMKLDKAPTESYADIGGLEQQIQEIKESVELPLTHPELYEEMG 221
Cdd:PTZ00454  96 LSTLNRELLKPNASVALHRHSHAVVDILPPEADSSIQLLQMSEKPDVTYSDIGGLDIQKQEIREAVELPLTCPELYEQIG 175

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302675238 222 IKPPKGVILYGVPGTGKTLLAKAVANQTSATFLRIVGSELIQKYLGDGPKLVRELFRVAEEHAPSIVFIDEIDAVGTKRY 301
Cdd:PTZ00454 176 IDPPRGVLLYGPPGTGKTMLAKAVAHHTTATFIRVVGSEFVQKYLGEGPRMVRDVFRLARENAPSIIFIDEVDSIATKRF 255

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302675238 302 DSTSGGEREIQRTMLELLNQLDGFDTRGDVKVIMATNKIESLDPALIRPGRIDRKIEFPLPDVKTKRHIFRLHTSRMNLS 381
Cdd:PTZ00454 256 DAQTGADREVQRILLELLNQMDGFDQTTNVKVIMATNRADTLDPALLRPGRLDRKIEFPLPDRRQKRLIFQTITSKMNLS 335

                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 302675238 382 EDVDLEEFVMTKDDLSGADIKAVCTEAGLLALRERRMRVTKADFTSAREKVLyRKNEGT 440
Cdd:PTZ00454 336 EEVDLEDFVSRPEKISAADIAAICQEAGMQAVRKNRYVILPKDFEKGYKTVV-RKTDRD 393
RPT1 COG1222
ATP-dependent 26S proteasome regulatory subunit [Posttranslational modification, protein ...
 170-441 1.08e-131

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


Pssm-ID: 440835 [Multi-domain]  Cd Length: 326  Bit Score: 382.82  E-value: 1.08e-131
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302675238 170 QDDADPMVSVMKLDKAPTESYADIGGLEQQIQEIKESVELPLTHPELYEEMGIKPPKGVILYGVPGTGKTLLAKAVANQT 249
Cdd:COG1222   57 QKRLGTPRGTAVPAESPDVTFDDIGGLDEQIEEIREAVELPLKNPELFRKYGIEPPKGVLLYGPPGTGKTLLAKAVAGEL 136

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302675238 250 SATFLRIVGSELIQKYLGDGPKLVRELFRVAEEHAPSIVFIDEIDAVGTKRYDSTSGGerEIQRTMLELLNQLDGFDTRG 329
Cdd:COG1222  137 GAPFIRVRGSELVSKYIGEGARNVREVFELAREKAPSIIFIDEIDAIAARRTDDGTSG--EVQRTVNQLLAELDGFESRG 214

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302675238 330 DVKVIMATNKIESLDPALIRPGRIDRKIEFPLPDVKTKRHIFRLHTSRMNLSEDVDLEEFVMTKDDLSGADIKAVCTEAG 409
Cdd:COG1222  215 DVLIIAATNRPDLLDPALLRPGRFDRVIEVPLPDEEAREEILKIHLRDMPLADDVDLDKLAKLTEGFSGADLKAIVTEAG 294

                        250       260       270
                 ....*....|....*....|....*....|..
gi 302675238 410 LLALRERRMRVTKADFTSAREKVLYRKNEGTP 441
Cdd:COG1222  295 MFAIREGRDTVTMEDLEKAIEKVKKKTETATN 326
RecA-like_PAN_like cd19502
proteasome activating nucleotidase PAN and related proteasome subunits; This subfamily ...
 189-359 7.35e-113

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: 328.91  E-value: 7.35e-113
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302675238 189 SYADIGGLEQQIQEIKESVELPLTHPELYEEMGIKPPKGVILYGVPGTGKTLLAKAVANQTSATFLRIVGSELIQKYLGD 268
Cdd:cd19502    1 TYEDIGGLDEQIREIREVVELPLKHPELFEELGIEPPKGVLLYGPPGTGKTLLAKAVANHTDATFIRVVGSELVQKYIGE 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302675238 269 GPKLVRELFRVAEEHAPSIVFIDEIDAVGTKRYDSTSGGEREIQRTMLELLNQLDGFDTRGDVKVIMATNKIESLDPALI 348
Cdd:cd19502   81 GARLVRELFEMAREKAPSIIFIDEIDAIGAKRFDSGTGGDREVQRTMLELLNQLDGFDPRGNIKVIMATNRPDILDPALL 160

                        170
                 ....*....|.
gi 302675238 349 RPGRIDRKIEF 359
Cdd:cd19502  161 RPGRFDRKIEF 171
SpoVK COG0464
AAA+-type ATPase, SpoVK/Ycf46/Vps4 family [Cell wall/membrane/envelope biogenesis, Cell cycle ...
 190-437 3.34e-81

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: 255.99  E-value: 3.34e-81
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302675238 190 YADIGGLEQQIQEIKESVELPLTHPELYEEMGIKPPKGVILYGVPGTGKTLLAKAVANQTSATFLRIVGSELIQKYLGDG 269
Cdd:COG0464  156 LDDLGGLEEVKEELRELVALPLKRPELREEYGLPPPRGLLLYGPPGTGKTLLARALAGELGLPLIEVDLSDLVSKYVGET 235

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302675238 270 PKLVRELFRVAEEHAPSIVFIDEIDAVGTKRydsTSGGEREIQRTMLELLNQLDGFdtRGDVKVIMATNKIESLDPALIR 349
Cdd:COG0464  236 EKNLREVFDKARGLAPCVLFIDEADALAGKR---GEVGDGVGRRVVNTLLTEMEEL--RSDVVVIAATNRPDLLDPALLR 310

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302675238 350 pgRIDRKIEFPLPDVKTKRHIFRLHTSRMNLSEDVDLEEFVMTKDDLSGADIKAVCTEAGLLALRERRMRVTKADFTSAR 429
Cdd:COG0464  311 --RFDEIIFFPLPDAEERLEIFRIHLRKRPLDEDVDLEELAEATEGLSGADIRNVVRRAALQALRLGREPVTTEDLLEAL 388


                 ....*....
gi 302675238 430 EKV-LYRKN 437
Cdd:COG0464  389 EREdIFLKR 397
FtsH_fam TIGR01241
ATP-dependent metalloprotease FtsH; HflB(FtsH) is a pleiotropic protein required for correct ...
 180-434 2.38e-80

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: 256.83  E-value: 2.38e-80
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302675238  180 MKLDKAPTESYADIGGLEQQIQEIKESVELpLTHPELYEEMGIKPPKGVILYGVPGTGKTLLAKAVANQTSATFLRIVGS 259
Cdd:TIGR01241  44 LLNEEKPKVTFKDVAGIDEAKEELMEIVDF-LKNPSKFTKLGAKIPKGVLLVGPPGTGKTLLAKAVAGEAGVPFFSISGS 122

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302675238  260 ELIQKYLGDGPKLVRELFRVAEEHAPSIVFIDEIDAVGTKRYDSTSGGEREIQRTMLELLNQLDGFDTRGDVKVIMATNK 339
Cdd:TIGR01241 123 DFVEMFVGVGASRVRDLFEQAKKNAPCIIFIDEIDAVGRQRGAGLGGGNDEREQTLNQLLVEMDGFGTNTGVIVIAATNR 202

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302675238  340 IESLDPALIRPGRIDRKIEFPLPDVKTKRHIFRLHTSRMNLSEDVDLEEFVMTKDDLSGADIKAVCTEAGLLALRERRMR 419
Cdd:TIGR01241 203 PDVLDPALLRPGRFDRQVVVDLPDIKGREEILKVHAKNKKLAPDVDLKAVARRTPGFSGADLANLLNEAALLAARKNKTE 282

                         250
                  ....*....|....*
gi 302675238  420 VTKADFTSAREKVLY 434
Cdd:TIGR01241 283 ITMNDIEEAIDRVIA 297
CDC48 TIGR01243
AAA family ATPase, CDC48 subfamily; This subfamily of the AAA family ATPases includes two ...
 186-432 6.41e-75

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: 248.67  E-value: 6.41e-75
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302675238  186 PTESYADIGGLEQQIQEIKESVELPLTHPELYEEMGIKPPKGVILYGVPGTGKTLLAKAVANQTSATFLRIVGSELIQKY 265
Cdd:TIGR01243 448 PNVRWSDIGGLEEVKQELREAVEWPLKHPEIFEKMGIRPPKGVLLFGPPGTGKTLLAKAVATESGANFIAVRGPEILSKW 527

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302675238  266 LGDGPKLVRELFRVAEEHAPSIVFIDEIDAVGTKRydSTSGGEREIQRTMLELLNQLDGFDTRGDVKVIMATNKIESLDP 345
Cdd:TIGR01243 528 VGESEKAIREIFRKARQAAPAIIFFDEIDAIAPAR--GARFDTSVTDRIVNQLLTEMDGIQELSNVVVIAATNRPDILDP 605

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302675238  346 ALIRPGRIDRKIEFPLPDVKTKRHIFRLHTSRMNLSEDVDLEEFVMTKDDLSGADIKAVCTEAGLLALRE---------- 415
Cdd:TIGR01243 606 ALLRPGRFDRLILVPPPDEEARKEIFKIHTRSMPLAEDVDLEELAEMTEGYTGADIEAVCREAAMAALREsigspakekl 685

                         250       260
                  ....*....|....*....|....*
gi 302675238  416 --------RRMRVTKADFTSAREKV 432
Cdd:TIGR01243 686 evgeeeflKDLKVEMRHFLEALKKV 710
CDC48 TIGR01243
AAA family ATPase, CDC48 subfamily; This subfamily of the AAA family ATPases includes two ...
 177-425 1.78e-74

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: 247.51  E-value: 1.78e-74
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302675238  177 VSVMKLDKAPTESYADIGGLEQQIQEIKESVELPLTHPELYEEMGIKPPKGVILYGVPGTGKTLLAKAVANQTSATFLRI 256
Cdd:TIGR01243 164 VREEIERKVPKVTYEDIGGLKEAKEKIREMVELPMKHPELFEHLGIEPPKGVLLYGPPGTGKTLLAKAVANEAGAYFISI 243

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302675238  257 VGSELIQKYLGDGPKLVRELFRVAEEHAPSIVFIDEIDAVGTKRYDSTsgGEREiQRTMLELLNQLDGFDTRGDVKVIMA 336
Cdd:TIGR01243 244 NGPEIMSKYYGESEERLREIFKEAEENAPSIIFIDEIDAIAPKREEVT--GEVE-KRVVAQLLTLMDGLKGRGRVIVIGA 320

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302675238  337 TNKIESLDPALIRPGRIDRKIEFPLPDVKTKRHIFRLHTSRMNLSEDVDLEEFVMTKDDLSGADIKAVCTEAGLLALReR 416
Cdd:TIGR01243 321 TNRPDALDPALRRPGRFDREIVIRVPDKRARKEILKVHTRNMPLAEDVDLDKLAEVTHGFVGADLAALAKEAAMAALR-R 399


                  ....*....
gi 302675238  417 RMRVTKADF 425
Cdd:TIGR01243 400 FIREGKINF 408
HflB COG0465
ATP-dependent Zn proteases [Posttranslational modification, protein turnover, chaperones];
183-433 6.90e-73

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


Pssm-ID: 440233 [Multi-domain]  Cd Length: 583  Bit Score: 239.55  E-value: 6.90e-73
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302675238 183 DKAPTESYADIGGLEQQIQEIKESVELpLTHPELYEEMGIKPPKGVILYGVPGTGKTLLAKAVANQTSATFLRIVGSELI 262
Cdd:COG0465  134 EDKPKVTFDDVAGVDEAKEELQEIVDF-LKDPEKFTRLGAKIPKGVLLVGPPGTGKTLLAKAVAGEAGVPFFSISGSDFV 212

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302675238 263 QKYLGDGPKLVRELFRVAEEHAPSIVFIDEIDAVGTKRyDSTSGG---EREiqRTmlelLNQL----DGFDTRGDVKVIM 335
Cdd:COG0465  213 EMFVGVGASRVRDLFEQAKKNAPCIIFIDEIDAVGRQR-GAGLGGghdERE--QT----LNQLlvemDGFEGNEGVIVIA 285

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302675238 336 ATNKIESLDPALIRPGRIDRKIEFPLPDVKTKRHIFRLHTSRMNLSEDVDLEE-------FvmtkddlSGADIKAVCTEA 408
Cdd:COG0465  286 ATNRPDVLDPALLRPGRFDRQVVVDLPDVKGREAILKVHARKKPLAPDVDLEViarrtpgF-------SGADLANLVNEA 358

                        250       260
                 ....*....|....*....|....*
gi 302675238 409 GLLALRERRMRVTKADFTSAREKVL 433
Cdd:COG0465  359 ALLAARRNKKAVTMEDFEEAIDRVI 383
RecA-like_CDC48_NLV2_r1-like cd19503
first of two ATPase domains of CDC48 and NLV2, and similar ATPase domains; CDC48 in yeast and ...
 192-359 1.93e-68

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: 214.85  E-value: 1.93e-68
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302675238 192 DIGGLEQQIQEIKESVELPLTHPELYEEMGIKPPKGVILYGVPGTGKTLLAKAVANQTSATFLRIVGSELIQKYLGDGPK 271
Cdd:cd19503    1 DIGGLDEQIASLKELIELPLKYPELFRALGLKPPRGVLLHGPPGTGKTLLARAVANEAGANFLSISGPSIVSKYLGESEK 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302675238 272 LVRELFRVAEEHAPSIVFIDEIDAVGTKRYDSTSGGEReiqRTMLELLNQLDGFDTRGDVKVIMATNKIESLDPALIRPG 351
Cdd:cd19503   81 NLREIFEEARSHAPSIIFIDEIDALAPKREEDQREVER---RVVAQLLTLMDGMSSRGKVVVIAATNRPDAIDPALRRPG 157


                 ....*...
gi 302675238 352 RIDRKIEF 359
Cdd:cd19503  158 RFDREVEI 165
RecA-like_FtsH cd19501
ATP-dependent zinc metalloprotease FtsH; FtsH ATPase is a processive, ATP-dependent zinc ...
 189-357 1.35e-65

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: 207.86  E-value: 1.35e-65
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302675238 189 SYADIGGLEQQIQEIKESVELpLTHPELYEEMGIKPPKGVILYGVPGTGKTLLAKAVANQTSATFLRIVGSELIQKYLGD 268
Cdd:cd19501    2 TFKDVAGCEEAKEELKEVVEF-LKNPEKFTKLGAKIPKGVLLVGPPGTGKTLLAKAVAGEAGVPFFSISGSDFVEMFVGV 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302675238 269 GPKLVRELFRVAEEHAPSIVFIDEIDAVGTKRYDSTSGGEREIQRTMLELLNQLDGFDTRGDVKVIMATNKIESLDPALI 348
Cdd:cd19501   81 GASRVRDLFEQAKKNAPCIVFIDEIDAVGRKRGAGLGGGHDEREQTLNQLLVEMDGFESNTGVIVIAATNRPDVLDPALL 160


                 ....*....
gi 302675238 349 RPGRIDRKI 357
Cdd:cd19501  161 RPGRFDRQV 169
RecA-like_CDC48_r1-like cd19519
first of two ATPase domains of CDC48 and similar ATPase domains; CDC48 in yeast and p97 or VCP ...
 192-360 8.11e-65

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: 205.75  E-value: 8.11e-65
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302675238 192 DIGGLEQQIQEIKESVELPLTHPELYEEMGIKPPKGVILYGVPGTGKTLLAKAVANQTSATFLRIVGSELIQKYLGDGPK 271
Cdd:cd19519    1 DIGGCRKQLAQIREMVELPLRHPELFKAIGIKPPRGILLYGPPGTGKTLIARAVANETGAFFFLINGPEIMSKLAGESES 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302675238 272 LVRELFRVAEEHAPSIVFIDEIDAVGTKRYDSTSGGEReiqRTMLELLNQLDGFDTRGDVKVIMATNKIESLDPALIRPG 351
Cdd:cd19519   81 NLRKAFEEAEKNAPAIIFIDEIDAIAPKREKTHGEVER---RIVSQLLTLMDGLKQRAHVIVMAATNRPNSIDPALRRFG 157


                 ....*....
gi 302675238 352 RIDRKIEFP 360
Cdd:cd19519  158 RFDREIDIG 166
ftsH CHL00176
cell division protein; Validated
 189-441 9.62e-65

cell division protein; Validated


Pssm-ID: 214386 [Multi-domain]  Cd Length: 638  Bit Score: 219.54  E-value: 9.62e-65
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302675238 189 SYADIGGLEQQIQEIKESVELpLTHPELYEEMGIKPPKGVILYGVPGTGKTLLAKAVANQTSATFLRIVGSELIQKYLGD 268
Cdd:CHL00176 181 TFRDIAGIEEAKEEFEEVVSF-LKKPERFTAVGAKIPKGVLLVGPPGTGKTLLAKAIAGEAEVPFFSISGSEFVEMFVGV 259

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302675238 269 GPKLVRELFRVAEEHAPSIVFIDEIDAVGTKRYDSTSGGEREIQRTMLELLNQLDGFDTRGDVKVIMATNKIESLDPALI 348
Cdd:CHL00176 260 GAARVRDLFKKAKENSPCIVFIDEIDAVGRQRGAGIGGGNDEREQTLNQLLTEMDGFKGNKGVIVIAATNRVDILDAALL 339

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302675238 349 RPGRIDRKIEFPLPDVKTKRHIFRLHTSRMNLSEDVDLEEFVMTKDDLSGADIKAVCTEAGLLALRERRMRVTKADFTSA 428
Cdd:CHL00176 340 RPGRFDRQITVSLPDREGRLDILKVHARNKKLSPDVSLELIARRTPGFSGADLANLLNEAAILTARRKKATITMKEIDTA 419

                        250
                 ....*....|...
gi 302675238 429 REKVLyRKNEGTP 441
Cdd:CHL00176 420 IDRVI-AGLEGTP 431
RecA-like_CDC48_r2-like cd19511
second of two ATPase domains of CDC48/p97, PEX1 and -6, VAT and NVL, and similar ATPase ...
 201-357 4.67e-60

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: 193.27  E-value: 4.67e-60
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302675238 201 QEIKESVELPLTHPELYEEMGIKPPKGVILYGVPGTGKTLLAKAVANQTSATFLRIVGSELIQKYLGDGPKLVRELFRVA 280
Cdd:cd19511    3 RELKEAVEWPLKHPDAFKRLGIRPPKGVLLYGPPGCGKTLLAKALASEAGLNFISVKGPELFSKYVGESERAVREIFQKA 82

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 302675238 281 EEHAPSIVFIDEIDAVGTKRYDSTSGGEREiqRTMLELLNQLDGFDTRGDVKVIMATNKIESLDPALIRPGRIDRKI 357
Cdd:cd19511   83 RQAAPCIIFFDEIDSLAPRRGQSDSSGVTD--RVVSQLLTELDGIESLKGVVVIAATNRPDMIDPALLRPGRLDKLI 157
hflB PRK10733
ATP-dependent zinc metalloprotease FtsH;
189-433 4.69e-59

ATP-dependent zinc metalloprotease FtsH;


Pssm-ID: 182683 [Multi-domain]  Cd Length: 644  Bit Score: 204.50  E-value: 4.69e-59
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302675238 189 SYADIGGLEQQIQEIKESVELpLTHPELYEEMGIKPPKGVILYGVPGTGKTLLAKAVANQTSATFLRIVGSELIQKYLGD 268
Cdd:PRK10733 150 TFADVAGCDEAKEEVAELVEY-LREPSRFQKLGGKIPKGVLMVGPPGTGKTLLAKAIAGEAKVPFFTISGSDFVEMFVGV 228

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302675238 269 GPKLVRELFRVAEEHAPSIVFIDEIDAVGTKRYDSTSGGEREIQRTMLELLNQLDGFDTRGDVKVIMATNKIESLDPALI 348
Cdd:PRK10733 229 GASRVRDMFEQAKKAAPCIIFIDEIDAVGRQRGAGLGGGHDEREQTLNQMLVEMDGFEGNEGIIVIAATNRPDVLDPALL 308

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302675238 349 RPGRIDRKIEFPLPDVKTKRHIFRLHTSRMNLSEDVDLEEFVMTKDDLSGADIKAVCTEAGLLALRERRMRVTKADFTSA 428
Cdd:PRK10733 309 RPGRFDRQVVVGLPDVRGREQILKVHMRRVPLAPDIDAAIIARGTPGFSGADLANLVNEAALFAARGNKRVVSMVEFEKA 388


                 ....*
gi 302675238 429 REKVL 433
Cdd:PRK10733 389 KDKIM 393
RecA-like_protease cd19481
proteases similar to RecA; RecA-like NTPases. This family includes the NTP binding domain of ...
 199-359 3.88e-58

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: 188.26  E-value: 3.88e-58
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302675238 199 QIQEIKESVELPLTHPELyEEMGIKPPKGVILYGVPGTGKTLLAKAVANQTSATFLRIVGSELIQKYLGDGPKLVRELFR 278
Cdd:cd19481    1 LKASLREAVEAPRRGSRL-RRYGLGLPKGILLYGPPGTGKTLLAKALAGELGLPLIVVKLSSLLSKYVGESEKNLRKIFE 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302675238 279 VAEEHAPSIVFIDEIDAVGTKRydSTSGGEREIQRTMLELLNQLDGFDTRGDVKVIMATNKIESLDPALIRPGRIDRKIE 358
Cdd:cd19481   80 RARRLAPCILFIDEIDAIGRKR--DSSGESGELRRVLNQLLTELDGVNSRSKVLVIAATNRPDLLDPALLRPGRFDEVIE 157


                 .
gi 302675238 359 F 359
Cdd:cd19481  158 F 158
RecA-like_VCP_r2 cd19529
second of two ATPase domains of Valosin-containing protein-like ATPase (VAT) and similar ...
 201-357 3.75e-57

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: 185.78  E-value: 3.75e-57
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302675238 201 QEIKESVELPLTHPELYEEMGIKPPKGVILYGVPGTGKTLLAKAVANQTSATFLRIVGSELIQKYLGDGPKLVRELFRVA 280
Cdd:cd19529    3 QELKEAVEWPLLKPEVFKRLGIRPPKGILLYGPPGTGKTLLAKAVATESNANFISVKGPELLSKWVGESEKAIREIFRKA 82

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 302675238 281 EEHAPSIVFIDEIDAVGTKRYDSTSGGEREiqRTMLELLNQLDGFDTRGDVKVIMATNKIESLDPALIRPGRIDRKI 357
Cdd:cd19529   83 RQVAPCVIFFDEIDSIAPRRGTTGDSGVTE--RVVNQLLTELDGLEEMNGVVVIAATNRPDIIDPALLRAGRFDRLI 157
AAA pfam00004
ATPase family associated with various cellular activities (AAA); AAA family proteins often ...
 228-361 7.61e-51

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


Pssm-ID: 459627 [Multi-domain]  Cd Length: 130  Bit Score: 168.16  E-value: 7.61e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302675238  228 VILYGVPGTGKTLLAKAVANQTSATFLRIVGSELIQKYLGDGPKLVRELFRVAEEHAPSIVFIDEIDAVGTKRYdstSGG 307
Cdd:pfam00004   1 LLLYGPPGTGKTTLAKAVAKELGAPFIEISGSELVSKYVGESEKRLRELFEAAKKLAPCVIFIDEIDALAGSRG---SGG 77

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 302675238  308 EREIQRTMLELLNQLDGFDTR-GDVKVIMATNKIESLDPALIrpGRIDRKIEFPL 361
Cdd:pfam00004  78 DSESRRVVNQLLTELDGFTSSnSKVIVIAATNRPDKLDPALL--GRFDRIIEFPL 130
COG1223 COG1223
Predicted ATPase, AAA+ superfamily [General function prediction only];
192-443 4.56e-50

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


Pssm-ID: 440836 [Multi-domain]  Cd Length: 246  Bit Score: 170.06  E-value: 4.56e-50
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302675238 192 DIGGLEQQIQEIKEsVELPLTHPELYEEMGIKPPKGVILYGVPGTGKTLLAKAVANQTSATFLRIVGSELIQKYLGDGPK 271
Cdd:COG1223    3 DVVGQEEAKKKLKL-IIKELRRRENLRKFGLWPPRKILFYGPPGTGKTMLAEALAGELKLPLLTVRLDSLIGSYLGETAR 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302675238 272 LVRELFRVAEEhAPSIVFIDEIDAVGTKRYDSTSGGerEIQRTMLELLNQLDGFdtRGDVKVIMATNKIESLDPALIRpg 351
Cdd:COG1223   82 NLRKLFDFARR-APCVIFFDEFDAIAKDRGDQNDVG--EVKRVVNALLQELDGL--PSGSVVIAATNHPELLDSALWR-- 154

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302675238 352 RIDRKIEFPLPDVKTKRHIFRLHTSRMNLSEDVDLEEFVMTKDDLSGADIKAVCTEAGLLALRERRMRVTKADFTSAREK 431
Cdd:COG1223  155 RFDEVIEFPLPDKEERKEILELNLKKFPLPFELDLKKLAKKLEGLSGADIEKVLKTALKKAILEDREKVTKEDLEEALKQ 234

                        250
                 ....*....|..
gi 302675238 432 VLYRKNEGTPEG 443
Cdd:COG1223  235 RKERKKEPKKEG 246
RecA-like_CDC48_r2-like cd19528
second of two ATPase domains of CDC48 and similar ATPase domains; CDC48 in yeast and p97 or ...
 201-357 8.80e-49

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: 163.84  E-value: 8.80e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302675238 201 QEIKESVELPLTHPELYEEMGIKPPKGVILYGVPGTGKTLLAKAVANQTSATFLRIVGSELIQKYLGDGPKLVRELFRVA 280
Cdd:cd19528    3 RELQELVQYPVEHPDKFLKFGMTPSKGVLFYGPPGCGKTLLAKAIANECQANFISVKGPELLTMWFGESEANVRDIFDKA 82

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 302675238 281 EEHAPSIVFIDEIDAVGTKRYDSTSGGEREIQRTMLELLNQLDGFDTRGDVKVIMATNKIESLDPALIRPGRIDRKI 357
Cdd:cd19528   83 RAAAPCVLFFDELDSIAKARGGNIGDAGGAADRVINQILTEMDGMNTKKNVFIIGATNRPDIIDPAILRPGRLDQLI 159
RecA-like_VPS4-like cd19509
ATPase domain of VPS4, ATAD1, K, KTNA1, Spastin, FIGL-1 and similar ATPase domains; This ...
 193-357 1.74e-46

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: 157.90  E-value: 1.74e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302675238 193 IGGLEQQIQEIKESVELPLTHPELYEeMGIKPPKGVILYGVPGTGKTLLAKAVANQTSATFLRIVGSELIQKYLGDGPKL 272
Cdd:cd19509    1 IAGLDDAKEALKEAVILPSLRPDLFP-GLRGPPRGILLYGPPGTGKTLLARAVASESGSTFFSISASSLVSKWVGESEKI 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302675238 273 VRELFRVAEEHAPSIVFIDEIDAVGTKRYDSTSGGEREIqRTmlELLNQLDGFDTRGD--VKVIMATNKIESLDPALIRp 350
Cdd:cd19509   80 VRALFALARELQPSIIFIDEIDSLLSERGSGEHEASRRV-KT--EFLVQMDGVLNKPEdrVLVLGATNRPWELDEAFLR- 155


                 ....*..
gi 302675238 351 gRIDRKI 357
Cdd:cd19509  156 -RFEKRI 161
RecA-like_Yta7-like cd19517
ATPase domain of Saccharomyces cerevisiae Yta7 and similar ATPase domains; Saccharomyces ...
 192-359 2.26e-46

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: 158.06  E-value: 2.26e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302675238 192 DIGGLEQQIQEIKESVELPLTHPELYEEMGIKPPKGVILYGVPGTGKTLLAKAVANQTSA-----TFLRIVGSELIQKYL 266
Cdd:cd19517    1 DIGGLSHYINQLKEMVFFPLLYPEVFAKFKITPPRGVLFHGPPGTGKTLMARALAAECSKggqkvSFFMRKGADCLSKWV 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302675238 267 GDGPKLVRELFRVAEEHAPSIVFIDEIDAVGTKRYDSTSGGEREIQRTMLELlnqLDGFDTRGDVKVIMATNKIESLDPA 346
Cdd:cd19517   81 GEAERQLRLLFEEAYRMQPSIIFFDEIDGLAPVRSSKQEQIHASIVSTLLAL---MDGLDNRGQVVVIGATNRPDALDPA 157

                        170
                 ....*....|...
gi 302675238 347 LIRPGRIDRKIEF 359
Cdd:cd19517  158 LRRPGRFDREFYF 170
RecA-like_NVL_r1-like cd19518
first of two ATPase domains of NVL (nuclear VCP-like protein) and similar ATPase domains; NVL ...
 192-357 6.23e-45

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


Pssm-ID: 410926 [Multi-domain]  Cd Length: 169  Bit Score: 154.10  E-value: 6.23e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302675238 192 DIGGLEQQIQEIKESVELPLTHPELYEEMGIKPPKGVILYGVPGTGKTLLAKAVANQTSATFLRIVGSELIQKYLGDGPK 271
Cdd:cd19518    1 DIGGMDSTLKELCELLIHPILPPEYFQHLGVEPPRGVLLHGPPGCGKTMLANAIAGELKVPFLKISATEIVSGVSGESEE 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302675238 272 LVRELFRVAEEHAPSIVFIDEIDAVGTKRydstSGGEREIQRTML-ELLNQLDGF----DTRGDVKVIMATNKIESLDPA 346
Cdd:cd19518   81 KIRELFDQAISNAPCIVFIDEIDAITPKR----ESAQREMERRIVsQLLTCMDELnnekTAGGPVLVIGATNRPDSLDPA 156

                        170
                 ....*....|.
gi 302675238 347 LIRPGRIDRKI 357
Cdd:cd19518  157 LRRAGRFDREI 167
RecA-like_NVL_r2-like cd19530
second of two ATPase domains of NVL (nuclear VCP-like protein) and similar ATPase domains; NVL ...
 196-355 6.72e-43

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


Pssm-ID: 410938 [Multi-domain]  Cd Length: 161  Bit Score: 148.40  E-value: 6.72e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302675238 196 LEQQIQEIKESVELPLTHPELYEEMGIKPPKGVILYGVPGTGKTLLAKAVANQTSATFLRIVGSELIQKYLGDGPKLVRE 275
Cdd:cd19530    1 LDHVREELTMSILRPIKRPDIYKALGIDLPTGVLLYGPPGCGKTLLAKAVANESGANFISVKGPELLNKYVGESERAVRQ 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302675238 276 LFRVAEEHAPSIVFIDEIDAVGTKRYDSTSGGereIQRTMLELLNQLDGFDTRGDVKVIMATNKIESLDPALIRPGRIDR 355
Cdd:cd19530   81 VFQRARASAPCVIFFDEVDALVPKRGDGGSWA---SERVVNQLLTEMDGLEERSNVFVIAATNRPDIIDPAMLRPGRLDK 157
RecA-like_ATAD1 cd19520
ATPase domain of ATPase family AAA domain-containing protein 1 and similar ATPase domains; ...
 192-349 3.27e-42

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: 146.80  E-value: 3.27e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302675238 192 DIGGLEQQIQEIKESVELPLTHPELYEEMGI-KPPKGVILYGVPGTGKTLLAKAVANQTSATFLRIVGSELIQKYLGDGP 270
Cdd:cd19520    1 DIGGLDEVITELKELVILPLQRPELFDNSRLlQPPKGVLLYGPPGCGKTMLAKATAKEAGARFINLQVSSLTDKWYGESQ 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302675238 271 KLVRELFRVAEEHAPSIVFIDEIDAVGTKRydstSGGEREIQRTM-LELLNQLDGFDTRGDVKVIM--ATNKIESLDPAL 347
Cdd:cd19520   81 KLVAAVFSLASKLQPSIIFIDEIDSFLRQR----SSTDHEATAMMkAEFMSLWDGLSTDGNCRVIVmgATNRPQDLDEAI 156


                 ..
gi 302675238 348 IR 349
Cdd:cd19520  157 LR 158
RecA-like_PEX6_r2 cd19527
second of two ATPase domains of Peroxisomal biogenesis factor 6 (PEX6); PEX6(also known as ...
 202-355 3.79e-40

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: 141.11  E-value: 3.79e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302675238 202 EIKESVELPLTHPELYEEmGIKPPKGVILYGVPGTGKTLLAKAVANQTSATFLRIVGSELIQKYLGDGPKLVRELFRVAE 281
Cdd:cd19527    4 EILDTIQLPLEHPELFSS-GLRKRSGILLYGPPGTGKTLLAKAIATECSLNFLSVKGPELINMYIGESEANVREVFQKAR 82

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 302675238 282 EHAPSIVFIDEIDAVGTKRYDS-TSGGerEIQRTMLELLNQLDGF-DTRGDVKVIMATNKIESLDPALIRPGRIDR 355
Cdd:cd19527   83 DAKPCVIFFDELDSLAPSRGNSgDSGG--VMDRVVSQLLAELDGMsSSGQDVFVIGATNRPDLLDPALLRPGRFDK 156
RecA-like_VPS4 cd19521
ATPase domain of vacuolar protein sorting-associated protein 4; Vacuolar protein ...
 186-357 7.78e-40

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: 140.77  E-value: 7.78e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302675238 186 PTESYADIGGLEQQIQEIKESVELPLTHPELYEEmGIKPPKGVILYGVPGTGKTLLAKAVANQTSATFLRIVGSELIQKY 265
Cdd:cd19521    2 PNVKWEDVAGLEGAKEALKEAVILPVKFPHLFTG-NRKPWSGILLYGPPGTGKSYLAKAVATEANSTFFSVSSSDLVSKW 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302675238 266 LGDGPKLVRELFRVAEEHAPSIVFIDEIDAVGTKRYDSTSGGEREIQRtmlELLNQLDGF--DTRGdVKVIMATNKIESL 343
Cdd:cd19521   81 MGESEKLVKQLFAMARENKPSIIFIDEVDSLCGTRGEGESEASRRIKT---ELLVQMNGVgnDSQG-VLVLGATNIPWQL 156

                        170
                 ....*....|....
gi 302675238 344 DPALIRpgRIDRKI 357
Cdd:cd19521  157 DSAIRR--RFEKRI 168
RecA-like_spastin cd19524
ATPase domain of spastin; Spastin is an ATP-dependent microtubule-severing protein involved in ...
 192-349 3.84e-39

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: 138.83  E-value: 3.84e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302675238 192 DIGGLEQQIQEIKESVELPLTHPELYeeMGIK-PPKGVILYGVPGTGKTLLAKAVANQTSATFLRIVGSELIQKYLGDGP 270
Cdd:cd19524    1 DIAGQDLAKQALQEMVILPSLRPELF--TGLRaPARGLLLFGPPGNGKTMLAKAVAAESNATFFNISAASLTSKYVGEGE 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302675238 271 KLVRELFRVAEEHAPSIVFIDEIDAVGTKRYDSTSGGEReiqRTMLELLNQLDGFDTRGD--VKVIMATNKIESLDPALI 348
Cdd:cd19524   79 KLVRALFAVARELQPSIIFIDEVDSLLSERSEGEHEASR---RLKTEFLIEFDGVQSNGDdrVLVMGATNRPQELDDAVL 155


                 .
gi 302675238 349 R 349
Cdd:cd19524  156 R 156
RecA-like_Figl-1 cd19525
ATPase domain of Fidgetin-Like 1 (FIGL-1); FIGL-1 may participate in DNA repair in the nucleus; ...
 182-349 3.92e-39

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: 139.35  E-value: 3.92e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302675238 182 LDKAPTESYADIGGLEQQIQEIKESVELPLTHPELYeeMGIK-PPKGVILYGVPGTGKTLLAKAVANQTSATFLRIVGSE 260
Cdd:cd19525   13 MDHGPPINWADIAGLEFAKKTIKEIVVWPMLRPDIF--TGLRgPPKGILLFGPPGTGKTLIGKCIASQSGATFFSISASS 90

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302675238 261 LIQKYLGDGPKLVRELFRVAEEHAPSIVFIDEIDAVGTKRYDSTSGGEREIQRtmlELLNQLDGFDTRGDVKVIM--ATN 338
Cdd:cd19525   91 LTSKWVGEGEKMVRALFSVARCKQPAVIFIDEIDSLLSQRGEGEHESSRRIKT---EFLVQLDGATTSSEDRILVvgATN 167

                        170
                 ....*....|.
gi 302675238 339 KIESLDPALIR 349
Cdd:cd19525  168 RPQEIDEAARR 178
RecA-like_PEX1_r2 cd19526
second of two ATPase domains of Peroxisomal biogenesis factor 1 (PEX1); PEX1(also known as ...
 203-358 7.30e-39

second of two ATPase domains of Peroxisomal biogenesis factor 1 (PEX1); PEX1(also known as Peroxin-1)/PEX6 is a protein unfoldase; PEX1 and PEX6 form a heterohexameric Type-2 AAA-ATPase complex and are essential for peroxisome biogenesis as they are required for the import of folded proteins into the peroxisomal matrix. PEX-1 is required for stability of PEX5. This subfamily belongs to the RecA-like NTPase family which includes the NTP binding domain of F1 and V1 H(+)ATPases, DnaB and related helicases as well as bacterial RecA and related eukaryotic and archaeal recombinases. The RecA-like NTPase family also includes bacterial conjugation proteins and related DNA transfer proteins involved in type II and type IV secretion.


Pssm-ID: 410934 [Multi-domain]  Cd Length: 158  Bit Score: 137.56  E-value: 7.30e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302675238 203 IKESVELPLTHPELYEEMGIKPPKGVILYGVPGTGKTLLAKAVANQTSATFLRIVGSELIQKYLGDGPKLVRELFRVAEE 282
Cdd:cd19526    5 LEETIEWPSKYPKIFASSPLRLRSGILLYGPPGCGKTLLASAIASECGLNFISVKGPELLNKYIGASEQNVRDLFSRAQS 84

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 302675238 283 HAPSIVFIDEIDAVGTKR-YDSTSGGEREIQrtmlELLNQLDGFDTRGDVKVIMATNKIESLDPALIRPGRIDRKIE 358
Cdd:cd19526   85 AKPCILFFDEFDSIAPKRgHDSTGVTDRVVN----QLLTQLDGVEGLDGVYVLAATSRPDLIDPALLRPGRLDKLVY 157
RecA-like_KTNA1 cd19522
Katanin p60 ATPase-containing subunit A1; Katanin p60 ATPase-containing subunit A1 (KTNA1) is ...
 192-357 2.02e-36

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: 131.65  E-value: 2.02e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302675238 192 DIGGLEQQIQEIKESVELPLTHPELYEemGIKPP-KGVILYGVPGTGKTLLAKAVANQTSATFLRIVGSELIQKYLGDGP 270
Cdd:cd19522    1 DIADLEEAKKLLEEAVVLPMWMPEFFK--GIRRPwKGVLMVGPPGTGKTLLAKAVATECGTTFFNVSSSTLTSKYRGESE 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302675238 271 KLVRELFRVAEEHAPSIVFIDEIDAVGTKRydSTSGGEREIQRTMLELLNQLDGF-------DTRGDVKVIMATNKIESL 343
Cdd:cd19522   79 KLVRLLFEMARFYAPTTIFIDEIDSICSRR--GTSEEHEASRRVKSELLVQMDGVggasendDPSKMVMVLAATNFPWDI 156

                        170
                 ....*....|....
gi 302675238 344 DPALIRpgRIDRKI 357
Cdd:cd19522  157 DEALRR--RLEKRI 168
RecA-like_fidgetin cd19523
ATPase domain of fidgetin; Fidgetin (FIGN) is a ATP-dependent microtubule severing protein. ...
 192-349 9.69e-29

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: 110.74  E-value: 9.69e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302675238 192 DIGGLEQQIQEIKESVELPLTHPELYEEMgIKPPKGVILYGVPGTGKTLLAKAVANQTSATFLRIVGSELIQKYLGDGPK 271
Cdd:cd19523    1 DIAGLGALKAAIKEEVLWPLLRPDAFSGL-LRLPRSILLFGPRGTGKTLLGRCLASQLGATFLRLRGSTLVAKWAGEGEK 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302675238 272 LVRELFRVAEEHAPSIVFIDEIDAVGTKRYDstsgGEREIQRTMLELLNQLDGFDTRGD--VKVIMATNKIESLDPALIR 349
Cdd:cd19523   80 ILQASFLAARCRQPSVLFISDLDALLSSQDD----EASPVGRLQVELLAQLDGVLGSGEdgVLVVCTTSKPEEIDESLRR 155
RecA-like_NSF-SEC18_r1-like cd19504
first of two ATPase domains of NSF and SEC18, and similar ATPase domains; ...
 193-358 6.51e-28

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: 109.12  E-value: 6.51e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302675238 193 IGGLEQQIQEI-KESVELPLTHPELYEEMGIKPPKGVILYGVPGTGKTLLAKAVANQTSATFLRIV-GSELIQKYLGDGP 270
Cdd:cd19504    2 IGGLDKEFSDIfRRAFASRVFPPEIVEQLGCKHVKGILLYGPPGTGKTLMARQIGKMLNAREPKIVnGPEILNKYVGESE 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302675238 271 KLVRELFRVAEEHAPS--------IVFIDEIDAVGTKRyDSTSGGEREIQRTMLELLNQLDGFDTRGDVKVIMATNKIES 342
Cdd:cd19504   82 ANIRKLFADAEEEQRRlgansglhIIIFDEIDAICKQR-GSMAGSTGVHDTVVNQLLSKIDGVEQLNNILVIGMTNRKDL 160

                        170
                 ....*....|....*.
gi 302675238 343 LDPALIRPGRIDRKIE 358
Cdd:cd19504  161 IDEALLRPGRLEVQME 176
AAA cd00009
The AAA+ (ATPases Associated with a wide variety of cellular Activities) superfamily ...
 194-361 8.07e-27

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: 105.31  E-value: 8.07e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302675238 194 GGLEQQIQEIKESVELPlthpelyeemgikPPKGVILYGVPGTGKTLLAKAVANQT---SATFLRIVGSELIQKYLG--- 267
Cdd:cd00009    1 VGQEEAIEALREALELP-------------PPKNLLLYGPPGTGKTTLARAIANELfrpGAPFLYLNASDLLEGLVVael 67

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302675238 268 DGPKLVRELFRVAEEHAPSIVFIDEIDAVGtkrydstsggeREIQRTMLELLNQL-DGFDTRGDVKVIMATNKIESLDPA 346
Cdd:cd00009   68 FGHFLVRLLFELAEKAKPGVLFIDEIDSLS-----------RGAQNALLRVLETLnDLRIDRENVRVIGATNRPLLGDLD 136

                        170
                 ....*....|....*
gi 302675238 347 LIRPGRIDRKIEFPL 361
Cdd:cd00009  137 RALYDRLDIRIVIPL 151
ycf46 CHL00195
Ycf46; Provisional
 185-417 1.06e-24

Ycf46; Provisional


Pssm-ID: 177094 [Multi-domain]  Cd Length: 489  Bit Score: 106.26  E-value: 1.06e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302675238 185 APTESYADIGGLEQQIQEIKESVElplTHPELYEEMGIKPPKGVILYGVPGTGKTLLAKAVANQTSATFLRIVGSELIQK 264
Cdd:CHL00195 222 SVNEKISDIGGLDNLKDWLKKRST---SFSKQASNYGLPTPRGLLLVGIQGTGKSLTAKAIANDWQLPLLRLDVGKLFGG 298

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302675238 265 YLGDGPKLVRELFRVAEEHAPSIVFIDEIDAVGTKRYDST-SGGEREIQRTMLELLNQldgfdTRGDVKVIMATNKIESL 343
Cdd:CHL00195 299 IVGESESRMRQMIRIAEALSPCILWIDEIDKAFSNSESKGdSGTTNRVLATFITWLSE-----KKSPVFVVATANNIDLL 373

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 302675238 344 DPALIRPGRIDRKIEFPLPDVKTKRHIFRLHTS--RMNLSEDVDLEEFVMTKDDLSGADIKAVCTEAGLLALRERR 417
Cdd:CHL00195 374 PLEILRKGRFDEIFFLDLPSLEEREKIFKIHLQkfRPKSWKKYDIKKLSKLSNKFSGAEIEQSIIEAMYIAFYEKR 449
RecA-like_Ycf46-like cd19507
ATPase domain of Ycf46 and similar ATPase domains; Ycf46 may play a role in the regulation of ...
 192-355 1.25e-23

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: 96.67  E-value: 1.25e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302675238 192 DIGGLEQqiqeIKESVEL--PLTHPElYEEMGIKPPKGVILYGVPGTGKTLLAKAVANQTSATFLRIVGSELIQKYLGDG 269
Cdd:cd19507    1 DVGGLDN----LKDWLKKrkAAFSKQ-ASAYGLPTPKGLLLVGIQGTGKSLTAKAIAGVWQLPLLRLDMGRLFGGLVGES 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302675238 270 PKLVRELFRVAEEHAPSIVFIDEID-AVGTKRYDSTSGGEREIQRTMLELLNQldgfdTRGDVKVIMATNKIESLDPALI 348
Cdd:cd19507   76 ESRLRQMIQTAEAIAPCVLWIDEIEkGFSNADSKGDSGTSSRVLGTFLTWLQE-----KKKPVFVVATANNVQSLPPELL 150


                 ....*..
gi 302675238 349 RPGRIDR 355
Cdd:cd19507  151 RKGRFDE 157
RecA-like_BCS1 cd19510
Mitochondrial chaperone BCS1; Mitochondrial chaperone BCS1 is necessary for the assembly of ...
 203-359 2.02e-22

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: 93.18  E-value: 2.02e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302675238 203 IKESVELPLTHPELYEEMGIKPPKGVILYGVPGTGKTLLAKAVANqtsatFLR--IVGSELIQKYLGDgpKLVRELFRVA 280
Cdd:cd19510    1 IIDDLKDFIKNEDWYNDRGIPYRRGYLLYGPPGTGKSSFIAALAG-----ELDydICDLNLSEVVLTD--DRLNHLLNTA 73

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302675238 281 EEHapSIVFIDEIDAV-----GTKRYDSTSGGEREIqrTMLELLNQLDGFDTRGDVKVIMATNKIESLDPALIRPGRIDR 355
Cdd:cd19510   74 PKQ--SIILLEDIDAAfesreHNKKNPSAYGGLSRV--TFSGLLNALDGVASSEERIVFMTTNHIERLDPALIRPGRVDM 149


                 ....
gi 302675238 356 KIEF 359
Cdd:cd19510  150 KIYM 153
AAA smart00382
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ...
 224-363 1.16e-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: 1.16e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302675238   224 PPKGVILYGVPGTGKTLLAKAVANQ---TSATFLRIVGSEL--------------IQKYLGDGPKLVRELFRVAEEHAPS 286
Cdd:smart00382   1 PGEVILIVGPPGSGKTTLARALARElgpPGGGVIYIDGEDIleevldqllliivgGKKASGSGELRLRLALALARKLKPD 80

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 302675238   287 IVFIDEIDAVGTKrydstsggEREIQRTMLELLNQLDGFDTRGDVKVIMATNKIESLDPALIRPgRIDRKIEFPLPD 363
Cdd:smart00382  81 VLILDEITSLLDA--------EQEALLLLLEELRLLLLLKSEKNLTVILTTNDEKDLGPALLRR-RFDRRIVLLLIL 148
RecA-like_Pch2-like cd19508
ATPase domain of Pachytene checkpoint 2 (Pch2) and similar ATPase domains; Pch2 (known as ...
 228-348 2.27e-13

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: 68.63  E-value: 2.27e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302675238 228 VILYGVPGTGKTLLAKAVANQTS---------ATFLRIVGSELIQKYLGDGPKLVRELFR-----VAEEHAPSIVFIDEI 293
Cdd:cd19508   55 VLLHGPPGTGKTSLCKALAQKLSirlssryryGQLIEINSHSLFSKWFSESGKLVTKMFQkiqelIDDKDALVFVLIDEV 134

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 302675238 294 DAVGTKRYDSTSGGE-REIQRTMLELLNQLDGFDTRGDVKVIMATNKIESLDPALI 348
Cdd:cd19508  135 ESLAAARSASSSGTEpSDAIRVVNAVLTQIDRIKRYHNNVILLTSNLLEKIDVAFV 190
AAA_lid_3 pfam17862
AAA+ lid domain; This entry represents the alpha helical AAA+ lid domain that is found to the ...
 383-425 1.29e-10

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: 56.39  E-value: 1.29e-10
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 302675238  383 DVDLEEFVMTKDDLSGADIKAVCTEAGLLALRERRMRVTKADF 425
Cdd:pfam17862   1 DVDLEELAERTEGFSGADLEALCREAALAALRRGLEAVTQEDL 43
Prot_ATP_ID_OB pfam16450
Proteasomal ATPase OB C-terminal domain; This is the interdomain (ID) or oligonucleotide ...
 115-169 2.16e-09

Proteasomal ATPase OB C-terminal domain; This is the interdomain (ID) or oligonucleotide binding (OB) domain of proteasomal ATPase


Pssm-ID: 465118 [Multi-domain]  Cd Length: 56  Bit Score: 53.28  E-value: 2.16e-09
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 302675238  115 VGTMEEIVDDDHAIISTSSGPEFYVSIMSYVDKDLLEPGCQVLLHHKTQSIVGVL 169
Cdd:pfam16450   1 VATVVEVLDDGRALVKSSGGEERVVRLAGSLDEEKLRPGDRVLLDPRSGYALEVL 55
RarA COG2256
Replication-associated recombination protein RarA (DNA-dependent ATPase) [Replication, ...
 228-293 2.00e-08

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


Pssm-ID: 441857 [Multi-domain]  Cd Length: 439  Bit Score: 56.22  E-value: 2.00e-08
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 302675238 228 VILYGVPGTGKTLLAKAVANQTSATFLRI--VGSeliqkylgdGPKLVRELFRVAEEHA----PSIVFIDEI 293
Cdd:COG2256   52 MILWGPPGTGKTTLARLIANATDAEFVALsaVTS---------GVKDIREVIEEARERRaygrRTILFVDEI 114
RecA-like_ATAD3-like cd19512
ATPase domains of ATPase AAA-domain protein 3A (ATAD3A), -3B, and -3C, and similar ATPase ...
 226-359 2.44e-08

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: 52.91  E-value: 2.44e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302675238 226 KGVILYGVPGTGKTLLAKAVANQTSATFLRIVGSELIQkyLG-DGPKLVRELFRVAEEHAPS-IVFIDEIDAVGTKRyds 303
Cdd:cd19512   23 RNILFYGPPGTGKTLFAKKLALHSGMDYAIMTGGDVAP--MGrEGVTAIHKVFDWANTSRRGlLLFVDEADAFLRKR--- 97

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 302675238 304 TSGGEREIQRTMLELLNQLDGFDTRgDVKVIMATNKIESLDPALirPGRIDRKIEF 359
Cdd:cd19512   98 STEKISEDLRAALNAFLYRTGEQSN-KFMLVLASNQPEQFDWAI--NDRIDEMVEF 150
PRK13342 PRK13342
recombination factor protein RarA; Reviewed
 228-293 1.05e-07

recombination factor protein RarA; Reviewed


Pssm-ID: 237355 [Multi-domain]  Cd Length: 413  Bit Score: 53.94  E-value: 1.05e-07
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302675238 228 VILYGVPGTGKTLLAKAVANQTSATFLRIVGSEliqkylgDGPKLVRELFRVAEEHAPS----IVFIDEI 293
Cdd:PRK13342  39 MILWGPPGTGKTTLARIIAGATDAPFEALSAVT-------SGVKDLREVIEEARQRRSAgrrtILFIDEI 101
RecA-like_Ycf2 cd19505
ATPase domain of plant YCF2; Ycf2 is a chloroplast ATPase which has an essential function; ...
 219-359 1.14e-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: 1.14e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302675238 219 EMGIKPPKGVILYGVPGTGKTLLAKAVANQTSATFLRIVGSELIQKYLGDGPKLVR--------------ELFRVAEEHA 284
Cdd:cd19505    6 RLGLSPSKGILLIGSIETGRSYLIKSLAANSYVPLIRISLNKLLYNKPDFGNDDWIdgmlilkeslhrlnLQFELAKAMS 85

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 302675238 285 PSIVFIDEIDAVGTKRydSTSGGErEIQRTMLELLNQLDGFDTRGDVK----VIMATNKIESLDPALIRPGRIDRKIEF 359
Cdd:cd19505   86 PCIIWIPNIHELNVNR--STQNLE-EDPKLLLGLLLNYLSRDFEKSSTrnilVIASTHIPQKVDPALIAPNRLDTCINI 161
MoxR COG0714
MoxR-like ATPase [General function prediction only]; MoxR-like ATPase is part of the Pathway ...
 228-294 4.38e-06

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


Pssm-ID: 440478 [Multi-domain]  Cd Length: 292  Bit Score: 48.24  E-value: 4.38e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302675238 228 VILYGVPGTGKTLLAKAVANQTSATFLRI-----------VGSELIQKYLGD-----GPklvreLFRvaeehapSIVFID 291
Cdd:COG0714   34 LLLEGVPGVGKTTLAKALARALGLPFIRIqftpdllpsdiLGTYIYDQQTGEfefrpGP-----LFA-------NVLLAD 101


                 ...
gi 302675238 292 EID 294
Cdd:COG0714  102 EIN 104
DUF815 pfam05673
Protein of unknown function (DUF815); This family consists of several bacterial proteins of ...
 191-291 9.01e-06

Protein of unknown function (DUF815); This family consists of several bacterial proteins of unknown function.


Pssm-ID: 428578 [Multi-domain]  Cd Length: 250  Bit Score: 46.76  E-value: 9.01e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302675238  191 ADIGGLEQQIQEIKESVELPLTHpelyeemgiKPPKGVILYGVPGTGKTLLAKAVANQTSATFLRIVgsELIQKYLGDGP 270
Cdd:pfam05673  28 DDLVGIERQKEALIRNTRRFLAG---------LPANNVLLWGARGTGKSSLVKALLNEYADQGLRLI--EVDKEDLGDLP 96

                          90       100
                  ....*....|....*....|.
gi 302675238  271 KLVRELFRVAEEHapsIVFID 291
Cdd:pfam05673  97 DLVDLLRDRPYRF---ILFCD 114
RecA-like_HslU cd19498
ATP-dependent protease ATPase subunit HslU; HslU is a component of the ATP-dependent protease ...
 225-319 1.83e-05

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: 45.06  E-value: 1.83e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302675238 225 PKGVILYGVPGTGKTLLAKAVANQTSATFLRIVGSELIQ-KYLG-DGPKLVRELfrvaeehAPSIVFIDEIDAVGTKRYD 302
Cdd:cd19498   46 PKNILMIGPTGVGKTEIARRLAKLAGAPFIKVEATKFTEvGYVGrDVESIIRDL-------VEGIVFIDEIDKIAKRGGS 118

                         90
                 ....*....|....*...
gi 302675238 303 STSGGERE-IQRTMLELL 319
Cdd:cd19498  119 SGPDVSREgVQRDLLPIV 136
T7SS_EccA TIGR03922
type VII secretion AAA-ATPase EccA; This model represents the AAA family ATPase, EccA, of the ...
 195-360 2.43e-05

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: 46.76  E-value: 2.43e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302675238  195 GLE---QQIQEIKESVELPLTHpelyEEMGIKPP---KGVILYGVPGTGKTLLAKAVANQTSA-TFLR------IVGSEL 261
Cdd:TIGR03922 280 GLErvkRQVAALKSSTAMALAR----AERGLPVAqtsNHMLFAGPPGTGKTTIARVVAKIYCGlGVLRkplvreVSRADL 355

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302675238  262 IQKYLGDGPKLVRELFrvaEEHAPSIVFIDEIDAVGTKRYDSTSGGEREIQRTMLELLNqldgfDTRGDVKVIMA----- 336
Cdd:TIGR03922 356 IGQYIGESEAKTNEII---DSALGGVLFLDEAYTLVETGYGQKDPFGLEAIDTLLARME-----NDRDRLVVIGAgyrkd 427

                         170       180
                  ....*....|....*....|....
gi 302675238  337 TNKIESLDPALirPGRIDRKIEFP 360
Cdd:TIGR03922 428 LDKFLEVNEGL--RSRFTRVIEFP 449
AAA_2 pfam07724
AAA domain (Cdc48 subfamily); This Pfam entry includes some of the AAA proteins not detected ...
 225-338 2.57e-05

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


Pssm-ID: 400187 [Multi-domain]  Cd Length: 168  Bit Score: 44.49  E-value: 2.57e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302675238  225 PKGVILY-GVPGTGKTLLAKAVANQ---TSATFLRIVGSELIQKYL-----GDGPKLVR-----ELFRVAEEHAPSIVFI 290
Cdd:pfam07724   2 PIGSFLFlGPTGVGKTELAKALAELlfgDERALIRIDMSEYMEEHSvsrliGAPPGYVGyeeggQLTEAVRRKPYSIVLI 81

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 302675238  291 DEIDAVGtkrydstsggeREIQRTMLELL-------NQLDGFDTRgDVKVIMATN 338
Cdd:pfam07724  82 DEIEKAH-----------PGVQNDLLQILeggtltdKQGRTVDFK-NTLFIMTGN 124
TIGR02928 TIGR02928
orc1/cdc6 family replication initiation protein; Members of this protein family are found ...
 193-432 2.69e-05

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


Pssm-ID: 274354 [Multi-domain]  Cd Length: 365  Bit Score: 46.09  E-value: 2.69e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302675238  193 IGGLEQQIQEIKEsvelplthpELYEEMGIKPPKGVILYGVPGTGKTLLAKAVANQ----TSATFLRI------------ 256
Cdd:TIGR02928  17 IVHRDEQIEELAK---------ALRPILRGSRPSNVFIYGKTGTGKTAVTKYVMKEleeaAEDRDVRVvtvyvncqildt 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302675238  257 ---VGSELIQKYLGDGP----------KLVRELFRVAEEHAPSIVFI-DEIDavgtkrYDSTSGGEREIQRTMLELLNQL 322
Cdd:TIGR02928  88 lyqVLVELANQLRGSGEevpttglstsEVFRRLYKELNERGDSLIIVlDEID------YLVGDDDDLLYQLSRARSNGDL 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302675238  323 DGfdtrGDVKVIMATNKI---ESLDPAlIRPGRIDRKIEFPLPDVKTKRHIFRlHTSRMNLSEDVDLEEFVMTKDDLSGA 399
Cdd:TIGR02928 162 DN----AKVGVIGISNDLkfrENLDPR-VKSSLCEEEIIFPPYDAEELRDILE-NRAEKAFYDGVLDDGVIPLCAALAAQ 235

                         250       260       270
                  ....*....|....*....|....*....|....*....
gi 302675238  400 DI----KAVCT--EAGLLALRERRMRVTKADFTSAREKV 432
Cdd:TIGR02928 236 EHgdarKAIDLlrVAGEIAEREGAERVTEDHVEKAQEKI 274
AAA_5 pfam07728
AAA domain (dynein-related subfamily); This Pfam entry includes some of the AAA proteins not ...
 227-349 6.91e-05

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: 42.66  E-value: 6.91e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302675238  227 GVILYGVPGTGKTLLAKAVANQTS-ATFLRIVGS------ELIQKYL--GDGPKLV-RELFRVAEEhaPSIVFIDEIDAv 296
Cdd:pfam07728   1 GVLLVGPPGTGKTELAERLAAALSnRPVFYVQLTrdtteeDLFGRRNidPGGASWVdGPLVRAARE--GEIAVLDEINR- 77

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 302675238  297 gtkrydstsgGEREIQRTMLELLN-----QLDGFDTRG----DVKVIMATN----KIESLDPALIR 349
Cdd:pfam07728  78 ----------ANPDVLNSLLSLLDerrllLPDGGELVKaapdGFRLIATMNpldrGLNELSPALRS 133
McrB COG1401
5-methylcytosine-specific restriction endonuclease McrBC, GTP-binding regulatory subunit McrB ...
 185-293 7.10e-05

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


Pssm-ID: 441011 [Multi-domain]  Cd Length: 477  Bit Score: 45.15  E-value: 7.10e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302675238 185 APTESYADIGGLEQQIQEIKESVELPLTHPELYEEMG-------------IKPPKGVILYGVPGTGKTLLAKAVANQTSA 251
Cdd:COG1401  168 APEDLSADALAAELSAAEELYSEDLESEDDYLKDLLRekfeetleaflaaLKTKKNVILAGPPGTGKTYLARRLAEALGG 247

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 302675238 252 T---FLRIV-------GSELIQKY---LGDG-----PKLVRELFRVAEEH--APSIVFIDEI 293
Cdd:COG1401  248 EdngRIEFVqfhpswsYEDFLLGYrpsLDEGkyeptPGIFLRFCLKAEKNpdKPYVLIIDEI 309
RecA-like_ClpB_Hsp104-like cd19499
Chaperone protein ClpB/Hsp104 subfamily; Bacterial Caseinolytic peptidase B (ClpB) and ...
 223-359 7.22e-05

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: 43.32  E-value: 7.22e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302675238 223 KPPKGVILYGVPGTGKTLLAKAVA---NQTSATFLRIVGSELIQKY-----LGDGPKLV--RELFRVAEE---HAPSIVF 289
Cdd:cd19499   39 RPIGSFLFLGPTGVGKTELAKALAellFGDEDNLIRIDMSEYMEKHsvsrlIGAPPGYVgyTEGGQLTEAvrrKPYSVVL 118

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 302675238 290 IDEIDAVgtkrydstsggEREIQRTMLELLNqlDGF--DTRG---DVK---VIMATNkieSLDPALIrpGRIDRKIEF 359
Cdd:cd19499  119 LDEIEKA-----------HPDVQNLLLQVLD--DGRltDSHGrtvDFKntiIIMTSN---HFRPEFL--NRIDEIVVF 178
RecA-like_superfamily cd01120
RecA-like_NTPases; RecA-like NTPases. This superfamily includes the NTP binding domain of F1 ...
 228-322 1.17e-04

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: 41.72  E-value: 1.17e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302675238 228 VILYGVPGTGKTLLAKAVANQTSATFLRIVGSELIQKYLgdgpklvRELFRVAEEHAPSIVFIDEIDAVGTKRYDSTSGG 307
Cdd:cd01120    1 ILITGPPGSGKTTLLLQFAEQALLSDEPVIFISFLDTIL-------EAIEDLIEEKKLDIIIIDSLSSLARASQGDRSSE 73

                         90
                 ....*....|....*
gi 302675238 308 EREIQRTMLELLNQL 322
Cdd:cd01120   74 LLEDLAKLLRAARNT 88
AAA_3 pfam07726
ATPase family associated with various cellular activities (AAA); This Pfam entry includes some ...
 228-256 1.44e-04

ATPase family associated with various cellular activities (AAA); This Pfam entry includes some of the AAA proteins not detected by the pfam00004 model.


Pssm-ID: 429622 [Multi-domain]  Cd Length: 131  Bit Score: 41.39  E-value: 1.44e-04
                          10        20
                  ....*....|....*....|....*....
gi 302675238  228 VILYGVPGTGKTLLAKAVANQTSATFLRI 256
Cdd:pfam07726   2 VLLEGVPGLAKTLLVRTLARSLGLDFRRI 30
CDC6 COG1474
Cdc6-related protein, AAA superfamily ATPase [Replication, recombination and repair];
197-360 2.55e-04

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


Pssm-ID: 441083 [Multi-domain]  Cd Length: 389  Bit Score: 42.91  E-value: 2.55e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302675238 197 EQQIQEIKESVElPLTHPElyeemgikPPKGVILYGVPGTGKTLLAKAVANQ---------TSATFLRI----------V 257
Cdd:COG1474   32 EEEIEELASALR-PALRGE--------RPSNVLIYGPTGTGKTAVAKYVLEEleeeaeergVDVRVVYVncrqastryrV 102

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302675238 258 GSELIQKyLGDGP----------KLVRELFRVAEEHAPSIVFI-DEIDAVGTKRYDstsggerEIQRTMLELLNQLDGfd 326
Cdd:COG1474  103 LSRILEE-LGSGEdipstglstdELFDRLYEALDERDGVLVVVlDEIDYLVDDEGD-------DLLYQLLRANEELEG-- 172

                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 302675238 327 trGDVKVIMATNKI---ESLDPALIRPGRiDRKIEFP 360
Cdd:COG1474  173 --ARVGVIGISNDLeflENLDPRVKSSLG-EEEIVFP 206
PRK04195 PRK04195
replication factor C large subunit; Provisional
 223-247 4.70e-04

replication factor C large subunit; Provisional


Pssm-ID: 235250 [Multi-domain]  Cd Length: 482  Bit Score: 42.22  E-value: 4.70e-04
                         10        20
                 ....*....|....*....|....*
gi 302675238 223 KPPKGVILYGVPGTGKTLLAKAVAN 247
Cdd:PRK04195  37 KPKKALLLYGPPGVGKTSLAHALAN 61
44 PHA02544
clamp loader, small subunit; Provisional
 229-363 6.55e-04

clamp loader, small subunit; Provisional


Pssm-ID: 222866 [Multi-domain]  Cd Length: 316  Bit Score: 41.51  E-value: 6.55e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302675238 229 ILY-GVPGTGKTLLAKAVANQTSATFLRIVGSEliqkylgDGPKLVR-ELFRVAE----EHAPSIVFIDEIDAVGTKryd 302
Cdd:PHA02544  46 LLHsPSPGTGKTTVAKALCNEVGAEVLFVNGSD-------CRIDFVRnRLTRFAStvslTGGGKVIIIDEFDRLGLA--- 115

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 302675238 303 stsggerEIQRTMLELLNQLDgfdtrGDVKVIMATNKIESLDPALIrpGRIdRKIEFPLPD 363
Cdd:PHA02544 116 -------DAQRHLRSFMEAYS-----KNCSFIITANNKNGIIEPLR--SRC-RVIDFGVPT 161
COG0645 COG0645
Predicted kinase, contains AAA domain [General function prediction only];
228-300 1.37e-03

Predicted kinase, contains AAA domain [General function prediction only];


Pssm-ID: 440410 [Multi-domain]  Cd Length: 164  Bit Score: 39.13  E-value: 1.37e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302675238 228 VILYGVPGTGKTLLAKAVANQTSATFLRI-------VGSEL--IQKYLGDGPKLVRELFRVAEEHA---PSIVfideIDA 295
Cdd:COG0645    2 ILVCGLPGSGKSTLARALAERLGAVRLRSdvvrkrlFGAGLapLERSPEATARTYARLLALARELLaagRSVI----LDA 77


                 ....*
gi 302675238 296 VGTKR 300
Cdd:COG0645   78 TFLRR 82
PRK13341 PRK13341
AAA family ATPase;
229-256 1.56e-03

AAA family ATPase;


Pssm-ID: 237354 [Multi-domain]  Cd Length: 725  Bit Score: 40.81  E-value: 1.56e-03
                         10        20
                 ....*....|....*....|....*...
gi 302675238 229 ILYGVPGTGKTLLAKAVANQTSATFLRI 256
Cdd:PRK13341  56 ILYGPPGVGKTTLARIIANHTRAHFSSL 83
ruvB PRK00080
Holliday junction branch migration DNA helicase RuvB;
228-293 1.77e-03

Holliday junction branch migration DNA helicase RuvB;


Pssm-ID: 234619 [Multi-domain]  Cd Length: 328  Bit Score: 40.11  E-value: 1.77e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 302675238 228 VILYGVPGTGKTLLAKAVANQTSATfLRIVGSELIQKyLGDgpkLVReLFRVAEEHapSIVFIDEI 293
Cdd:PRK00080  54 VLLYGPPGLGKTTLANIIANEMGVN-IRITSGPALEK-PGD---LAA-ILTNLEEG--DVLFIDEI 111
RecA-like_Lon cd19500
lon protease homolog 2 peroxisomal; Lon protease (also known as Lon peptidase) is an ...
 226-319 2.06e-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: 39.08  E-value: 2.06e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302675238 226 KGVIL--YGVPGTGKTLLAKAVANQTSATFLRI-VG-----SELI---QKYLGDGPKLVRELFRVAEEHAPSIVfIDEID 294
Cdd:cd19500   36 KGPILclVGPPGVGKTSLGKSIARALGRKFVRIsLGgvrdeAEIRghrRTYVGAMPGRIIQALKKAGTNNPVFL-LDEID 114

                         90       100
                 ....*....|....*....|....*.
gi 302675238 295 AVGTK-RYDSTSGgereiqrtMLELL 319
Cdd:cd19500  115 KIGSSfRGDPASA--------LLEVL 132
AAA_22 pfam13401
AAA domain;
228-336 2.06e-03

AAA domain;


Pssm-ID: 379165 [Multi-domain]  Cd Length: 129  Bit Score: 38.09  E-value: 2.06e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302675238  228 VILYGVPGTGKTLLAKAVANQ-----------------TSATFLRIVGSELIQKYLGDGPK--LVRELFRVAEEHAPSIV 288
Cdd:pfam13401   8 LVLTGESGTGKTTLLRRLLEQlpevrdsvvfvdlpsgtSPKDLLRALLRALGLPLSGRLSKeeLLAALQQLLLALAVAVV 87

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 302675238  289 F-IDEIDAvgtkrydstsggereIQRTMLELLNQLDGFDTRGdVKVIMA 336
Cdd:pfam13401  88 LiIDEAQH---------------LSLEALEELRDLLNLSSKL-LQLILV 120
Prot_ATP_OB_N pfam17758
Proteasomal ATPase OB N-terminal domain; This is N-terminal oligonucleotide binding (OB) ...
 115-169 2.46e-03

Proteasomal ATPase OB N-terminal domain; This is N-terminal oligonucleotide binding (OB) domain of proteasomal ATPase


Pssm-ID: 436018  Cd Length: 62  Bit Score: 36.37  E-value: 2.46e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 302675238  115 VGTMEEIVDDDHAIISTSSGPEFYVSIMSYVDKDLLEPGCQVLLHHKtQSIVGVL 169
Cdd:pfam17758   2 YGTFLRVDDDDGTADVSVGGRRMRVAVSPTVDASELRPGQQVRLNEA-LVVVGAL 55
COG2842 COG2842
Bacteriophage DNA transposition protein, AAA+ family ATPase [Mobilome: prophages, transposons]; ...
 228-294 3.95e-03

Bacteriophage DNA transposition protein, AAA+ family ATPase [Mobilome: prophages, transposons];


Pssm-ID: 442090 [Multi-domain]  Cd Length: 254  Bit Score: 38.78  E-value: 3.95e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302675238 228 VILYGVPGTGKTLLAKAVANQ-------------TSATFLRIVGSELiqkYLGDGPKLVRELFRVAEEH---APSIVFID 291
Cdd:COG2842   53 GVVYGESGVGKTTAAREYANRnpnviyvtaspswTSKELLEELAEEL---GIPAPPGTIADLRDRILERlagTGRLLIID 129


                 ...
gi 302675238 292 EID 294
Cdd:COG2842  130 EAD 132
PRK08116 PRK08116
hypothetical protein; Validated
 188-267 6.01e-03

hypothetical protein; Validated


Pssm-ID: 236153 [Multi-domain]  Cd Length: 268  Bit Score: 38.46  E-value: 6.01e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302675238 188 ESYADIGGLEQQIQEIKESVELplthpelYEEMGiKPPKGVILYGVPGTGKTLLAKAVANqtsatflrivgsELIQKYLG 267
Cdd:PRK08116  85 ENFLFDKGSEKAYKIARKYVKK-------FEEMK-KENVGLLLWGSVGTGKTYLAACIAN------------ELIEKGVP 144
RecA-like_IQCA1 cd19506
ATPase domain of IQ and AAA domain-containing protein 1 (IQCA1); IQCA1 (also known as dynein ...
 226-292 9.83e-03

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


Pssm-ID: 410914 [Multi-domain]  Cd Length: 160  Bit Score: 36.74  E-value: 9.83e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 302675238 226 KGVILYGVPGTGKTLLAKAVANQTSATFLRIVGSELIQKYLGDG--PKLVRELFRVAEEHAPSIVFIDE 292
Cdd:cd19506   27 KSLLLAGPSGVGKKMLVHAICTETGANLFNLSPSNIAGKYPGKNglQMMLHLVLKVARQLQPSVIWIGD 95
DnaC COG1484
DNA replication protein DnaC [Replication, recombination and repair];
222-248 9.88e-03

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


Pssm-ID: 441093 [Multi-domain]  Cd Length: 242  Bit Score: 37.45  E-value: 9.88e-03
                         10        20
                 ....*....|....*....|....*..
gi 302675238 222 IKPPKGVILYGVPGTGKTLLAKAVANQ 248
Cdd:COG1484   96 IERGENLILLGPPGTGKTHLAIALGHE 122
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

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