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Conserved domains on  [gi|2130390347|gb|KAH7604549|]
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Proteasomal ATPase OB C-terminal domain [[Candida] glabrata]

Protein Classification

26S proteasome regulatory subunit 4( domain architecture ID 1002609)

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

Gene Ontology:  GO:0036402|GO:0016887|GO:0043161|GO:0005524

Graphical summary

 Zoom to residue level

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List of domain hits

 Name Accession Description Interval E-value
PTZ00361 super family cl33178
26 proteosome regulatory subunit 4-like protein; Provisional
 2-433 0e+00

26 proteosome regulatory subunit 4-like protein; Provisional


The actual alignment was detected with superfamily member PTZ00361:

Pssm-ID: 185575 [Multi-domain]  Cd Length: 438  Bit Score: 706.53  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130390347   2 GQGVSQDKKKKKGGKPKYE-PPVQSKFGRKKRKGGPATAEKLPNVVPSTRCKLKLLRMERIKDHLLLEEEFVTNSEILKP 80
Cdd:PTZ00361    6 GQGNNQKDKNKKKEKKKKEsPPPPHEIKRKKKRKGPDAASKLPKVTPNTKCRLRLLKLERIKDYLLLEEEFITNQEAQKP 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130390347  81 FEKKQEEEKKQLEEIRGNPLSIGTLEEIIDDDHAIVTSPTMPDYYVSILSFVDKELLEPGCSVLLHHKTMSIVGVLQDDA 160
Cdd:PTZ00361   86 AQEKNEAELKKVDDLRGSPLSVGTLEEIIDENHAIVSSSVGPEYYVNILSFVDKEQLEPGCSVLLHNKTHSVVGILLDEV 165

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130390347 161 DPMVSVMKIDKSPTESYSDIGGLESQIQEIKESVELPLTHPELYEEMGIKPPKGVILYGAPGTGKTLLAKAVANQTSATF 240
Cdd:PTZ00361  166 DPLVSVMKVDKAPLESYADIGGLEQQIQEIKEAVELPLTHPELYDDIGIKPPKGVILYGPPGTGKTLLAKAVANETSATF 245

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130390347 241 LRIVGSELIQKYLGDGPRLCRQIFKVAAENAPSIVFIDEIDAIGTKRYDSNSGGEREIQRTMLELLNQLDGFDDRGDVKV 320
Cdd:PTZ00361  246 LRVVGSELIQKYLGDGPKLVRELFRVAEENAPSIVFIDEIDAIGTKRYDATSGGEKEIQRTMLELLNQLDGFDSRGDVKV 325

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130390347 321 IMATNKIESLDPALIRPGRIDRKILFENPDLSTKRKILGIHTSKMNLSSDVDLENLVTSKDDLSGADIQAMCTEAGLLAL 400
Cdd:PTZ00361  326 IMATNRIESLDPALIRPGRIDRKIEFPNPDEKTKRRIFEIHTSKMTLAEDVDLEEFIMAKDELSGADIKAICTEAGLLAL 405

                         410       420       430
                  ....*....|....*....|....*....|...
gi 2130390347 401 RERRMQVTAEDFKQAKERVMKNKIEENLEGLYL 433
Cdd:PTZ00361  406 RERRMKVTQADFRKAKEKVLYRKKGNIPEGLYL 438
 
Name Accession Description Interval E-value
PTZ00361 PTZ00361
26 proteosome regulatory subunit 4-like protein; Provisional
 2-433 0e+00

26 proteosome regulatory subunit 4-like protein; Provisional


Pssm-ID: 185575 [Multi-domain]  Cd Length: 438  Bit Score: 706.53  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130390347   2 GQGVSQDKKKKKGGKPKYE-PPVQSKFGRKKRKGGPATAEKLPNVVPSTRCKLKLLRMERIKDHLLLEEEFVTNSEILKP 80
Cdd:PTZ00361    6 GQGNNQKDKNKKKEKKKKEsPPPPHEIKRKKKRKGPDAASKLPKVTPNTKCRLRLLKLERIKDYLLLEEEFITNQEAQKP 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130390347  81 FEKKQEEEKKQLEEIRGNPLSIGTLEEIIDDDHAIVTSPTMPDYYVSILSFVDKELLEPGCSVLLHHKTMSIVGVLQDDA 160
Cdd:PTZ00361   86 AQEKNEAELKKVDDLRGSPLSVGTLEEIIDENHAIVSSSVGPEYYVNILSFVDKEQLEPGCSVLLHNKTHSVVGILLDEV 165

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130390347 161 DPMVSVMKIDKSPTESYSDIGGLESQIQEIKESVELPLTHPELYEEMGIKPPKGVILYGAPGTGKTLLAKAVANQTSATF 240
Cdd:PTZ00361  166 DPLVSVMKVDKAPLESYADIGGLEQQIQEIKEAVELPLTHPELYDDIGIKPPKGVILYGPPGTGKTLLAKAVANETSATF 245

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130390347 241 LRIVGSELIQKYLGDGPRLCRQIFKVAAENAPSIVFIDEIDAIGTKRYDSNSGGEREIQRTMLELLNQLDGFDDRGDVKV 320
Cdd:PTZ00361  246 LRVVGSELIQKYLGDGPKLVRELFRVAEENAPSIVFIDEIDAIGTKRYDATSGGEKEIQRTMLELLNQLDGFDSRGDVKV 325

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130390347 321 IMATNKIESLDPALIRPGRIDRKILFENPDLSTKRKILGIHTSKMNLSSDVDLENLVTSKDDLSGADIQAMCTEAGLLAL 400
Cdd:PTZ00361  326 IMATNRIESLDPALIRPGRIDRKIEFPNPDEKTKRRIFEIHTSKMTLAEDVDLEEFIMAKDELSGADIKAICTEAGLLAL 405

                         410       420       430
                  ....*....|....*....|....*....|...
gi 2130390347 401 RERRMQVTAEDFKQAKERVMKNKIEENLEGLYL 433
Cdd:PTZ00361  406 RERRMKVTQADFRKAKEKVLYRKKGNIPEGLYL 438
RPT1 COG1222
ATP-dependent 26S proteasome regulatory subunit [Posttranslational modification, protein ...
 157-423 4.34e-129

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


Pssm-ID: 440835 [Multi-domain]  Cd Length: 326  Bit Score: 375.50  E-value: 4.34e-129
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130390347 157 QDDADPMVSVMKIDKSPTESYSDIGGLESQIQEIKESVELPLTHPELYEEMGIKPPKGVILYGAPGTGKTLLAKAVANQT 236
Cdd:COG1222    57 QKRLGTPRGTAVPAESPDVTFDDIGGLDEQIEEIREAVELPLKNPELFRKYGIEPPKGVLLYGPPGTGKTLLAKAVAGEL 136

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130390347 237 SATFLRIVGSELIQKYLGDGPRLCRQIFKVAAENAPSIVFIDEIDAIGTKRYDSNSGGerEIQRTMLELLNQLDGFDDRG 316
Cdd:COG1222   137 GAPFIRVRGSELVSKYIGEGARNVREVFELAREKAPSIIFIDEIDAIAARRTDDGTSG--EVQRTVNQLLAELDGFESRG 214

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130390347 317 DVKVIMATNKIESLDPALIRPGRIDRKILFENPDLSTKRKILGIHTSKMNLSSDVDLENLVTSKDDLSGADIQAMCTEAG 396
Cdd:COG1222   215 DVLIIAATNRPDLLDPALLRPGRFDRVIEVPLPDEEAREEILKIHLRDMPLADDVDLDKLAKLTEGFSGADLKAIVTEAG 294

                         250       260
                  ....*....|....*....|....*..
gi 2130390347 397 LLALRERRMQVTAEDFKQAKERVMKNK 423
Cdd:COG1222   295 MFAIREGRDTVTMEDLEKAIEKVKKKT 321
RecA-like_PAN_like cd19502
proteasome activating nucleotidase PAN and related proteasome subunits; This subfamily ...
 176-346 2.53e-109

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: 319.28  E-value: 2.53e-109
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130390347 176 SYSDIGGLESQIQEIKESVELPLTHPELYEEMGIKPPKGVILYGAPGTGKTLLAKAVANQTSATFLRIVGSELIQKYLGD 255
Cdd:cd19502     1 TYEDIGGLDEQIREIREVVELPLKHPELFEELGIEPPKGVLLYGPPGTGKTLLAKAVANHTDATFIRVVGSELVQKYIGE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130390347 256 GPRLCRQIFKVAAENAPSIVFIDEIDAIGTKRYDSNSGGEREIQRTMLELLNQLDGFDDRGDVKVIMATNKIESLDPALI 335
Cdd:cd19502    81 GARLVRELFEMAREKAPSIIFIDEIDAIGAKRFDSGTGGDREVQRTMLELLNQLDGFDPRGNIKVIMATNRPDILDPALL 160

                         170
                  ....*....|.
gi 2130390347 336 RPGRIDRKILF 346
Cdd:cd19502   161 RPGRFDRKIEF 171
FtsH_fam TIGR01241
ATP-dependent metalloprotease FtsH; HflB(FtsH) is a pleiotropic protein required for correct ...
 167-420 1.13e-79

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: 254.52  E-value: 1.13e-79
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130390347 167 MKIDKSPTESYSDIGGLESQIQEIKESVELpLTHPELYEEMGIKPPKGVILYGAPGTGKTLLAKAVANQTSATFLRIVGS 246
Cdd:TIGR01241  44 LLNEEKPKVTFKDVAGIDEAKEELMEIVDF-LKNPSKFTKLGAKIPKGVLLVGPPGTGKTLLAKAVAGEAGVPFFSISGS 122

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130390347 247 ELIQKYLGDGPRLCRQIFKVAAENAPSIVFIDEIDAIGTKRYDSNSGGEREIQRTMLELLNQLDGFDDRGDVKVIMATNK 326
Cdd:TIGR01241 123 DFVEMFVGVGASRVRDLFEQAKKNAPCIIFIDEIDAVGRQRGAGLGGGNDEREQTLNQLLVEMDGFGTNTGVIVIAATNR 202

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130390347 327 IESLDPALIRPGRIDRKILFENPDLSTKRKILGIHTSKMNLSSDVDLENLVTSKDDLSGADIQAMCTEAGLLALRERRMQ 406
Cdd:TIGR01241 203 PDVLDPALLRPGRFDRQVVVDLPDIKGREEILKVHAKNKKLAPDVDLKAVARRTPGFSGADLANLLNEAALLAARKNKTE 282

                         250
                  ....*....|....
gi 2130390347 407 VTAEDFKQAKERVM 420
Cdd:TIGR01241 283 ITMNDIEEAIDRVI 296
AAA pfam00004
ATPase family associated with various cellular activities (AAA); AAA family proteins often ...
 215-347 5.56e-47

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: 157.76  E-value: 5.56e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130390347 215 VILYGAPGTGKTLLAKAVANQTSATFLRIVGSELIQKYLGDGPRLCRQIFKVAAENAPSIVFIDEIDAIGTKRydsNSGG 294
Cdd:pfam00004   1 LLLYGPPGTGKTTLAKAVAKELGAPFIEISGSELVSKYVGESEKRLRELFEAAKKLAPCVIFIDEIDALAGSR---GSGG 77

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 2130390347 295 EREIQRTMLELLNQLDGFDDR-GDVKVIMATNKIESLDPALIrpGRIDRKILFE 347
Cdd:pfam00004  78 DSESRRVVNQLLTELDGFTSSnSKVIVIAATNRPDKLDPALL--GRFDRIIEFP 129
AAA smart00382
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ...
 211-350 1.28e-16

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: 76.64  E-value: 1.28e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130390347  211 PPKGVILYGAPGTGKTLLAKAVANQ---TSATFLRIVGSEL--------------IQKYLGDGPRLCRQIFKVAAENAPS 273
Cdd:smart00382   1 PGEVILIVGPPGSGKTTLARALARElgpPGGGVIYIDGEDIleevldqllliivgGKKASGSGELRLRLALALARKLKPD 80

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2130390347  274 IVFIDEIDAIGTKrydsnsggEREIQRTMLELLNQLDGFDDRGDVKVIMATNKIESLDPALIRPgRIDRKILFENPD 350
Cdd:smart00382  81 VLILDEITSLLDA--------EQEALLLLLEELRLLLLLKSEKNLTVILTTNDEKDLGPALLRR-RFDRRIVLLLIL 148
 
Name Accession Description Interval E-value
PTZ00361 PTZ00361
26 proteosome regulatory subunit 4-like protein; Provisional
 2-433 0e+00

26 proteosome regulatory subunit 4-like protein; Provisional


Pssm-ID: 185575 [Multi-domain]  Cd Length: 438  Bit Score: 706.53  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130390347   2 GQGVSQDKKKKKGGKPKYE-PPVQSKFGRKKRKGGPATAEKLPNVVPSTRCKLKLLRMERIKDHLLLEEEFVTNSEILKP 80
Cdd:PTZ00361    6 GQGNNQKDKNKKKEKKKKEsPPPPHEIKRKKKRKGPDAASKLPKVTPNTKCRLRLLKLERIKDYLLLEEEFITNQEAQKP 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130390347  81 FEKKQEEEKKQLEEIRGNPLSIGTLEEIIDDDHAIVTSPTMPDYYVSILSFVDKELLEPGCSVLLHHKTMSIVGVLQDDA 160
Cdd:PTZ00361   86 AQEKNEAELKKVDDLRGSPLSVGTLEEIIDENHAIVSSSVGPEYYVNILSFVDKEQLEPGCSVLLHNKTHSVVGILLDEV 165

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130390347 161 DPMVSVMKIDKSPTESYSDIGGLESQIQEIKESVELPLTHPELYEEMGIKPPKGVILYGAPGTGKTLLAKAVANQTSATF 240
Cdd:PTZ00361  166 DPLVSVMKVDKAPLESYADIGGLEQQIQEIKEAVELPLTHPELYDDIGIKPPKGVILYGPPGTGKTLLAKAVANETSATF 245

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130390347 241 LRIVGSELIQKYLGDGPRLCRQIFKVAAENAPSIVFIDEIDAIGTKRYDSNSGGEREIQRTMLELLNQLDGFDDRGDVKV 320
Cdd:PTZ00361  246 LRVVGSELIQKYLGDGPKLVRELFRVAEENAPSIVFIDEIDAIGTKRYDATSGGEKEIQRTMLELLNQLDGFDSRGDVKV 325

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130390347 321 IMATNKIESLDPALIRPGRIDRKILFENPDLSTKRKILGIHTSKMNLSSDVDLENLVTSKDDLSGADIQAMCTEAGLLAL 400
Cdd:PTZ00361  326 IMATNRIESLDPALIRPGRIDRKIEFPNPDEKTKRRIFEIHTSKMTLAEDVDLEEFIMAKDELSGADIKAICTEAGLLAL 405

                         410       420       430
                  ....*....|....*....|....*....|...
gi 2130390347 401 RERRMQVTAEDFKQAKERVMKNKIEENLEGLYL 433
Cdd:PTZ00361  406 RERRMKVTQADFRKAKEKVLYRKKGNIPEGLYL 438
PRK03992 PRK03992
proteasome-activating nucleotidase; Provisional
 99-429 1.15e-168

proteasome-activating nucleotidase; Provisional


Pssm-ID: 179699 [Multi-domain]  Cd Length: 389  Bit Score: 478.56  E-value: 1.15e-168
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130390347  99 PLSIGTLEEIIDDDHAIVTSPTMPDYYVSILSFVDKELLEPGCSVLLHHKTMSIVGVLQDDADPMVSVMKIDKSPTESYS 178
Cdd:PRK03992   52 PLIVATVLEVLDDGRVVVKSSGGPQFLVNVSPFIDREKLKPGARVALNQQSLAIVEVLPSEKDPRVQAMEVIESPNVTYE 131

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130390347 179 DIGGLESQIQEIKESVELPLTHPELYEEMGIKPPKGVILYGAPGTGKTLLAKAVANQTSATFLRIVGSELIQKYLGDGPR 258
Cdd:PRK03992  132 DIGGLEEQIREVREAVELPLKKPELFEEVGIEPPKGVLLYGPPGTGKTLLAKAVAHETNATFIRVVGSELVQKFIGEGAR 211

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130390347 259 LCRQIFKVAAENAPSIVFIDEIDAIGTKRYDSNSGGEREIQRTMLELLNQLDGFDDRGDVKVIMATNKIESLDPALIRPG 338
Cdd:PRK03992  212 LVRELFELAREKAPSIIFIDEIDAIAAKRTDSGTSGDREVQRTLMQLLAEMDGFDPRGNVKIIAATNRIDILDPAILRPG 291

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130390347 339 RIDRKILFENPDLSTKRKILGIHTSKMNLSSDVDLENLVTSKDDLSGADIQAMCTEAGLLALRERRMQVTAEDFKQAKER 418
Cdd:PRK03992  292 RFDRIIEVPLPDEEGRLEILKIHTRKMNLADDVDLEELAELTEGASGADLKAICTEAGMFAIRDDRTEVTMEDFLKAIEK 371

                         330
                  ....*....|.
gi 2130390347 419 VMKNKIEENLE 429
Cdd:PRK03992  372 VMGKEEKDSME 382
PTZ00454 PTZ00454
26S protease regulatory subunit 6B-like protein; Provisional
 53-426 4.05e-154

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


Pssm-ID: 240423 [Multi-domain]  Cd Length: 398  Bit Score: 441.89  E-value: 4.05e-154
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130390347  53 LKLLRMERIKDHLLLEEEFVTNSEilKPFEKKQEEEKKQLEEIRGNPLSIGTLEEIIDDDHAIVTSPTMPDYYVSILSFV 132
Cdd:PTZ00454   22 EKLKELEKELEFLDIQEEYIKEEQ--KNLKRELIRAKEEVKRIQSVPLVIGQFLEMIDSNYGIVSSTSGSNYYVRILSTL 99

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130390347 133 DKELLEPGCSVLLHHKTMSIVGVLQDDADPMVSVMKIDKSPTESYSDIGGLESQIQEIKESVELPLTHPELYEEMGIKPP 212
Cdd:PTZ00454  100 NRELLKPNASVALHRHSHAVVDILPPEADSSIQLLQMSEKPDVTYSDIGGLDIQKQEIREAVELPLTCPELYEQIGIDPP 179

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130390347 213 KGVILYGAPGTGKTLLAKAVANQTSATFLRIVGSELIQKYLGDGPRLCRQIFKVAAENAPSIVFIDEIDAIGTKRYDSNS 292
Cdd:PTZ00454  180 RGVLLYGPPGTGKTMLAKAVAHHTTATFIRVVGSEFVQKYLGEGPRMVRDVFRLARENAPSIIFIDEVDSIATKRFDAQT 259

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130390347 293 GGEREIQRTMLELLNQLDGFDDRGDVKVIMATNKIESLDPALIRPGRIDRKILFENPDLSTKRKILGIHTSKMNLSSDVD 372
Cdd:PTZ00454  260 GADREVQRILLELLNQMDGFDQTTNVKVIMATNRADTLDPALLRPGRLDRKIEFPLPDRRQKRLIFQTITSKMNLSEEVD 339

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....
gi 2130390347 373 LENLVTSKDDLSGADIQAMCTEAGLLALRERRMQVTAEDFKQAKERVMKNKIEE 426
Cdd:PTZ00454  340 LEDFVSRPEKISAADIAAICQEAGMQAVRKNRYVILPKDFEKGYKTVVRKTDRD 393
RPT1 COG1222
ATP-dependent 26S proteasome regulatory subunit [Posttranslational modification, protein ...
 157-423 4.34e-129

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


Pssm-ID: 440835 [Multi-domain]  Cd Length: 326  Bit Score: 375.50  E-value: 4.34e-129
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130390347 157 QDDADPMVSVMKIDKSPTESYSDIGGLESQIQEIKESVELPLTHPELYEEMGIKPPKGVILYGAPGTGKTLLAKAVANQT 236
Cdd:COG1222    57 QKRLGTPRGTAVPAESPDVTFDDIGGLDEQIEEIREAVELPLKNPELFRKYGIEPPKGVLLYGPPGTGKTLLAKAVAGEL 136

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130390347 237 SATFLRIVGSELIQKYLGDGPRLCRQIFKVAAENAPSIVFIDEIDAIGTKRYDSNSGGerEIQRTMLELLNQLDGFDDRG 316
Cdd:COG1222   137 GAPFIRVRGSELVSKYIGEGARNVREVFELAREKAPSIIFIDEIDAIAARRTDDGTSG--EVQRTVNQLLAELDGFESRG 214

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130390347 317 DVKVIMATNKIESLDPALIRPGRIDRKILFENPDLSTKRKILGIHTSKMNLSSDVDLENLVTSKDDLSGADIQAMCTEAG 396
Cdd:COG1222   215 DVLIIAATNRPDLLDPALLRPGRFDRVIEVPLPDEEAREEILKIHLRDMPLADDVDLDKLAKLTEGFSGADLKAIVTEAG 294

                         250       260
                  ....*....|....*....|....*..
gi 2130390347 397 LLALRERRMQVTAEDFKQAKERVMKNK 423
Cdd:COG1222   295 MFAIREGRDTVTMEDLEKAIEKVKKKT 321
RecA-like_PAN_like cd19502
proteasome activating nucleotidase PAN and related proteasome subunits; This subfamily ...
 176-346 2.53e-109

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: 319.28  E-value: 2.53e-109
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130390347 176 SYSDIGGLESQIQEIKESVELPLTHPELYEEMGIKPPKGVILYGAPGTGKTLLAKAVANQTSATFLRIVGSELIQKYLGD 255
Cdd:cd19502     1 TYEDIGGLDEQIREIREVVELPLKHPELFEELGIEPPKGVLLYGPPGTGKTLLAKAVANHTDATFIRVVGSELVQKYIGE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130390347 256 GPRLCRQIFKVAAENAPSIVFIDEIDAIGTKRYDSNSGGEREIQRTMLELLNQLDGFDDRGDVKVIMATNKIESLDPALI 335
Cdd:cd19502    81 GARLVRELFEMAREKAPSIIFIDEIDAIGAKRFDSGTGGDREVQRTMLELLNQLDGFDPRGNIKVIMATNRPDILDPALL 160

                         170
                  ....*....|.
gi 2130390347 336 RPGRIDRKILF 346
Cdd:cd19502   161 RPGRFDRKIEF 171
FtsH_fam TIGR01241
ATP-dependent metalloprotease FtsH; HflB(FtsH) is a pleiotropic protein required for correct ...
 167-420 1.13e-79

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: 254.52  E-value: 1.13e-79
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130390347 167 MKIDKSPTESYSDIGGLESQIQEIKESVELpLTHPELYEEMGIKPPKGVILYGAPGTGKTLLAKAVANQTSATFLRIVGS 246
Cdd:TIGR01241  44 LLNEEKPKVTFKDVAGIDEAKEELMEIVDF-LKNPSKFTKLGAKIPKGVLLVGPPGTGKTLLAKAVAGEAGVPFFSISGS 122

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130390347 247 ELIQKYLGDGPRLCRQIFKVAAENAPSIVFIDEIDAIGTKRYDSNSGGEREIQRTMLELLNQLDGFDDRGDVKVIMATNK 326
Cdd:TIGR01241 123 DFVEMFVGVGASRVRDLFEQAKKNAPCIIFIDEIDAVGRQRGAGLGGGNDEREQTLNQLLVEMDGFGTNTGVIVIAATNR 202

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130390347 327 IESLDPALIRPGRIDRKILFENPDLSTKRKILGIHTSKMNLSSDVDLENLVTSKDDLSGADIQAMCTEAGLLALRERRMQ 406
Cdd:TIGR01241 203 PDVLDPALLRPGRFDRQVVVDLPDIKGREEILKVHAKNKKLAPDVDLKAVARRTPGFSGADLANLLNEAALLAARKNKTE 282

                         250
                  ....*....|....
gi 2130390347 407 VTAEDFKQAKERVM 420
Cdd:TIGR01241 283 ITMNDIEEAIDRVI 296
SpoVK COG0464
AAA+-type ATPase, SpoVK/Ycf46/Vps4 family [Cell wall/membrane/envelope biogenesis, Cell cycle ...
 177-419 2.03e-76

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


Pssm-ID: 440232 [Multi-domain]  Cd Length: 397  Bit Score: 243.28  E-value: 2.03e-76
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130390347 177 YSDIGGLESQIQEIKESVELPLTHPELYEEMGIKPPKGVILYGAPGTGKTLLAKAVANQTSATFLRIVGSELIQKYLGDG 256
Cdd:COG0464   156 LDDLGGLEEVKEELRELVALPLKRPELREEYGLPPPRGLLLYGPPGTGKTLLARALAGELGLPLIEVDLSDLVSKYVGET 235

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130390347 257 PRLCRQIFKVAAENAPSIVFIDEIDAIGTKRYDSNSG-GEREIQrtmlELLNQLDGFddRGDVKVIMATNKIESLDPALI 335
Cdd:COG0464   236 EKNLREVFDKARGLAPCVLFIDEADALAGKRGEVGDGvGRRVVN----TLLTEMEEL--RSDVVVIAATNRPDLLDPALL 309

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130390347 336 RpgRIDRKILFENPDLSTKRKILGIHTSKMNLSSDVDLENLVTSKDDLSGADIQAMCTEAGLLALRERRMQVTAEDFKQA 415
Cdd:COG0464   310 R--RFDEIIFFPLPDAEERLEIFRIHLRKRPLDEDVDLEELAEATEGLSGADIRNVVRRAALQALRLGREPVTTEDLLEA 387


                  ....
gi 2130390347 416 KERV 419
Cdd:COG0464   388 LERE 391
CDC48 TIGR01243
AAA family ATPase, CDC48 subfamily; This subfamily of the AAA family ATPases includes two ...
 164-428 3.69e-76

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: 251.36  E-value: 3.69e-76
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130390347 164 VSVMKIDKSPTESYSDIGGLESQIQEIKESVELPLTHPELYEEMGIKPPKGVILYGAPGTGKTLLAKAVANQTSATFLRI 243
Cdd:TIGR01243 164 VREEIERKVPKVTYEDIGGLKEAKEKIREMVELPMKHPELFEHLGIEPPKGVLLYGPPGTGKTLLAKAVANEAGAYFISI 243

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130390347 244 VGSELIQKYLGDGPRLCRQIFKVAAENAPSIVFIDEIDAIGTKRYDSNsgGEREiQRTMLELLNQLDGFDDRGDVKVIMA 323
Cdd:TIGR01243 244 NGPEIMSKYYGESEERLREIFKEAEENAPSIIFIDEIDAIAPKREEVT--GEVE-KRVVAQLLTLMDGLKGRGRVIVIGA 320

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130390347 324 TNKIESLDPALIRPGRIDRKILFENPDLSTKRKILGIHTSKMNLSSDVDLENLVTSKDDLSGADIQAMCTEAGLLALRE- 402
Cdd:TIGR01243 321 TNRPDALDPALRRPGRFDREIVIRVPDKRARKEILKVHTRNMPLAEDVDLDKLAEVTHGFVGADLAALAKEAAMAALRRf 400

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....
gi 2130390347 403 ------------------RRMQVTAEDFKQAKERVMKNKIEENL 428
Cdd:TIGR01243 401 iregkinfeaeeipaevlKELKVTMKDFMEALKMVEPSAIREVL 444
CDC48 TIGR01243
AAA family ATPase, CDC48 subfamily; This subfamily of the AAA family ATPases includes two ...
 173-422 8.55e-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: 245.20  E-value: 8.55e-74
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130390347 173 PTESYSDIGGLESQIQEIKESVELPLTHPELYEEMGIKPPKGVILYGAPGTGKTLLAKAVANQTSATFLRIVGSELIQKY 252
Cdd:TIGR01243 448 PNVRWSDIGGLEEVKQELREAVEWPLKHPEIFEKMGIRPPKGVLLFGPPGTGKTLLAKAVATESGANFIAVRGPEILSKW 527

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130390347 253 LGDGPRLCRQIFKVAAENAPSIVFIDEIDAIGTKRydSNSGGEREIQRTMLELLNQLDGFDDRGDVKVIMATNKIESLDP 332
Cdd:TIGR01243 528 VGESEKAIREIFRKARQAAPAIIFFDEIDAIAPAR--GARFDTSVTDRIVNQLLTEMDGIQELSNVVVIAATNRPDILDP 605

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130390347 333 ALIRPGRIDRKILFENPDLSTKRKILGIHTSKMNLSSDVDLENLVTSKDDLSGADIQAMCTEAGLLALRERRMQVTAEDF 412
Cdd:TIGR01243 606 ALLRPGRFDRLILVPPPDEEARKEIFKIHTRSMPLAEDVDLEELAEMTEGYTGADIEAVCREAAMAALRESIGSPAKEKL 685

                         250
                  ....*....|
gi 2130390347 413 KQAKERVMKN 422
Cdd:TIGR01243 686 EVGEEEFLKD 695
HflB COG0465
ATP-dependent Zn proteases [Posttranslational modification, protein turnover, chaperones];
170-420 9.93e-72

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


Pssm-ID: 440233 [Multi-domain]  Cd Length: 583  Bit Score: 236.09  E-value: 9.93e-72
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130390347 170 DKSPTESYSDIGGLESQIQEIKESVELpLTHPELYEEMGIKPPKGVILYGAPGTGKTLLAKAVANQTSATFLRIVGSELI 249
Cdd:COG0465   134 EDKPKVTFDDVAGVDEAKEELQEIVDF-LKDPEKFTRLGAKIPKGVLLVGPPGTGKTLLAKAVAGEAGVPFFSISGSDFV 212

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130390347 250 QKYLGDGPRLCRQIFKVAAENAPSIVFIDEIDAIGTKRyDSNSGG---EREiqRTmlelLNQL----DGFDDRGDVKVIM 322
Cdd:COG0465   213 EMFVGVGASRVRDLFEQAKKNAPCIIFIDEIDAVGRQR-GAGLGGghdERE--QT----LNQLlvemDGFEGNEGVIVIA 285

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130390347 323 ATNKIESLDPALIRPGRIDRKILFENPDLSTKRKILGIHTSKMNLSSDVDLENLVTSKDDLSGADIQAMCTEAGLLALRE 402
Cdd:COG0465   286 ATNRPDVLDPALLRPGRFDRQVVVDLPDVKGREAILKVHARKKPLAPDVDLEVIARRTPGFSGADLANLVNEAALLAARR 365

                         250
                  ....*....|....*...
gi 2130390347 403 RRMQVTAEDFKQAKERVM 420
Cdd:COG0465   366 NKKAVTMEDFEEAIDRVI 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 ...
 179-346 1.35e-66

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: 209.84  E-value: 1.35e-66
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130390347 179 DIGGLESQIQEIKESVELPLTHPELYEEMGIKPPKGVILYGAPGTGKTLLAKAVANQTSATFLRIVGSELIQKYLGDGPR 258
Cdd:cd19503     1 DIGGLDEQIASLKELIELPLKYPELFRALGLKPPRGVLLHGPPGTGKTLLARAVANEAGANFLSISGPSIVSKYLGESEK 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130390347 259 LCRQIFKVAAENAPSIVFIDEIDAIGTKRYDSNSGGEReiqRTMLELLNQLDGFDDRGDVKVIMATNKIESLDPALIRPG 338
Cdd:cd19503    81 NLREIFEEARSHAPSIIFIDEIDALAPKREEDQREVER---RVVAQLLTLMDGMSSRGKVVVIAATNRPDAIDPALRRPG 157


                  ....*...
gi 2130390347 339 RIDRKILF 346
Cdd:cd19503   158 RFDREVEI 165
RecA-like_CDC48_r1-like cd19519
first of two ATPase domains of CDC48 and similar ATPase domains; CDC48 in yeast and p97 or VCP ...
 179-344 7.53e-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: 205.36  E-value: 7.53e-65
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130390347 179 DIGGLESQIQEIKESVELPLTHPELYEEMGIKPPKGVILYGAPGTGKTLLAKAVANQTSATFLRIVGSELIQKYLGDGPR 258
Cdd:cd19519     1 DIGGCRKQLAQIREMVELPLRHPELFKAIGIKPPRGILLYGPPGTGKTLIARAVANETGAFFFLINGPEIMSKLAGESES 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130390347 259 LCRQIFKVAAENAPSIVFIDEIDAIGTKRYDSNSGGEReiqRTMLELLNQLDGFDDRGDVKVIMATNKIESLDPALIRPG 338
Cdd:cd19519    81 NLRKAFEEAEKNAPAIIFIDEIDAIAPKREKTHGEVER---RIVSQLLTLMDGLKQRAHVIVMAATNRPNSIDPALRRFG 157


                  ....*.
gi 2130390347 339 RIDRKI 344
Cdd:cd19519   158 RFDREI 163
ftsH CHL00176
cell division protein; Validated
 176-419 3.29e-64

cell division protein; Validated


Pssm-ID: 214386 [Multi-domain]  Cd Length: 638  Bit Score: 217.61  E-value: 3.29e-64
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130390347 176 SYSDIGGLESQIQEIKESVELpLTHPELYEEMGIKPPKGVILYGAPGTGKTLLAKAVANQTSATFLRIVGSELIQKYLGD 255
Cdd:CHL00176  181 TFRDIAGIEEAKEEFEEVVSF-LKKPERFTAVGAKIPKGVLLVGPPGTGKTLLAKAIAGEAEVPFFSISGSEFVEMFVGV 259

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130390347 256 GPRLCRQIFKVAAENAPSIVFIDEIDAIGTKRYDSNSGGEREIQRTMLELLNQLDGFDDRGDVKVIMATNKIESLDPALI 335
Cdd:CHL00176  260 GAARVRDLFKKAKENSPCIVFIDEIDAVGRQRGAGIGGGNDEREQTLNQLLTEMDGFKGNKGVIVIAATNRVDILDAALL 339

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130390347 336 RPGRIDRKILFENPDLSTKRKILGIHTSKMNLSSDVDLENLVTSKDDLSGADIQAMCTEAGLLALRERRMQVTAEDFKQA 415
Cdd:CHL00176  340 RPGRFDRQITVSLPDREGRLDILKVHARNKKLSPDVSLELIARRTPGFSGADLANLLNEAAILTARRKKATITMKEIDTA 419


                  ....
gi 2130390347 416 KERV 419
Cdd:CHL00176  420 IDRV 423
RecA-like_FtsH cd19501
ATP-dependent zinc metalloprotease FtsH; FtsH ATPase is a processive, ATP-dependent zinc ...
 176-344 4.63e-63

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: 200.92  E-value: 4.63e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130390347 176 SYSDIGGLESQIQEIKESVELpLTHPELYEEMGIKPPKGVILYGAPGTGKTLLAKAVANQTSATFLRIVGSELIQKYLGD 255
Cdd:cd19501     2 TFKDVAGCEEAKEELKEVVEF-LKNPEKFTKLGAKIPKGVLLVGPPGTGKTLLAKAVAGEAGVPFFSISGSDFVEMFVGV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130390347 256 GPRLCRQIFKVAAENAPSIVFIDEIDAIGTKRYDSNSGGEREIQRTMLELLNQLDGFDDRGDVKVIMATNKIESLDPALI 335
Cdd:cd19501    81 GASRVRDLFEQAKKNAPCIVFIDEIDAVGRKRGAGLGGGHDEREQTLNQLLVEMDGFESNTGVIVIAATNRPDVLDPALL 160


                  ....*....
gi 2130390347 336 RPGRIDRKI 344
Cdd:cd19501   161 RPGRFDRQV 169
RecA-like_CDC48_r2-like cd19511
second of two ATPase domains of CDC48/p97, PEX1 and -6, VAT and NVL, and similar ATPase ...
 188-344 3.58e-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: 3.58e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130390347 188 QEIKESVELPLTHPELYEEMGIKPPKGVILYGAPGTGKTLLAKAVANQTSATFLRIVGSELIQKYLGDGPRLCRQIFKVA 267
Cdd:cd19511     3 RELKEAVEWPLKHPDAFKRLGIRPPKGVLLYGPPGCGKTLLAKALASEAGLNFISVKGPELFSKYVGESERAVREIFQKA 82

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2130390347 268 AENAPSIVFIDEIDAIGTKRYDSNSGGEREiqRTMLELLNQLDGFDDRGDVKVIMATNKIESLDPALIRPGRIDRKI 344
Cdd:cd19511    83 RQAAPCIIFFDEIDSLAPRRGQSDSSGVTD--RVVSQLLTELDGIESLKGVVVIAATNRPDMIDPALLRPGRLDKLI 157
hflB PRK10733
ATP-dependent zinc metalloprotease FtsH;
176-420 2.00e-57

ATP-dependent zinc metalloprotease FtsH;


Pssm-ID: 182683 [Multi-domain]  Cd Length: 644  Bit Score: 199.49  E-value: 2.00e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130390347 176 SYSDIGGLESQIQEIKESVELpLTHPELYEEMGIKPPKGVILYGAPGTGKTLLAKAVANQTSATFLRIVGSELIQKYLGD 255
Cdd:PRK10733  150 TFADVAGCDEAKEEVAELVEY-LREPSRFQKLGGKIPKGVLMVGPPGTGKTLLAKAIAGEAKVPFFTISGSDFVEMFVGV 228

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130390347 256 GPRLCRQIFKVAAENAPSIVFIDEIDAIGTKRYDSNSGGEREIQRTMLELLNQLDGFDDRGDVKVIMATNKIESLDPALI 335
Cdd:PRK10733  229 GASRVRDMFEQAKKAAPCIIFIDEIDAVGRQRGAGLGGGHDEREQTLNQMLVEMDGFEGNEGIIVIAATNRPDVLDPALL 308

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130390347 336 RPGRIDRKILFENPDLSTKRKILGIHTSKMNLSSDVDLENLVTSKDDLSGADIQAMCTEAGLLALRERRMQVTAEDFKQA 415
Cdd:PRK10733  309 RPGRFDRQVVVGLPDVRGREQILKVHMRRVPLAPDIDAAIIARGTPGFSGADLANLVNEAALFAARGNKRVVSMVEFEKA 388


                  ....*
gi 2130390347 416 KERVM 420
Cdd:PRK10733  389 KDKIM 393
RecA-like_VCP_r2 cd19529
second of two ATPase domains of Valosin-containing protein-like ATPase (VAT) and similar ...
 188-345 7.39e-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: 184.62  E-value: 7.39e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130390347 188 QEIKESVELPLTHPELYEEMGIKPPKGVILYGAPGTGKTLLAKAVANQTSATFLRIVGSELIQKYLGDGPRLCRQIFKVA 267
Cdd:cd19529     3 QELKEAVEWPLLKPEVFKRLGIRPPKGILLYGPPGTGKTLLAKAVATESNANFISVKGPELLSKWVGESEKAIREIFRKA 82

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2130390347 268 AENAPSIVFIDEIDAIGTKRYDSNSGGEREiqRTMLELLNQLDGFDDRGDVKVIMATNKIESLDPALIRPGRIDRKIL 345
Cdd:cd19529    83 RQVAPCVIFFDEIDSIAPRRGTTGDSGVTE--RVVNQLLTELDGLEEMNGVVVIAATNRPDIIDPALLRAGRFDRLIY 158
RecA-like_protease cd19481
proteases similar to RecA; RecA-like NTPases. This family includes the NTP binding domain of ...
 186-346 3.92e-54

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: 177.47  E-value: 3.92e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130390347 186 QIQEIKESVELPLTHPELyEEMGIKPPKGVILYGAPGTGKTLLAKAVANQTSATFLRIVGSELIQKYLGDGPRLCRQIFK 265
Cdd:cd19481     1 LKASLREAVEAPRRGSRL-RRYGLGLPKGILLYGPPGTGKTLLAKALAGELGLPLIVVKLSSLLSKYVGESEKNLRKIFE 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130390347 266 VAAENAPSIVFIDEIDAIGTKRydSNSGGEREIQRTMLELLNQLDGFDDRGDVKVIMATNKIESLDPALIRPGRIDRKIL 345
Cdd:cd19481    80 RARRLAPCILFIDEIDAIGRKR--DSSGESGELRRVLNQLLTELDGVNSRSKVLVIAATNRPDLLDPALLRPGRFDEVIE 157


                  .
gi 2130390347 346 F 346
Cdd:cd19481   158 F 158
COG1223 COG1223
Predicted ATPase, AAA+ superfamily [General function prediction only];
178-430 3.34e-49

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


Pssm-ID: 440836 [Multi-domain]  Cd Length: 246  Bit Score: 167.75  E-value: 3.34e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130390347 178 SDIGGLESQIQEIKEsVELPLTHPELYEEMGIKPPKGVILYGAPGTGKTLLAKAVANQTSATFLRIVGSELIQKYLGDGP 257
Cdd:COG1223     2 DDVVGQEEAKKKLKL-IIKELRRRENLRKFGLWPPRKILFYGPPGTGKTMLAEALAGELKLPLLTVRLDSLIGSYLGETA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130390347 258 RLCRQIFKvAAENAPSIVFIDEIDAIGTKRYDSNSGGerEIQRTMLELLNQLDGFddRGDVKVIMATNKIESLDPALIRp 337
Cdd:COG1223    81 RNLRKLFD-FARRAPCVIFFDEFDAIAKDRGDQNDVG--EVKRVVNALLQELDGL--PSGSVVIAATNHPELLDSALWR- 154

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130390347 338 gRIDRKILFENPDLSTKRKILGIHTSKMNLSSDVDLENLVTSKDDLSGADIQAMCTEAGLLALRERRMQVTAEDFKQAKE 417
Cdd:COG1223   155 -RFDEVIEFPLPDKEERKEILELNLKKFPLPFELDLKKLAKKLEGLSGADIEKVLKTALKKAILEDREKVTKEDLEEALK 233

                         250
                  ....*....|...
gi 2130390347 418 RVMKNKIEENLEG 430
Cdd:COG1223   234 QRKERKKEPKKEG 246
RecA-like_CDC48_r2-like cd19528
second of two ATPase domains of CDC48 and similar ATPase domains; CDC48 in yeast and p97 or ...
 188-344 3.70e-48

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: 161.91  E-value: 3.70e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130390347 188 QEIKESVELPLTHPELYEEMGIKPPKGVILYGAPGTGKTLLAKAVANQTSATFLRIVGSELIQKYLGDGPRLCRQIFKVA 267
Cdd:cd19528     3 RELQELVQYPVEHPDKFLKFGMTPSKGVLFYGPPGCGKTLLAKAIANECQANFISVKGPELLTMWFGESEANVRDIFDKA 82

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2130390347 268 AENAPSIVFIDEIDAIGTKRYDSNSGGEREIQRTMLELLNQLDGFDDRGDVKVIMATNKIESLDPALIRPGRIDRKI 344
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 ...
 180-345 2.64e-47

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: 159.83  E-value: 2.64e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130390347 180 IGGLESQIQEIKESVELPLTHPELYEeMGIKPPKGVILYGAPGTGKTLLAKAVANQTSATFLRIVGSELIQKYLGDGPRL 259
Cdd:cd19509     1 IAGLDDAKEALKEAVILPSLRPDLFP-GLRGPPRGILLYGPPGTGKTLLARAVASESGSTFFSISASSLVSKWVGESEKI 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130390347 260 CRQIFKVAAENAPSIVFIDEIDAIGTKRYDSNSGGEREIqRTmlELLNQLDGF--DDRGDVKVIMATNKIESLDPALIRp 337
Cdd:cd19509    80 VRALFALARELQPSIIFIDEIDSLLSERGSGEHEASRRV-KT--EFLVQMDGVlnKPEDRVLVLGATNRPWELDEAFLR- 155


                  ....*...
gi 2130390347 338 gRIDRKIL 345
Cdd:cd19509   156 -RFEKRIY 162
AAA pfam00004
ATPase family associated with various cellular activities (AAA); AAA family proteins often ...
 215-347 5.56e-47

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: 157.76  E-value: 5.56e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130390347 215 VILYGAPGTGKTLLAKAVANQTSATFLRIVGSELIQKYLGDGPRLCRQIFKVAAENAPSIVFIDEIDAIGTKRydsNSGG 294
Cdd:pfam00004   1 LLLYGPPGTGKTTLAKAVAKELGAPFIEISGSELVSKYVGESEKRLRELFEAAKKLAPCVIFIDEIDALAGSR---GSGG 77

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 2130390347 295 EREIQRTMLELLNQLDGFDDR-GDVKVIMATNKIESLDPALIrpGRIDRKILFE 347
Cdd:pfam00004  78 DSESRRVVNQLLTELDGFTSSnSKVIVIAATNRPDKLDPALL--GRFDRIIEFP 129
RecA-like_Yta7-like cd19517
ATPase domain of Saccharomyces cerevisiae Yta7 and similar ATPase domains; Saccharomyces ...
 179-346 7.62e-47

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: 158.83  E-value: 7.62e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130390347 179 DIGGLESQIQEIKESVELPLTHPELYEEMGIKPPKGVILYGAPGTGKTLLAKAVANQTS------ATFLRiVGSELIQKY 252
Cdd:cd19517     1 DIGGLSHYINQLKEMVFFPLLYPEVFAKFKITPPRGVLFHGPPGTGKTLMARALAAECSkggqkvSFFMR-KGADCLSKW 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130390347 253 LGDGPRLCRQIFKVAAENAPSIVFIDEIDAIGTKRYDSNSGGEREIQRTMLELlnqLDGFDDRGDVKVIMATNKIESLDP 332
Cdd:cd19517    80 VGEAERQLRLLFEEAYRMQPSIIFFDEIDGLAPVRSSKQEQIHASIVSTLLAL---MDGLDNRGQVVVIGATNRPDALDP 156

                         170
                  ....*....|....
gi 2130390347 333 ALIRPGRIDRKILF 346
Cdd:cd19517   157 ALRRPGRFDREFYF 170
RecA-like_NVL_r2-like cd19530
second of two ATPase domains of NVL (nuclear VCP-like protein) and similar ATPase domains; NVL ...
 183-346 1.96e-46

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: 157.65  E-value: 1.96e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130390347 183 LESQIQEIKESVELPLTHPELYEEMGIKPPKGVILYGAPGTGKTLLAKAVANQTSATFLRIVGSELIQKYLGDGPRLCRQ 262
Cdd:cd19530     1 LDHVREELTMSILRPIKRPDIYKALGIDLPTGVLLYGPPGCGKTLLAKAVANESGANFISVKGPELLNKYVGESERAVRQ 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130390347 263 IFKVAAENAPSIVFIDEIDAIGTKRYDSNSGGereIQRTMLELLNQLDGFDDRGDVKVIMATNKIESLDPALIRPGRIDr 342
Cdd:cd19530    81 VFQRARASAPCVIFFDEVDALVPKRGDGGSWA---SERVVNQLLTEMDGLEERSNVFVIAATNRPDIIDPAMLRPGRLD- 156


                  ....
gi 2130390347 343 KILF 346
Cdd:cd19530   157 KTLY 160
RecA-like_NVL_r1-like cd19518
first of two ATPase domains of NVL (nuclear VCP-like protein) and similar ATPase domains; NVL ...
 179-344 3.44e-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: 154.48  E-value: 3.44e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130390347 179 DIGGLESQIQEIKESVELPLTHPELYEEMGIKPPKGVILYGAPGTGKTLLAKAVANQTSATFLRIVGSELIQKYLGDGPR 258
Cdd:cd19518     1 DIGGMDSTLKELCELLIHPILPPEYFQHLGVEPPRGVLLHGPPGCGKTMLANAIAGELKVPFLKISATEIVSGVSGESEE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130390347 259 LCRQIFKVAAENAPSIVFIDEIDAIGTKRydsnSGGEREIQRTML-ELLNQLDGF----DDRGDVKVIMATNKIESLDPA 333
Cdd:cd19518    81 KIRELFDQAISNAPCIVFIDEIDAITPKR----ESAQREMERRIVsQLLTCMDELnnekTAGGPVLVIGATNRPDSLDPA 156

                         170
                  ....*....|.
gi 2130390347 334 LIRPGRIDRKI 344
Cdd:cd19518   157 LRRAGRFDREI 167
RecA-like_ATAD1 cd19520
ATPase domain of ATPase family AAA domain-containing protein 1 and similar ATPase domains; ...
 179-336 2.69e-40

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: 141.41  E-value: 2.69e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130390347 179 DIGGLESQIQEIKESVELPLTHPELYEEMGI-KPPKGVILYGAPGTGKTLLAKAVANQTSATFLRIVGSELIQKYLGDGP 257
Cdd:cd19520     1 DIGGLDEVITELKELVILPLQRPELFDNSRLlQPPKGVLLYGPPGCGKTMLAKATAKEAGARFINLQVSSLTDKWYGESQ 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130390347 258 RLCRQIFKVAAENAPSIVFIDEIDAIGTKRydsnSGGEREIQRTM-LELLNQLDGF--DDRGDVKVIMATNKIESLDPAL 334
Cdd:cd19520    81 KLVAAVFSLASKLQPSIIFIDEIDSFLRQR----SSTDHEATAMMkAEFMSLWDGLstDGNCRVIVMGATNRPQDLDEAI 156


                  ..
gi 2130390347 335 IR 336
Cdd:cd19520   157 LR 158
RecA-like_VPS4 cd19521
ATPase domain of vacuolar protein sorting-associated protein 4; Vacuolar protein ...
 173-344 6.89e-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: 6.89e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130390347 173 PTESYSDIGGLESQIQEIKESVELPLTHPELYEEmGIKPPKGVILYGAPGTGKTLLAKAVANQTSATFLRIVGSELIQKY 252
Cdd:cd19521     2 PNVKWEDVAGLEGAKEALKEAVILPVKFPHLFTG-NRKPWSGILLYGPPGTGKSYLAKAVATEANSTFFSVSSSDLVSKW 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130390347 253 LGDGPRLCRQIFKVAAENAPSIVFIDEIDAIGTKRYDSNSGGEREIQRtmlELLNQLDGF-DDRGDVKVIMATNKIESLD 331
Cdd:cd19521    81 MGESEKLVKQLFAMARENKPSIIFIDEVDSLCGTRGEGESEASRRIKT---ELLVQMNGVgNDSQGVLVLGATNIPWQLD 157

                         170
                  ....*....|...
gi 2130390347 332 PALIRpgRIDRKI 344
Cdd:cd19521   158 SAIRR--RFEKRI 168
RecA-like_PEX6_r2 cd19527
second of two ATPase domains of Peroxisomal biogenesis factor 6 (PEX6); PEX6(also known as ...
 189-342 2.56e-39

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: 138.80  E-value: 2.56e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130390347 189 EIKESVELPLTHPELYEEmGIKPPKGVILYGAPGTGKTLLAKAVANQTSATFLRIVGSELIQKYLGDGPRLCRQIFKVAA 268
Cdd:cd19527     4 EILDTIQLPLEHPELFSS-GLRKRSGILLYGPPGTGKTLLAKAIATECSLNFLSVKGPELINMYIGESEANVREVFQKAR 82

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2130390347 269 ENAPSIVFIDEIDAIGTKRYDS-NSGGerEIQRTMLELLNQLDGFDDRG-DVKVIMATNKIESLDPALIRPGRIDR 342
Cdd:cd19527    83 DAKPCVIFFDELDSLAPSRGNSgDSGG--VMDRVVSQLLAELDGMSSSGqDVFVIGATNRPDLLDPALLRPGRFDK 156
RecA-like_PEX1_r2 cd19526
second of two ATPase domains of Peroxisomal biogenesis factor 1 (PEX1); PEX1(also known as ...
 190-345 7.53e-38

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: 134.86  E-value: 7.53e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130390347 190 IKESVELPLTHPELYEEMGIKPPKGVILYGAPGTGKTLLAKAVANQTSATFLRIVGSELIQKYLGDGPRLCRQIFKVAAE 269
Cdd:cd19526     5 LEETIEWPSKYPKIFASSPLRLRSGILLYGPPGCGKTLLASAIASECGLNFISVKGPELLNKYIGASEQNVRDLFSRAQS 84

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2130390347 270 NAPSIVFIDEIDAIGTKRYDSNSGgerEIQRTMLELLNQLDGFDDRGDVKVIMATNKIESLDPALIRPGRIDRKIL 345
Cdd:cd19526    85 AKPCILFFDEFDSIAPKRGHDSTG---VTDRVVNQLLTQLDGVEGLDGVYVLAATSRPDLIDPALLRPGRLDKLVY 157
RecA-like_spastin cd19524
ATPase domain of spastin; Spastin is an ATP-dependent microtubule-severing protein involved in ...
 179-336 1.66e-37

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: 134.21  E-value: 1.66e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130390347 179 DIGGLESQIQEIKESVELPLTHPELYeeMGIK-PPKGVILYGAPGTGKTLLAKAVANQTSATFLRIVGSELIQKYLGDGP 257
Cdd:cd19524     1 DIAGQDLAKQALQEMVILPSLRPELF--TGLRaPARGLLLFGPPGNGKTMLAKAVAAESNATFFNISAASLTSKYVGEGE 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130390347 258 RLCRQIFKVAAENAPSIVFIDEIDAIGTKRYDSNSGGEReiqRTMLELLNQLDGFDDRGD--VKVIMATNKIESLDPALI 335
Cdd:cd19524    79 KLVRALFAVARELQPSIIFIDEVDSLLSERSEGEHEASR---RLKTEFLIEFDGVQSNGDdrVLVMGATNRPQELDDAVL 155


                  .
gi 2130390347 336 R 336
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; ...
 169-336 4.11e-37

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: 133.96  E-value: 4.11e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130390347 169 IDKSPTESYSDIGGLESQIQEIKESVELPLTHPELYeeMGIK-PPKGVILYGAPGTGKTLLAKAVANQTSATFLRIVGSE 247
Cdd:cd19525    13 MDHGPPINWADIAGLEFAKKTIKEIVVWPMLRPDIF--TGLRgPPKGILLFGPPGTGKTLIGKCIASQSGATFFSISASS 90

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130390347 248 LIQKYLGDGPRLCRQIFKVAAENAPSIVFIDEIDAIGTKRYDSNSGGEREIQRtmlELLNQLDGF----DDRgdVKVIMA 323
Cdd:cd19525    91 LTSKWVGEGEKMVRALFSVARCKQPAVIFIDEIDSLLSQRGEGEHESSRRIKT---EFLVQLDGAttssEDR--ILVVGA 165

                         170
                  ....*....|...
gi 2130390347 324 TNKIESLDPALIR 336
Cdd:cd19525   166 TNRPQEIDEAARR 178
RecA-like_KTNA1 cd19522
Katanin p60 ATPase-containing subunit A1; Katanin p60 ATPase-containing subunit A1 (KTNA1) is ...
 179-344 4.68e-35

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: 127.79  E-value: 4.68e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130390347 179 DIGGLESQIQEIKESVELPLTHPELYEemGIKPP-KGVILYGAPGTGKTLLAKAVANQTSATFLRIVGSELIQKYLGDGP 257
Cdd:cd19522     1 DIADLEEAKKLLEEAVVLPMWMPEFFK--GIRRPwKGVLMVGPPGTGKTLLAKAVATECGTTFFNVSSSTLTSKYRGESE 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130390347 258 RLCRQIFKVAAENAPSIVFIDEIDAIGTKRydsNSGGEREI-QRTMLELLNQLDGF-------DDRGDVKVIMATNKIES 329
Cdd:cd19522    79 KLVRLLFEMARFYAPTTIFIDEIDSICSRR---GTSEEHEAsRRVKSELLVQMDGVggasendDPSKMVMVLAATNFPWD 155

                         170
                  ....*....|....*
gi 2130390347 330 LDPALIRpgRIDRKI 344
Cdd:cd19522   156 IDEALRR--RLEKRI 168
RecA-like_fidgetin cd19523
ATPase domain of fidgetin; Fidgetin (FIGN) is a ATP-dependent microtubule severing protein. ...
 179-336 3.68e-28

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: 109.20  E-value: 3.68e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130390347 179 DIGGLESQIQEIKESVELPLTHPELYEEMgIKPPKGVILYGAPGTGKTLLAKAVANQTSATFLRIVGSELIQKYLGDGPR 258
Cdd:cd19523     1 DIAGLGALKAAIKEEVLWPLLRPDAFSGL-LRLPRSILLFGPRGTGKTLLGRCLASQLGATFLRLRGSTLVAKWAGEGEK 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130390347 259 LCRQIFKVAAENAPSIVFIDEIDAIGTKRYDsnsgGEREIQRTMLELLNQLDGFDDRGD--VKVIMATNKIESLDPALIR 336
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; ...
 180-344 5.89e-25

first of two ATPase domains of NSF and SEC18, and similar ATPase domains; N-ethylmaleimide-sensitive factor (NSF) and Saccharomyces cerevisiae Vesicular-fusion protein Sec18, key factors for eukaryotic trafficking, are ATPases and SNARE disassembly chaperones. NSF/Sec18 activate or prime SNAREs, the terminal catalysts of membrane fusion. Sec18/NSF associates with SNARE complexes through binding Sec17/alpha-SNAP. Sec18 has an N-terminal cap domain and two nucleotide-binding domains (D1 and D2) which form the two rings of the hexameric complex. The hydrolysis of ATP by D1 generates most of the energy necessary to disassemble inactive SNARE bundles, while the D2 ring binds ATP to stabilize the homohexamer. This subfamily includes the first (D1) ATPase domain of NSF/Sec18, and belongs to the RecA-like NTPase family which includes the NTP binding domain of F1 and V1 H(+)ATPases, DnaB and related helicases as well as bacterial RecA and related eukaryotic and archaeal recombinases. The RecA-like NTPase family also includes bacterial conjugation proteins and related DNA transfer proteins involved in type II and type IV secretion.


Pssm-ID: 410912 [Multi-domain]  Cd Length: 177  Bit Score: 100.64  E-value: 5.89e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130390347 180 IGGLESQIQEI-KESVELPLTHPELYEEMGIKPPKGVILYGAPGTGKTLLAKAVANQTSATFLRIV-GSELIQKYLGDGP 257
Cdd:cd19504     2 IGGLDKEFSDIfRRAFASRVFPPEIVEQLGCKHVKGILLYGPPGTGKTLMARQIGKMLNAREPKIVnGPEILNKYVGESE 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130390347 258 RLCRQIFKVA--------AENAPSIVFIDEIDAIGTKRyDSNSGGEREIQRTMLELLNQLDGFDDRGDVKVIMATNKIES 329
Cdd:cd19504    82 ANIRKLFADAeeeqrrlgANSGLHIIIFDEIDAICKQR-GSMAGSTGVHDTVVNQLLSKIDGVEQLNNILVIGMTNRKDL 160

                         170
                  ....*....|....*
gi 2130390347 330 LDPALIRPGRIDRKI 344
Cdd:cd19504   161 IDEALLRPGRLEVQM 175
AAA cd00009
The AAA+ (ATPases Associated with a wide variety of cellular Activities) superfamily ...
 181-347 8.05e-25

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


Pssm-ID: 99707 [Multi-domain]  Cd Length: 151  Bit Score: 99.53  E-value: 8.05e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130390347 181 GGLESQIQEIKESVELPlthpelyeemgikPPKGVILYGAPGTGKTLLAKAVANQT---SATFLRIVGSELIQKYLG--- 254
Cdd:cd00009     1 VGQEEAIEALREALELP-------------PPKNLLLYGPPGTGKTTLARAIANELfrpGAPFLYLNASDLLEGLVVael 67

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130390347 255 DGPRLCRQIFKVAAENAPSIVFIDEIDAIGtkrydsnsggeREIQRTMLELLNQL-DGFDDRGDVKVIMATNKIESLDPA 333
Cdd:cd00009    68 FGHFLVRLLFELAEKAKPGVLFIDEIDSLS-----------RGAQNALLRVLETLnDLRIDRENVRVIGATNRPLLGDLD 136

                         170
                  ....*....|....
gi 2130390347 334 LIRPGRIDRKILFE 347
Cdd:cd00009   137 RALYDRLDIRIVIP 150
ycf46 CHL00195
Ycf46; Provisional
 172-426 1.27e-22

Ycf46; Provisional


Pssm-ID: 177094 [Multi-domain]  Cd Length: 489  Bit Score: 99.71  E-value: 1.27e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130390347 172 SPTESYSDIGGLESQIQEIKESVElplTHPELYEEMGIKPPKGVILYGAPGTGKTLLAKAVANQTSATFLRIVGSELIQK 251
Cdd:CHL00195  222 SVNEKISDIGGLDNLKDWLKKRST---SFSKQASNYGLPTPRGLLLVGIQGTGKSLTAKAIANDWQLPLLRLDVGKLFGG 298

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130390347 252 YLGDGPRLCRQIFKVAAENAPSIVFIDEIDAIGTKRYDSN-SGGEREIQRTMLELLNQldgfdDRGDVKVIMATNKIESL 330
Cdd:CHL00195  299 IVGESESRMRQMIRIAEALSPCILWIDEIDKAFSNSESKGdSGTTNRVLATFITWLSE-----KKSPVFVVATANNIDLL 373

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130390347 331 DPALIRPGRIDrKILFEN-PDLSTKRKILGIHTSKMNLSS--DVDLENLVTSKDDLSGADIQAMCTEAGLLALRERRmQV 407
Cdd:CHL00195  374 PLEILRKGRFD-EIFFLDlPSLEEREKIFKIHLQKFRPKSwkKYDIKKLSKLSNKFSGAEIEQSIIEAMYIAFYEKR-EF 451

                         250       260
                  ....*....|....*....|....*
gi 2130390347 408 TAEDFKQAKERVM------KNKIEE 426
Cdd:CHL00195  452 TTDDILLALKQFIplaqteKEQIEA 476
RecA-like_Ycf46-like cd19507
ATPase domain of Ycf46 and similar ATPase domains; Ycf46 may play a role in the regulation of ...
 208-346 4.74e-22

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: 92.05  E-value: 4.74e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130390347 208 GIKPPKGVILYGAPGTGKTLLAKAVANQTSATFLRIVGSELIQKYLGDGPRLCRQIFKVAAENAPSIVFIDEID-AIGTK 286
Cdd:cd19507    27 GLPTPKGLLLVGIQGTGKSLTAKAIAGVWQLPLLRLDMGRLFGGLVGESESRLRQMIQTAEAIAPCVLWIDEIEkGFSNA 106

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130390347 287 RYDSNSGGEREIQRTMLELLNQldgfdDRGDVKVIMATNKIESLDPALIRPGRIDRkILF 346
Cdd:cd19507   107 DSKGDSGTSSRVLGTFLTWLQE-----KKKPVFVVATANNVQSLPPELLRKGRFDE-IFF 160
RecA-like_BCS1 cd19510
Mitochondrial chaperone BCS1; Mitochondrial chaperone BCS1 is necessary for the assembly of ...
 190-346 3.64e-20

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


Pssm-ID: 410918 [Multi-domain]  Cd Length: 153  Bit Score: 86.64  E-value: 3.64e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130390347 190 IKESVELPLTHPELYEEMGIKPPKGVILYGAPGTGKTLLAKAVANqtsatFLR--IVGSELIQKYLGDgpRLCRQIFKVA 267
Cdd:cd19510     1 IIDDLKDFIKNEDWYNDRGIPYRRGYLLYGPPGTGKSSFIAALAG-----ELDydICDLNLSEVVLTD--DRLNHLLNTA 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130390347 268 AENapSIVFIDEIDA-----IGTKRYDSNSGGEREIqrTMLELLNQLDGFDDRGDVKVIMATNKIESLDPALIRPGRIDR 342
Cdd:cd19510    74 PKQ--SIILLEDIDAafesrEHNKKNPSAYGGLSRV--TFSGLLNALDGVASSEERIVFMTTNHIERLDPALIRPGRVDM 149


                  ....
gi 2130390347 343 KILF 346
Cdd:cd19510   150 KIYM 153
AAA smart00382
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ...
 211-350 1.28e-16

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: 76.64  E-value: 1.28e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130390347  211 PPKGVILYGAPGTGKTLLAKAVANQ---TSATFLRIVGSEL--------------IQKYLGDGPRLCRQIFKVAAENAPS 273
Cdd:smart00382   1 PGEVILIVGPPGSGKTTLARALARElgpPGGGVIYIDGEDIleevldqllliivgGKKASGSGELRLRLALALARKLKPD 80

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2130390347  274 IVFIDEIDAIGTKrydsnsggEREIQRTMLELLNQLDGFDDRGDVKVIMATNKIESLDPALIRPgRIDRKILFENPD 350
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 ...
 215-335 8.44e-12

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: 64.00  E-value: 8.44e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130390347 215 VILYGAPGTGKTLLAKAVANQTS---------ATFLRIVGSELIQKYLGDGPRLCRQIFK-----VAAENAPSIVFIDEI 280
Cdd:cd19508    55 VLLHGPPGTGKTSLCKALAQKLSirlssryryGQLIEINSHSLFSKWFSESGKLVTKMFQkiqelIDDKDALVFVLIDEV 134

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 2130390347 281 DAIGTKRYDSNSGGE-REIQRTMLELLNQLDGFDDRGDVKVIMATNKIESLDPALI 335
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 ...
 370-414 1.96e-11

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: 58.70  E-value: 1.96e-11
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 2130390347 370 DVDLENLVTSKDDLSGADIQAMCTEAGLLALRERRMQVTAEDFKQ 414
Cdd:pfam17862   1 DVDLEELAERTEGFSGADLEALCREAALAALRRGLEAVTQEDLEE 45
Prot_ATP_ID_OB pfam16450
Proteasomal ATPase OB C-terminal domain; This is the interdomain (ID) or oligonucleotide ...
 102-156 2.02e-10

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: 55.98  E-value: 2.02e-10
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 2130390347 102 IGTLEEIIDDDHAIVTSPTMPDYYVSILSFVDKELLEPGCSVLLHHKTMSIVGVL 156
Cdd:pfam16450   1 VATVVEVLDDGRALVKSSGGEERVVRLAGSLDEEKLRPGDRVLLDPRSGYALEVL 55
CDC6 COG1474
Cdc6-related protein, AAA superfamily ATPase [Replication, recombination and repair];
184-431 8.06e-08

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


Pssm-ID: 441083 [Multi-domain]  Cd Length: 389  Bit Score: 54.08  E-value: 8.06e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130390347 184 ESQIQEIKESVElPLTHPElyeemgikPPKGVILYGAPGTGKTLLAKAVANQ---------TSATFLRI----------V 244
Cdd:COG1474    32 EEEIEELASALR-PALRGE--------RPSNVLIYGPTGTGKTAVAKYVLEEleeeaeergVDVRVVYVncrqastryrV 102

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130390347 245 GSELIQKyLGDGP----------RLCRQIFKVAAENAPSIVFI-DEIDAIGTKRYDsnsggereiqrtmlELLNQL---D 310
Cdd:COG1474   103 LSRILEE-LGSGEdipstglstdELFDRLYEALDERDGVLVVVlDEIDYLVDDEGD--------------DLLYQLlraN 167

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130390347 311 GFDDRGDVKVIMATNKI---ESLDPALIRPGRiDRKILFENPDLSTKRKILGiHTSKMNLSSDV---DLENLVTskdDLS 384
Cdd:COG1474   168 EELEGARVGVIGISNDLeflENLDPRVKSSLG-EEEIVFPPYDADELRDILE-DRAELAFYDGVlsdEVIPLIA---ALA 242

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....
gi 2130390347 385 GAD-------IQAMcTEAGLLALRERRMQVTAEDFKQAKERVMKNKIEENLEGL 431
Cdd:COG1474   243 AQEhgdarkaIDLL-RVAGEIAEREGSDRVTEEHVREAREKIERDRLLEVLRGL 295
RarA COG2256
Replication-associated recombination protein RarA (DNA-dependent ATPase) [Replication, ...
 215-280 1.00e-07

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


Pssm-ID: 441857 [Multi-domain]  Cd Length: 439  Bit Score: 53.91  E-value: 1.00e-07
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2130390347 215 VILYGAPGTGKTLLAKAVANQTSATFLRI--VGS---ELiqkylgdgprlcRQIFKVAAENA----PSIVFIDEI 280
Cdd:COG2256    52 MILWGPPGTGKTTLARLIANATDAEFVALsaVTSgvkDI------------REVIEEARERRaygrRTILFVDEI 114
RecA-like_ATAD3-like cd19512
ATPase domains of ATPase AAA-domain protein 3A (ATAD3A), -3B, and -3C, and similar ATPase ...
 213-346 1.03e-07

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: 50.99  E-value: 1.03e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130390347 213 KGVILYGAPGTGKTLLAKAVANQTSATFLRIVGSELIQkyLG-DGPRLCRQIFKVA-AENAPSIVFIDEIDAIGTKRyds 290
Cdd:cd19512    23 RNILFYGPPGTGKTLFAKKLALHSGMDYAIMTGGDVAP--MGrEGVTAIHKVFDWAnTSRRGLLLFVDEADAFLRKR--- 97

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 2130390347 291 NSGGEREIQRTMLELLNQLDGfDDRGDVKVIMATNKIESLDPALirPGRIDRKILF 346
Cdd:cd19512    98 STEKISEDLRAALNAFLYRTG-EQSNKFMLVLASNQPEQFDWAI--NDRIDEMVEF 150
RecA-like_Ycf2 cd19505
ATPase domain of plant YCF2; Ycf2 is a chloroplast ATPase which has an essential function; ...
 206-344 1.25e-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: 50.84  E-value: 1.25e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130390347 206 EMGIKPPKGVILYGAPGTGKTLLAKAVANQTSATFLRIVGSELIQ---KYLGDGPRLCRQI-----------FKVAAENA 271
Cdd:cd19505     6 RLGLSPSKGILLIGSIETGRSYLIKSLAANSYVPLIRISLNKLLYnkpDFGNDDWIDGMLIlkeslhrlnlqFELAKAMS 85

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2130390347 272 PSIVFIDEIDAIGTKRYDSNSGGEReiqRTMLELLNQLDGFDDRGDVK----VIMATNKIESLDPALIRPGRIDRKI 344
Cdd:cd19505    86 PCIIWIPNIHELNVNRSTQNLEEDP---KLLLGLLLNYLSRDFEKSSTrnilVIASTHIPQKVDPALIAPNRLDTCI 159
PRK13342 PRK13342
recombination factor protein RarA; Reviewed
 215-280 2.08e-07

recombination factor protein RarA; Reviewed


Pssm-ID: 237355 [Multi-domain]  Cd Length: 413  Bit Score: 52.78  E-value: 2.08e-07
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2130390347 215 VILYGAPGTGKTLLAKAVANQTSATFLRI--VGS---ELiqkylgdgprlcRQIFKVAAENAPS----IVFIDEI 280
Cdd:PRK13342   39 MILWGPPGTGKTTLARIIAGATDAPFEALsaVTSgvkDL------------REVIEEARQRRSAgrrtILFIDEI 101
TIGR02928 TIGR02928
orc1/cdc6 family replication initiation protein; Members of this protein family are found ...
 165-431 4.60e-07

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: 51.48  E-value: 4.60e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130390347 165 SVMKIDKSPtesySDIGGLESQIQEIKEsvelplthpELYEEMGIKPPKGVILYGAPGTGKTLLAKAVANQ----TSATF 240
Cdd:TIGR02928   6 DLLEPDYVP----DRIVHRDEQIEELAK---------ALRPILRGSRPSNVFIYGKTGTGKTAVTKYVMKEleeaAEDRD 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130390347 241 LRI---------------VGSELIQKYLGDGP----------RLCRQIFKVAAENAPSIVFI-DEIDAIgtkrydSNSGG 294
Cdd:TIGR02928  73 VRVvtvyvncqildtlyqVLVELANQLRGSGEevpttglstsEVFRRLYKELNERGDSLIIVlDEIDYL------VGDDD 146

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130390347 295 EREIQRTMLELLNQLDGfddrGDVKVIMATNKI---ESLDPAlIRPGRIDRKILFENPDLSTKRKILGiHTSKMNLSSDV 371
Cdd:TIGR02928 147 DLLYQLSRARSNGDLDN----AKVGVIGISNDLkfrENLDPR-VKSSLCEEEIIFPPYDAEELRDILE-NRAEKAFYDGV 220

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2130390347 372 ---DLENLVTSKDDLSGADI-QAMCT--EAGLLALRERRMQVTAEDFKQAKERVMKNKIEENLEGL 431
Cdd:TIGR02928 221 lddGVIPLCAALAAQEHGDArKAIDLlrVAGEIAEREGAERVTEDHVEKAQEKIEKDRLLELIRGL 286
AAA_5 pfam07728
AAA domain (dynein-related subfamily); This Pfam entry includes some of the AAA proteins not ...
 214-336 1.37e-06

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


Pssm-ID: 400191 [Multi-domain]  Cd Length: 135  Bit Score: 47.29  E-value: 1.37e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130390347 214 GVILYGAPGTGKTLLAKAVANQTS-ATFLRIVGS------ELIQKYL--GDGPRLCRQIFKVAAENApSIVFIDEIDAIg 284
Cdd:pfam07728   1 GVLLVGPPGTGKTELAERLAAALSnRPVFYVQLTrdtteeDLFGRRNidPGGASWVDGPLVRAAREG-EIAVLDEINRA- 78

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2130390347 285 tkrydsnsggEREIQRTMLELLN-----QLDGF----DDRGDVKVIMATN----KIESLDPALIR 336
Cdd:pfam07728  79 ----------NPDVLNSLLSLLDerrllLPDGGelvkAAPDGFRLIATMNpldrGLNELSPALRS 133
DUF815 pfam05673
Protein of unknown function (DUF815); This family consists of several bacterial proteins of ...
 178-278 3.13e-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: 48.30  E-value: 3.13e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130390347 178 SDIGGLESQIQEIKESVELPLTHpelyeemgiKPPKGVILYGAPGTGKTLLAKAVANQTSATFLRIVgsELIQKYLGDGP 257
Cdd:pfam05673  28 DDLVGIERQKEALIRNTRRFLAG---------LPANNVLLWGARGTGKSSLVKALLNEYADQGLRLI--EVDKEDLGDLP 96

                          90       100
                  ....*....|....*....|.
gi 2130390347 258 RLCRQIfkvAAENAPSIVFID 278
Cdd:pfam05673  97 DLVDLL---RDRPYRFILFCD 114
MoxR COG0714
MoxR-like ATPase [General function prediction only]; MoxR-like ATPase is part of the Pathway ...
 215-281 1.18e-05

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: 46.70  E-value: 1.18e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130390347 215 VILYGAPGTGKTLLAKAVANQTSATFLRI-----------VGSELIQKYLGD-----GPrlcrqIFKvaaenapSIVFID 278
Cdd:COG0714    34 LLLEGVPGVGKTTLAKALARALGLPFIRIqftpdllpsdiLGTYIYDQQTGEfefrpGP-----LFA-------NVLLAD 101


                  ...
gi 2130390347 279 EID 281
Cdd:COG0714   102 EIN 104
McrB COG1401
5-methylcytosine-specific restriction endonuclease McrBC, GTP-binding regulatory subunit McrB ...
 209-280 1.44e-05

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


Pssm-ID: 441011 [Multi-domain]  Cd Length: 477  Bit Score: 47.07  E-value: 1.44e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130390347 209 IKPPKGVILYGAPGTGKTLLAKAVANQTSAT---FLRIV-------GSELIQKY----------LGDGP--RLCRQifkv 266
Cdd:COG1401   218 LKTKKNVILAGPPGTGKTYLARRLAEALGGEdngRIEFVqfhpswsYEDFLLGYrpsldegkyePTPGIflRFCLK---- 293

                          90
                  ....*....|....*.
gi 2130390347 267 AAEN--APSIVFIDEI 280
Cdd:COG1401   294 AEKNpdKPYVLIIDEI 309
PRK04195 PRK04195
replication factor C large subunit; Provisional
 210-298 1.97e-05

replication factor C large subunit; Provisional


Pssm-ID: 235250 [Multi-domain]  Cd Length: 482  Bit Score: 46.84  E-value: 1.97e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130390347 210 KPPKGVILYGAPGTGKTLLAKAVAN-------------QTSATFL-RIVGSELIQKYLGDGPRlcrqifkvaaenapSIV 275
Cdd:PRK04195   37 KPKKALLLYGPPGVGKTSLAHALANdygwevielnasdQRTADVIeRVAGEAATSGSLFGARR--------------KLI 102

                          90       100
                  ....*....|....*....|...
gi 2130390347 276 FIDEIDAIgTKRYDsnSGGEREI 298
Cdd:PRK04195  103 LLDEVDGI-HGNED--RGGARAI 122
RecA-like_HslU cd19498
ATP-dependent protease ATPase subunit HslU; HslU is a component of the ATP-dependent protease ...
 212-306 3.15e-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: 44.29  E-value: 3.15e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130390347 212 PKGVILYGAPGTGKTLLAKAVANQTSATFLRIVGSELIQ-KYLGdgprlcRQIFKVAAENAPSIVFIDEIDAIGTKRYDS 290
Cdd:cd19498    46 PKNILMIGPTGVGKTEIARRLAKLAGAPFIKVEATKFTEvGYVG------RDVESIIRDLVEGIVFIDEIDKIAKRGGSS 119

                          90
                  ....*....|....*..
gi 2130390347 291 NSGGERE-IQRTMLELL 306
Cdd:cd19498   120 GPDVSREgVQRDLLPIV 136
AAA_2 pfam07724
AAA domain (Cdc48 subfamily); This Pfam entry includes some of the AAA proteins not detected ...
 212-306 5.48e-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: 43.34  E-value: 5.48e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130390347 212 PKGVILY-GAPGTGKTLLAKAVANQ---TSATFLRIVGSELIQKYL--------------GDGPRLCRQIFKvaaeNAPS 273
Cdd:pfam07724   2 PIGSFLFlGPTGVGKTELAKALAELlfgDERALIRIDMSEYMEEHSvsrligappgyvgyEEGGQLTEAVRR----KPYS 77

                          90       100       110
                  ....*....|....*....|....*....|...
gi 2130390347 274 IVFIDEIDAIGtkrydsnsggeREIQRTMLELL 306
Cdd:pfam07724  78 IVLIDEIEKAH-----------PGVQNDLLQIL 99
RecA-like_ClpB_Hsp104-like cd19499
Chaperone protein ClpB/Hsp104 subfamily; Bacterial Caseinolytic peptidase B (ClpB) and ...
 210-346 5.93e-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: 5.93e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130390347 210 KPPKGVILYGAPGTGKTLLAKAVA---NQTSATFLRIVGSELIQKYlgDGPRLCR------------QIFKVAAENAPSI 274
Cdd:cd19499    39 RPIGSFLFLGPTGVGKTELAKALAellFGDEDNLIRIDMSEYMEKH--SVSRLIGappgyvgyteggQLTEAVRRKPYSV 116

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130390347 275 VFIDEIDAigtkrydsnsgGEREIQRTMLELLNqlDGF--DDRG---DVK---VIMATNkieSLDPALIrpGRIDRKILF 346
Cdd:cd19499   117 VLLDEIEK-----------AHPDVQNLLLQVLD--DGRltDSHGrtvDFKntiIIMTSN---HFRPEFL--NRIDEIVVF 178
RecA-like_Lon cd19500
lon protease homolog 2 peroxisomal; Lon protease (also known as Lon peptidase) is an ...
 213-334 1.46e-04

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: 42.55  E-value: 1.46e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130390347 213 KGVIL--YGAPGTGKTLLAKAVANQTSATFLRI-VG-----SELI---QKYLGDGPRLCRQIFKVAAENAPSIVfIDEID 281
Cdd:cd19500    36 KGPILclVGPPGVGKTSLGKSIARALGRKFVRIsLGgvrdeAEIRghrRTYVGAMPGRIIQALKKAGTNNPVFL-LDEID 114

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2130390347 282 AIGTK-RYDSNSGgereiqrtMLELLN--QLDGFDDR--------GDVKVIMATNKIESLDPAL 334
Cdd:cd19500   115 KIGSSfRGDPASA--------LLEVLDpeQNSTFSDHyldvpfdlSKVLFIATANSLDTIPGPL 170
T7SS_EccA TIGR03922
type VII secretion AAA-ATPase EccA; This model represents the AAA family ATPase, EccA, of the ...
 182-347 3.15e-04

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: 42.91  E-value: 3.15e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130390347 182 GLES---QIQEIKESVELPLTHpelyEEMGIKPP---KGVILYGAPGTGKTLLAKAVANQTSA-TFLR------IVGSEL 248
Cdd:TIGR03922 280 GLERvkrQVAALKSSTAMALAR----AERGLPVAqtsNHMLFAGPPGTGKTTIARVVAKIYCGlGVLRkplvreVSRADL 355

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130390347 249 IQKYLGDGPRLCRQIFKVAAEnapSIVFIDEIDAIGTKRYDSNSGGEREIQRTMLELLNqldgfDDRGDVKVIMA----- 323
Cdd:TIGR03922 356 IGQYIGESEAKTNEIIDSALG---GVLFLDEAYTLVETGYGQKDPFGLEAIDTLLARME-----NDRDRLVVIGAgyrkd 427

                         170       180
                  ....*....|....*....|....
gi 2130390347 324 TNKIESLDPALirPGRIDRKILFE 347
Cdd:TIGR03922 428 LDKFLEVNEGL--RSRFTRVIEFP 449
RecA-like_superfamily cd01120
RecA-like_NTPases; RecA-like NTPases. This superfamily includes the NTP binding domain of F1 ...
 215-309 3.44e-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: 40.18  E-value: 3.44e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130390347 215 VILYGAPGTGKTLLAKAVANQTSATFLRIVGSELIQKYLgdgprlcRQIFKVAAENAPSIVFIDEIDAIGTKRYDSNSGG 294
Cdd:cd01120     1 ILITGPPGSGKTTLLLQFAEQALLSDEPVIFISFLDTIL-------EAIEDLIEEKKLDIIIIDSLSSLARASQGDRSSE 73

                          90
                  ....*....|....*
gi 2130390347 295 EREIQRTMLELLNQL 309
Cdd:cd01120    74 LLEDLAKLLRAARNT 88
PRK13341 PRK13341
AAA family ATPase;
216-387 3.55e-04

AAA family ATPase;


Pssm-ID: 237354 [Multi-domain]  Cd Length: 725  Bit Score: 43.12  E-value: 3.55e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130390347 216 ILYGAPGTGKTLLAKAVANQTSATFLRIVG-----SELiqkylgdgprlcRQIFKVAAE-----NAPSIVFIDEIdaigt 285
Cdd:PRK13341   56 ILYGPPGVGKTTLARIIANHTRAHFSSLNAvlagvKDL------------RAEVDRAKErlerhGKRTILFIDEV----- 118

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130390347 286 KRYDSNSggereiQRTMLELLnqldgfdDRGDVKVIMAT--NKIESLDPALIRPGRIDRKILFENPDL------STKRKI 357
Cdd:PRK13341  119 HRFNKAQ------QDALLPWV-------ENGTITLIGATteNPYFEVNKALVSRSRLFRLKSLSDEDLhqllkrALQDKE 185

                         170       180       190
                  ....*....|....*....|....*....|
gi 2130390347 358 LGIHTSKMNLSSDVdLENLVtskdDLSGAD 387
Cdd:PRK13341  186 RGYGDRKVDLEPEA-EKHLV----DVANGD 210
44 PHA02544
clamp loader, small subunit; Provisional
 216-334 3.59e-04

clamp loader, small subunit; Provisional


Pssm-ID: 222866 [Multi-domain]  Cd Length: 316  Bit Score: 42.28  E-value: 3.59e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130390347 216 ILY-GAPGTGKTLLAKAVANQTSATFLRIVGSEL-IQKYLGDGPRLCRQifkVAAENAPSIVFIDEIDAIGTKrydsnsg 293
Cdd:PHA02544   46 LLHsPSPGTGKTTVAKALCNEVGAEVLFVNGSDCrIDFVRNRLTRFAST---VSLTGGGKVIIIDEFDRLGLA------- 115

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 2130390347 294 gerEIQRTMLELLNQLDgfddrGDVKVIMATNKIESLDPAL 334
Cdd:PHA02544  116 ---DAQRHLRSFMEAYS-----KNCSFIITANNKNGIIEPL 148
DnaC COG1484
DNA replication protein DnaC [Replication, recombination and repair];
209-235 7.17e-04

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


Pssm-ID: 441093 [Multi-domain]  Cd Length: 242  Bit Score: 40.92  E-value: 7.17e-04
                          10        20
                  ....*....|....*....|....*..
gi 2130390347 209 IKPPKGVILYGAPGTGKTLLAKAVANQ 235
Cdd:COG1484    96 IERGENLILLGPPGTGKTHLAIALGHE 122
ruvB PRK00080
Holliday junction branch migration DNA helicase RuvB;
215-280 1.16e-03

Holliday junction branch migration DNA helicase RuvB;


Pssm-ID: 234619 [Multi-domain]  Cd Length: 328  Bit Score: 40.88  E-value: 1.16e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2130390347 215 VILYGAPGTGKTLLAKAVANQTSATfLRIVGSELIQKyLGDgprlcrqifkVAA------ENapSIVFIDEI 280
Cdd:PRK00080   54 VLLYGPPGLGKTTLANIIANEMGVN-IRITSGPALEK-PGD----------LAAiltnleEG--DVLFIDEI 111
RecA-like_ClpX cd19497
ATP-dependent Clp protease ATP-binding subunit ClpX; ClpX is a component of the ATP-dependent ...
 215-286 1.50e-03

ATP-dependent Clp protease ATP-binding subunit ClpX; ClpX is a component of the ATP-dependent protease ClpXP. In ClpXP, ClpX ATPase serves to specifically recognize, unfold, and translocate protein substrates into the chamber of ClpP protease for degradation. This RecA-like_ClpX domain subfamily belongs to the RecA-like NTPase family which includes the NTP binding domain of F1 and V1 H(+)ATPases, DnaB and related helicases as well as bacterial RecA and related eukaryotic and archaeal recombinases. The RecA-like NTPase family also includes bacterial conjugation proteins and related DNA transfer proteins involved in type II and type IV secretion.


Pssm-ID: 410905 [Multi-domain]  Cd Length: 251  Bit Score: 39.89  E-value: 1.50e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130390347 215 VILYGAPGTGKTLLAK----------AVANQTSATFLRIVG-------SELIQKYLGDGPRlcrqifkvaAENApsIVFI 277
Cdd:cd19497    53 ILLIGPTGSGKTLLAQtlakildvpfAIADATTLTEAGYVGedvenilLKLLQAADYDVER---------AQRG--IVYI 121


                  ....*....
gi 2130390347 278 DEIDAIGTK 286
Cdd:cd19497   122 DEIDKIARK 130
COG2842 COG2842
Bacteriophage DNA transposition protein, AAA+ family ATPase [Mobilome: prophages, transposons]; ...
 215-281 1.76e-03

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


Pssm-ID: 442090 [Multi-domain]  Cd Length: 254  Bit Score: 39.94  E-value: 1.76e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130390347 215 VILYGAPGTGKTLLAKAVANQ-------------TSATFLRIVGSEL-IQKYLGDGPRLCRQIFKVAAENaPSIVFIDEI 280
Cdd:COG2842    53 GVVYGESGVGKTTAAREYANRnpnviyvtaspswTSKELLEELAEELgIPAPPGTIADLRDRILERLAGT-GRLLIIDEA 131


                  .
gi 2130390347 281 D 281
Cdd:COG2842   132 D 132
PRK08116 PRK08116
hypothetical protein; Validated
 204-299 3.23e-03

hypothetical protein; Validated


Pssm-ID: 236153 [Multi-domain]  Cd Length: 268  Bit Score: 39.23  E-value: 3.23e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130390347 204 YEEMGiKPPKGVILYGAPGTGKTLLAKAVANqtsatflrivgsELIQKYLGdgprlcrqifkVAAENAPSIvfIDEIdai 283
Cdd:PRK08116  107 FEEMK-KENVGLLLWGSVGTGKTYLAACIAN------------ELIEKGVP-----------VIFVNFPQL--LNRI--- 157

                          90
                  ....*....|....*.
gi 2130390347 284 gtKRYDSNSGGEREIQ 299
Cdd:PRK08116  158 --KSTYKSSGKEDENE 171
RecA-like_IQCA1 cd19506
ATPase domain of IQ and AAA domain-containing protein 1 (IQCA1); IQCA1 (also known as dynein ...
 213-279 3.88e-03

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


Pssm-ID: 410914 [Multi-domain]  Cd Length: 160  Bit Score: 37.89  E-value: 3.88e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2130390347 213 KGVILYGAPGTGKTLLAKAVANQTSATFLRIVGSELIQKYLGDG--PRLCRQIFKVAAENAPSIVFIDE 279
Cdd:cd19506    27 KSLLLAGPSGVGKKMLVHAICTETGANLFNLSPSNIAGKYPGKNglQMMLHLVLKVARQLQPSVIWIGD 95
COG0645 COG0645
Predicted kinase, contains AAA domain [General function prediction only];
215-243 4.09e-03

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


Pssm-ID: 440410 [Multi-domain]  Cd Length: 164  Bit Score: 37.97  E-value: 4.09e-03
                          10        20
                  ....*....|....*....|....*....
gi 2130390347 215 VILYGAPGTGKTLLAKAVANQTSATFLRI 243
Cdd:COG0645     2 ILVCGLPGSGKSTLARALAERLGAVRLRS 30
 
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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