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Conserved domains on  [gi|126131656|ref|XP_001382353|]
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26S protease regulatory subunit 4-like protein [Scheffersomyces stipitis CBS 6054]

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
 31-434 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: 724.64  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126131656  31 KKRRKGPDTAVKLPSVYPNTRCKLKLLKLERIKDHLLLEEEFVTNQEAFQPTEAKQAEEREKVDELRGYPMSIGTLEEII 110
Cdd:PTZ00361  35 KKKRKGPDAASKLPKVTPNTKCRLRLLKLERIKDYLLLEEEFITNQEAQKPAQEKNEAELKKVDDLRGSPLSVGTLEEII 114

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126131656 111 DDDHAIVSSTAGSEYYVSIMSFVDKGLLEPGCSVLLHHKTVSVVGVLQDDADPMVSVMKLDKSPTESYADIGGLESQIQE 190
Cdd:PTZ00361 115 DENHAIVSSSVGPEYYVNILSFVDKEQLEPGCSVLLHNKTHSVVGILLDEVDPLVSVMKVDKAPLESYADIGGLEQQIQE 194

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126131656 191 IKEAVELPLTHPELYEEMGIKPPKGVILYGAPGTGKTLLAKAVANQTSATFLRIVGSELIQKYLGDGPRLCRQIFQIAGE 270
Cdd:PTZ00361 195 IKEAVELPLTHPELYDDIGIKPPKGVILYGPPGTGKTLLAKAVANETSATFLRVVGSELIQKYLGDGPKLVRELFRVAEE 274

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126131656 271 HAPSIVFIDEIDAIGTKRYESTSGGEREIQRTMLELLNQLDGFDDRGDIKVIMATNKIESLDPALIRPGRIDRKILFENP 350
Cdd:PTZ00361 275 NAPSIVFIDEIDAIGTKRYDATSGGEKEIQRTMLELLNQLDGFDSRGDVKVIMATNRIESLDPALIRPGRIDRKIEFPNP 354

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126131656 351 DANTKKKILTIHTSKMSLADDVNLDELVTSKDDLSGADIKAICTEAGLLALRERRMQVKADDFKSAKERVLKNKVEENLE 430
Cdd:PTZ00361 355 DEKTKRRIFEIHTSKMTLAEDVDLEEFIMAKDELSGADIKAICTEAGLLALRERRMKVTQADFRKAKEKVLYRKKGNIPE 434


                 ....
gi 126131656 431 GLYL 434
Cdd:PTZ00361 435 GLYL 438
 
Name Accession Description Interval E-value
PTZ00361 PTZ00361
26 proteosome regulatory subunit 4-like protein; Provisional
 31-434 0e+00

26 proteosome regulatory subunit 4-like protein; Provisional


Pssm-ID: 185575 [Multi-domain]  Cd Length: 438  Bit Score: 724.64  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126131656  31 KKRRKGPDTAVKLPSVYPNTRCKLKLLKLERIKDHLLLEEEFVTNQEAFQPTEAKQAEEREKVDELRGYPMSIGTLEEII 110
Cdd:PTZ00361  35 KKKRKGPDAASKLPKVTPNTKCRLRLLKLERIKDYLLLEEEFITNQEAQKPAQEKNEAELKKVDDLRGSPLSVGTLEEII 114

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126131656 111 DDDHAIVSSTAGSEYYVSIMSFVDKGLLEPGCSVLLHHKTVSVVGVLQDDADPMVSVMKLDKSPTESYADIGGLESQIQE 190
Cdd:PTZ00361 115 DENHAIVSSSVGPEYYVNILSFVDKEQLEPGCSVLLHNKTHSVVGILLDEVDPLVSVMKVDKAPLESYADIGGLEQQIQE 194

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126131656 191 IKEAVELPLTHPELYEEMGIKPPKGVILYGAPGTGKTLLAKAVANQTSATFLRIVGSELIQKYLGDGPRLCRQIFQIAGE 270
Cdd:PTZ00361 195 IKEAVELPLTHPELYDDIGIKPPKGVILYGPPGTGKTLLAKAVANETSATFLRVVGSELIQKYLGDGPKLVRELFRVAEE 274

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126131656 271 HAPSIVFIDEIDAIGTKRYESTSGGEREIQRTMLELLNQLDGFDDRGDIKVIMATNKIESLDPALIRPGRIDRKILFENP 350
Cdd:PTZ00361 275 NAPSIVFIDEIDAIGTKRYDATSGGEKEIQRTMLELLNQLDGFDSRGDVKVIMATNRIESLDPALIRPGRIDRKIEFPNP 354

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126131656 351 DANTKKKILTIHTSKMSLADDVNLDELVTSKDDLSGADIKAICTEAGLLALRERRMQVKADDFKSAKERVLKNKVEENLE 430
Cdd:PTZ00361 355 DEKTKRRIFEIHTSKMTLAEDVDLEEFIMAKDELSGADIKAICTEAGLLALRERRMKVTQADFRKAKEKVLYRKKGNIPE 434


                 ....
gi 126131656 431 GLYL 434
Cdd:PTZ00361 435 GLYL 438
RPT1 COG1222
ATP-dependent 26S proteasome regulatory subunit [Posttranslational modification, protein ...
 158-424 2.13e-128

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


Pssm-ID: 440835 [Multi-domain]  Cd Length: 326  Bit Score: 373.96  E-value: 2.13e-128
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126131656 158 QDDADPMVSVMKLDKSPTESYADIGGLESQIQEIKEAVELPLTHPELYEEMGIKPPKGVILYGAPGTGKTLLAKAVANQT 237
Cdd:COG1222   57 QKRLGTPRGTAVPAESPDVTFDDIGGLDEQIEEIREAVELPLKNPELFRKYGIEPPKGVLLYGPPGTGKTLLAKAVAGEL 136

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126131656 238 SATFLRIVGSELIQKYLGDGPRLCRQIFQIAGEHAPSIVFIDEIDAIGTKRYESTSGGerEIQRTMLELLNQLDGFDDRG 317
Cdd:COG1222  137 GAPFIRVRGSELVSKYIGEGARNVREVFELAREKAPSIIFIDEIDAIAARRTDDGTSG--EVQRTVNQLLAELDGFESRG 214

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126131656 318 DIKVIMATNKIESLDPALIRPGRIDRKILFENPDANTKKKILTIHTSKMSLADDVNLDELVTSKDDLSGADIKAICTEAG 397
Cdd:COG1222  215 DVLIIAATNRPDLLDPALLRPGRFDRVIEVPLPDEEAREEILKIHLRDMPLADDVDLDKLAKLTEGFSGADLKAIVTEAG 294

                        250       260
                 ....*....|....*....|....*..
gi 126131656 398 LLALRERRMQVKADDFKSAKERVLKNK 424
Cdd:COG1222  295 MFAIREGRDTVTMEDLEKAIEKVKKKT 321
RecA-like_PAN_like cd19502
proteasome activating nucleotidase PAN and related proteasome subunits; This subfamily ...
 177-347 8.99e-110

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: 320.44  E-value: 8.99e-110
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126131656 177 SYADIGGLESQIQEIKEAVELPLTHPELYEEMGIKPPKGVILYGAPGTGKTLLAKAVANQTSATFLRIVGSELIQKYLGD 256
Cdd:cd19502    1 TYEDIGGLDEQIREIREVVELPLKHPELFEELGIEPPKGVLLYGPPGTGKTLLAKAVANHTDATFIRVVGSELVQKYIGE 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126131656 257 GPRLCRQIFQIAGEHAPSIVFIDEIDAIGTKRYESTSGGEREIQRTMLELLNQLDGFDDRGDIKVIMATNKIESLDPALI 336
Cdd:cd19502   81 GARLVRELFEMAREKAPSIIFIDEIDAIGAKRFDSGTGGDREVQRTMLELLNQLDGFDPRGNIKVIMATNRPDILDPALL 160

                        170
                 ....*....|.
gi 126131656 337 RPGRIDRKILF 347
Cdd:cd19502  161 RPGRFDRKIEF 171
FtsH_fam TIGR01241
ATP-dependent metalloprotease FtsH; HflB(FtsH) is a pleiotropic protein required for correct ...
 168-421 1.36e-77

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: 249.12  E-value: 1.36e-77
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126131656  168 MKLDKSPTESYADIGGLESQIQEIKEAVELpLTHPELYEEMGIKPPKGVILYGAPGTGKTLLAKAVANQTSATFLRIVGS 247
Cdd:TIGR01241  44 LLNEEKPKVTFKDVAGIDEAKEELMEIVDF-LKNPSKFTKLGAKIPKGVLLVGPPGTGKTLLAKAVAGEAGVPFFSISGS 122

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126131656  248 ELIQKYLGDGPRLCRQIFQIAGEHAPSIVFIDEIDAIGTKRYESTSGGEREIQRTMLELLNQLDGFDDRGDIKVIMATNK 327
Cdd:TIGR01241 123 DFVEMFVGVGASRVRDLFEQAKKNAPCIIFIDEIDAVGRQRGAGLGGGNDEREQTLNQLLVEMDGFGTNTGVIVIAATNR 202

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126131656  328 IESLDPALIRPGRIDRKILFENPDANTKKKILTIHTSKMSLADDVNLDELVTSKDDLSGADIKAICTEAGLLALRERRMQ 407
Cdd:TIGR01241 203 PDVLDPALLRPGRFDRQVVVDLPDIKGREEILKVHAKNKKLAPDVDLKAVARRTPGFSGADLANLLNEAALLAARKNKTE 282

                         250
                  ....*....|....
gi 126131656  408 VKADDFKSAKERVL 421
Cdd:TIGR01241 283 ITMNDIEEAIDRVI 296
AAA pfam00004
ATPase family associated with various cellular activities (AAA); AAA family proteins often ...
 216-348 7.48e-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: 157.37  E-value: 7.48e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126131656  216 VILYGAPGTGKTLLAKAVANQTSATFLRIVGSELIQKYLGDGPRLCRQIFQIAGEHAPSIVFIDEIDAIGTKRYestSGG 295
Cdd:pfam00004   1 LLLYGPPGTGKTTLAKAVAKELGAPFIEISGSELVSKYVGESEKRLRELFEAAKKLAPCVIFIDEIDALAGSRG---SGG 77

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 126131656  296 EREIQRTMLELLNQLDGFDDR-GDIKVIMATNKIESLDPALIrpGRIDRKILFE 348
Cdd:pfam00004  78 DSESRRVVNQLLTELDGFTSSnSKVIVIAATNRPDKLDPALL--GRFDRIIEFP 129
AAA smart00382
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ...
 212-351 1.59e-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: 76.26  E-value: 1.59e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126131656   212 PPKGVILYGAPGTGKTLLAKAVANQ---TSATFLRIVGSEL--------------IQKYLGDGPRLCRQIFQIAGEHAPS 274
Cdd:smart00382   1 PGEVILIVGPPGSGKTTLARALARElgpPGGGVIYIDGEDIleevldqllliivgGKKASGSGELRLRLALALARKLKPD 80

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 126131656   275 IVFIDEIDAIGTKryestsggEREIQRTMLELLNQLDGFDDRGDIKVIMATNKIESLDPALIRPgRIDRKILFENPD 351
Cdd:smart00382  81 VLILDEITSLLDA--------EQEALLLLLEELRLLLLLKSEKNLTVILTTNDEKDLGPALLRR-RFDRRIVLLLIL 148
IS21_help_AAA NF038214
IS21-like element helper ATPase IstB; This protein family model resembles PF01695, but was ...
 216-293 2.11e-03

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


Pssm-ID: 439516  Cd Length: 232  Bit Score: 39.38  E-value: 2.11e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126131656 216 VILYGAPGTGKTLLAKAVANQ-----TSATFLRIvgSELIQKYL---GDGpRLCRQIFQIAGehaPSIVFIDEI-----D 282
Cdd:NF038214  93 VLLLGPPGTGKTHLAIALGYAacrqgYRVRFTTA--ADLVEQLAqarADG-RLGRLLRRLAR---YDLLIIDELgylpfS 166

                         90
                 ....*....|....*....
gi 126131656 283 AIGT--------KRYESTS 293
Cdd:NF038214 167 REGAnllfeliaDRYERGS 185
 
Name Accession Description Interval E-value
PTZ00361 PTZ00361
26 proteosome regulatory subunit 4-like protein; Provisional
 31-434 0e+00

26 proteosome regulatory subunit 4-like protein; Provisional


Pssm-ID: 185575 [Multi-domain]  Cd Length: 438  Bit Score: 724.64  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126131656  31 KKRRKGPDTAVKLPSVYPNTRCKLKLLKLERIKDHLLLEEEFVTNQEAFQPTEAKQAEEREKVDELRGYPMSIGTLEEII 110
Cdd:PTZ00361  35 KKKRKGPDAASKLPKVTPNTKCRLRLLKLERIKDYLLLEEEFITNQEAQKPAQEKNEAELKKVDDLRGSPLSVGTLEEII 114

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126131656 111 DDDHAIVSSTAGSEYYVSIMSFVDKGLLEPGCSVLLHHKTVSVVGVLQDDADPMVSVMKLDKSPTESYADIGGLESQIQE 190
Cdd:PTZ00361 115 DENHAIVSSSVGPEYYVNILSFVDKEQLEPGCSVLLHNKTHSVVGILLDEVDPLVSVMKVDKAPLESYADIGGLEQQIQE 194

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126131656 191 IKEAVELPLTHPELYEEMGIKPPKGVILYGAPGTGKTLLAKAVANQTSATFLRIVGSELIQKYLGDGPRLCRQIFQIAGE 270
Cdd:PTZ00361 195 IKEAVELPLTHPELYDDIGIKPPKGVILYGPPGTGKTLLAKAVANETSATFLRVVGSELIQKYLGDGPKLVRELFRVAEE 274

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126131656 271 HAPSIVFIDEIDAIGTKRYESTSGGEREIQRTMLELLNQLDGFDDRGDIKVIMATNKIESLDPALIRPGRIDRKILFENP 350
Cdd:PTZ00361 275 NAPSIVFIDEIDAIGTKRYDATSGGEKEIQRTMLELLNQLDGFDSRGDVKVIMATNRIESLDPALIRPGRIDRKIEFPNP 354

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126131656 351 DANTKKKILTIHTSKMSLADDVNLDELVTSKDDLSGADIKAICTEAGLLALRERRMQVKADDFKSAKERVLKNKVEENLE 430
Cdd:PTZ00361 355 DEKTKRRIFEIHTSKMTLAEDVDLEEFIMAKDELSGADIKAICTEAGLLALRERRMKVTQADFRKAKEKVLYRKKGNIPE 434


                 ....
gi 126131656 431 GLYL 434
Cdd:PTZ00361 435 GLYL 438
PRK03992 PRK03992
proteasome-activating nucleotidase; Provisional
 90-430 1.56e-167

proteasome-activating nucleotidase; Provisional


Pssm-ID: 179699 [Multi-domain]  Cd Length: 389  Bit Score: 475.48  E-value: 1.56e-167
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126131656  90 REKVDELRGYPMSIGTLEEIIDDDHAIVSSTAGSEYYVSIMSFVDKGLLEPGCSVLLHHKTVSVVGVLQDDADPMVSVMK 169
Cdd:PRK03992  42 KSELEKLKSPPLIVATVLEVLDDGRVVVKSSGGPQFLVNVSPFIDREKLKPGARVALNQQSLAIVEVLPSEKDPRVQAME 121

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126131656 170 LDKSPTESYADIGGLESQIQEIKEAVELPLTHPELYEEMGIKPPKGVILYGAPGTGKTLLAKAVANQTSATFLRIVGSEL 249
Cdd:PRK03992 122 VIESPNVTYEDIGGLEEQIREVREAVELPLKKPELFEEVGIEPPKGVLLYGPPGTGKTLLAKAVAHETNATFIRVVGSEL 201

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126131656 250 IQKYLGDGPRLCRQIFQIAGEHAPSIVFIDEIDAIGTKRYESTSGGEREIQRTMLELLNQLDGFDDRGDIKVIMATNKIE 329
Cdd:PRK03992 202 VQKFIGEGARLVRELFELAREKAPSIIFIDEIDAIAAKRTDSGTSGDREVQRTLMQLLAEMDGFDPRGNVKIIAATNRID 281

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126131656 330 SLDPALIRPGRIDRKILFENPDANTKKKILTIHTSKMSLADDVNLDELVTSKDDLSGADIKAICTEAGLLALRERRMQVK 409
Cdd:PRK03992 282 ILDPAILRPGRFDRIIEVPLPDEEGRLEILKIHTRKMNLADDVDLEELAELTEGASGADLKAICTEAGMFAIRDDRTEVT 361

                        330       340
                 ....*....|....*....|.
gi 126131656 410 ADDFKSAKERVLKNKVEENLE 430
Cdd:PRK03992 362 MEDFLKAIEKVMGKEEKDSME 382
PTZ00454 PTZ00454
26S protease regulatory subunit 6B-like protein; Provisional
 54-427 1.00e-151

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


Pssm-ID: 240423 [Multi-domain]  Cd Length: 398  Bit Score: 436.12  E-value: 1.00e-151
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126131656  54 LKLLKLERIKDHLLLEEEFVTNQEAFQPTEAKQAeeREKVDELRGYPMSIGTLEEIIDDDHAIVSSTAGSEYYVSIMSFV 133
Cdd:PTZ00454  22 EKLKELEKELEFLDIQEEYIKEEQKNLKRELIRA--KEEVKRIQSVPLVIGQFLEMIDSNYGIVSSTSGSNYYVRILSTL 99

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126131656 134 DKGLLEPGCSVLLHHKTVSVVGVLQDDADPMVSVMKLDKSPTESYADIGGLESQIQEIKEAVELPLTHPELYEEMGIKPP 213
Cdd:PTZ00454 100 NRELLKPNASVALHRHSHAVVDILPPEADSSIQLLQMSEKPDVTYSDIGGLDIQKQEIREAVELPLTCPELYEQIGIDPP 179

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126131656 214 KGVILYGAPGTGKTLLAKAVANQTSATFLRIVGSELIQKYLGDGPRLCRQIFQIAGEHAPSIVFIDEIDAIGTKRYESTS 293
Cdd:PTZ00454 180 RGVLLYGPPGTGKTMLAKAVAHHTTATFIRVVGSEFVQKYLGEGPRMVRDVFRLARENAPSIIFIDEVDSIATKRFDAQT 259

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126131656 294 GGEREIQRTMLELLNQLDGFDDRGDIKVIMATNKIESLDPALIRPGRIDRKILFENPDANTKKKILTIHTSKMSLADDVN 373
Cdd:PTZ00454 260 GADREVQRILLELLNQMDGFDQTTNVKVIMATNRADTLDPALLRPGRLDRKIEFPLPDRRQKRLIFQTITSKMNLSEEVD 339

                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....
gi 126131656 374 LDELVTSKDDLSGADIKAICTEAGLLALRERRMQVKADDFKSAKERVLKNKVEE 427
Cdd:PTZ00454 340 LEDFVSRPEKISAADIAAICQEAGMQAVRKNRYVILPKDFEKGYKTVVRKTDRD 393
RPT1 COG1222
ATP-dependent 26S proteasome regulatory subunit [Posttranslational modification, protein ...
 158-424 2.13e-128

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


Pssm-ID: 440835 [Multi-domain]  Cd Length: 326  Bit Score: 373.96  E-value: 2.13e-128
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126131656 158 QDDADPMVSVMKLDKSPTESYADIGGLESQIQEIKEAVELPLTHPELYEEMGIKPPKGVILYGAPGTGKTLLAKAVANQT 237
Cdd:COG1222   57 QKRLGTPRGTAVPAESPDVTFDDIGGLDEQIEEIREAVELPLKNPELFRKYGIEPPKGVLLYGPPGTGKTLLAKAVAGEL 136

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126131656 238 SATFLRIVGSELIQKYLGDGPRLCRQIFQIAGEHAPSIVFIDEIDAIGTKRYESTSGGerEIQRTMLELLNQLDGFDDRG 317
Cdd:COG1222  137 GAPFIRVRGSELVSKYIGEGARNVREVFELAREKAPSIIFIDEIDAIAARRTDDGTSG--EVQRTVNQLLAELDGFESRG 214

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126131656 318 DIKVIMATNKIESLDPALIRPGRIDRKILFENPDANTKKKILTIHTSKMSLADDVNLDELVTSKDDLSGADIKAICTEAG 397
Cdd:COG1222  215 DVLIIAATNRPDLLDPALLRPGRFDRVIEVPLPDEEAREEILKIHLRDMPLADDVDLDKLAKLTEGFSGADLKAIVTEAG 294

                        250       260
                 ....*....|....*....|....*..
gi 126131656 398 LLALRERRMQVKADDFKSAKERVLKNK 424
Cdd:COG1222  295 MFAIREGRDTVTMEDLEKAIEKVKKKT 321
RecA-like_PAN_like cd19502
proteasome activating nucleotidase PAN and related proteasome subunits; This subfamily ...
 177-347 8.99e-110

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: 320.44  E-value: 8.99e-110
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126131656 177 SYADIGGLESQIQEIKEAVELPLTHPELYEEMGIKPPKGVILYGAPGTGKTLLAKAVANQTSATFLRIVGSELIQKYLGD 256
Cdd:cd19502    1 TYEDIGGLDEQIREIREVVELPLKHPELFEELGIEPPKGVLLYGPPGTGKTLLAKAVANHTDATFIRVVGSELVQKYIGE 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126131656 257 GPRLCRQIFQIAGEHAPSIVFIDEIDAIGTKRYESTSGGEREIQRTMLELLNQLDGFDDRGDIKVIMATNKIESLDPALI 336
Cdd:cd19502   81 GARLVRELFEMAREKAPSIIFIDEIDAIGAKRFDSGTGGDREVQRTMLELLNQLDGFDPRGNIKVIMATNRPDILDPALL 160

                        170
                 ....*....|.
gi 126131656 337 RPGRIDRKILF 347
Cdd:cd19502  161 RPGRFDRKIEF 171
FtsH_fam TIGR01241
ATP-dependent metalloprotease FtsH; HflB(FtsH) is a pleiotropic protein required for correct ...
 168-421 1.36e-77

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: 249.12  E-value: 1.36e-77
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126131656  168 MKLDKSPTESYADIGGLESQIQEIKEAVELpLTHPELYEEMGIKPPKGVILYGAPGTGKTLLAKAVANQTSATFLRIVGS 247
Cdd:TIGR01241  44 LLNEEKPKVTFKDVAGIDEAKEELMEIVDF-LKNPSKFTKLGAKIPKGVLLVGPPGTGKTLLAKAVAGEAGVPFFSISGS 122

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126131656  248 ELIQKYLGDGPRLCRQIFQIAGEHAPSIVFIDEIDAIGTKRYESTSGGEREIQRTMLELLNQLDGFDDRGDIKVIMATNK 327
Cdd:TIGR01241 123 DFVEMFVGVGASRVRDLFEQAKKNAPCIIFIDEIDAVGRQRGAGLGGGNDEREQTLNQLLVEMDGFGTNTGVIVIAATNR 202

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126131656  328 IESLDPALIRPGRIDRKILFENPDANTKKKILTIHTSKMSLADDVNLDELVTSKDDLSGADIKAICTEAGLLALRERRMQ 407
Cdd:TIGR01241 203 PDVLDPALLRPGRFDRQVVVDLPDIKGREEILKVHAKNKKLAPDVDLKAVARRTPGFSGADLANLLNEAALLAARKNKTE 282

                         250
                  ....*....|....
gi 126131656  408 VKADDFKSAKERVL 421
Cdd:TIGR01241 283 ITMNDIEEAIDRVI 296
CDC48 TIGR01243
AAA family ATPase, CDC48 subfamily; This subfamily of the AAA family ATPases includes two ...
 165-423 6.15e-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: 250.98  E-value: 6.15e-76
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126131656  165 VSVMKLDKSPTESYADIGGLESQIQEIKEAVELPLTHPELYEEMGIKPPKGVILYGAPGTGKTLLAKAVANQTSATFLRI 244
Cdd:TIGR01243 164 VREEIERKVPKVTYEDIGGLKEAKEKIREMVELPMKHPELFEHLGIEPPKGVLLYGPPGTGKTLLAKAVANEAGAYFISI 243

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126131656  245 VGSELIQKYLGDGPRLCRQIFQIAGEHAPSIVFIDEIDAIGTKRYESTsgGEREiQRTMLELLNQLDGFDDRGDIKVIMA 324
Cdd:TIGR01243 244 NGPEIMSKYYGESEERLREIFKEAEENAPSIIFIDEIDAIAPKREEVT--GEVE-KRVVAQLLTLMDGLKGRGRVIVIGA 320

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126131656  325 TNKIESLDPALIRPGRIDRKILFENPDANTKKKILTIHTSKMSLADDVNLDELVTSKDDLSGADIKAICTEAGLLALRER 404
Cdd:TIGR01243 321 TNRPDALDPALRRPGRFDREIVIRVPDKRARKEILKVHTRNMPLAEDVDLDKLAEVTHGFVGADLAALAKEAAMAALRRF 400

                         250       260
                  ....*....|....*....|
gi 126131656  405 RMQVKAD-DFKSAKERVLKN 423
Cdd:TIGR01243 401 IREGKINfEAEEIPAEVLKE 420
CDC48 TIGR01243
AAA family ATPase, CDC48 subfamily; This subfamily of the AAA family ATPases includes two ...
 174-425 3.42e-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: 246.36  E-value: 3.42e-74
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126131656  174 PTESYADIGGLESQIQEIKEAVELPLTHPELYEEMGIKPPKGVILYGAPGTGKTLLAKAVANQTSATFLRIVGSELIQKY 253
Cdd:TIGR01243 448 PNVRWSDIGGLEEVKQELREAVEWPLKHPEIFEKMGIRPPKGVLLFGPPGTGKTLLAKAVATESGANFIAVRGPEILSKW 527

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126131656  254 LGDGPRLCRQIFQIAGEHAPSIVFIDEIDAIGTKRyeSTSGGEREIQRTMLELLNQLDGFDDRGDIKVIMATNKIESLDP 333
Cdd:TIGR01243 528 VGESEKAIREIFRKARQAAPAIIFFDEIDAIAPAR--GARFDTSVTDRIVNQLLTEMDGIQELSNVVVIAATNRPDILDP 605

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126131656  334 ALIRPGRIDRKILFENPDANTKKKILTIHTSKMSLADDVNLDELVTSKDDLSGADIKAICTEAGLLALRERRMQVKADDF 413
Cdd:TIGR01243 606 ALLRPGRFDRLILVPPPDEEARKEIFKIHTRSMPLAEDVDLEELAEMTEGYTGADIEAVCREAAMAALRESIGSPAKEKL 685

                         250
                  ....*....|..
gi 126131656  414 KSAKERVLKNKV 425
Cdd:TIGR01243 686 EVGEEEFLKDLK 697
SpoVK COG0464
AAA+-type ATPase, SpoVK/Ycf46/Vps4 family [Cell wall/membrane/envelope biogenesis, Cell cycle ...
 178-420 6.22e-74

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: 236.73  E-value: 6.22e-74
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126131656 178 YADIGGLESQIQEIKEAVELPLTHPELYEEMGIKPPKGVILYGAPGTGKTLLAKAVANQTSATFLRIVGSELIQKYLGDG 257
Cdd:COG0464  156 LDDLGGLEEVKEELRELVALPLKRPELREEYGLPPPRGLLLYGPPGTGKTLLARALAGELGLPLIEVDLSDLVSKYVGET 235

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126131656 258 PRLCRQIFQIAGEHAPSIVFIDEIDAIGTKRYESTSGGEREIQRTmleLLNQLDGFddRGDIKVIMATNKIESLDPALIR 337
Cdd:COG0464  236 EKNLREVFDKARGLAPCVLFIDEADALAGKRGEVGDGVGRRVVNT---LLTEMEEL--RSDVVVIAATNRPDLLDPALLR 310

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126131656 338 pgRIDRKILFENPDANTKKKILTIHTSKMSLADDVNLDELVTSKDDLSGADIKAICTEAGLLALRERRMQVKADDFKSAK 417
Cdd:COG0464  311 --RFDEIIFFPLPDAEERLEIFRIHLRKRPLDEDVDLEELAEATEGLSGADIRNVVRRAALQALRLGREPVTTEDLLEAL 388


                 ...
gi 126131656 418 ERV 420
Cdd:COG0464  389 ERE 391
RecA-like_CDC48_NLV2_r1-like cd19503
first of two ATPase domains of CDC48 and NLV2, and similar ATPase domains; CDC48 in yeast and ...
 180-347 1.58e-67

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: 212.15  E-value: 1.58e-67
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126131656 180 DIGGLESQIQEIKEAVELPLTHPELYEEMGIKPPKGVILYGAPGTGKTLLAKAVANQTSATFLRIVGSELIQKYLGDGPR 259
Cdd:cd19503    1 DIGGLDEQIASLKELIELPLKYPELFRALGLKPPRGVLLHGPPGTGKTLLARAVANEAGANFLSISGPSIVSKYLGESEK 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126131656 260 LCRQIFQIAGEHAPSIVFIDEIDAIGTKRYESTSGGEReiqRTMLELLNQLDGFDDRGDIKVIMATNKIESLDPALIRPG 339
Cdd:cd19503   81 NLREIFEEARSHAPSIIFIDEIDALAPKREEDQREVER---RVVAQLLTLMDGMSSRGKVVVIAATNRPDAIDPALRRPG 157


                 ....*...
gi 126131656 340 RIDRKILF 347
Cdd:cd19503  158 RFDREVEI 165
HflB COG0465
ATP-dependent Zn proteases [Posttranslational modification, protein turnover, chaperones];
171-425 1.89e-67

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


Pssm-ID: 440233 [Multi-domain]  Cd Length: 583  Bit Score: 224.92  E-value: 1.89e-67
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126131656 171 DKSPTESYADIGGLESQIQEIKEAVELpLTHPELYEEMGIKPPKGVILYGAPGTGKTLLAKAVANQTSATFLRIVGSELI 250
Cdd:COG0465  134 EDKPKVTFDDVAGVDEAKEELQEIVDF-LKDPEKFTRLGAKIPKGVLLVGPPGTGKTLLAKAVAGEAGVPFFSISGSDFV 212

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126131656 251 QKYLGDGPRLCRQIFQIAGEHAPSIVFIDEIDAIGTKRYESTSGG--EREiqRTmlelLNQL----DGFDDRGDIKVIMA 324
Cdd:COG0465  213 EMFVGVGASRVRDLFEQAKKNAPCIIFIDEIDAVGRQRGAGLGGGhdERE--QT----LNQLlvemDGFEGNEGVIVIAA 286

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126131656 325 TNKIESLDPALIRPGRIDRKILFENPDANTKKKILTIHTSKMSLADDVNLDELVTSKDDLSGADIKAICTEAGLLALRER 404
Cdd:COG0465  287 TNRPDVLDPALLRPGRFDRQVVVDLPDVKGREAILKVHARKKPLAPDVDLEVIARRTPGFSGADLANLVNEAALLAARRN 366

                        250       260
                 ....*....|....*....|....*.
gi 126131656 405 RMQVKADDFKSAKERVL-----KNKV 425
Cdd:COG0465  367 KKAVTMEDFEEAIDRVIagperKSRV 392
RecA-like_CDC48_r1-like cd19519
first of two ATPase domains of CDC48 and similar ATPase domains; CDC48 in yeast and p97 or VCP ...
 180-345 2.83e-63

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: 201.51  E-value: 2.83e-63
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126131656 180 DIGGLESQIQEIKEAVELPLTHPELYEEMGIKPPKGVILYGAPGTGKTLLAKAVANQTSATFLRIVGSELIQKYLGDGPR 259
Cdd:cd19519    1 DIGGCRKQLAQIREMVELPLRHPELFKAIGIKPPRGILLYGPPGTGKTLIARAVANETGAFFFLINGPEIMSKLAGESES 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126131656 260 LCRQIFQIAGEHAPSIVFIDEIDAIGTKRYESTsgGEREiQRTMLELLNQLDGFDDRGDIKVIMATNKIESLDPALIRPG 339
Cdd:cd19519   81 NLRKAFEEAEKNAPAIIFIDEIDAIAPKREKTH--GEVE-RRIVSQLLTLMDGLKQRAHVIVMAATNRPNSIDPALRRFG 157


                 ....*.
gi 126131656 340 RIDRKI 345
Cdd:cd19519  158 RFDREI 163
RecA-like_FtsH cd19501
ATP-dependent zinc metalloprotease FtsH; FtsH ATPase is a processive, ATP-dependent zinc ...
 177-345 2.26e-62

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: 199.38  E-value: 2.26e-62
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126131656 177 SYADIGGLESQIQEIKEAVELpLTHPELYEEMGIKPPKGVILYGAPGTGKTLLAKAVANQTSATFLRIVGSELIQKYLGD 256
Cdd:cd19501    2 TFKDVAGCEEAKEELKEVVEF-LKNPEKFTKLGAKIPKGVLLVGPPGTGKTLLAKAVAGEAGVPFFSISGSDFVEMFVGV 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126131656 257 GPRLCRQIFQIAGEHAPSIVFIDEIDAIGTKRYESTSGGEREIQRTMLELLNQLDGFDDRGDIKVIMATNKIESLDPALI 336
Cdd:cd19501   81 GASRVRDLFEQAKKNAPCIVFIDEIDAVGRKRGAGLGGGHDEREQTLNQLLVEMDGFESNTGVIVIAATNRPDVLDPALL 160


                 ....*....
gi 126131656 337 RPGRIDRKI 345
Cdd:cd19501  161 RPGRFDRQV 169
ftsH CHL00176
cell division protein; Validated
 177-421 8.91e-62

cell division protein; Validated


Pssm-ID: 214386 [Multi-domain]  Cd Length: 638  Bit Score: 211.06  E-value: 8.91e-62
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126131656 177 SYADIGGLESQIQEIKEAVELpLTHPELYEEMGIKPPKGVILYGAPGTGKTLLAKAVANQTSATFLRIVGSELIQKYLGD 256
Cdd:CHL00176 181 TFRDIAGIEEAKEEFEEVVSF-LKKPERFTAVGAKIPKGVLLVGPPGTGKTLLAKAIAGEAEVPFFSISGSEFVEMFVGV 259

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126131656 257 GPRLCRQIFQIAGEHAPSIVFIDEIDAIGTKRYESTSGGEREIQRTMLELLNQLDGFDDRGDIKVIMATNKIESLDPALI 336
Cdd:CHL00176 260 GAARVRDLFKKAKENSPCIVFIDEIDAVGRQRGAGIGGGNDEREQTLNQLLTEMDGFKGNKGVIVIAATNRVDILDAALL 339

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126131656 337 RPGRIDRKILFENPDANTKKKILTIHTSKMSLADDVNLDELVTSKDDLSGADIKAICTEAGLLALRERRMQVKADDFKSA 416
Cdd:CHL00176 340 RPGRFDRQITVSLPDREGRLDILKVHARNKKLSPDVSLELIARRTPGFSGADLANLLNEAAILTARRKKATITMKEIDTA 419


                 ....*
gi 126131656 417 KERVL 421
Cdd:CHL00176 420 IDRVI 424
RecA-like_CDC48_r2-like cd19511
second of two ATPase domains of CDC48/p97, PEX1 and -6, VAT and NVL, and similar ATPase ...
 189-345 8.68e-59

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: 189.42  E-value: 8.68e-59
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126131656 189 QEIKEAVELPLTHPELYEEMGIKPPKGVILYGAPGTGKTLLAKAVANQTSATFLRIVGSELIQKYLGDGPRLCRQIFQIA 268
Cdd:cd19511    3 RELKEAVEWPLKHPDAFKRLGIRPPKGVLLYGPPGCGKTLLAKALASEAGLNFISVKGPELFSKYVGESERAVREIFQKA 82

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 126131656 269 GEHAPSIVFIDEIDAIGTKRYESTSGGEREiqRTMLELLNQLDGFDDRGDIKVIMATNKIESLDPALIRPGRIDRKI 345
Cdd:cd19511   83 RQAAPCIIFFDEIDSLAPRRGQSDSSGVTD--RVVSQLLTELDGIESLKGVVVIAATNRPDMIDPALLRPGRLDKLI 157
hflB PRK10733
ATP-dependent zinc metalloprotease FtsH;
177-421 5.17e-57

ATP-dependent zinc metalloprotease FtsH;


Pssm-ID: 182683 [Multi-domain]  Cd Length: 644  Bit Score: 198.33  E-value: 5.17e-57
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126131656 177 SYADIGGLESQIQEIKEAVELpLTHPELYEEMGIKPPKGVILYGAPGTGKTLLAKAVANQTSATFLRIVGSELIQKYLGD 256
Cdd:PRK10733 150 TFADVAGCDEAKEEVAELVEY-LREPSRFQKLGGKIPKGVLMVGPPGTGKTLLAKAIAGEAKVPFFTISGSDFVEMFVGV 228

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126131656 257 GPRLCRQIFQIAGEHAPSIVFIDEIDAIGTKRYESTSGGEREIQRTMLELLNQLDGFDDRGDIKVIMATNKIESLDPALI 336
Cdd:PRK10733 229 GASRVRDMFEQAKKAAPCIIFIDEIDAVGRQRGAGLGGGHDEREQTLNQMLVEMDGFEGNEGIIVIAATNRPDVLDPALL 308

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126131656 337 RPGRIDRKILFENPDANTKKKILTIHTSKMSLADDVNLDELVTSKDDLSGADIKAICTEAGLLALRERRMQVKADDFKSA 416
Cdd:PRK10733 309 RPGRFDRQVVVGLPDVRGREQILKVHMRRVPLAPDIDAAIIARGTPGFSGADLANLVNEAALFAARGNKRVVSMVEFEKA 388


                 ....*
gi 126131656 417 KERVL 421
Cdd:PRK10733 389 KDKIM 393
RecA-like_VCP_r2 cd19529
second of two ATPase domains of Valosin-containing protein-like ATPase (VAT) and similar ...
 189-346 2.85e-56

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: 183.08  E-value: 2.85e-56
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126131656 189 QEIKEAVELPLTHPELYEEMGIKPPKGVILYGAPGTGKTLLAKAVANQTSATFLRIVGSELIQKYLGDGPRLCRQIFQIA 268
Cdd:cd19529    3 QELKEAVEWPLLKPEVFKRLGIRPPKGILLYGPPGTGKTLLAKAVATESNANFISVKGPELLSKWVGESEKAIREIFRKA 82

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 126131656 269 GEHAPSIVFIDEIDAIGTKRYESTSGGEREiqRTMLELLNQLDGFDDRGDIKVIMATNKIESLDPALIRPGRIDRKIL 346
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 ...
 187-347 2.08e-55

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: 180.94  E-value: 2.08e-55
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126131656 187 QIQEIKEAVELPLTHPELyEEMGIKPPKGVILYGAPGTGKTLLAKAVANQTSATFLRIVGSELIQKYLGDGPRLCRQIFQ 266
Cdd:cd19481    1 LKASLREAVEAPRRGSRL-RRYGLGLPKGILLYGPPGTGKTLLAKALAGELGLPLIVVKLSSLLSKYVGESEKNLRKIFE 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126131656 267 IAGEHAPSIVFIDEIDAIGTKRyeSTSGGEREIQRTMLELLNQLDGFDDRGDIKVIMATNKIESLDPALIRPGRIDRKIL 346
Cdd:cd19481   80 RARRLAPCILFIDEIDAIGRKR--DSSGESGELRRVLNQLLTELDGVNSRSKVLVIAATNRPDLLDPALLRPGRFDEVIE 157


                 .
gi 126131656 347 F 347
Cdd:cd19481  158 F 158
RecA-like_CDC48_r2-like cd19528
second of two ATPase domains of CDC48 and similar ATPase domains; CDC48 in yeast and p97 or ...
 189-345 1.96e-47

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: 159.98  E-value: 1.96e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126131656 189 QEIKEAVELPLTHPELYEEMGIKPPKGVILYGAPGTGKTLLAKAVANQTSATFLRIVGSELIQKYLGDGPRLCRQIFQIA 268
Cdd:cd19528    3 RELQELVQYPVEHPDKFLKFGMTPSKGVLFYGPPGCGKTLLAKAIANECQANFISVKGPELLTMWFGESEANVRDIFDKA 82

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 126131656 269 GEHAPSIVFIDEIDAIGTKRYESTSGGEREIQRTMLELLNQLDGFDDRGDIKVIMATNKIESLDPALIRPGRIDRKI 345
Cdd:cd19528   83 RAAAPCVLFFDELDSIAKARGGNIGDAGGAADRVINQILTEMDGMNTKKNVFIIGATNRPDIIDPAILRPGRLDQLI 159
RecA-like_Yta7-like cd19517
ATPase domain of Saccharomyces cerevisiae Yta7 and similar ATPase domains; Saccharomyces ...
 180-347 4.54e-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: 159.60  E-value: 4.54e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126131656 180 DIGGLESQIQEIKEAVELPLTHPELYEEMGIKPPKGVILYGAPGTGKTLLAKAVANQTS------ATFLRiVGSELIQKY 253
Cdd:cd19517    1 DIGGLSHYINQLKEMVFFPLLYPEVFAKFKITPPRGVLFHGPPGTGKTLMARALAAECSkggqkvSFFMR-KGADCLSKW 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126131656 254 LGDGPRLCRQIFQIAGEHAPSIVFIDEIDAIGTKRYESTSGGEREIQRTMLELlnqLDGFDDRGDIKVIMATNKIESLDP 333
Cdd:cd19517   80 VGEAERQLRLLFEEAYRMQPSIIFFDEIDGLAPVRSSKQEQIHASIVSTLLAL---MDGLDNRGQVVVIGATNRPDALDP 156

                        170
                 ....*....|....
gi 126131656 334 ALIRPGRIDRKILF 347
Cdd:cd19517  157 ALRRPGRFDREFYF 170
AAA pfam00004
ATPase family associated with various cellular activities (AAA); AAA family proteins often ...
 216-348 7.48e-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: 157.37  E-value: 7.48e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126131656  216 VILYGAPGTGKTLLAKAVANQTSATFLRIVGSELIQKYLGDGPRLCRQIFQIAGEHAPSIVFIDEIDAIGTKRYestSGG 295
Cdd:pfam00004   1 LLLYGPPGTGKTTLAKAVAKELGAPFIEISGSELVSKYVGESEKRLRELFEAAKKLAPCVIFIDEIDALAGSRG---SGG 77

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 126131656  296 EREIQRTMLELLNQLDGFDDR-GDIKVIMATNKIESLDPALIrpGRIDRKILFE 348
Cdd:pfam00004  78 DSESRRVVNQLLTELDGFTSSnSKVIVIAATNRPDKLDPALL--GRFDRIIEFP 129
RecA-like_VPS4-like cd19509
ATPase domain of VPS4, ATAD1, K, KTNA1, Spastin, FIGL-1 and similar ATPase domains; This ...
 181-346 2.72e-46

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


Pssm-ID: 410917 [Multi-domain]  Cd Length: 163  Bit Score: 157.13  E-value: 2.72e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126131656 181 IGGLESQIQEIKEAVELPLTHPELYEeMGIKPPKGVILYGAPGTGKTLLAKAVANQTSATFLRIVGSELIQKYLGDGPRL 260
Cdd:cd19509    1 IAGLDDAKEALKEAVILPSLRPDLFP-GLRGPPRGILLYGPPGTGKTLLARAVASESGSTFFSISASSLVSKWVGESEKI 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126131656 261 CRQIFQIAGEHAPSIVFIDEIDAIGTKRYESTSGGEREIqRTmlELLNQLDGF--DDRGDIKVIMATNKIESLDPALIRp 338
Cdd:cd19509   80 VRALFALARELQPSIIFIDEIDSLLSERGSGEHEASRRV-KT--EFLVQMDGVlnKPEDRVLVLGATNRPWELDEAFLR- 155


                 ....*...
gi 126131656 339 gRIDRKIL 346
Cdd:cd19509  156 -RFEKRIY 162
COG1223 COG1223
Predicted ATPase, AAA+ superfamily [General function prediction only];
180-427 1.01e-45

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


Pssm-ID: 440836 [Multi-domain]  Cd Length: 246  Bit Score: 158.51  E-value: 1.01e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126131656 180 DIGGLESQIQEIKEAVElPLTHPELYEEMGIKPPKGVILYGAPGTGKTLLAKAVANQTSATFLRIVGSELIQKYLGDGPR 259
Cdd:COG1223    3 DVVGQEEAKKKLKLIIK-ELRRRENLRKFGLWPPRKILFYGPPGTGKTMLAEALAGELKLPLLTVRLDSLIGSYLGETAR 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126131656 260 LCRQIFQIAgEHAPSIVFIDEIDAIGTKR-YESTSGgerEIQRTMLELLNQLDGFddRGDIKVIMATNKIESLDPALIRp 338
Cdd:COG1223   82 NLRKLFDFA-RRAPCVIFFDEFDAIAKDRgDQNDVG---EVKRVVNALLQELDGL--PSGSVVIAATNHPELLDSALWR- 154

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126131656 339 gRIDRKILFENPDANTKKKILTIHTSKMSLADDVNLDELVTSKDDLSGADIKAICTEAGLLALRERRMQVKADDFKSA-- 416
Cdd:COG1223  155 -RFDEVIEFPLPDKEERKEILELNLKKFPLPFELDLKKLAKKLEGLSGADIEKVLKTALKKAILEDREKVTKEDLEEAlk 233

                        250
                 ....*....|...
gi 126131656 417 --KERVLKNKVEE 427
Cdd:COG1223  234 qrKERKKEPKKEG 246
RecA-like_NVL_r2-like cd19530
second of two ATPase domains of NVL (nuclear VCP-like protein) and similar ATPase domains; NVL ...
 184-347 1.95e-45

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: 154.95  E-value: 1.95e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126131656 184 LESQIQEIKEAVELPLTHPELYEEMGIKPPKGVILYGAPGTGKTLLAKAVANQTSATFLRIVGSELIQKYLGDGPRLCRQ 263
Cdd:cd19530    1 LDHVREELTMSILRPIKRPDIYKALGIDLPTGVLLYGPPGCGKTLLAKAVANESGANFISVKGPELLNKYVGESERAVRQ 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126131656 264 IFQIAGEHAPSIVFIDEIDAIGTKRYESTSGGereIQRTMLELLNQLDGFDDRGDIKVIMATNKIESLDPALIRPGRIDr 343
Cdd:cd19530   81 VFQRARASAPCVIFFDEVDALVPKRGDGGSWA---SERVVNQLLTEMDGLEERSNVFVIAATNRPDIIDPAMLRPGRLD- 156


                 ....
gi 126131656 344 KILF 347
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 ...
 180-345 8.35e-44

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: 151.02  E-value: 8.35e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126131656 180 DIGGLESQIQEIKEAVELPLTHPELYEEMGIKPPKGVILYGAPGTGKTLLAKAVANQTSATFLRIVGSELIQKYLGDGPR 259
Cdd:cd19518    1 DIGGMDSTLKELCELLIHPILPPEYFQHLGVEPPRGVLLHGPPGCGKTMLANAIAGELKVPFLKISATEIVSGVSGESEE 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126131656 260 LCRQIFQIAGEHAPSIVFIDEIDAIGTKRyESTSggeREIQRTML-ELLNQLDGF----DDRGDIKVIMATNKIESLDPA 334
Cdd:cd19518   81 KIRELFDQAISNAPCIVFIDEIDAITPKR-ESAQ---REMERRIVsQLLTCMDELnnekTAGGPVLVIGATNRPDSLDPA 156

                        170
                 ....*....|.
gi 126131656 335 LIRPGRIDRKI 345
Cdd:cd19518  157 LRRAGRFDREI 167
RecA-like_VPS4 cd19521
ATPase domain of vacuolar protein sorting-associated protein 4; Vacuolar protein ...
 174-345 2.62e-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: 141.92  E-value: 2.62e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126131656 174 PTESYADIGGLESQIQEIKEAVELPLTHPELYEEmGIKPPKGVILYGAPGTGKTLLAKAVANQTSATFLRIVGSELIQKY 253
Cdd:cd19521    2 PNVKWEDVAGLEGAKEALKEAVILPVKFPHLFTG-NRKPWSGILLYGPPGTGKSYLAKAVATEANSTFFSVSSSDLVSKW 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126131656 254 LGDGPRLCRQIFQIAGEHAPSIVFIDEIDAIGTKRYESTSGGEREIQRtmlELLNQLDGF-DDRGDIKVIMATNKIESLD 332
Cdd:cd19521   81 MGESEKLVKQLFAMARENKPSIIFIDEVDSLCGTRGEGESEASRRIKT---ELLVQMNGVgNDSQGVLVLGATNIPWQLD 157

                        170
                 ....*....|...
gi 126131656 333 PALIRpgRIDRKI 345
Cdd:cd19521  158 SAIRR--RFEKRI 168
RecA-like_ATAD1 cd19520
ATPase domain of ATPase family AAA domain-containing protein 1 and similar ATPase domains; ...
 180-337 1.06e-39

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: 139.87  E-value: 1.06e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126131656 180 DIGGLESQIQEIKEAVELPLTHPELYEEMGI-KPPKGVILYGAPGTGKTLLAKAVANQTSATFLRIVGSELIQKYLGDGP 258
Cdd:cd19520    1 DIGGLDEVITELKELVILPLQRPELFDNSRLlQPPKGVLLYGPPGCGKTMLAKATAKEAGARFINLQVSSLTDKWYGESQ 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126131656 259 RLCRQIFQIAGEHAPSIVFIDEIDAIGTKRyestSGGEREIQRTM-LELLNQLDGFDDRGDIKVIM--ATNKIESLDPAL 335
Cdd:cd19520   81 KLVAAVFSLASKLQPSIIFIDEIDSFLRQR----SSTDHEATAMMkAEFMSLWDGLSTDGNCRVIVmgATNRPQDLDEAI 156


                 ..
gi 126131656 336 IR 337
Cdd:cd19520  157 LR 158
RecA-like_PEX6_r2 cd19527
second of two ATPase domains of Peroxisomal biogenesis factor 6 (PEX6); PEX6(also known as ...
 190-343 7.29e-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: 137.64  E-value: 7.29e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126131656 190 EIKEAVELPLTHPELYEEmGIKPPKGVILYGAPGTGKTLLAKAVANQTSATFLRIVGSELIQKYLGDGPRLCRQIFQIAG 269
Cdd:cd19527    4 EILDTIQLPLEHPELFSS-GLRKRSGILLYGPPGTGKTLLAKAIATECSLNFLSVKGPELINMYIGESEANVREVFQKAR 82

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 126131656 270 EHAPSIVFIDEIDAIGTKRYES-TSGGerEIQRTMLELLNQLDGFDDRG-DIKVIMATNKIESLDPALIRPGRIDR 343
Cdd:cd19527   83 DAKPCVIFFDELDSLAPSRGNSgDSGG--VMDRVVSQLLAELDGMSSSGqDVFVIGATNRPDLLDPALLRPGRFDK 156
RecA-like_Figl-1 cd19525
ATPase domain of Fidgetin-Like 1 (FIGL-1); FIGL-1 may participate in DNA repair in the nucleus; ...
 170-337 1.54e-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: 135.12  E-value: 1.54e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126131656 170 LDKSPTESYADIGGLESQIQEIKEAVELPLTHPELYeeMGIK-PPKGVILYGAPGTGKTLLAKAVANQTSATFLRIVGSE 248
Cdd:cd19525   13 MDHGPPINWADIAGLEFAKKTIKEIVVWPMLRPDIF--TGLRgPPKGILLFGPPGTGKTLIGKCIASQSGATFFSISASS 90

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126131656 249 LIQKYLGDGPRLCRQIFQIAGEHAPSIVFIDEIDAIGTKRYESTSGGEREIQRtmlELLNQLDGF----DDRgdIKVIMA 324
Cdd:cd19525   91 LTSKWVGEGEKMVRALFSVARCKQPAVIFIDEIDSLLSQRGEGEHESSRRIKT---EFLVQLDGAttssEDR--ILVVGA 165

                        170
                 ....*....|...
gi 126131656 325 TNKIESLDPALIR 337
Cdd:cd19525  166 TNRPQEIDEAARR 178
RecA-like_spastin cd19524
ATPase domain of spastin; Spastin is an ATP-dependent microtubule-severing protein involved in ...
 180-337 5.78e-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: 132.67  E-value: 5.78e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126131656 180 DIGGLESQIQEIKEAVELPLTHPELYeeMGIK-PPKGVILYGAPGTGKTLLAKAVANQTSATFLRIVGSELIQKYLGDGP 258
Cdd:cd19524    1 DIAGQDLAKQALQEMVILPSLRPELF--TGLRaPARGLLLFGPPGNGKTMLAKAVAAESNATFFNISAASLTSKYVGEGE 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126131656 259 RLCRQIFQIAGEHAPSIVFIDEIDAIGTKRYESTSGGEReiqRTMLELLNQLDGFDDRGDIKVIM--ATNKIESLDPALI 336
Cdd:cd19524   79 KLVRALFAVARELQPSIIFIDEVDSLLSERSEGEHEASR---RLKTEFLIEFDGVQSNGDDRVLVmgATNRPQELDDAVL 155


                 .
gi 126131656 337 R 337
Cdd:cd19524  156 R 156
RecA-like_PEX1_r2 cd19526
second of two ATPase domains of Peroxisomal biogenesis factor 1 (PEX1); PEX1(also known as ...
 191-346 1.33e-36

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: 131.40  E-value: 1.33e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126131656 191 IKEAVELPLTHPELYEEMGIKPPKGVILYGAPGTGKTLLAKAVANQTSATFLRIVGSELIQKYLGDGPRLCRQIFQIAGE 270
Cdd:cd19526    5 LEETIEWPSKYPKIFASSPLRLRSGILLYGPPGCGKTLLASAIASECGLNFISVKGPELLNKYIGASEQNVRDLFSRAQS 84

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 126131656 271 HAPSIVFIDEIDAIGTKRYESTSGgerEIQRTMLELLNQLDGFDDRGDIKVIMATNKIESLDPALIRPGRIDRKIL 346
Cdd:cd19526   85 AKPCILFFDEFDSIAPKRGHDSTG---VTDRVVNQLLTQLDGVEGLDGVYVLAATSRPDLIDPALLRPGRLDKLVY 157
RecA-like_KTNA1 cd19522
Katanin p60 ATPase-containing subunit A1; Katanin p60 ATPase-containing subunit A1 (KTNA1) is ...
 180-345 5.71e-36

Katanin p60 ATPase-containing subunit A1; Katanin p60 ATPase-containing subunit A1 (KTNA1) is the catalytic subunit of the Katanin complex which is severs microtubules in an ATP-dependent manner, and is implicated in multiple aspects of microtubule dynamics. In addition to the p60 catalytic ATPase subunit, Katanin contains an accessory subunit (p80 or p80-like). The microtubule-severing activity of the ATPase is essential for female meiotic spindle assembly, and male gamete production; and the katanin complex severing microtubules is under tight regulation during the transition from the meiotic to mitotic stage to allow proper embryogenesis. This subfamily belongs to the RecA-like NTPase family which includes the NTP binding domain of F1 and V1 H(+)ATPases, DnaB and related helicases as well as bacterial RecA and related eukaryotic and archaeal recombinases. The RecA-like NTPase family also includes bacterial conjugation proteins and related DNA transfer proteins involved in type II and type IV secretion.


Pssm-ID: 410930 [Multi-domain]  Cd Length: 170  Bit Score: 130.10  E-value: 5.71e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126131656 180 DIGGLESQIQEIKEAVELPLTHPELYEemGIKPP-KGVILYGAPGTGKTLLAKAVANQTSATFLRIVGSELIQKYLGDGP 258
Cdd:cd19522    1 DIADLEEAKKLLEEAVVLPMWMPEFFK--GIRRPwKGVLMVGPPGTGKTLLAKAVATECGTTFFNVSSSTLTSKYRGESE 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126131656 259 RLCRQIFQIAGEHAPSIVFIDEIDAIGTKRyeSTSGGEREIQRTMLELLNQLDGF-------DDRGDIKVIMATNKIESL 331
Cdd:cd19522   79 KLVRLLFEMARFYAPTTIFIDEIDSICSRR--GTSEEHEASRRVKSELLVQMDGVggasendDPSKMVMVLAATNFPWDI 156

                        170
                 ....*....|....
gi 126131656 332 DPALIRpgRIDRKI 345
Cdd:cd19522  157 DEALRR--RLEKRI 168
RecA-like_fidgetin cd19523
ATPase domain of fidgetin; Fidgetin (FIGN) is a ATP-dependent microtubule severing protein. ...
 180-337 9.42e-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: 108.05  E-value: 9.42e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126131656 180 DIGGLESQIQEIKEAVELPLTHPELYEEMgIKPPKGVILYGAPGTGKTLLAKAVANQTSATFLRIVGSELIQKYLGDGPR 259
Cdd:cd19523    1 DIAGLGALKAAIKEEVLWPLLRPDAFSGL-LRLPRSILLFGPRGTGKTLLGRCLASQLGATFLRLRGSTLVAKWAGEGEK 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126131656 260 LCRQIFQIAGEHAPSIVFIDEIDAIGTKRYEstsgGEREIQRTMLELLNQLDGFDDRGD--IKVIMATNKIESLDPALIR 337
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; ...
 181-345 2.58e-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: 101.80  E-value: 2.58e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126131656 181 IGGLESQIQEI-KEAVELPLTHPELYEEMGIKPPKGVILYGAPGTGKTLLAKAVANQTSATFLRIV-GSELIQKYLGDGP 258
Cdd:cd19504    2 IGGLDKEFSDIfRRAFASRVFPPEIVEQLGCKHVKGILLYGPPGTGKTLMARQIGKMLNAREPKIVnGPEILNKYVGESE 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126131656 259 RLCRQIFQIAGEHAPS--------IVFIDEIDAIGTKRyESTSGGEREIQRTMLELLNQLDGFDDRGDIKVIMATNKIES 330
Cdd:cd19504   82 ANIRKLFADAEEEQRRlgansglhIIIFDEIDAICKQR-GSMAGSTGVHDTVVNQLLSKIDGVEQLNNILVIGMTNRKDL 160

                        170
                 ....*....|....*
gi 126131656 331 LDPALIRPGRIDRKI 345
Cdd:cd19504  161 IDEALLRPGRLEVQM 175
AAA cd00009
The AAA+ (ATPases Associated with a wide variety of cellular Activities) superfamily ...
 182-348 5.27e-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: 99.91  E-value: 5.27e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126131656 182 GGLESQIQEIKEAVELPlthpelyeemgikPPKGVILYGAPGTGKTLLAKAVANQT---SATFLRIVGSELIQKYLG--- 255
Cdd:cd00009    1 VGQEEAIEALREALELP-------------PPKNLLLYGPPGTGKTTLARAIANELfrpGAPFLYLNASDLLEGLVVael 67

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126131656 256 DGPRLCRQIFQIAGEHAPSIVFIDEIDAIGtkryestsggeREIQRTMLELLNQL-DGFDDRGDIKVIMATNKIESLDPA 334
Cdd:cd00009   68 FGHFLVRLLFELAEKAKPGVLFIDEIDSLS-----------RGAQNALLRVLETLnDLRIDRENVRVIGATNRPLLGDLD 136

                        170
                 ....*....|....
gi 126131656 335 LIRPGRIDRKILFE 348
Cdd:cd00009  137 RALYDRLDIRIVIP 150
RecA-like_Ycf46-like cd19507
ATPase domain of Ycf46 and similar ATPase domains; Ycf46 may play a role in the regulation of ...
 180-347 1.39e-21

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: 90.89  E-value: 1.39e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126131656 180 DIGGLE---SQIQEIKEAVELPlthpelYEEMGIKPPKGVILYGAPGTGKTLLAKAVANQTSATFLRIVGSELIQKYLGD 256
Cdd:cd19507    1 DVGGLDnlkDWLKKRKAAFSKQ------ASAYGLPTPKGLLLVGIQGTGKSLTAKAIAGVWQLPLLRLDMGRLFGGLVGE 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126131656 257 GPRLCRQIFQIAGEHAPSIVFIDEID-AIGTKRYESTSGGEREIQRTMLELLNQldgfdDRGDIKVIMATNKIESLDPAL 335
Cdd:cd19507   75 SESRLRQMIQTAEAIAPCVLWIDEIEkGFSNADSKGDSGTSSRVLGTFLTWLQE-----KKKPVFVVATANNVQSLPPEL 149

                        170
                 ....*....|..
gi 126131656 336 IRPGRIDRkILF 347
Cdd:cd19507  150 LRKGRFDE-IFF 160
ycf46 CHL00195
Ycf46; Provisional
 173-405 4.78e-20

Ycf46; Provisional


Pssm-ID: 177094 [Multi-domain]  Cd Length: 489  Bit Score: 92.00  E-value: 4.78e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126131656 173 SPTESYADIGGLESQIQEIKEAVElplTHPELYEEMGIKPPKGVILYGAPGTGKTLLAKAVANQTSATFLRIVGSELIQK 252
Cdd:CHL00195 222 SVNEKISDIGGLDNLKDWLKKRST---SFSKQASNYGLPTPRGLLLVGIQGTGKSLTAKAIANDWQLPLLRLDVGKLFGG 298

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126131656 253 YLGDGPRLCRQIFQIAGEHAPSIVFIDEIDAIGTKRYEST-SGGEREIQRTMLELLNQldgfdDRGDIKVIMATNKIESL 331
Cdd:CHL00195 299 IVGESESRMRQMIRIAEALSPCILWIDEIDKAFSNSESKGdSGTTNRVLATFITWLSE-----KKSPVFVVATANNIDLL 373

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 126131656 332 DPALIRPGRIDrKILFEN-PDANTKKKILTIHTSKMSLA--DDVNLDELVTSKDDLSGADIKAICTEAGLLALRERR 405
Cdd:CHL00195 374 PLEILRKGRFD-EIFFLDlPSLEEREKIFKIHLQKFRPKswKKYDIKKLSKLSNKFSGAEIEQSIIEAMYIAFYEKR 449
RecA-like_BCS1 cd19510
Mitochondrial chaperone BCS1; Mitochondrial chaperone BCS1 is necessary for the assembly of ...
 191-347 1.27e-19

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: 85.10  E-value: 1.27e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126131656 191 IKEAVELPLTHPELYEEMGIKPPKGVILYGAPGTGKTLLAKAVANqtsatFLR--IVGSELIQKYLGDgpRLCRQIFQIA 268
Cdd:cd19510    1 IIDDLKDFIKNEDWYNDRGIPYRRGYLLYGPPGTGKSSFIAALAG-----ELDydICDLNLSEVVLTD--DRLNHLLNTA 73

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126131656 269 GEHapSIVFIDEIDA-----IGTKRYESTSGGEREIqrTMLELLNQLDGFDDRGDIKVIMATNKIESLDPALIRPGRIDR 343
Cdd:cd19510   74 PKQ--SIILLEDIDAafesrEHNKKNPSAYGGLSRV--TFSGLLNALDGVASSEERIVFMTTNHIERLDPALIRPGRVDM 149


                 ....
gi 126131656 344 KILF 347
Cdd:cd19510  150 KIYM 153
AAA smart00382
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ...
 212-351 1.59e-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: 76.26  E-value: 1.59e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126131656   212 PPKGVILYGAPGTGKTLLAKAVANQ---TSATFLRIVGSEL--------------IQKYLGDGPRLCRQIFQIAGEHAPS 274
Cdd:smart00382   1 PGEVILIVGPPGSGKTTLARALARElgpPGGGVIYIDGEDIleevldqllliivgGKKASGSGELRLRLALALARKLKPD 80

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 126131656   275 IVFIDEIDAIGTKryestsggEREIQRTMLELLNQLDGFDDRGDIKVIMATNKIESLDPALIRPgRIDRKILFENPD 351
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 ...
 216-336 2.41e-11

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: 62.85  E-value: 2.41e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126131656 216 VILYGAPGTGKTLLAKAVANQTS---------ATFLRIVGSELIQKYLGDGPRLCRQIFQ-----IAGEHAPSIVFIDEI 281
Cdd:cd19508   55 VLLHGPPGTGKTSLCKALAQKLSirlssryryGQLIEINSHSLFSKWFSESGKLVTKMFQkiqelIDDKDALVFVLIDEV 134

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 126131656 282 DAIGTKRYESTSGGE-REIQRTMLELLNQLDGFDDRGDIKVIMATNKIESLDPALI 336
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 ...
 371-415 6.22e-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: 57.16  E-value: 6.22e-11
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 126131656  371 DVNLDELVTSKDDLSGADIKAICTEAGLLALRERRMQVKADDFKS 415
Cdd:pfam17862   1 DVDLEELAERTEGFSGADLEALCREAALAALRRGLEAVTQEDLEE 45
Prot_ATP_ID_OB pfam16450
Proteasomal ATPase OB C-terminal domain; This is the interdomain (ID) or oligonucleotide ...
 103-157 3.71e-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: 55.21  E-value: 3.71e-10
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 126131656  103 IGTLEEIIDDDHAIVSSTAGSEYYVSIMSFVDKGLLEPGCSVLLHHKTVSVVGVL 157
Cdd:pfam16450   1 VATVVEVLDDGRALVKSSGGEERVVRLAGSLDEEKLRPGDRVLLDPRSGYALEVL 55
CDC6 COG1474
Cdc6-related protein, AAA superfamily ATPase [Replication, recombination and repair];
185-432 5.64e-10

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


Pssm-ID: 441083 [Multi-domain]  Cd Length: 389  Bit Score: 60.63  E-value: 5.64e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126131656 185 ESQIQEIKEAVElPLTHPElyeemgikPPKGVILYGAPGTGKTLLAKAVANQ---------TSATFLRI----------V 245
Cdd:COG1474   32 EEEIEELASALR-PALRGE--------RPSNVLIYGPTGTGKTAVAKYVLEEleeeaeergVDVRVVYVncrqastryrV 102

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126131656 246 GSELIQKyLGDGP----------RLCRQIFQIAGEHAPSIVFI-DEIDAIGTKRYEstsggereiqrtmlELLNQL---D 311
Cdd:COG1474  103 LSRILEE-LGSGEdipstglstdELFDRLYEALDERDGVLVVVlDEIDYLVDDEGD--------------DLLYQLlraN 167

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126131656 312 GFDDRGDIKVIMATNKI---ESLDPALIRPGRiDRKILFENPDANTKKKILTiHTSKMSLADDVnLDELVTSK-DDLSGA 387
Cdd:COG1474  168 EELEGARVGVIGISNDLeflENLDPRVKSSLG-EEEIVFPPYDADELRDILE-DRAELAFYDGV-LSDEVIPLiAALAAQ 244

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|.
gi 126131656 388 DI----KAICT--EAGLLALRERRMQVKADDFKSAKERVLKNKVEENLEGL 432
Cdd:COG1474  245 EHgdarKAIDLlrVAGEIAEREGSDRVTEEHVREAREKIERDRLLEVLRGL 295
TIGR02928 TIGR02928
orc1/cdc6 family replication initiation protein; Members of this protein family are found ...
 181-432 1.35e-09

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: 59.57  E-value: 1.35e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126131656  181 IGGLESQIQEIKEAvelplthpeLYEEMGIKPPKGVILYGAPGTGKTLLAKAVANQ----TSATFLRI------------ 244
Cdd:TIGR02928  17 IVHRDEQIEELAKA---------LRPILRGSRPSNVFIYGKTGTGKTAVTKYVMKEleeaAEDRDVRVvtvyvncqildt 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126131656  245 ---VGSELIQKYLGDGP----------RLCRQIFQIAGEHAPSIVFI-DEIDAIgtkryeSTSGGEREIQRTMLELLNQL 310
Cdd:TIGR02928  88 lyqVLVELANQLRGSGEevpttglstsEVFRRLYKELNERGDSLIIVlDEIDYL------VGDDDDLLYQLSRARSNGDL 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126131656  311 DGfddrGDIKVIMATNKI---ESLDPAlIRPGRIDRKILFENPDANTKKKILTiHTSKMSLADDVNLDELVTSKDDLSGA 387
Cdd:TIGR02928 162 DN----AKVGVIGISNDLkfrENLDPR-VKSSLCEEEIIFPPYDAEELRDILE-NRAEKAFYDGVLDDGVIPLCAALAAQ 235

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|.
gi 126131656  388 DI----KAICT--EAGLLALRERRMQVKADDFKSAKERVLKNKVEENLEGL 432
Cdd:TIGR02928 236 EHgdarKAIDLlrVAGEIAEREGAERVTEDHVEKAQEKIEKDRLLELIRGL 286
RecA-like_Ycf2 cd19505
ATPase domain of plant YCF2; Ycf2 is a chloroplast ATPase which has an essential function; ...
 207-345 2.01e-08

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: 53.15  E-value: 2.01e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126131656 207 EMGIKPPKGVILYGAPGTGKTLLAKAVANQTSATFLRIVGSELIQ---KYLGDGPRLCRQI-----------FQIAGEHA 272
Cdd:cd19505    6 RLGLSPSKGILLIGSIETGRSYLIKSLAANSYVPLIRISLNKLLYnkpDFGNDDWIDGMLIlkeslhrlnlqFELAKAMS 85

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 126131656 273 PSIVFIDEIDAIGTKRYESTSGGEReiqRTMLELLNQLDGFDDRGD----IKVIMATNKIESLDPALIRPGRIDRKI 345
Cdd:cd19505   86 PCIIWIPNIHELNVNRSTQNLEEDP---KLLLGLLLNYLSRDFEKSstrnILVIASTHIPQKVDPALIAPNRLDTCI 159
RecA-like_ATAD3-like cd19512
ATPase domains of ATPase AAA-domain protein 3A (ATAD3A), -3B, and -3C, and similar ATPase ...
 184-347 4.89e-08

ATPase domains of ATPase AAA-domain protein 3A (ATAD3A), -3B, and -3C, and similar ATPase domains; ATPase AAA-domain protein 3 (ATAD3) is a ubiquitously expressed mitochondrial protein involved in mitochondrial dynamics, DNA-nucleoid structural organization, cholesterol transport and steroidogenesis. The ATAD3 gene family in human comprises three paralog genes: ATAD3A, ATAD3B and ATAD3C. This subfamily belongs to the RecA-like NTPase family which includes the NTP binding domain of F1 and V1 H(+)ATPases, DnaB and related helicases as well as bacterial RecA and related eukaryotic and archaeal recombinases. The RecA-like NTPase family also includes bacterial conjugation proteins and related DNA transfer proteins involved in type II and type IV secretion.


Pssm-ID: 410920 [Multi-domain]  Cd Length: 150  Bit Score: 52.14  E-value: 4.89e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126131656 184 LESQIQEIKEAVELPLTHPELYeemgikppKGVILYGAPGTGKTLLAKAVANQTSATFLRIVGSELIQkyLG-DGPRLCR 262
Cdd:cd19512    1 LEARVRDIAIATRNTKKNKGLY--------RNILFYGPPGTGKTLFAKKLALHSGMDYAIMTGGDVAP--MGrEGVTAIH 70

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126131656 263 QIFQIAGEHAPS-IVFIDEIDAIGTKRyesTSGGEREIQRTMLELLNQLDGfDDRGDIKVIMATNKIESLDPALirPGRI 341
Cdd:cd19512   71 KVFDWANTSRRGlLLFVDEADAFLRKR---STEKISEDLRAALNAFLYRTG-EQSNKFMLVLASNQPEQFDWAI--NDRI 144


                 ....*.
gi 126131656 342 DRKILF 347
Cdd:cd19512  145 DEMVEF 150
RarA COG2256
Replication-associated recombination protein RarA (DNA-dependent ATPase) [Replication, ...
 216-281 1.88e-07

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


Pssm-ID: 441857 [Multi-domain]  Cd Length: 439  Bit Score: 53.14  E-value: 1.88e-07
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 126131656 216 VILYGAPGTGKTLLAKAVANQTSATFLRI--VGS---ELiqkylgdgprlcRQIFQIAGEHA----PSIVFIDEI 281
Cdd:COG2256   52 MILWGPPGTGKTTLARLIANATDAEFVALsaVTSgvkDI------------REVIEEARERRaygrRTILFVDEI 114
PRK13342 PRK13342
recombination factor protein RarA; Reviewed
 216-281 5.43e-07

recombination factor protein RarA; Reviewed


Pssm-ID: 237355 [Multi-domain]  Cd Length: 413  Bit Score: 51.62  E-value: 5.43e-07
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 126131656 216 VILYGAPGTGKTLLAKAVANQTSATFLRI--VGS---ELiqkylgdgprlcRQIFQIAGEHAPS----IVFIDEI 281
Cdd:PRK13342  39 MILWGPPGTGKTTLARIIAGATDAPFEALsaVTSgvkDL------------REVIEEARQRRSAgrrtILFIDEI 101
RecA-like_HslU cd19498
ATP-dependent protease ATPase subunit HslU; HslU is a component of the ATP-dependent protease ...
 213-307 5.05e-06

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: 46.60  E-value: 5.05e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126131656 213 PKGVILYGAPGTGKTLLAKAVANQTSATFLRIVGSELIQ-KYLGdgprlcRQIFQIAGEHAPSIVFIDEIDAIGTKRYES 291
Cdd:cd19498   46 PKNILMIGPTGVGKTEIARRLAKLAGAPFIKVEATKFTEvGYVG------RDVESIIRDLVEGIVFIDEIDKIAKRGGSS 119

                         90
                 ....*....|....*..
gi 126131656 292 TSGGERE-IQRTMLELL 307
Cdd:cd19498  120 GPDVSREgVQRDLLPIV 136
MoxR COG0714
MoxR-like ATPase [General function prediction only]; MoxR-like ATPase is part of the Pathway ...
 216-282 8.32e-06

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


Pssm-ID: 440478 [Multi-domain]  Cd Length: 292  Bit Score: 47.47  E-value: 8.32e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126131656 216 VILYGAPGTGKTLLAKAVANQTSATFLRI-----------VGSELIQKYLGD-----GPrlcrqIFQiagehapSIVFID 279
Cdd:COG0714   34 LLLEGVPGVGKTTLAKALARALGLPFIRIqftpdllpsdiLGTYIYDQQTGEfefrpGP-----LFA-------NVLLAD 101


                 ...
gi 126131656 280 EID 282
Cdd:COG0714  102 EIN 104
AAA_5 pfam07728
AAA domain (dynein-related subfamily); This Pfam entry includes some of the AAA proteins not ...
 215-337 1.24e-05

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


Pssm-ID: 400191 [Multi-domain]  Cd Length: 135  Bit Score: 44.59  E-value: 1.24e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126131656  215 GVILYGAPGTGKTLLAKAVANQTS-ATFLRIVGS------ELIQKYL--GDGPRLCRQIFQIAGEHApSIVFIDEIDAIg 285
Cdd:pfam07728   1 GVLLVGPPGTGKTELAERLAAALSnRPVFYVQLTrdtteeDLFGRRNidPGGASWVDGPLVRAAREG-EIAVLDEINRA- 78

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 126131656  286 tkryestsggEREIQRTMLELLN-----QLDGF----DDRGDIKVIMATN----KIESLDPALIR 337
Cdd:pfam07728  79 ----------NPDVLNSLLSLLDerrllLPDGGelvkAAPDGFRLIATMNpldrGLNELSPALRS 133
DUF815 pfam05673
Protein of unknown function (DUF815); This family consists of several bacterial proteins of ...
 179-279 1.78e-05

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: 45.99  E-value: 1.78e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126131656  179 ADIGGLESQIQEIKEAVELPLTHpelyeemgiKPPKGVILYGAPGTGKTLLAKAVANQTSATFLRIVgsELIQKYLGDGP 258
Cdd:pfam05673  28 DDLVGIERQKEALIRNTRRFLAG---------LPANNVLLWGARGTGKSSLVKALLNEYADQGLRLI--EVDKEDLGDLP 96

                          90       100
                  ....*....|....*....|.
gi 126131656  259 RLCRqifQIAGEHAPSIVFID 279
Cdd:pfam05673  97 DLVD---LLRDRPYRFILFCD 114
RecA-like_superfamily cd01120
RecA-like_NTPases; RecA-like NTPases. This superfamily includes the NTP binding domain of F1 ...
 216-310 1.99e-05

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


Pssm-ID: 410865 [Multi-domain]  Cd Length: 119  Bit Score: 43.65  E-value: 1.99e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126131656 216 VILYGAPGTGKTLLAKAVANQTSATFLRIVGSELIQKYLgdgprlcRQIFQIAGEHAPSIVFIDEIDAIGTKRYESTSGG 295
Cdd:cd01120    1 ILITGPPGSGKTTLLLQFAEQALLSDEPVIFISFLDTIL-------EAIEDLIEEKKLDIIIIDSLSSLARASQGDRSSE 73

                         90
                 ....*....|....*
gi 126131656 296 EREIQRTMLELLNQL 310
Cdd:cd01120   74 LLEDLAKLLRAARNT 88
AAA_2 pfam07724
AAA domain (Cdc48 subfamily); This Pfam entry includes some of the AAA proteins not detected ...
 213-307 5.00e-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: 43.72  E-value: 5.00e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126131656  213 PKGVILY-GAPGTGKTLLAKAVANQ---TSATFLRIVGSELIQKYL--------------GDGPRLCRQIFQiageHAPS 274
Cdd:pfam07724   2 PIGSFLFlGPTGVGKTELAKALAELlfgDERALIRIDMSEYMEEHSvsrligappgyvgyEEGGQLTEAVRR----KPYS 77

                          90       100       110
                  ....*....|....*....|....*....|...
gi 126131656  275 IVFIDEIDAIGtkryestsggeREIQRTMLELL 307
Cdd:pfam07724  78 IVLIDEIEKAH-----------PGVQNDLLQIL 99
PRK04195 PRK04195
replication factor C large subunit; Provisional
 211-299 1.09e-04

replication factor C large subunit; Provisional


Pssm-ID: 235250 [Multi-domain]  Cd Length: 482  Bit Score: 44.53  E-value: 1.09e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126131656 211 KPPKGVILYGAPGTGKTLLAKAVANqtsaTFlrivGSELI------QKYLGDgprlcrqIFQIAGEHAPS---------I 275
Cdd:PRK04195  37 KPKKALLLYGPPGVGKTSLAHALAN----DY----GWEVIelnasdQRTADV-------IERVAGEAATSgslfgarrkL 101

                         90       100
                 ....*....|....*....|....*
gi 126131656 276 VFIDEIDAI-GTKRYestsGGEREI 299
Cdd:PRK04195 102 ILLDEVDGIhGNEDR----GGARAI 122
McrB COG1401
5-methylcytosine-specific restriction endonuclease McrBC, GTP-binding regulatory subunit McrB ...
 210-281 1.47e-04

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


Pssm-ID: 441011 [Multi-domain]  Cd Length: 477  Bit Score: 43.99  E-value: 1.47e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126131656 210 IKPPKGVILYGAPGTGKTLLAKAVANQTSAT---FLRIV-------GSELIQKY----------LGDGP--RLCRQifqi 267
Cdd:COG1401  218 LKTKKNVILAGPPGTGKTYLARRLAEALGGEdngRIEFVqfhpswsYEDFLLGYrpsldegkyePTPGIflRFCLK---- 293

                         90
                 ....*....|....*.
gi 126131656 268 AGEH--APSIVFIDEI 281
Cdd:COG1401  294 AEKNpdKPYVLIIDEI 309
RecA-like_ClpB_Hsp104-like cd19499
Chaperone protein ClpB/Hsp104 subfamily; Bacterial Caseinolytic peptidase B (ClpB) and ...
 211-347 1.77e-04

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: 42.16  E-value: 1.77e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126131656 211 KPPKGVILYGAPGTGKTLLAKAVA---NQTSATFLRIVGSELIQKY-----LGDGP--RLCRQIFQIAGE---HAPSIVF 277
Cdd:cd19499   39 RPIGSFLFLGPTGVGKTELAKALAellFGDEDNLIRIDMSEYMEKHsvsrlIGAPPgyVGYTEGGQLTEAvrrKPYSVVL 118

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 126131656 278 IDEIDAigtkryestsgGEREIQRTMLELLNqlDGF--DDRG---DIK---VIMATNkieSLDPALIrpGRIDRKILF 347
Cdd:cd19499  119 LDEIEK-----------AHPDVQNLLLQVLD--DGRltDSHGrtvDFKntiIIMTSN---HFRPEFL--NRIDEIVVF 178
T7SS_EccA TIGR03922
type VII secretion AAA-ATPase EccA; This model represents the AAA family ATPase, EccA, of the ...
 183-376 2.98e-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: 2.98e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126131656  183 GLES---QIQEIKEAVELPLTHpelyEEMGIKPP---KGVILYGAPGTGKTLLAKAVANQTSA-TFLR------IVGSEL 249
Cdd:TIGR03922 280 GLERvkrQVAALKSSTAMALAR----AERGLPVAqtsNHMLFAGPPGTGKTTIARVVAKIYCGlGVLRkplvreVSRADL 355

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126131656  250 IQKYLGD-GPRLCRQIFQIAGehapSIVFIDEIDAIGTKRYESTSGGEREIQRTMLELLNqldgfDDRGDIKVIMA---- 324
Cdd:TIGR03922 356 IGQYIGEsEAKTNEIIDSALG----GVLFLDEAYTLVETGYGQKDPFGLEAIDTLLARME-----NDRDRLVVIGAgyrk 426

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 126131656  325 -TNKIESLDPALirPGRIDRKILFenpDANTKKKILTIhTSKMSLADDVNLDE 376
Cdd:TIGR03922 427 dLDKFLEVNEGL--RSRFTRVIEF---PSYSPDELVEI-ARRMATERDSVLDD 473
44 PHA02544
clamp loader, small subunit; Provisional
 217-335 3.53e-04

clamp loader, small subunit; Provisional


Pssm-ID: 222866 [Multi-domain]  Cd Length: 316  Bit Score: 42.28  E-value: 3.53e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126131656 217 ILY-GAPGTGKTLLAKAVANQTSATFLRIVGSEL-IQKYLGDGPRLCRQIFQIAGehaPSIVFIDEIDAIGTKryestsg 294
Cdd:PHA02544  46 LLHsPSPGTGKTTVAKALCNEVGAEVLFVNGSDCrIDFVRNRLTRFASTVSLTGG---GKVIIIDEFDRLGLA------- 115

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 126131656 295 gerEIQRTMLELLNQLDgfddrGDIKVIMATNKIESLDPAL 335
Cdd:PHA02544 116 ---DAQRHLRSFMEAYS-----KNCSFIITANNKNGIIEPL 148
RecA-like_Lon cd19500
lon protease homolog 2 peroxisomal; Lon protease (also known as Lon peptidase) is an ...
 214-285 6.26e-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: 40.62  E-value: 6.26e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126131656 214 KGVIL--YGAPGTGKTLLAKAVANQTSATFLRI-VG-----SELI---QKYLGDGPRLCRQIFQIAGEHAPSIVfIDEID 282
Cdd:cd19500   36 KGPILclVGPPGVGKTSLGKSIARALGRKFVRIsLGgvrdeAEIRghrRTYVGAMPGRIIQALKKAGTNNPVFL-LDEID 114


                 ...
gi 126131656 283 AIG 285
Cdd:cd19500  115 KIG 117
DnaC COG1484
DNA replication protein DnaC [Replication, recombination and repair];
210-236 8.24e-04

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


Pssm-ID: 441093 [Multi-domain]  Cd Length: 242  Bit Score: 40.92  E-value: 8.24e-04
                         10        20
                 ....*....|....*....|....*..
gi 126131656 210 IKPPKGVILYGAPGTGKTLLAKAVANQ 236
Cdd:COG1484   96 IERGENLILLGPPGTGKTHLAIALGHE 122
PRK13341 PRK13341
AAA family ATPase;
217-244 8.46e-04

AAA family ATPase;


Pssm-ID: 237354 [Multi-domain]  Cd Length: 725  Bit Score: 41.58  E-value: 8.46e-04
                         10        20
                 ....*....|....*....|....*...
gi 126131656 217 ILYGAPGTGKTLLAKAVANQTSATFLRI 244
Cdd:PRK13341  56 ILYGPPGVGKTTLARIIANHTRAHFSSL 83
ruvB PRK00080
Holliday junction branch migration DNA helicase RuvB;
216-281 1.69e-03

Holliday junction branch migration DNA helicase RuvB;


Pssm-ID: 234619 [Multi-domain]  Cd Length: 328  Bit Score: 40.11  E-value: 1.69e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 126131656 216 VILYGAPGTGKTLLAKAVANQTSATfLRIVGSELIQKyLGDgprlcrqifqIAG------EHapSIVFIDEI 281
Cdd:PRK00080  54 VLLYGPPGLGKTTLANIIANEMGVN-IRITSGPALEK-PGD----------LAAiltnleEG--DVLFIDEI 111
IS21_help_AAA NF038214
IS21-like element helper ATPase IstB; This protein family model resembles PF01695, but was ...
 216-293 2.11e-03

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


Pssm-ID: 439516  Cd Length: 232  Bit Score: 39.38  E-value: 2.11e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126131656 216 VILYGAPGTGKTLLAKAVANQ-----TSATFLRIvgSELIQKYL---GDGpRLCRQIFQIAGehaPSIVFIDEI-----D 282
Cdd:NF038214  93 VLLLGPPGTGKTHLAIALGYAacrqgYRVRFTTA--ADLVEQLAqarADG-RLGRLLRRLAR---YDLLIIDELgylpfS 166

                         90
                 ....*....|....*....
gi 126131656 283 AIGT--------KRYESTS 293
Cdd:NF038214 167 REGAnllfeliaDRYERGS 185
COG2842 COG2842
Bacteriophage DNA transposition protein, AAA+ family ATPase [Mobilome: prophages, transposons]; ...
 216-282 2.12e-03

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


Pssm-ID: 442090 [Multi-domain]  Cd Length: 254  Bit Score: 39.55  E-value: 2.12e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126131656 216 VILYGAPGTGKTLLAKAVANQ-------------TSATFLRIVGSEL-IQKYLGDGPRLCRQI-FQIAGEHAPsiVFIDE 280
Cdd:COG2842   53 GVVYGESGVGKTTAAREYANRnpnviyvtaspswTSKELLEELAEELgIPAPPGTIADLRDRIlERLAGTGRL--LIIDE 130


                 ..
gi 126131656 281 ID 282
Cdd:COG2842  131 AD 132
AAA_22 pfam13401
AAA domain;
216-324 2.74e-03

AAA domain;


Pssm-ID: 379165 [Multi-domain]  Cd Length: 129  Bit Score: 37.71  E-value: 2.74e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126131656  216 VILYGAPGTGKTLLAKAVANQ-----------------TSATFLRIVGSEL--IQKYLGDGPRLCRQIFQIAGEHAPSIV 276
Cdd:pfam13401   8 LVLTGESGTGKTTLLRRLLEQlpevrdsvvfvdlpsgtSPKDLLRALLRALglPLSGRLSKEELLAALQQLLLALAVAVV 87

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 126131656  277 F-IDEIDAigtkryestsggereIQRTMLELLNQLDGFdDRGDIKVIMA 324
Cdd:pfam13401  88 LiIDEAQH---------------LSLEALEELRDLLNL-SSKLLQLILV 120
RecA-like_ClpX cd19497
ATP-dependent Clp protease ATP-binding subunit ClpX; ClpX is a component of the ATP-dependent ...
 216-287 2.80e-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: 39.12  E-value: 2.80e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126131656 216 VILYGAPGTGKTLLAK----------AVANQTSATFLRIVG-------SELIQKYLGDGPRLCRqifqiagehapSIVFI 278
Cdd:cd19497   53 ILLIGPTGSGKTLLAQtlakildvpfAIADATTLTEAGYVGedvenilLKLLQAADYDVERAQR-----------GIVYI 121


                 ....*....
gi 126131656 279 DEIDAIGTK 287
Cdd:cd19497  122 DEIDKIARK 130
PRK08116 PRK08116
hypothetical protein; Validated
 205-267 2.86e-03

hypothetical protein; Validated


Pssm-ID: 236153 [Multi-domain]  Cd Length: 268  Bit Score: 39.23  E-value: 2.86e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 126131656 205 YEEMGiKPPKGVILYGAPGTGKTLLAKAVANqtsatflrivgsELIQKYLgdgPRLCRQIFQI 267
Cdd:PRK08116 107 FEEMK-KENVGLLLWGSVGTGKTYLAACIAN------------ELIEKGV---PVIFVNFPQL 153
Prot_ATP_OB_N pfam17758
Proteasomal ATPase OB N-terminal domain; This is N-terminal oligonucleotide binding (OB) ...
 102-157 4.44e-03

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


Pssm-ID: 436018  Cd Length: 62  Bit Score: 35.60  E-value: 4.44e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 126131656  102 SIGTLEEIIDDDHAIVSSTAGSEYYVSIMSFVDKGLLEPGCSVLLHHKTVsVVGVL 157
Cdd:pfam17758   1 TYGTFLRVDDDDGTADVSVGGRRMRVAVSPTVDASELRPGQQVRLNEALV-VVGAL 55
COG0645 COG0645
Predicted kinase, contains AAA domain [General function prediction only];
216-244 6.26e-03

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


Pssm-ID: 440410 [Multi-domain]  Cd Length: 164  Bit Score: 37.20  E-value: 6.26e-03
                         10        20
                 ....*....|....*....|....*....
gi 126131656 216 VILYGAPGTGKTLLAKAVANQTSATFLRI 244
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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