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Conserved domains on  [gi|1148885657|gb|AQS27602|]
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hypothetical protein [Mus musculus]

Protein Classification

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
PRK03992 super family cl32052
proteasome-activating nucleotidase; Provisional
34-410 2.49e-178

proteasome-activating nucleotidase; Provisional


The actual alignment was detected with superfamily member PRK03992:

Pssm-ID: 179699 [Multi-domain]  Cd Length: 389  Bit Score: 502.44  E-value: 2.49e-178
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148885657  34 YLSKIEELQLIVNDKSQNLRRLQAQRNELNAKVRLLREELQLLQEQGSYVGEVVRAMDKKKVLVKVHPEGKFVVDVDKNI 113
Cdd:PRK03992    6 LEERNSELEEQIRQLELKLRDLEAENEKLERELERLKSELEKLKSPPLIVATVLEVLDDGRVVVKSSGGPQFLVNVSPFI 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148885657 114 DINDVTPNCRVALRNDSYTLHKILPNKVDPLVSLMMVEKVPDSTYEMIGGLDKQIKEIKEVIELPVKHPELFEALGIAQP 193
Cdd:PRK03992   86 DREKLKPGARVALNQQSLAIVEVLPSEKDPRVQAMEVIESPNVTYEDIGGLEEQIREVREAVELPLKKPELFEEVGIEPP 165
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148885657 194 KGVLLYGPPGTGKTLLARAVAHHTDCTFIRVSGSELVQKFIGEGARMVRELFVMAREHAPSIIFMDEIDSIGSSRLEGGS 273
Cdd:PRK03992  166 KGVLLYGPPGTGKTLLAKAVAHETNATFIRVVGSELVQKFIGEGARLVRELFELAREKAPSIIFIDEIDAIAAKRTDSGT 245
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148885657 274 GGDSEVQRTMLELLNQLDGFEATKNIKVIMATNRIDILDSALLRPGRIDRKIEFPPPNEEARLDILKIHSRKMNLTRGIN 353
Cdd:PRK03992  246 SGDREVQRTLMQLLAEMDGFDPRGNVKIIAATNRIDILDPAILRPGRFDRIIEVPLPDEEGRLEILKIHTRKMNLADDVD 325
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1148885657 354 LRKIAELMPGASGAEVKGVCTEAGMYALRERRVHVTQEDFEMAVAKVMQKDSEKNMS 410
Cdd:PRK03992  326 LEELAELTEGASGADLKAICTEAGMFAIRDDRTEVTMEDFLKAIEKVMGKEEKDSME 382
 
Name Accession Description Interval E-value
PRK03992 PRK03992
proteasome-activating nucleotidase; Provisional
34-410 2.49e-178

proteasome-activating nucleotidase; Provisional


Pssm-ID: 179699 [Multi-domain]  Cd Length: 389  Bit Score: 502.44  E-value: 2.49e-178
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148885657  34 YLSKIEELQLIVNDKSQNLRRLQAQRNELNAKVRLLREELQLLQEQGSYVGEVVRAMDKKKVLVKVHPEGKFVVDVDKNI 113
Cdd:PRK03992    6 LEERNSELEEQIRQLELKLRDLEAENEKLERELERLKSELEKLKSPPLIVATVLEVLDDGRVVVKSSGGPQFLVNVSPFI 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148885657 114 DINDVTPNCRVALRNDSYTLHKILPNKVDPLVSLMMVEKVPDSTYEMIGGLDKQIKEIKEVIELPVKHPELFEALGIAQP 193
Cdd:PRK03992   86 DREKLKPGARVALNQQSLAIVEVLPSEKDPRVQAMEVIESPNVTYEDIGGLEEQIREVREAVELPLKKPELFEEVGIEPP 165
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148885657 194 KGVLLYGPPGTGKTLLARAVAHHTDCTFIRVSGSELVQKFIGEGARMVRELFVMAREHAPSIIFMDEIDSIGSSRLEGGS 273
Cdd:PRK03992  166 KGVLLYGPPGTGKTLLAKAVAHETNATFIRVVGSELVQKFIGEGARLVRELFELAREKAPSIIFIDEIDAIAAKRTDSGT 245
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148885657 274 GGDSEVQRTMLELLNQLDGFEATKNIKVIMATNRIDILDSALLRPGRIDRKIEFPPPNEEARLDILKIHSRKMNLTRGIN 353
Cdd:PRK03992  246 SGDREVQRTLMQLLAEMDGFDPRGNVKIIAATNRIDILDPAILRPGRFDRIIEVPLPDEEGRLEILKIHTRKMNLADDVD 325
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1148885657 354 LRKIAELMPGASGAEVKGVCTEAGMYALRERRVHVTQEDFEMAVAKVMQKDSEKNMS 410
Cdd:PRK03992  326 LEELAELTEGASGADLKAICTEAGMFAIRDDRTEVTMEDFLKAIEKVMGKEEKDSME 382
RPT1 COG1222
ATP-dependent 26S proteasome regulatory subunit [Posttranslational modification, protein ...
150-407 9.89e-141

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


Pssm-ID: 440835 [Multi-domain]  Cd Length: 326  Bit Score: 404.39  E-value: 9.89e-141
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148885657 150 VEKVPDSTYEMIGGLDKQIKEIKEVIELPVKHPELFEALGIAQPKGVLLYGPPGTGKTLLARAVAHHTDCTFIRVSGSEL 229
Cdd:COG1222    69 PAESPDVTFDDIGGLDEQIEEIREAVELPLKNPELFRKYGIEPPKGVLLYGPPGTGKTLLAKAVAGELGAPFIRVRGSEL 148
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148885657 230 VQKFIGEGARMVRELFVMAREHAPSIIFMDEIDSIGSSRLEGGSGGdsEVQRTMLELLNQLDGFEATKNIKVIMATNRID 309
Cdd:COG1222   149 VSKYIGEGARNVREVFELAREKAPSIIFIDEIDAIAARRTDDGTSG--EVQRTVNQLLAELDGFESRGDVLIIAATNRPD 226
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148885657 310 ILDSALLRPGRIDRKIEFPPPNEEARLDILKIHSRKMNLTRGINLRKIAELMPGASGAEVKGVCTEAGMYALRERRVHVT 389
Cdd:COG1222   227 LLDPALLRPGRFDRVIEVPLPDEEAREEILKIHLRDMPLADDVDLDKLAKLTEGFSGADLKAIVTEAGMFAIREGRDTVT 306
                         250
                  ....*....|....*...
gi 1148885657 390 QEDFEMAVAKVMQKDSEK 407
Cdd:COG1222   307 MEDLEKAIEKVKKKTETA 324
RecA-like_PAN_like cd19502
proteasome activating nucleotidase PAN and related proteasome subunits; This subfamily ...
157-327 1.44e-124

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: 357.42  E-value: 1.44e-124
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148885657 157 TYEMIGGLDKQIKEIKEVIELPVKHPELFEALGIAQPKGVLLYGPPGTGKTLLARAVAHHTDCTFIRVSGSELVQKFIGE 236
Cdd:cd19502     1 TYEDIGGLDEQIREIREVVELPLKHPELFEELGIEPPKGVLLYGPPGTGKTLLAKAVANHTDATFIRVVGSELVQKYIGE 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148885657 237 GARMVRELFVMAREHAPSIIFMDEIDSIGSSRLEGGSGGDSEVQRTMLELLNQLDGFEATKNIKVIMATNRIDILDSALL 316
Cdd:cd19502    81 GARLVRELFEMAREKAPSIIFIDEIDAIGAKRFDSGTGGDREVQRTMLELLNQLDGFDPRGNIKVIMATNRPDILDPALL 160
                         170
                  ....*....|.
gi 1148885657 317 RPGRIDRKIEF 327
Cdd:cd19502   161 RPGRFDRKIEF 171
FtsH_fam TIGR01241
ATP-dependent metalloprotease FtsH; HflB(FtsH) is a pleiotropic protein required for correct ...
146-413 1.89e-86

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: 271.47  E-value: 1.89e-86
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148885657 146 SLMMVEKVPDSTYEMIGGLDKQIKEIKEVIELpVKHPELFEALGIAQPKGVLLYGPPGTGKTLLARAVAHHTDCTFIRVS 225
Cdd:TIGR01241  42 AKLLNEEKPKVTFKDVAGIDEAKEELMEIVDF-LKNPSKFTKLGAKIPKGVLLVGPPGTGKTLLAKAVAGEAGVPFFSIS 120
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148885657 226 GSELVQKFIGEGARMVRELFVMAREHAPSIIFMDEIDSIGSSRLEGGSGGDSEVQRTMLELLNQLDGFEATKNIKVIMAT 305
Cdd:TIGR01241 121 GSDFVEMFVGVGASRVRDLFEQAKKNAPCIIFIDEIDAVGRQRGAGLGGGNDEREQTLNQLLVEMDGFGTNTGVIVIAAT 200
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148885657 306 NRIDILDSALLRPGRIDRKIEFPPPNEEARLDILKIHSRKMNLTRGINLRKIAELMPGASGAEVKGVCTEAGMYALRERR 385
Cdd:TIGR01241 201 NRPDVLDPALLRPGRFDRQVVVDLPDIKGREEILKVHAKNKKLAPDVDLKAVARRTPGFSGADLANLLNEAALLAARKNK 280
                         250       260
                  ....*....|....*....|....*...
gi 1148885657 386 VHVTQEDFEMAVAKVMQKDSEKNMSIKK 413
Cdd:TIGR01241 281 TEITMNDIEEAIDRVIAGPEKKSRVISE 308
AAA pfam00004
ATPase family associated with various cellular activities (AAA); AAA family proteins often ...
196-328 3.05e-53

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


Pssm-ID: 459627 [Multi-domain]  Cd Length: 130  Bit Score: 173.55  E-value: 3.05e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148885657 196 VLLYGPPGTGKTLLARAVAHHTDCTFIRVSGSELVQKFIGEGARMVRELFVMAREHAPSIIFMDEIDSIGSSRlegGSGG 275
Cdd:pfam00004   1 LLLYGPPGTGKTTLAKAVAKELGAPFIEISGSELVSKYVGESEKRLRELFEAAKKLAPCVIFIDEIDALAGSR---GSGG 77
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1148885657 276 DSEVQRTMLELLNQLDGFE-ATKNIKVIMATNRIDILDSALLrpGRIDRKIEFP 328
Cdd:pfam00004  78 DSESRRVVNQLLTELDGFTsSNSKVIVIAATNRPDKLDPALL--GRFDRIIEFP 129
AAA smart00382
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ...
192-331 3.89e-20

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: 86.27  E-value: 3.89e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148885657  192 QPKGVLLYGPPGTGKTLLARAVAHHTDCT---FIRVSGSEL--------------VQKFIGEGARMVRELFVMAREHAPS 254
Cdd:smart00382   1 PGEVILIVGPPGSGKTTLARALARELGPPgggVIYIDGEDIleevldqllliivgGKKASGSGELRLRLALALARKLKPD 80
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1148885657  255 IIFMDEIDSIGSSRleggsggdSEVQRTMLELLNQLDGFEATKNIKVIMATNRIDILDSALLRPgRIDRKIEFPPPN 331
Cdd:smart00382  81 VLILDEITSLLDAE--------QEALLLLLEELRLLLLLKSEKNLTVILTTNDEKDLGPALLRR-RFDRRIVLLLIL 148
IS21_help_AAA NF038214
IS21-like element helper ATPase IstB; This protein family model resembles PF01695, but was ...
190-215 9.22e-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: 37.45  E-value: 9.22e-03
                          10        20
                  ....*....|....*....|....*.
gi 1148885657 190 IAQPKGVLLYGPPGTGKTLLARAVAH 215
Cdd:NF038214   87 IERAENVLLLGPPGTGKTHLAIALGY 112
 
Name Accession Description Interval E-value
PRK03992 PRK03992
proteasome-activating nucleotidase; Provisional
34-410 2.49e-178

proteasome-activating nucleotidase; Provisional


Pssm-ID: 179699 [Multi-domain]  Cd Length: 389  Bit Score: 502.44  E-value: 2.49e-178
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148885657  34 YLSKIEELQLIVNDKSQNLRRLQAQRNELNAKVRLLREELQLLQEQGSYVGEVVRAMDKKKVLVKVHPEGKFVVDVDKNI 113
Cdd:PRK03992    6 LEERNSELEEQIRQLELKLRDLEAENEKLERELERLKSELEKLKSPPLIVATVLEVLDDGRVVVKSSGGPQFLVNVSPFI 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148885657 114 DINDVTPNCRVALRNDSYTLHKILPNKVDPLVSLMMVEKVPDSTYEMIGGLDKQIKEIKEVIELPVKHPELFEALGIAQP 193
Cdd:PRK03992   86 DREKLKPGARVALNQQSLAIVEVLPSEKDPRVQAMEVIESPNVTYEDIGGLEEQIREVREAVELPLKKPELFEEVGIEPP 165
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148885657 194 KGVLLYGPPGTGKTLLARAVAHHTDCTFIRVSGSELVQKFIGEGARMVRELFVMAREHAPSIIFMDEIDSIGSSRLEGGS 273
Cdd:PRK03992  166 KGVLLYGPPGTGKTLLAKAVAHETNATFIRVVGSELVQKFIGEGARLVRELFELAREKAPSIIFIDEIDAIAAKRTDSGT 245
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148885657 274 GGDSEVQRTMLELLNQLDGFEATKNIKVIMATNRIDILDSALLRPGRIDRKIEFPPPNEEARLDILKIHSRKMNLTRGIN 353
Cdd:PRK03992  246 SGDREVQRTLMQLLAEMDGFDPRGNVKIIAATNRIDILDPAILRPGRFDRIIEVPLPDEEGRLEILKIHTRKMNLADDVD 325
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1148885657 354 LRKIAELMPGASGAEVKGVCTEAGMYALRERRVHVTQEDFEMAVAKVMQKDSEKNMS 410
Cdd:PRK03992  326 LEELAELTEGASGADLKAICTEAGMFAIRDDRTEVTMEDFLKAIEKVMGKEEKDSME 382
RPT1 COG1222
ATP-dependent 26S proteasome regulatory subunit [Posttranslational modification, protein ...
150-407 9.89e-141

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


Pssm-ID: 440835 [Multi-domain]  Cd Length: 326  Bit Score: 404.39  E-value: 9.89e-141
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148885657 150 VEKVPDSTYEMIGGLDKQIKEIKEVIELPVKHPELFEALGIAQPKGVLLYGPPGTGKTLLARAVAHHTDCTFIRVSGSEL 229
Cdd:COG1222    69 PAESPDVTFDDIGGLDEQIEEIREAVELPLKNPELFRKYGIEPPKGVLLYGPPGTGKTLLAKAVAGELGAPFIRVRGSEL 148
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148885657 230 VQKFIGEGARMVRELFVMAREHAPSIIFMDEIDSIGSSRLEGGSGGdsEVQRTMLELLNQLDGFEATKNIKVIMATNRID 309
Cdd:COG1222   149 VSKYIGEGARNVREVFELAREKAPSIIFIDEIDAIAARRTDDGTSG--EVQRTVNQLLAELDGFESRGDVLIIAATNRPD 226
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148885657 310 ILDSALLRPGRIDRKIEFPPPNEEARLDILKIHSRKMNLTRGINLRKIAELMPGASGAEVKGVCTEAGMYALRERRVHVT 389
Cdd:COG1222   227 LLDPALLRPGRFDRVIEVPLPDEEAREEILKIHLRDMPLADDVDLDKLAKLTEGFSGADLKAIVTEAGMFAIREGRDTVT 306
                         250
                  ....*....|....*...
gi 1148885657 390 QEDFEMAVAKVMQKDSEK 407
Cdd:COG1222   307 MEDLEKAIEKVKKKTETA 324
PTZ00361 PTZ00361
26 proteosome regulatory subunit 4-like protein; Provisional
83-403 3.21e-130

26 proteosome regulatory subunit 4-like protein; Provisional


Pssm-ID: 185575 [Multi-domain]  Cd Length: 438  Bit Score: 381.81  E-value: 3.21e-130
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148885657  83 VGEVVRAMDKKKVLVKVHPEGKFVVDVDKNIDINDVTPNCRVALRNDSYTLHKILPNKVDPLVSLMMVEKVPDSTYEMIG 162
Cdd:PTZ00361  107 VGTLEEIIDENHAIVSSSVGPEYYVNILSFVDKEQLEPGCSVLLHNKTHSVVGILLDEVDPLVSVMKVDKAPLESYADIG 186
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148885657 163 GLDKQIKEIKEVIELPVKHPELFEALGIAQPKGVLLYGPPGTGKTLLARAVAHHTDCTFIRVSGSELVQKFIGEGARMVR 242
Cdd:PTZ00361  187 GLEQQIQEIKEAVELPLTHPELYDDIGIKPPKGVILYGPPGTGKTLLAKAVANETSATFLRVVGSELIQKYLGDGPKLVR 266
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148885657 243 ELFVMAREHAPSIIFMDEIDSIGSSRLEGGSGGDSEVQRTMLELLNQLDGFEATKNIKVIMATNRIDILDSALLRPGRID 322
Cdd:PTZ00361  267 ELFRVAEENAPSIVFIDEIDAIGTKRYDATSGGEKEIQRTMLELLNQLDGFDSRGDVKVIMATNRIESLDPALIRPGRID 346
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148885657 323 RKIEFPPPNEEARLDILKIHSRKMNLTRGINLRKIAELMPGASGAEVKGVCTEAGMYALRERRVHVTQEDFEMAVAKVMQ 402
Cdd:PTZ00361  347 RKIEFPNPDEKTKRRIFEIHTSKMTLAEDVDLEEFIMAKDELSGADIKAICTEAGLLALRERRMKVTQADFRKAKEKVLY 426

                  .
gi 1148885657 403 K 403
Cdd:PTZ00361  427 R 427
RecA-like_PAN_like cd19502
proteasome activating nucleotidase PAN and related proteasome subunits; This subfamily ...
157-327 1.44e-124

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: 357.42  E-value: 1.44e-124
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148885657 157 TYEMIGGLDKQIKEIKEVIELPVKHPELFEALGIAQPKGVLLYGPPGTGKTLLARAVAHHTDCTFIRVSGSELVQKFIGE 236
Cdd:cd19502     1 TYEDIGGLDEQIREIREVVELPLKHPELFEELGIEPPKGVLLYGPPGTGKTLLAKAVANHTDATFIRVVGSELVQKYIGE 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148885657 237 GARMVRELFVMAREHAPSIIFMDEIDSIGSSRLEGGSGGDSEVQRTMLELLNQLDGFEATKNIKVIMATNRIDILDSALL 316
Cdd:cd19502    81 GARLVRELFEMAREKAPSIIFIDEIDAIGAKRFDSGTGGDREVQRTMLELLNQLDGFDPRGNIKVIMATNRPDILDPALL 160
                         170
                  ....*....|.
gi 1148885657 317 RPGRIDRKIEF 327
Cdd:cd19502   161 RPGRFDRKIEF 171
PTZ00454 PTZ00454
26S protease regulatory subunit 6B-like protein; Provisional
83-406 3.74e-121

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


Pssm-ID: 240423 [Multi-domain]  Cd Length: 398  Bit Score: 357.54  E-value: 3.74e-121
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148885657  83 VGEVVRAMDKKKVLVKVHPEGKFVVDVDKNIDINDVTPNCRVALRNDSYTLHKILPNKVDPLVSLMMVEKVPDSTYEMIG 162
Cdd:PTZ00454   69 IGQFLEMIDSNYGIVSSTSGSNYYVRILSTLNRELLKPNASVALHRHSHAVVDILPPEADSSIQLLQMSEKPDVTYSDIG 148
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148885657 163 GLDKQIKEIKEVIELPVKHPELFEALGIAQPKGVLLYGPPGTGKTLLARAVAHHTDCTFIRVSGSELVQKFIGEGARMVR 242
Cdd:PTZ00454  149 GLDIQKQEIREAVELPLTCPELYEQIGIDPPRGVLLYGPPGTGKTMLAKAVAHHTTATFIRVVGSEFVQKYLGEGPRMVR 228
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148885657 243 ELFVMAREHAPSIIFMDEIDSIGSSRLEGGSGGDSEVQRTMLELLNQLDGFEATKNIKVIMATNRIDILDSALLRPGRID 322
Cdd:PTZ00454  229 DVFRLARENAPSIIFIDEVDSIATKRFDAQTGADREVQRILLELLNQMDGFDQTTNVKVIMATNRADTLDPALLRPGRLD 308
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148885657 323 RKIEFPPPNEEARLDILKIHSRKMNLTRGINLRKIAELMPGASGAEVKGVCTEAGMYALRERRVHVTQEDFEMAVAKVMQ 402
Cdd:PTZ00454  309 RKIEFPLPDRRQKRLIFQTITSKMNLSEEVDLEDFVSRPEKISAADIAAICQEAGMQAVRKNRYVILPKDFEKGYKTVVR 388

                  ....
gi 1148885657 403 KDSE 406
Cdd:PTZ00454  389 KTDR 392
FtsH_fam TIGR01241
ATP-dependent metalloprotease FtsH; HflB(FtsH) is a pleiotropic protein required for correct ...
146-413 1.89e-86

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: 271.47  E-value: 1.89e-86
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148885657 146 SLMMVEKVPDSTYEMIGGLDKQIKEIKEVIELpVKHPELFEALGIAQPKGVLLYGPPGTGKTLLARAVAHHTDCTFIRVS 225
Cdd:TIGR01241  42 AKLLNEEKPKVTFKDVAGIDEAKEELMEIVDF-LKNPSKFTKLGAKIPKGVLLVGPPGTGKTLLAKAVAGEAGVPFFSIS 120
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148885657 226 GSELVQKFIGEGARMVRELFVMAREHAPSIIFMDEIDSIGSSRLEGGSGGDSEVQRTMLELLNQLDGFEATKNIKVIMAT 305
Cdd:TIGR01241 121 GSDFVEMFVGVGASRVRDLFEQAKKNAPCIIFIDEIDAVGRQRGAGLGGGNDEREQTLNQLLVEMDGFGTNTGVIVIAAT 200
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148885657 306 NRIDILDSALLRPGRIDRKIEFPPPNEEARLDILKIHSRKMNLTRGINLRKIAELMPGASGAEVKGVCTEAGMYALRERR 385
Cdd:TIGR01241 201 NRPDVLDPALLRPGRFDRQVVVDLPDIKGREEILKVHAKNKKLAPDVDLKAVARRTPGFSGADLANLLNEAALLAARKNK 280
                         250       260
                  ....*....|....*....|....*...
gi 1148885657 386 VHVTQEDFEMAVAKVMQKDSEKNMSIKK 413
Cdd:TIGR01241 281 TEITMNDIEEAIDRVIAGPEKKSRVISE 308
HflB COG0465
ATP-dependent Zn proteases [Posttranslational modification, protein turnover, chaperones];
148-401 2.12e-83

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


Pssm-ID: 440233 [Multi-domain]  Cd Length: 583  Bit Score: 266.13  E-value: 2.12e-83
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148885657 148 MMVEKVPDSTYEMIGGLDKQIKEIKEVIE-LpvKHPELFEALGIAQPKGVLLYGPPGTGKTLLARAVAHHTDCTFIRVSG 226
Cdd:COG0465   131 LYDEDKPKVTFDDVAGVDEAKEELQEIVDfL--KDPEKFTRLGAKIPKGVLLVGPPGTGKTLLAKAVAGEAGVPFFSISG 208
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148885657 227 SELVQKFIGEGARMVRELFVMAREHAPSIIFMDEIDSIGSSRLEGGSGGDSEVQRTmlelLNQL----DGFEATKNIKVI 302
Cdd:COG0465   209 SDFVEMFVGVGASRVRDLFEQAKKNAPCIIFIDEIDAVGRQRGAGLGGGHDEREQT----LNQLlvemDGFEGNEGVIVI 284
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148885657 303 MATNRIDILDSALLRPGRIDRKIEFPPPNEEARLDILKIHSRKMNLTRGINLRKIAELMPGASGAEVKGVCTEAGMYALR 382
Cdd:COG0465   285 AATNRPDVLDPALLRPGRFDRQVVVDLPDVKGREAILKVHARKKPLAPDVDLEVIARRTPGFSGADLANLVNEAALLAAR 364
                         250
                  ....*....|....*....
gi 1148885657 383 ERRVHVTQEDFEMAVAKVM 401
Cdd:COG0465   365 RNKKAVTMEDFEEAIDRVI 383
SpoVK COG0464
AAA+-type ATPase, SpoVK/Ycf46/Vps4 family [Cell wall/membrane/envelope biogenesis, Cell cycle ...
150-400 2.07e-82

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: 258.30  E-value: 2.07e-82
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148885657 150 VEKVPDSTYEMIGGLDKQIKEIKEVIELPVKHPELFEALGIAQPKGVLLYGPPGTGKTLLARAVAHHTDCTFIRVSGSEL 229
Cdd:COG0464   148 LLELREAILDDLGGLEEVKEELRELVALPLKRPELREEYGLPPPRGLLLYGPPGTGKTLLARALAGELGLPLIEVDLSDL 227
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148885657 230 VQKFIGEGARMVRELFVMAREHAPSIIFMDEIDSIGSSRlegGSGGDSEVQRTMLELLNQLDGFEatKNIKVIMATNRID 309
Cdd:COG0464   228 VSKYVGETEKNLREVFDKARGLAPCVLFIDEADALAGKR---GEVGDGVGRRVVNTLLTEMEELR--SDVVVIAATNRPD 302
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148885657 310 ILDSALLRpgRIDRKIEFPPPNEEARLDILKIHSRKMNLTRGINLRKIAELMPGASGAEVKGVCTEAGMYALRERRVHVT 389
Cdd:COG0464   303 LLDPALLR--RFDEIIFFPLPDAEERLEIFRIHLRKRPLDEDVDLEELAEATEGLSGADIRNVVRRAALQALRLGREPVT 380
                         250
                  ....*....|.
gi 1148885657 390 QEDFEMAVAKV 400
Cdd:COG0464   381 TEDLLEALERE 391
CDC48 TIGR01243
AAA family ATPase, CDC48 subfamily; This subfamily of the AAA family ATPases includes two ...
82-409 1.03e-79

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: 260.22  E-value: 1.03e-79
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148885657  82 YVGEVVRAMDKK---KVLVKVHPEGKfvVDVDKNIDINDVTPNCRVALRNDSYTLHKILPNkvdpLVSLMMVEkVPDSTY 158
Cdd:TIGR01243 380 FVGADLAALAKEaamAALRRFIREGK--INFEAEEIPAEVLKELKVTMKDFMEALKMVEPS----AIREVLVE-VPNVRW 452
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148885657 159 EMIGGLDKQIKEIKEVIELPVKHPELFEALGIAQPKGVLLYGPPGTGKTLLARAVAHHTDCTFIRVSGSELVQKFIGEGA 238
Cdd:TIGR01243 453 SDIGGLEEVKQELREAVEWPLKHPEIFEKMGIRPPKGVLLFGPPGTGKTLLAKAVATESGANFIAVRGPEILSKWVGESE 532
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148885657 239 RMVRELFVMAREHAPSIIFMDEIDSIGSSRleGGSGGDSEVQRTMLELLNQLDGFEATKNIKVIMATNRIDILDSALLRP 318
Cdd:TIGR01243 533 KAIREIFRKARQAAPAIIFFDEIDAIAPAR--GARFDTSVTDRIVNQLLTEMDGIQELSNVVVIAATNRPDILDPALLRP 610
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148885657 319 GRIDRKIEFPPPNEEARLDILKIHSRKMNLTRGINLRKIAELMPGASGAEVKGVCTEAGMYALRE--------------- 383
Cdd:TIGR01243 611 GRFDRLILVPPPDEEARKEIFKIHTRSMPLAEDVDLEELAEMTEGYTGADIEAVCREAAMAALREsigspakeklevgee 690
                         330       340
                  ....*....|....*....|....*....
gi 1148885657 384 ---RRVHVTQEDFEMAVAKVMQKDSEKNM 409
Cdd:TIGR01243 691 eflKDLKVEMRHFLEALKKVKPSVSKEDM 719
ftsH CHL00176
cell division protein; Validated
150-400 5.59e-75

cell division protein; Validated


Pssm-ID: 214386 [Multi-domain]  Cd Length: 638  Bit Score: 245.73  E-value: 5.59e-75
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148885657 150 VEKVPDS--TYEMIGGLDKQIKEIKEVIELpVKHPELFEALGIAQPKGVLLYGPPGTGKTLLARAVAHHTDCTFIRVSGS 227
Cdd:CHL00176  172 FQMEADTgiTFRDIAGIEEAKEEFEEVVSF-LKKPERFTAVGAKIPKGVLLVGPPGTGKTLLAKAIAGEAEVPFFSISGS 250
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148885657 228 ELVQKFIGEGARMVRELFVMAREHAPSIIFMDEIDSIGSSRLEGGSGGDSEVQRTMLELLNQLDGFEATKNIKVIMATNR 307
Cdd:CHL00176  251 EFVEMFVGVGAARVRDLFKKAKENSPCIVFIDEIDAVGRQRGAGIGGGNDEREQTLNQLLTEMDGFKGNKGVIVIAATNR 330
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148885657 308 IDILDSALLRPGRIDRKIEFPPPNEEARLDILKIHSRKMNLTRGINLRKIAELMPGASGAEVKGVCTEAGMYALRERRVH 387
Cdd:CHL00176  331 VDILDAALLRPGRFDRQITVSLPDREGRLDILKVHARNKKLSPDVSLELIARRTPGFSGADLANLLNEAAILTARRKKAT 410
                         250
                  ....*....|...
gi 1148885657 388 VTQEDFEMAVAKV 400
Cdd:CHL00176  411 ITMKEIDTAIDRV 423
CDC48 TIGR01243
AAA family ATPase, CDC48 subfamily; This subfamily of the AAA family ATPases includes two ...
145-413 5.70e-71

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: 237.11  E-value: 5.70e-71
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148885657 145 VSLMMVEKVPDSTYEMIGGLDKQIKEIKEVIELPVKHPELFEALGIAQPKGVLLYGPPGTGKTLLARAVAHHTDCTFIRV 224
Cdd:TIGR01243 164 VREEIERKVPKVTYEDIGGLKEAKEKIREMVELPMKHPELFEHLGIEPPKGVLLYGPPGTGKTLLAKAVANEAGAYFISI 243
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148885657 225 SGSELVQKFIGEGARMVRELFVMAREHAPSIIFMDEIDSIGSSRLEggSGGDSEvQRTMLELLNQLDGFEATKNIKVIMA 304
Cdd:TIGR01243 244 NGPEIMSKYYGESEERLREIFKEAEENAPSIIFIDEIDAIAPKREE--VTGEVE-KRVVAQLLTLMDGLKGRGRVIVIGA 320
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148885657 305 TNRIDILDSALLRPGRIDRKIEFPPPNEEARLDILKIHSRKMNLTRGINLRKIAELMPGASGAEVKGVCTEAGMYALReR 384
Cdd:TIGR01243 321 TNRPDALDPALRRPGRFDREIVIRVPDKRARKEILKVHTRNMPLAEDVDLDKLAEVTHGFVGADLAALAKEAAMAALR-R 399
                         250       260
                  ....*....|....*....|....*....
gi 1148885657 385 RVHVTQEDFEmavAKVMQKDSEKNMSIKK 413
Cdd:TIGR01243 400 FIREGKINFE---AEEIPAEVLKELKVTM 425
RecA-like_FtsH cd19501
ATP-dependent zinc metalloprotease FtsH; FtsH ATPase is a processive, ATP-dependent zinc ...
161-325 2.34e-69

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: 216.71  E-value: 2.34e-69
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148885657 161 IGGLDKQIKEIKEVIELpVKHPELFEALGIAQPKGVLLYGPPGTGKTLLARAVAHHTDCTFIRVSGSELVQKFIGEGARM 240
Cdd:cd19501     6 VAGCEEAKEELKEVVEF-LKNPEKFTKLGAKIPKGVLLVGPPGTGKTLLAKAVAGEAGVPFFSISGSDFVEMFVGVGASR 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148885657 241 VRELFVMAREHAPSIIFMDEIDSIGSSRLEGGSGGDSEVQRTMLELLNQLDGFEATKNIKVIMATNRIDILDSALLRPGR 320
Cdd:cd19501    85 VRDLFEQAKKNAPCIVFIDEIDAVGRKRGAGLGGGHDEREQTLNQLLVEMDGFESNTGVIVIAATNRPDVLDPALLRPGR 164

                  ....*
gi 1148885657 321 IDRKI 325
Cdd:cd19501   165 FDRQV 169
RecA-like_CDC48_NLV2_r1-like cd19503
first of two ATPase domains of CDC48 and NLV2, and similar ATPase domains; CDC48 in yeast and ...
161-327 3.97e-69

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: 216.00  E-value: 3.97e-69
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148885657 161 IGGLDKQIKEIKEVIELPVKHPELFEALGIAQPKGVLLYGPPGTGKTLLARAVAHHTDCTFIRVSGSELVQKFIGEGARM 240
Cdd:cd19503     2 IGGLDEQIASLKELIELPLKYPELFRALGLKPPRGVLLHGPPGTGKTLLARAVANEAGANFLSISGPSIVSKYLGESEKN 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148885657 241 VRELFVMAREHAPSIIFMDEIDSIGSSRLEGGSGGDSevqRTMLELLNQLDGFEATKNIKVIMATNRIDILDSALLRPGR 320
Cdd:cd19503    82 LREIFEEARSHAPSIIFIDEIDALAPKREEDQREVER---RVVAQLLTLMDGMSSRGKVVVIAATNRPDAIDPALRRPGR 158

                  ....*..
gi 1148885657 321 IDRKIEF 327
Cdd:cd19503   159 FDREVEI 165
RecA-like_CDC48_r2-like cd19511
second of two ATPase domains of CDC48/p97, PEX1 and -6, VAT and NVL, and similar ATPase ...
169-325 1.01e-67

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: 212.14  E-value: 1.01e-67
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148885657 169 KEIKEVIELPVKHPELFEALGIAQPKGVLLYGPPGTGKTLLARAVAHHTDCTFIRVSGSELVQKFIGEGARMVRELFVMA 248
Cdd:cd19511     3 RELKEAVEWPLKHPDAFKRLGIRPPKGVLLYGPPGCGKTLLAKALASEAGLNFISVKGPELFSKYVGESERAVREIFQKA 82
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1148885657 249 REHAPSIIFMDEIDSIGSSRleGGSGGDSEVQRTMLELLNQLDGFEATKNIKVIMATNRIDILDSALLRPGRIDRKI 325
Cdd:cd19511    83 RQAAPCIIFFDEIDSLAPRR--GQSDSSGVTDRVVSQLLTELDGIESLKGVVVIAATNRPDMIDPALLRPGRLDKLI 157
hflB PRK10733
ATP-dependent zinc metalloprotease FtsH;
148-409 1.22e-64

ATP-dependent zinc metalloprotease FtsH;


Pssm-ID: 182683 [Multi-domain]  Cd Length: 644  Bit Score: 218.37  E-value: 1.22e-64
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148885657 148 MMVEKVPDSTYEMIGGLDKQIKEIKEVIELpVKHPELFEALGIAQPKGVLLYGPPGTGKTLLARAVAHHTDCTFIRVSGS 227
Cdd:PRK10733  141 MLTEDQIKTTFADVAGCDEAKEEVAELVEY-LREPSRFQKLGGKIPKGVLMVGPPGTGKTLLAKAIAGEAKVPFFTISGS 219
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148885657 228 ELVQKFIGEGARMVRELFVMAREHAPSIIFMDEIDSIGSSRLEGGSGGDSEVQRTMLELLNQLDGFEATKNIKVIMATNR 307
Cdd:PRK10733  220 DFVEMFVGVGASRVRDMFEQAKKAAPCIIFIDEIDAVGRQRGAGLGGGHDEREQTLNQMLVEMDGFEGNEGIIVIAATNR 299
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148885657 308 IDILDSALLRPGRIDRKIEFPPPNEEARLDILKIHSRKMNLTRGINLRKIAELMPGASGAEVKGVCTEAGMYALRERRVH 387
Cdd:PRK10733  300 PDVLDPALLRPGRFDRQVVVGLPDVRGREQILKVHMRRVPLAPDIDAAIIARGTPGFSGADLANLVNEAALFAARGNKRV 379
                         250       260
                  ....*....|....*....|..
gi 1148885657 388 VTQEDFEMAVAKVMQKDSEKNM 409
Cdd:PRK10733  380 VSMVEFEKAKDKIMMGAERRSM 401
RecA-like_protease cd19481
proteases similar to RecA; RecA-like NTPases. This family includes the NTP binding domain of ...
167-327 1.94e-62

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: 198.28  E-value: 1.94e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148885657 167 QIKEIKEVIELPVKHPELfEALGIAQPKGVLLYGPPGTGKTLLARAVAHHTDCTFIRVSGSELVQKFIGEGARMVRELFV 246
Cdd:cd19481     1 LKASLREAVEAPRRGSRL-RRYGLGLPKGILLYGPPGTGKTLLAKALAGELGLPLIVVKLSSLLSKYVGESEKNLRKIFE 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148885657 247 MAREHAPSIIFMDEIDSIGSSRleGGSGGDSEVQRTMLELLNQLDGFEATKNIKVIMATNRIDILDSALLRPGRIDRKIE 326
Cdd:cd19481    80 RARRLAPCILFIDEIDAIGRKR--DSSGESGELRRVLNQLLTELDGVNSRSKVLVIAATNRPDLLDPALLRPGRFDEVIE 157

                  .
gi 1148885657 327 F 327
Cdd:cd19481   158 F 158
RecA-like_VCP_r2 cd19529
second of two ATPase domains of Valosin-containing protein-like ATPase (VAT) and similar ...
169-325 5.86e-59

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: 189.63  E-value: 5.86e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148885657 169 KEIKEVIELPVKHPELFEALGIAQPKGVLLYGPPGTGKTLLARAVAHHTDCTFIRVSGSELVQKFIGEGARMVRELFVMA 248
Cdd:cd19529     3 QELKEAVEWPLLKPEVFKRLGIRPPKGILLYGPPGTGKTLLAKAVATESNANFISVKGPELLSKWVGESEKAIREIFRKA 82
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1148885657 249 REHAPSIIFMDEIDSIGSSRlegGSGGDSEV-QRTMLELLNQLDGFEATKNIKVIMATNRIDILDSALLRPGRIDRKI 325
Cdd:cd19529    83 RQVAPCVIFFDEIDSIAPRR---GTTGDSGVtERVVNQLLTELDGLEEMNGVVVIAATNRPDIIDPALLRAGRFDRLI 157
RecA-like_CDC48_r1-like cd19519
first of two ATPase domains of CDC48 and similar ATPase domains; CDC48 in yeast and p97 or VCP ...
161-328 9.18e-59

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: 189.18  E-value: 9.18e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148885657 161 IGGLDKQIKEIKEVIELPVKHPELFEALGIAQPKGVLLYGPPGTGKTLLARAVAHHTDCTFIRVSGSELVQKFIGEGARM 240
Cdd:cd19519     2 IGGCRKQLAQIREMVELPLRHPELFKAIGIKPPRGILLYGPPGTGKTLIARAVANETGAFFFLINGPEIMSKLAGESESN 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148885657 241 VRELFVMAREHAPSIIFMDEIDSIGSSRLEggSGGDSEvQRTMLELLNQLDGFEATKNIKVIMATNRIDILDSALLRPGR 320
Cdd:cd19519    82 LRKAFEEAEKNAPAIIFIDEIDAIAPKREK--THGEVE-RRIVSQLLTLMDGLKQRAHVIVMAATNRPNSIDPALRRFGR 158

                  ....*...
gi 1148885657 321 IDRKIEFP 328
Cdd:cd19519   159 FDREIDIG 166
COG1223 COG1223
Predicted ATPase, AAA+ superfamily [General function prediction only];
164-399 4.57e-56

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


Pssm-ID: 440836 [Multi-domain]  Cd Length: 246  Bit Score: 185.09  E-value: 4.57e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148885657 164 LDKQIKEIKEVIELPVKHPELFEALGIAQPKGVLLYGPPGTGKTLLARAVAHHTDCTFIRVSGSELVQKFIGEGARMVRE 243
Cdd:COG1223     6 GQEEAKKKLKLIIKELRRRENLRKFGLWPPRKILFYGPPGTGKTMLAEALAGELKLPLLTVRLDSLIGSYLGETARNLRK 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148885657 244 LFVMAREhAPSIIFMDEIDSIGSSRleGGSGGDSEVQRTMLELLNQLDGFEAtkNIKVIMATNRIDILDSALLRpgRIDR 323
Cdd:COG1223    86 LFDFARR-APCVIFFDEFDAIAKDR--GDQNDVGEVKRVVNALLQELDGLPS--GSVVIAATNHPELLDSALWR--RFDE 158
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1148885657 324 KIEFPPPNEEARLDILKIHSRKMNLTRGINLRKIAELMPGASGAEVKGVCTEAGMYALRERRVHVTQEDFEMAVAK 399
Cdd:COG1223   159 VIEFPLPDKEERKEILELNLKKFPLPFELDLKKLAKKLEGLSGADIEKVLKTALKKAILEDREKVTKEDLEEALKQ 234
RecA-like_CDC48_r2-like cd19528
second of two ATPase domains of CDC48 and similar ATPase domains; CDC48 in yeast and p97 or ...
169-325 5.85e-54

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: 176.55  E-value: 5.85e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148885657 169 KEIKEVIELPVKHPELFEALGIAQPKGVLLYGPPGTGKTLLARAVAHHTDCTFIRVSGSELVQKFIGEGARMVRELFVMA 248
Cdd:cd19528     3 RELQELVQYPVEHPDKFLKFGMTPSKGVLFYGPPGCGKTLLAKAIANECQANFISVKGPELLTMWFGESEANVRDIFDKA 82
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1148885657 249 REHAPSIIFMDEIDSIGSSRleGGSGGDS--EVQRTMLELLNQLDGFEATKNIKVIMATNRIDILDSALLRPGRIDRKI 325
Cdd:cd19528    83 RAAAPCVLFFDELDSIAKAR--GGNIGDAggAADRVINQILTEMDGMNTKKNVFIIGATNRPDIIDPAILRPGRLDQLI 159
AAA pfam00004
ATPase family associated with various cellular activities (AAA); AAA family proteins often ...
196-328 3.05e-53

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


Pssm-ID: 459627 [Multi-domain]  Cd Length: 130  Bit Score: 173.55  E-value: 3.05e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148885657 196 VLLYGPPGTGKTLLARAVAHHTDCTFIRVSGSELVQKFIGEGARMVRELFVMAREHAPSIIFMDEIDSIGSSRlegGSGG 275
Cdd:pfam00004   1 LLLYGPPGTGKTTLAKAVAKELGAPFIEISGSELVSKYVGESEKRLRELFEAAKKLAPCVIFIDEIDALAGSR---GSGG 77
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1148885657 276 DSEVQRTMLELLNQLDGFE-ATKNIKVIMATNRIDILDSALLrpGRIDRKIEFP 328
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 ...
161-325 1.76e-51

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: 170.23  E-value: 1.76e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148885657 161 IGGLDKQIKEIKEVIELPVKHPELFeALGIAQPKGVLLYGPPGTGKTLLARAVAHHTDCTFIRVSGSELVQKFIGEGARM 240
Cdd:cd19509     1 IAGLDDAKEALKEAVILPSLRPDLF-PGLRGPPRGILLYGPPGTGKTLLARAVASESGSTFFSISASSLVSKWVGESEKI 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148885657 241 VRELFVMAREHAPSIIFMDEIDSIGSSRleggSGGDSEVQRTM-LELLNQLDGFEATKN--IKVIMATNRIDILDSALLR 317
Cdd:cd19509    80 VRALFALARELQPSIIFIDEIDSLLSER----GSGEHEASRRVkTEFLVQMDGVLNKPEdrVLVLGATNRPWELDEAFLR 155

                  ....*...
gi 1148885657 318 pgRIDRKI 325
Cdd:cd19509   156 --RFEKRI 161
RecA-like_NVL_r2-like cd19530
second of two ATPase domains of NVL (nuclear VCP-like protein) and similar ATPase domains; NVL ...
164-323 8.32e-50

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: 165.74  E-value: 8.32e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148885657 164 LDKQIKEIKEVIELPVKHPELFEALGIAQPKGVLLYGPPGTGKTLLARAVAHHTDCTFIRVSGSELVQKFIGEGARMVRE 243
Cdd:cd19530     1 LDHVREELTMSILRPIKRPDIYKALGIDLPTGVLLYGPPGCGKTLLAKAVANESGANFISVKGPELLNKYVGESERAVRQ 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148885657 244 LFVMAREHAPSIIFMDEIDSIGSSRLEGGSGGdseVQRTMLELLNQLDGFEATKNIKVIMATNRIDILDSALLRPGRIDR 323
Cdd:cd19530    81 VFQRARASAPCVIFFDEVDALVPKRGDGGSWA---SERVVNQLLTEMDGLEERSNVFVIAATNRPDIIDPAMLRPGRLDK 157
RecA-like_PEX1_r2 cd19526
second of two ATPase domains of Peroxisomal biogenesis factor 1 (PEX1); PEX1(also known as ...
171-326 2.66e-49

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: 164.52  E-value: 2.66e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148885657 171 IKEVIELPVKHPELFEALGIAQPKGVLLYGPPGTGKTLLARAVAHHTDCTFIRVSGSELVQKFIGEGARMVRELFVMARE 250
Cdd:cd19526     5 LEETIEWPSKYPKIFASSPLRLRSGILLYGPPGCGKTLLASAIASECGLNFISVKGPELLNKYIGASEQNVRDLFSRAQS 84
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1148885657 251 HAPSIIFMDEIDSIGSSRleggsGGDSE--VQRTMLELLNQLDGFEATKNIKVIMATNRIDILDSALLRPGRIDRKIE 326
Cdd:cd19526    85 AKPCILFFDEFDSIAPKR-----GHDSTgvTDRVVNQLLTQLDGVEGLDGVYVLAATSRPDLIDPALLRPGRLDKLVY 157
RecA-like_PEX6_r2 cd19527
second of two ATPase domains of Peroxisomal biogenesis factor 6 (PEX6); PEX6(also known as ...
169-323 6.48e-46

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: 155.75  E-value: 6.48e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148885657 169 KEIKEVIELPVKHPELFeALGIAQPKGVLLYGPPGTGKTLLARAVAHHTDCTFIRVSGSELVQKFIGEGARMVRELFVMA 248
Cdd:cd19527     3 KEILDTIQLPLEHPELF-SSGLRKRSGILLYGPPGTGKTLLAKAIATECSLNFLSVKGPELINMYIGESEANVREVFQKA 81
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1148885657 249 REHAPSIIFMDEIDSIGSSRlegGSGGDSE--VQRTMLELLNQLDGFEAT-KNIKVIMATNRIDILDSALLRPGRIDR 323
Cdd:cd19527    82 RDAKPCVIFFDELDSLAPSR---GNSGDSGgvMDRVVSQLLAELDGMSSSgQDVFVIGATNRPDLLDPALLRPGRFDK 156
RecA-like_NVL_r1-like cd19518
first of two ATPase domains of NVL (nuclear VCP-like protein) and similar ATPase domains; NVL ...
161-325 3.70e-45

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


Pssm-ID: 410926 [Multi-domain]  Cd Length: 169  Bit Score: 154.10  E-value: 3.70e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148885657 161 IGGLDKQIKEIKEVIELPVKHPELFEALGIAQPKGVLLYGPPGTGKTLLARAVAHHTDCTFIRVSGSELVQKFIGEGARM 240
Cdd:cd19518     2 IGGMDSTLKELCELLIHPILPPEYFQHLGVEPPRGVLLHGPPGCGKTMLANAIAGELKVPFLKISATEIVSGVSGESEEK 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148885657 241 VRELFVMAREHAPSIIFMDEIDSIGSSRlEGGSgGDSEvQRTMLELLNQLDGF----EATKNIKVIMATNRIDILDSALL 316
Cdd:cd19518    82 IRELFDQAISNAPCIVFIDEIDAITPKR-ESAQ-REME-RRIVSQLLTCMDELnnekTAGGPVLVIGATNRPDSLDPALR 158

                  ....*....
gi 1148885657 317 RPGRIDRKI 325
Cdd:cd19518   159 RAGRFDREI 167
RecA-like_VPS4 cd19521
ATPase domain of vacuolar protein sorting-associated protein 4; Vacuolar protein ...
154-325 3.06e-43

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: 149.24  E-value: 3.06e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148885657 154 PDSTYEMIGGLDKQIKEIKEVIELPVKHPELFEalGIAQP-KGVLLYGPPGTGKTLLARAVAHHTDCTFIRVSGSELVQK 232
Cdd:cd19521     2 PNVKWEDVAGLEGAKEALKEAVILPVKFPHLFT--GNRKPwSGILLYGPPGTGKSYLAKAVATEANSTFFSVSSSDLVSK 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148885657 233 FIGEGARMVRELFVMAREHAPSIIFMDEIDSIGSSRLEGGSggdSEVQRTMLELLNQLDGF-EATKNIKVIMATNRIDIL 311
Cdd:cd19521    80 WMGESEKLVKQLFAMARENKPSIIFIDEVDSLCGTRGEGES---EASRRIKTELLVQMNGVgNDSQGVLVLGATNIPWQL 156
                         170
                  ....*....|....
gi 1148885657 312 DSALLRpgRIDRKI 325
Cdd:cd19521   157 DSAIRR--RFEKRI 168
RecA-like_Yta7-like cd19517
ATPase domain of Saccharomyces cerevisiae Yta7 and similar ATPase domains; Saccharomyces ...
161-327 3.94e-43

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: 148.81  E-value: 3.94e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148885657 161 IGGLDKQIKEIKEVIELPVKHPELFEALGIAQPKGVLLYGPPGTGKTLLARAVAHHTD-----CTFIRVSGSELVQKFIG 235
Cdd:cd19517     2 IGGLSHYINQLKEMVFFPLLYPEVFAKFKITPPRGVLFHGPPGTGKTLMARALAAECSkggqkVSFFMRKGADCLSKWVG 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148885657 236 EGARMVRELFVMAREHAPSIIFMDEIDSIGSSRLEGGSGGDSEVQRTMLELlnqLDGFEATKNIKVIMATNRIDILDSAL 315
Cdd:cd19517    82 EAERQLRLLFEEAYRMQPSIIFFDEIDGLAPVRSSKQEQIHASIVSTLLAL---MDGLDNRGQVVVIGATNRPDALDPAL 158
                         170
                  ....*....|..
gi 1148885657 316 LRPGRIDRKIEF 327
Cdd:cd19517   159 RRPGRFDREFYF 170
RecA-like_ATAD1 cd19520
ATPase domain of ATPase family AAA domain-containing protein 1 and similar ATPase domains; ...
161-317 4.77e-43

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: 148.34  E-value: 4.77e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148885657 161 IGGLDKQIKEIKEVIELPVKHPELFEALGIAQ-PKGVLLYGPPGTGKTLLARAVAHHTDCTFIRVSGSELVQKFIGEGAR 239
Cdd:cd19520     2 IGGLDEVITELKELVILPLQRPELFDNSRLLQpPKGVLLYGPPGCGKTMLAKATAKEAGARFINLQVSSLTDKWYGESQK 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148885657 240 MVRELFVMAREHAPSIIFMDEIDSIGSSRleggSGGDSEVQRTM-LELLNQLDGFEATKNIKVIM--ATNRIDILDSALL 316
Cdd:cd19520    82 LVAAVFSLASKLQPSIIFIDEIDSFLRQR----SSTDHEATAMMkAEFMSLWDGLSTDGNCRVIVmgATNRPQDLDEAIL 157

                  .
gi 1148885657 317 R 317
Cdd:cd19520   158 R 158
RecA-like_KTNA1 cd19522
Katanin p60 ATPase-containing subunit A1; Katanin p60 ATPase-containing subunit A1 (KTNA1) is ...
161-325 1.16e-40

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: 142.43  E-value: 1.16e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148885657 161 IGGLDKQIKEIKEVIELPVKHPELFEalGIAQP-KGVLLYGPPGTGKTLLARAVAHHTDCTFIRVSGSELVQKFIGEGAR 239
Cdd:cd19522     2 IADLEEAKKLLEEAVVLPMWMPEFFK--GIRRPwKGVLMVGPPGTGKTLLAKAVATECGTTFFNVSSSTLTSKYRGESEK 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148885657 240 MVRELFVMAREHAPSIIFMDEIDSIGSSRleGGSGGDSEVQRTMLELLNQLDGF-------EATKNIKVIMATNRIDILD 312
Cdd:cd19522    80 LVRLLFEMARFYAPTTIFIDEIDSICSRR--GTSEEHEASRRVKSELLVQMDGVggasendDPSKMVMVLAATNFPWDID 157
                         170
                  ....*....|...
gi 1148885657 313 SALLRpgRIDRKI 325
Cdd:cd19522   158 EALRR--RLEKRI 168
RecA-like_Figl-1 cd19525
ATPase domain of Fidgetin-Like 1 (FIGL-1); FIGL-1 may participate in DNA repair in the nucleus; ...
144-317 1.46e-40

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: 142.43  E-value: 1.46e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148885657 144 LVSLMMVEKV---PDSTYEMIGGLDKQIKEIKEVIELPVKHPELFEALGiAQPKGVLLYGPPGTGKTLLARAVAHHTDCT 220
Cdd:cd19525     4 MIELIMSEIMdhgPPINWADIAGLEFAKKTIKEIVVWPMLRPDIFTGLR-GPPKGILLFGPPGTGKTLIGKCIASQSGAT 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148885657 221 FIRVSGSELVQKFIGEGARMVRELFVMAREHAPSIIFMDEIDSIGSSRlegGSGGDSEVQRTMLELLNQLDGFEATKN-- 298
Cdd:cd19525    83 FFSISASSLTSKWVGEGEKMVRALFSVARCKQPAVIFIDEIDSLLSQR---GEGEHESSRRIKTEFLVQLDGATTSSEdr 159
                         170
                  ....*....|....*....
gi 1148885657 299 IKVIMATNRIDILDSALLR 317
Cdd:cd19525   160 ILVVGATNRPQEIDEAARR 178
RecA-like_spastin cd19524
ATPase domain of spastin; Spastin is an ATP-dependent microtubule-severing protein involved in ...
161-317 2.76e-39

ATPase domain of spastin; Spastin is an ATP-dependent microtubule-severing protein involved in microtubule dynamics; it specifically recognizes and cuts microtubules that are polyglutamylated. This subfamily belongs to the RecA-like NTPase family which includes the NTP binding domain of F1 and V1 H(+)ATPases, DnaB and related helicases as well as bacterial RecA and related eukaryotic and archaeal recombinases. The RecA-like NTPase family also includes bacterial conjugation proteins and related DNA transfer proteins involved in type II and type IV secretion.


Pssm-ID: 410932 [Multi-domain]  Cd Length: 164  Bit Score: 138.44  E-value: 2.76e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148885657 161 IGGLDKQIKEIKEVIELPVKHPELFEALGiAQPKGVLLYGPPGTGKTLLARAVAHHTDCTFIRVSGSELVQKFIGEGARM 240
Cdd:cd19524     2 IAGQDLAKQALQEMVILPSLRPELFTGLR-APARGLLLFGPPGNGKTMLAKAVAAESNATFFNISAASLTSKYVGEGEKL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148885657 241 VRELFVMAREHAPSIIFMDEIDSIGSSRleggSGGDSEVQRTM-LELLNQLDGFEATKNIKVIM--ATNRIDILDSALLR 317
Cdd:cd19524    81 VRALFAVARELQPSIIFIDEVDSLLSER----SEGEHEASRRLkTEFLIEFDGVQSNGDDRVLVmgATNRPQELDDAVLR 156
RecA-like_NSF-SEC18_r1-like cd19504
first of two ATPase domains of NSF and SEC18, and similar ATPase domains; ...
161-326 1.94e-35

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: 128.76  E-value: 1.94e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148885657 161 IGGLDKQIKEI-KEVIELPVKHPELFEALGIAQPKGVLLYGPPGTGKTLLARAVAHHTDCTFIR-VSGSELVQKFIGEGA 238
Cdd:cd19504     2 IGGLDKEFSDIfRRAFASRVFPPEIVEQLGCKHVKGILLYGPPGTGKTLMARQIGKMLNAREPKiVNGPEILNKYVGESE 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148885657 239 RMVRELFVMAREHAPS--------IIFMDEIDSIGSSRleGGSGGDSEVQRTML-ELLNQLDGFEATKNIKVIMATNRID 309
Cdd:cd19504    82 ANIRKLFADAEEEQRRlgansglhIIIFDEIDAICKQR--GSMAGSTGVHDTVVnQLLSKIDGVEQLNNILVIGMTNRKD 159
                         170
                  ....*....|....*..
gi 1148885657 310 ILDSALLRPGRIDRKIE 326
Cdd:cd19504   160 LIDEALLRPGRLEVQME 176
RecA-like_fidgetin cd19523
ATPase domain of fidgetin; Fidgetin (FIGN) is a ATP-dependent microtubule severing protein. ...
161-317 1.26e-30

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: 115.37  E-value: 1.26e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148885657 161 IGGLDKQIKEIKEVIELPVKHPELFEALgIAQPKGVLLYGPPGTGKTLLARAVAHHTDCTFIRVSGSELVQKFIGEGARM 240
Cdd:cd19523     2 IAGLGALKAAIKEEVLWPLLRPDAFSGL-LRLPRSILLFGPRGTGKTLLGRCLASQLGATFLRLRGSTLVAKWAGEGEKI 80
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1148885657 241 VRELFVMAREHAPSIIFMDEIDSIGSSRLEggsgGDSEVQRTMLELLNQLDGF--EATKNIKVIMATNRIDILDSALLR 317
Cdd:cd19523    81 LQASFLAARCRQPSVLFISDLDALLSSQDD----EASPVGRLQVELLAQLDGVlgSGEDGVLVVCTTSKPEEIDESLRR 155
AAA cd00009
The AAA+ (ATPases Associated with a wide variety of cellular Activities) superfamily ...
162-329 4.07e-28

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: 108.39  E-value: 4.07e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148885657 162 GGLDKQIKEIKEVIELPvkhpelfealgiaQPKGVLLYGPPGTGKTLLARAVAHHT---DCTFIRVSGSELVQKFIGEGA 238
Cdd:cd00009     1 VGQEEAIEALREALELP-------------PPKNLLLYGPPGTGKTTLARAIANELfrpGAPFLYLNASDLLEGLVVAEL 67
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148885657 239 R---MVRELFVMAREHAPSIIFMDEIDSIGssrleggsggdSEVQRTMLELLNQL-DGFEATKNIKVIMATNRIDILDSA 314
Cdd:cd00009    68 FghfLVRLLFELAEKAKPGVLFIDEIDSLS-----------RGAQNALLRVLETLnDLRIDRENVRVIGATNRPLLGDLD 136
                         170
                  ....*....|....*
gi 1148885657 315 LLRPGRIDRKIEFPP 329
Cdd:cd00009   137 RALYDRLDIRIVIPL 151
ycf46 CHL00195
Ycf46; Provisional
189-412 3.95e-23

Ycf46; Provisional


Pssm-ID: 177094 [Multi-domain]  Cd Length: 489  Bit Score: 101.25  E-value: 3.95e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148885657 189 GIAQPKGVLLYGPPGTGKTLLARAVAHHTDCTFIRVSGSELVQKFIGEGARMVRELFVMAREHAPSIIFMDEID-SIGSS 267
Cdd:CHL00195  255 GLPTPRGLLLVGIQGTGKSLTAKAIANDWQLPLLRLDVGKLFGGIVGESESRMRQMIRIAEALSPCILWIDEIDkAFSNS 334
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148885657 268 RLEGGSGGDSEVQRTMLELLNqldgfEATKNIKVIMATNRIDILDSALLRPGRIDRKIEFPPPNEEARLDILKIHSRKM- 346
Cdd:CHL00195  335 ESKGDSGTTNRVLATFITWLS-----EKKSPVFVVATANNIDLLPLEILRKGRFDEIFFLDLPSLEEREKIFKIHLQKFr 409
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148885657 347 -NLTRGINLRKIAELMPGASGAEVKGVCTEAGMYALRERRvHVTQEDFEMAVAKVM---QKDSEKNMSIK 412
Cdd:CHL00195  410 pKSWKKYDIKKLSKLSNKFSGAEIEQSIIEAMYIAFYEKR-EFTTDDILLALKQFIplaQTEKEQIEALQ 478
RecA-like_Ycf46-like cd19507
ATPase domain of Ycf46 and similar ATPase domains; Ycf46 may play a role in the regulation of ...
186-323 1.51e-22

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


Pssm-ID: 410915 [Multi-domain]  Cd Length: 161  Bit Score: 93.20  E-value: 1.51e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148885657 186 EALGIAQPKGVLLYGPPGTGKTLLARAVAHHTDCTFIRVSGSELVQKFIGEGARMVRELFVMAREHAPSIIFMDEIDS-I 264
Cdd:cd19507    24 SAYGLPTPKGLLLVGIQGTGKSLTAKAIAGVWQLPLLRLDMGRLFGGLVGESESRLRQMIQTAEAIAPCVLWIDEIEKgF 103
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1148885657 265 GSSRLEGGSGGDSEVQRTMLELLNqldgfEATKNIKVIMATNRIDILDSALLRPGRIDR 323
Cdd:cd19507   104 SNADSKGDSGTSSRVLGTFLTWLQ-----EKKKPVFVVATANNVQSLPPELLRKGRFDE 157
RecA-like_BCS1 cd19510
Mitochondrial chaperone BCS1; Mitochondrial chaperone BCS1 is necessary for the assembly of ...
171-327 5.15e-21

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


Pssm-ID: 410918 [Multi-domain]  Cd Length: 153  Bit Score: 88.95  E-value: 5.15e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148885657 171 IKEVIELPVKHPELFEALGIAQPKGVLLYGPPGTGKTLLARAVAHHTDCTFIRVSGSELVQKfigegARMVRELfvMARE 250
Cdd:cd19510     1 IIDDLKDFIKNEDWYNDRGIPYRRGYLLYGPPGTGKSSFIAALAGELDYDICDLNLSEVVLT-----DDRLNHL--LNTA 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148885657 251 HAPSIIFMDEIDSIGSSRLEGGS-----GGDSEVqrTMLELLNQLDGFEATKNIKVIMATNRIDILDSALLRPGRIDRKI 325
Cdd:cd19510    74 PKQSIILLEDIDAAFESREHNKKnpsayGGLSRV--TFSGLLNALDGVASSEERIVFMTTNHIERLDPALIRPGRVDMKI 151

                  ..
gi 1148885657 326 EF 327
Cdd:cd19510   152 YM 153
AAA smart00382
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ...
192-331 3.89e-20

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: 86.27  E-value: 3.89e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148885657  192 QPKGVLLYGPPGTGKTLLARAVAHHTDCT---FIRVSGSEL--------------VQKFIGEGARMVRELFVMAREHAPS 254
Cdd:smart00382   1 PGEVILIVGPPGSGKTTLARALARELGPPgggVIYIDGEDIleevldqllliivgGKKASGSGELRLRLALALARKLKPD 80
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1148885657  255 IIFMDEIDSIGSSRleggsggdSEVQRTMLELLNQLDGFEATKNIKVIMATNRIDILDSALLRPgRIDRKIEFPPPN 331
Cdd:smart00382  81 VLILDEITSLLDAE--------QEALLLLLEELRLLLLLKSEKNLTVILTTNDEKDLGPALLRR-RFDRRIVLLLIL 148
RecA-like_Pch2-like cd19508
ATPase domain of Pachytene checkpoint 2 (Pch2) and similar ATPase domains; Pch2 (known as ...
190-315 1.71e-12

ATPase domain of Pachytene checkpoint 2 (Pch2) and similar ATPase domains; Pch2 (known as Thyroid hormone receptor interactor 13 (TRIP13) and 16E1BP) is a key regulator of specific chromosomal events, like the control of G2/prophase processes such as DNA break formation and recombination, checkpoint signaling, and chromosome synapsis. This subfamily belongs to the RecA-like NTPase family which includes the NTP binding domain of F1 and V1 H(+)ATPases, DnaB and related helicases as well as bacterial RecA and related eukaryotic and archaeal recombinases. The RecA-like NTPase family also includes bacterial conjugation proteins and related DNA transfer proteins involved in type II and type IV secretion


Pssm-ID: 410916 [Multi-domain]  Cd Length: 199  Bit Score: 65.93  E-value: 1.71e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148885657 190 IAQPKGVLLYGPPGTGKTLLARAVAHHTD---------CTFIRVSGSELVQKFIGEGARMVRELF-----VMAREHAPSI 255
Cdd:cd19508    49 ITWNRLVLLHGPPGTGKTSLCKALAQKLSirlssryryGQLIEINSHSLFSKWFSESGKLVTKMFqkiqeLIDDKDALVF 128
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1148885657 256 IFMDEIDSIGSSRLEGGSGGD-SEVQRTMLELLNQLDGFEATKNIKVIMATNRIDILDSAL 315
Cdd:cd19508   129 VLIDEVESLAAARSASSSGTEpSDAIRVVNAVLTQIDRIKRYHNNVILLTSNLLEKIDVAF 189
RecA-like_ATAD3-like cd19512
ATPase domains of ATPase AAA-domain protein 3A (ATAD3A), -3B, and -3C, and similar ATPase ...
194-327 1.36e-11

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: 62.16  E-value: 1.36e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148885657 194 KGVLLYGPPGTGKTLLARAVAHHTDCTFIRVSGSElVQKFIGEGARMVRELFVMAREHAPS-IIFMDEIDSIGSSRlegG 272
Cdd:cd19512    23 RNILFYGPPGTGKTLFAKKLALHSGMDYAIMTGGD-VAPMGREGVTAIHKVFDWANTSRRGlLLFVDEADAFLRKR---S 98
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1148885657 273 SGGDSEVQRTMLELLNQLDGfEATKNIKVIMATNRIDILDSALlrPGRIDRKIEF 327
Cdd:cd19512    99 TEKISEDLRAALNAFLYRTG-EQSNKFMLVLASNQPEQFDWAI--NDRIDEMVEF 150
TIGR02928 TIGR02928
orc1/cdc6 family replication initiation protein; Members of this protein family are found ...
154-400 1.86e-11

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: 64.96  E-value: 1.86e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148885657 154 PDSTYEMIGGLDKQIKEIKEvielpvkhpELFEALGIAQPKGVLLYGPPGTGKTLLARAVA----------------HHT 217
Cdd:TIGR02928  10 PDYVPDRIVHRDEQIEELAK---------ALRPILRGSRPSNVFIYGKTGTGKTAVTKYVMkeleeaaedrdvrvvtVYV 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148885657 218 DCTFIRVSG---SELVQKFIGEG----------ARMVRELFVMAREHAPSIIF-MDEIDSIgssrleGGSGGDSEVQRTM 283
Cdd:TIGR02928  81 NCQILDTLYqvlVELANQLRGSGeevpttglstSEVFRRLYKELNERGDSLIIvLDEIDYL------VGDDDDLLYQLSR 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148885657 284 LELLNQLDGFeatkNIKVIMATNRIDILDSalLRPgRI-----DRKIEFPPPNEEARLDILKiHSRKMNLTRGI----NL 354
Cdd:TIGR02928 155 ARSNGDLDNA----KVGVIGISNDLKFREN--LDP-RVksslcEEEIIFPPYDAEELRDILE-NRAEKAFYDGVlddgVI 226
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*...
gi 1148885657 355 RKIAELMPGASGAEVKGVCT--EAGMYALRERRVHVTQEDFEMAVAKV 400
Cdd:TIGR02928 227 PLCAALAAQEHGDARKAIDLlrVAGEIAEREGAERVTEDHVEKAQEKI 274
AAA_lid_3 pfam17862
AAA+ lid domain; This entry represents the alpha helical AAA+ lid domain that is found to the ...
352-394 8.22e-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: 56.78  E-value: 8.22e-11
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 1148885657 352 INLRKIAELMPGASGAEVKGVCTEAGMYALRERRVHVTQEDFE 394
Cdd:pfam17862   2 VDLEELAERTEGFSGADLEALCREAALAALRRGLEAVTQEDLE 44
RarA COG2256
Replication-associated recombination protein RarA (DNA-dependent ATPase) [Replication, ...
196-261 4.76e-10

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


Pssm-ID: 441857 [Multi-domain]  Cd Length: 439  Bit Score: 60.84  E-value: 4.76e-10
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148885657 196 VLLYGPPGTGKTLLARAVAHHTDCTFIRVSGselvqkfIGEGARMVRELFVMAREHA----PSIIFMDEI 261
Cdd:COG2256    52 MILWGPPGTGKTTLARLIANATDAEFVALSA-------VTSGVKDIREVIEEARERRaygrRTILFVDEI 114
RecA-like_Ycf2 cd19505
ATPase domain of plant YCF2; Ycf2 is a chloroplast ATPase which has an essential function; ...
188-327 8.95e-10

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: 57.00  E-value: 8.95e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148885657 188 LGIAQPKGVLLYGPPGTGKTLLARAVAHHTDCTFIRVSGSELVQK--------------FIGEGARMVRELFVMAREHAP 253
Cdd:cd19505     7 LGLSPSKGILLIGSIETGRSYLIKSLAANSYVPLIRISLNKLLYNkpdfgnddwidgmlILKESLHRLNLQFELAKAMSP 86
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1148885657 254 SIIFMDEIDSIGSSRleggSGGDSEVQRTML--ELLNQL-DGFE--ATKNIKVIMATNRIDILDSALLRPGRIDRKIEF 327
Cdd:cd19505    87 CIIWIPNIHELNVNR----STQNLEEDPKLLlgLLLNYLsRDFEksSTRNILVIASTHIPQKVDPALIAPNRLDTCINI 161
Prot_ATP_ID_OB pfam16450
Proteasomal ATPase OB C-terminal domain; This is the interdomain (ID) or oligonucleotide ...
83-138 1.28e-09

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


Pssm-ID: 465118 [Multi-domain]  Cd Length: 56  Bit Score: 53.66  E-value: 1.28e-09
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1148885657  83 VGEVVRAMDKKKVLVKVHPEGKFVVDVDKNIDINDVTPNCRVALRNDSYTLHKILP 138
Cdd:pfam16450   1 VATVVEVLDDGRALVKSSGGEERVVRLAGSLDEEKLRPGDRVLLDPRSGYALEVLP 56
RecA-like_HslU cd19498
ATP-dependent protease ATPase subunit HslU; HslU is a component of the ATP-dependent protease ...
193-287 1.40e-09

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: 57.00  E-value: 1.40e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148885657 193 PKGVLLYGPPGTGKTLLARAVAHHTDCTFIRVSGSELVQ-KFIGegarmvRELFVMAREHAPSIIFMDEIDSIGSSrlEG 271
Cdd:cd19498    46 PKNILMIGPTGVGKTEIARRLAKLAGAPFIKVEATKFTEvGYVG------RDVESIIRDLVEGIVFIDEIDKIAKR--GG 117
                          90
                  ....*....|....*....
gi 1148885657 272 GSGGDSE---VQRTMLELL 287
Cdd:cd19498   118 SSGPDVSregVQRDLLPIV 136
MoxR COG0714
MoxR-like ATPase [General function prediction only]; MoxR-like ATPase is part of the Pathway ...
196-402 1.85e-09

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: 58.26  E-value: 1.85e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148885657 196 VLLYGPPGTGKTLLARAVAHHTDCTFIRVSGSE--LVQKFIGEgarMV-----RELFVMARehaP---SIIFMDEIDsig 265
Cdd:COG0714    34 LLLEGVPGVGKTTLAKALARALGLPFIRIQFTPdlLPSDILGT---YIydqqtGEFEFRPG---PlfaNVLLADEIN--- 104
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148885657 266 ssRleggsgGDSEVQRTMLELLNQ----LDG--FEATKNIKVIMATNRIDI-----LDSALLrpgriDR---KIEFPPPN 331
Cdd:COG0714   105 --R------APPKTQSALLEAMEErqvtIPGgtYKLPEPFLVIATQNPIEQegtypLPEAQL-----DRfllKLYIGYPD 171
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1148885657 332 EEARLDILKIHSRkmnltrginlRKIAELMPGASGAEVKgvcteagmyALRE--RRVHVTQEDFEMAVAKVMQ 402
Cdd:COG0714   172 AEEEREILRRHTG----------RHLAEVEPVLSPEELL---------ALQElvRQVHVSEAVLDYIVDLVRA 225
AAA_2 pfam07724
AAA domain (Cdc48 subfamily); This Pfam entry includes some of the AAA proteins not detected ...
193-326 2.71e-09

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: 56.05  E-value: 2.71e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148885657 193 PKGV-LLYGPPGTGKTLLARAVA---HHTDCTFIRVSGSEL-----VQKFIGEGARMVR-----ELFVMAREHAPSIIFM 258
Cdd:pfam07724   2 PIGSfLFLGPTGVGKTELAKALAellFGDERALIRIDMSEYmeehsVSRLIGAPPGYVGyeeggQLTEAVRRKPYSIVLI 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148885657 259 DEIDSIgssrleggsggDSEVQRTMLELL----------NQLDgfeaTKNIKVIMATNR--IDILDSALLRPGRIDRKIE 326
Cdd:pfam07724  82 DEIEKA-----------HPGVQNDLLQILeggtltdkqgRTVD----FKNTLFIMTGNFgsEKISDASRLGDSPDYELLK 146
PRK13342 PRK13342
recombination factor protein RarA; Reviewed
196-261 3.57e-09

recombination factor protein RarA; Reviewed


Pssm-ID: 237355 [Multi-domain]  Cd Length: 413  Bit Score: 58.17  E-value: 3.57e-09
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148885657 196 VLLYGPPGTGKTLLARAVAHHTDCTFIRVSGSElvqkfigEGARMVRELFVMAREHAPS----IIFMDEI 261
Cdd:PRK13342   39 MILWGPPGTGKTTLARIIAGATDAPFEALSAVT-------SGVKDLREVIEEARQRRSAgrrtILFIDEI 101
AAA_5 pfam07728
AAA domain (dynein-related subfamily); This Pfam entry includes some of the AAA proteins not ...
195-317 1.32e-08

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


Pssm-ID: 400191 [Multi-domain]  Cd Length: 135  Bit Score: 53.07  E-value: 1.32e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148885657 195 GVLLYGPPGTGKTLLARAVAHHTDC--TFIRV-----SGSELVQK--FIGEGARMVRELFVMAREHApSIIFMDEIDSIg 265
Cdd:pfam07728   1 GVLLVGPPGTGKTELAERLAAALSNrpVFYVQltrdtTEEDLFGRrnIDPGGASWVDGPLVRAAREG-EIAVLDEINRA- 78
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1148885657 266 ssrleggsggDSEVQRTMLELLN-----QLDGFE----ATKNIKVIMATNRIDI----LDSALLR 317
Cdd:pfam07728  79 ----------NPDVLNSLLSLLDerrllLPDGGElvkaAPDGFRLIATMNPLDRglneLSPALRS 133
CDC6 COG1474
Cdc6-related protein, AAA superfamily ATPase [Replication, recombination and repair];
165-400 2.10e-08

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


Pssm-ID: 441083 [Multi-domain]  Cd Length: 389  Bit Score: 55.62  E-value: 2.10e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148885657 165 DKQIKEIKEVIElPVKHPElfealgiaQPKGVLLYGPPGTGKTLLARAVAHH---------TDCTFIRVSG--------- 226
Cdd:COG1474    32 EEEIEELASALR-PALRGE--------RPSNVLIYGPTGTGKTAVAKYVLEEleeeaeergVDVRVVYVNCrqastryrv 102
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148885657 227 -SELVQKFIGEG---------ARMVRELF-VMAREHAPSIIFMDEIDSIGSSRLEggsggdsevqrtmlELLNQL-DGFE 294
Cdd:COG1474   103 lSRILEELGSGEdipstglstDELFDRLYeALDERDGVLVVVLDEIDYLVDDEGD--------------DLLYQLlRANE 168
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148885657 295 ATKNIKV--IMATNRIDILD-------SALLrpgriDRKIEFPPPNEEARLDILKiHSRKMNLTRGI----NLRKIAELm 361
Cdd:COG1474   169 ELEGARVgvIGISNDLEFLEnldprvkSSLG-----EEEIVFPPYDADELRDILE-DRAELAFYDGVlsdeVIPLIAAL- 241
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*.
gi 1148885657 362 pgasGAEVKG-------VCTEAGMYALRERRVHVTQEDFEMAVAKV 400
Cdd:COG1474   242 ----AAQEHGdarkaidLLRVAGEIAEREGSDRVTEEHVREAREKI 283
44 PHA02544
clamp loader, small subunit; Provisional
171-340 5.85e-08

clamp loader, small subunit; Provisional


Pssm-ID: 222866 [Multi-domain]  Cd Length: 316  Bit Score: 53.84  E-value: 5.85e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148885657 171 IKEVIeLPVKHPELFEALgIAQ---PKGVLLYGPPGTGKTLLARAVAHHTDCTFIRVSGSELVQKFIGEgaRMVRELFVM 247
Cdd:PHA02544   20 IDECI-LPAADKETFKSI-VKKgriPNMLLHSPSPGTGKTTVAKALCNEVGAEVLFVNGSDCRIDFVRN--RLTRFASTV 95
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148885657 248 AREHAPSIIFMDEIDSIGSsrleggsggdSEVQRTMLELLNQLdgfeaTKNIKVIMATNRIDILDSALLrpGRIdRKIEF 327
Cdd:PHA02544   96 SLTGGGKVIIIDEFDRLGL----------ADAQRHLRSFMEAY-----SKNCSFIITANNKNGIIEPLR--SRC-RVIDF 157
                         170
                  ....*....|...
gi 1148885657 328 PPPNEEARLDILK 340
Cdd:PHA02544  158 GVPTKEEQIEMMK 170
RecA-like_ClpB_Hsp104-like cd19499
Chaperone protein ClpB/Hsp104 subfamily; Bacterial Caseinolytic peptidase B (ClpB) and ...
197-327 5.84e-07

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: 49.48  E-value: 5.84e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148885657 197 LLYGPPGTGKTLLARAVA---HHTDCTFIRVSGSEL-----VQKFIG---------EGARMVRELfvmaREHAPSIIFMD 259
Cdd:cd19499    45 LFLGPTGVGKTELAKALAellFGDEDNLIRIDMSEYmekhsVSRLIGappgyvgytEGGQLTEAV----RRKPYSVVLLD 120
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1148885657 260 EIDSigssrleggsgGDSEVQRTMLELLNqlDGFEATKNIKVIMATNRIDILDSALLRP---GRIDRKIEF 327
Cdd:cd19499   121 EIEK-----------AHPDVQNLLLQVLD--DGRLTDSHGRTVDFKNTIIIMTSNHFRPeflNRIDEIVVF 178
PRK04195 PRK04195
replication factor C large subunit; Provisional
193-264 5.86e-07

replication factor C large subunit; Provisional


Pssm-ID: 235250 [Multi-domain]  Cd Length: 482  Bit Score: 51.46  E-value: 5.86e-07
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1148885657 193 PKGVLLYGPPGTGKTLLARAVAHHTDCTFIRVSGS-----ELVQKFIGEGARMvRELFVMARehapSIIFMDEIDSI 264
Cdd:PRK04195   39 KKALLLYGPPGVGKTSLAHALANDYGWEVIELNASdqrtaDVIERVAGEAATS-GSLFGARR----KLILLDEVDGI 110
cdc6 PRK00411
ORC1-type DNA replication protein;
165-400 2.18e-06

ORC1-type DNA replication protein;


Pssm-ID: 234751 [Multi-domain]  Cd Length: 394  Bit Score: 49.46  E-value: 2.18e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148885657 165 DKQIKEIKEVIElpvkhpelfEALGIAQPKGVLLYGPPGTGKTLLARAV-----AHHTDCTFIRVSG----------SEL 229
Cdd:PRK00411   36 EEQIEELAFALR---------PALRGSRPLNVLIYGPPGTGKTTTVKKVfeeleEIAVKVVYVYINCqidrtryaifSEI 106
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148885657 230 VQKFIGEGARMV----RELFVMAREHAPS-----IIFMDEIDsigssRLEGGSGGDsevqrTMLELLNQLDGFEATKnIK 300
Cdd:PRK00411  107 ARQLFGHPPPSSglsfDELFDKIAEYLDErdrvlIVALDDIN-----YLFEKEGND-----VLYSLLRAHEEYPGAR-IG 175
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148885657 301 VIMATNRID---ILDS---ALLRPgridRKIEFPPPNEEARLDILKihSR-KMNLTRGI----NLRKIAELmpgasGAEV 369
Cdd:PRK00411  176 VIGISSDLTflyILDPrvkSVFRP----EEIYFPPYTADEIFDILK--DRvEEGFYPGVvddeVLDLIADL-----TARE 244
                         250       260       270
                  ....*....|....*....|....*....|....*...
gi 1148885657 370 KG---VCTE----AGMYALRERRVHVTQEDFEMAVAKV 400
Cdd:PRK00411  245 HGdarVAIDllrrAGLIAEREGSRKVTEEDVRKAYEKS 282
T7SS_EccA TIGR03922
type VII secretion AAA-ATPase EccA; This model represents the AAA family ATPase, EccA, of the ...
159-328 3.81e-06

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


Pssm-ID: 188437 [Multi-domain]  Cd Length: 557  Bit Score: 49.07  E-value: 3.81e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148885657 159 EMIG--GLDKQIKEIKEVIELPVKHPElfEALGIAQ-PKGVLLYGPPGTGKTLLARAVAHHTdC--------TFIRVSGS 227
Cdd:TIGR03922 277 EQIGleRVKRQVAALKSSTAMALARAE--RGLPVAQtSNHMLFAGPPGTGKTTIARVVAKIY-CglgvlrkpLVREVSRA 353
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148885657 228 ELVQKFIGEGARMVRELFVMAREhapSIIFMDEIDSIGSSRLEGGSGGDSEVQRTMLELL-NQLDGFeatkniKVIMATN 306
Cdd:TIGR03922 354 DLIGQYIGESEAKTNEIIDSALG---GVLFLDEAYTLVETGYGQKDPFGLEAIDTLLARMeNDRDRL------VVIGAGY 424
                         170       180
                  ....*....|....*....|....*..
gi 1148885657 307 RIDIlDSAL-----LRpGRIDRKIEFP 328
Cdd:TIGR03922 425 RKDL-DKFLevnegLR-SRFTRVIEFP 449
ABC_ATPase cd00267
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ...
196-317 4.72e-06

ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.


Pssm-ID: 213179 [Multi-domain]  Cd Length: 157  Bit Score: 46.47  E-value: 4.72e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148885657 196 VLLYGPPGTGKTLLARAVAHHTDCT--FIRVSGSELVQKFIGEGARMV----------RELFVMARE--HAPSIIFMDEI 261
Cdd:cd00267    28 VALVGPNGSGKSTLLRAIAGLLKPTsgEILIDGKDIAKLPLEELRRRIgyvpqlsggqRQRVALARAllLNPDLLLLDEP 107
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1148885657 262 DsigssrleggSGGDSEVQRTMLELLNQLdgfeATKNIKVIMATNRIDILDSALLR 317
Cdd:cd00267   108 T----------SGLDPASRERLLELLREL----AEEGRTVIIVTHDPELAELAADR 149
PRK13341 PRK13341
AAA family ATPase;
197-225 2.66e-05

AAA family ATPase;


Pssm-ID: 237354 [Multi-domain]  Cd Length: 725  Bit Score: 46.59  E-value: 2.66e-05
                          10        20
                  ....*....|....*....|....*....
gi 1148885657 197 LLYGPPGTGKTLLARAVAHHTDCTFIRVS 225
Cdd:PRK13341   56 ILYGPPGVGKTTLARIIANHTRAHFSSLN 84
TIP49 COG1224
DNA helicase TIP49, TBP-interacting protein [Transcription];
194-229 9.41e-05

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


Pssm-ID: 440837 [Multi-domain]  Cd Length: 452  Bit Score: 44.58  E-value: 9.41e-05
                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 1148885657 194 KGVLLYGPPGTGKTLLARAVAHH--TDCTFIRVSGSEL 229
Cdd:COG1224    65 KGILIVGPPGTGKTALAVAIARElgEDTPFVAISGSEI 102
DnaA COG0593
Chromosomal replication initiation ATPase DnaA [Replication, recombination and repair];
196-385 1.48e-04

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


Pssm-ID: 440358 [Multi-domain]  Cd Length: 303  Bit Score: 43.26  E-value: 1.48e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148885657 196 VLLYGPPGTGKTLLARAVAH-----HTDCTFIRVSGSELVQKFIgegaRMVRELFVMA-REHAPSI--IFMDEIDSIGss 267
Cdd:COG0593    37 LFLYGGVGLGKTHLLHAIGNealenNPGARVVYLTAEEFTNDFI----NAIRNNTIEEfKEKYRSVdvLLIDDIQFLA-- 110
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148885657 268 rleggsgGDSEVQRTMLELLNQLdgFEATKniKVIMATNR----IDILDSAL---LRPG---RIDrkiefpPPNEEARLD 337
Cdd:COG0593   111 -------GKEATQEEFFHTFNAL--REAGK--QIVLTSDRppkeLPGLEERLrsrLEWGlvvDIQ------PPDLETRIA 173
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 1148885657 338 IL--KIHSRKMNLTRGInLRKIAELMPGaSGAEVKGVCTEAGMYALRERR 385
Cdd:COG0593   174 ILrkKAADRGLELPDEV-LEYLARRIER-NVRELEGALNRLDAYALLTGR 221
AAA_16 pfam13191
AAA ATPase domain; This family of domains contain a P-loop motif that is characteriztic of the ...
163-216 1.99e-04

AAA ATPase domain; This family of domains contain a P-loop motif that is characteriztic of the AAA superfamily.


Pssm-ID: 433025 [Multi-domain]  Cd Length: 167  Bit Score: 41.72  E-value: 1.99e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1148885657 163 GLDKQIKEIKEvielpvkhpeLFEALGIAQPKGVLLYGPPGTGKTLLARAVAHH 216
Cdd:pfam13191   4 GREEELEQLLD----------ALDRVRSGRPPSVLLTGEAGTGKTTLLRELLRA 47
DnaC COG1484
DNA replication protein DnaC [Replication, recombination and repair];
190-216 2.38e-04

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


Pssm-ID: 441093 [Multi-domain]  Cd Length: 242  Bit Score: 42.46  E-value: 2.38e-04
                          10        20
                  ....*....|....*....|....*..
gi 1148885657 190 IAQPKGVLLYGPPGTGKTLLARAVAHH 216
Cdd:COG1484    96 IERGENLILLGPPGTGKTHLAIALGHE 122
RecA-like_Lon cd19500
lon protease homolog 2 peroxisomal; Lon protease (also known as Lon peptidase) is an ...
197-267 6.09e-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: 6.09e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148885657 197 LLYGPPGTGKTLLARAVAHHTDCTFIRVSgselvqkfIGeGARMVREL--------------FVMAREHAPS---IIFMD 259
Cdd:cd19500    41 CLVGPPGVGKTSLGKSIARALGRKFVRIS--------LG-GVRDEAEIrghrrtyvgampgrIIQALKKAGTnnpVFLLD 111

                  ....*...
gi 1148885657 260 EIDSIGSS 267
Cdd:cd19500   112 EIDKIGSS 119
McrB COG1401
5-methylcytosine-specific restriction endonuclease McrBC, GTP-binding regulatory subunit McrB ...
81-216 6.38e-04

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


Pssm-ID: 441011 [Multi-domain]  Cd Length: 477  Bit Score: 41.68  E-value: 6.38e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148885657  81 SYVGEVVRAMDKKKVLVKVHPEGKFVVDVDKNIDINDVTPNCRVALRNDSYTLHKILPNKVDPLVSLmmvekVPDSTYEM 160
Cdd:COG1401   117 GLLLELAERSDALEALERARLLLELADLEERAALETEVLEALEAELEELLAAPEDLSADALAAELSA-----AEELYSED 191
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1148885657 161 IGGLDKQIKE-IKEVIELPVKhpELFEALGIaqPKGVLLYGPPGTGKTLLARAVAHH 216
Cdd:COG1401   192 LESEDDYLKDlLREKFEETLE--AFLAALKT--KKNVILAGPPGTGKTYLARRLAEA 244
HolB COG0470
DNA polymerase III, delta prime subunit [Replication, recombination and repair];
193-220 6.62e-04

DNA polymerase III, delta prime subunit [Replication, recombination and repair];


Pssm-ID: 440238 [Multi-domain]  Cd Length: 289  Bit Score: 41.50  E-value: 6.62e-04
                          10        20
                  ....*....|....*....|....*...
gi 1148885657 193 PKGVLLYGPPGTGKTLLARAVAHHTDCT 220
Cdd:COG0470    18 PHALLLHGPPGIGKTTLALALARDLLCE 45
RecA-like_IQCA1 cd19506
ATPase domain of IQ and AAA domain-containing protein 1 (IQCA1); IQCA1 (also known as dynein ...
194-260 8.16e-04

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


Pssm-ID: 410914 [Multi-domain]  Cd Length: 160  Bit Score: 39.82  E-value: 8.16e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1148885657 194 KGVLLYGPPGTGKTLLARAVAHHTDCTFIRVSGSELVQKFIGEGA--RMVRELFVMAREHAPSIIFMDE 260
Cdd:cd19506    27 KSLLLAGPSGVGKKMLVHAICTETGANLFNLSPSNIAGKYPGKNGlqMMLHLVLKVARQLQPSVIWIGD 95
COG2842 COG2842
Bacteriophage DNA transposition protein, AAA+ family ATPase [Mobilome: prophages, transposons]; ...
196-394 8.56e-04

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


Pssm-ID: 442090 [Multi-domain]  Cd Length: 254  Bit Score: 40.71  E-value: 8.56e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148885657 196 VLLYGPPGTGKTLLARAVA-HHTDCTFIRVSGS----ELVQKF-----IGEGARMVRELFVMAREH---APSIIFMDEID 262
Cdd:COG2842    53 GVVYGESGVGKTTAAREYAnRNPNVIYVTASPSwtskELLEELaeelgIPAPPGTIADLRDRILERlagTGRLLIIDEAD 132
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148885657 263 sigssRLeggsggdsevQRTMLELLNQLdgFEATkNIKVIMATN--------RIDILDSallrpgRIDRKIEFPPPNEEA 334
Cdd:COG2842   133 -----HL----------KPKALEELRDI--HDET-GVGVVLIGMerlpaklkRYEQLYS------RIGFWVEFKPLSLED 188
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1148885657 335 RLDILKIHSrkmnltrGINLRKIAELMPGASGAEVKGVCT---EAGMYALRERRVHVTQEDFE 394
Cdd:COG2842   189 VRALAEAWG-------ELTDPDLLELLHRITRGNLRRLDRtlrLAARAAKRNGLTKITLDHVR 244
Lon COG0466
ATP-dependent Lon protease, bacterial type [Posttranslational modification, protein turnover, ...
197-225 1.41e-03

ATP-dependent Lon protease, bacterial type [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 440234 [Multi-domain]  Cd Length: 785  Bit Score: 40.77  E-value: 1.41e-03
                          10        20
                  ....*....|....*....|....*....
gi 1148885657 197 LLYGPPGTGKTLLARAVAHHTDCTFIRVS 225
Cdd:COG0466   356 CLVGPPGVGKTSLGKSIARALGRKFVRIS 384
TIP49 pfam06068
TIP49 P-loop domain; This family consists of the C-terminal region of several eukaryotic and ...
194-229 1.49e-03

TIP49 P-loop domain; This family consists of the C-terminal region of several eukaryotic and archaeal RuvB-like 1 (Pontin or TIP49a) and RuvB-like 2 (Reptin or TIP49b) proteins. The N-terminal domain contains the pfam00004 domain. In zebrafish, the liebeskummer (lik) mutation, causes development of hyperplastic embryonic hearts. lik encodes Reptin, a component of a DNA-stimulated ATPase complex. Beta-catenin and Pontin, a DNA-stimulated ATPase that is often part of complexes with Reptin, are in the same genetic pathways. The Reptin/Pontin ratio serves to regulate heart growth during development, at least in part via the beta-catenin pathway. TBP-interacting protein 49 (TIP49) was originally identified as a TBP-binding protein, and two related proteins are encoded by individual genes, tip49a and b. Although the function of this gene family has not been elucidated, they are supposed to play a critical role in nuclear events because they interact with various kinds of nuclear factors and have DNA helicase activities.TIP49a has been suggested to act as an autoantigen in some patients with autoimmune diseases.


Pssm-ID: 399217 [Multi-domain]  Cd Length: 347  Bit Score: 40.37  E-value: 1.49e-03
                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 1148885657 194 KGVLLYGPPGTGKTLLARAVAHH--TDCTFIRVSGSEL 229
Cdd:pfam06068  51 RAVLIAGPPGTGKTALAIAISKElgEDTPFTSISGSEV 88
ExeA COG3267
Type II secretory pathway ATPase component GspA/ExeA/MshM [Intracellular trafficking, ...
181-215 2.81e-03

Type II secretory pathway ATPase component GspA/ExeA/MshM [Intracellular trafficking, secretion, and vesicular transport, Extracellular structures];


Pssm-ID: 442498 [Multi-domain]  Cd Length: 261  Bit Score: 39.39  E-value: 2.81e-03
                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 1148885657 181 HPELFEAL--GIAQPKG-VLLYGPPGTGKTLLARAVAH 215
Cdd:COG3267    28 HREALARLeyALAQGGGfVVLTGEVGTGKTTLLRRLLE 65
ruvB PRK00080
Holliday junction branch migration DNA helicase RuvB;
196-261 3.00e-03

Holliday junction branch migration DNA helicase RuvB;


Pssm-ID: 234619 [Multi-domain]  Cd Length: 328  Bit Score: 39.34  E-value: 3.00e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1148885657 196 VLLYGPPGTGKTLLARAVAHHTDCTFIRVSGSELVQKfiGEGARMVRELfvmaREHapSIIFMDEI 261
Cdd:PRK00080   54 VLLYGPPGLGKTTLANIIANEMGVNIRITSGPALEKP--GDLAAILTNL----EEG--DVLFIDEI 111
ruvB TIGR00635
Holliday junction DNA helicase, RuvB subunit; All proteins in this family for which functions ...
169-360 3.26e-03

Holliday junction DNA helicase, RuvB subunit; All proteins in this family for which functions are known are 5'-3' DNA helicases that, as part of a complex with RuvA homologs serve as a 5'-3' Holliday junction helicase. RuvA specifically binds Holliday junctions as a sandwich of two tetramers and maintains the configuration of the junction. It forms a complex with two hexameric rings of RuvB, the subunit that contains helicase activity. The complex drives ATP-dependent branch migration of the Holliday junction recombination intermediate. The endonuclease RuvC resolves junctions. [DNA metabolism, DNA replication, recombination, and repair]


Pssm-ID: 129721 [Multi-domain]  Cd Length: 305  Bit Score: 39.21  E-value: 3.26e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148885657 169 KEIKEVIELPVKHPELFEAlgiaQPKGVLLYGPPGTGKTLLARAVAHHTDcTFIRVSGSELVQKfIGEGARMVRELfvma 248
Cdd:TIGR00635  10 EKVKEQLQLFIEAAKMRQE----ALDHLLLYGPPGLGKTTLAHIIANEMG-VNLKITSGPALEK-PGDLAAILTNL---- 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148885657 249 REHapSIIFMDEIDSIGssrleggsggdsevqRTMLELLN------QLD-----GFEA-TKNIKV-----IMATNRIDIL 311
Cdd:TIGR00635  80 EEG--DVLFIDEIHRLS---------------PAVEELLYpamedfRLDivigkGPSArSVRLDLppftlVGATTRAGML 142
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 1148885657 312 DSALL-RPGRIDRkIEFPPPNEEARldILKIHSRKMNLTrgINLRKIAEL 360
Cdd:TIGR00635 143 TSPLRdRFGIILR-LEFYTVEELAE--IVSRSAGLLNVE--IEPEAALEI 187
YifB COG0606
Predicted Mg-chelatase, contains ChlI-like and ATPase domains, YifB family [Posttranslational ...
196-211 5.43e-03

Predicted Mg-chelatase, contains ChlI-like and ATPase domains, YifB family [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 440371 [Multi-domain]  Cd Length: 502  Bit Score: 38.87  E-value: 5.43e-03
                          10
                  ....*....|....*.
gi 1148885657 196 VLLYGPPGTGKTLLAR 211
Cdd:COG0606   214 LLMIGPPGSGKTMLAR 229
Parvo_NS1 pfam01057
Parvovirus non-structural protein NS1; This family also contains the NS2 protein. Parvoviruses ...
196-215 5.75e-03

Parvovirus non-structural protein NS1; This family also contains the NS2 protein. Parvoviruses encode two non-structural proteins, NS1 and NS2. The mRNA for NS2 contains the coding sequence for the first 87 amino acids of NS1, then by an alternative splicing mechanism mRNA from a different reading frame, encoding the last 78 amino acids, makes up the full length of the NS2 mRNA. NS1, is the major non-structural protein. It is essential for DNA replication. It is an 83-kDa nuclear phosphoprotein. It has DNA helicase and ATPase activity.


Pssm-ID: 426020  Cd Length: 271  Bit Score: 38.44  E-value: 5.75e-03
                          10        20
                  ....*....|....*....|
gi 1148885657 196 VLLYGPPGTGKTLLARAVAH 215
Cdd:pfam01057 116 VWFYGPASTGKTNLAQAIAH 135
RuvB_N pfam05496
Holliday junction DNA helicase RuvB P-loop domain; The RuvB protein makes up part of the ...
196-215 6.26e-03

Holliday junction DNA helicase RuvB P-loop domain; The RuvB protein makes up part of the RuvABC revolvasome which catalyzes the resolution of Holliday junctions that arise during genetic recombination and DNA repair. Branch migration is catalyzed by the RuvB protein that is targeted to the Holliday junction by the structure specific RuvA protein. This family contains the N-terminal region of the protein.


Pssm-ID: 398900 [Multi-domain]  Cd Length: 159  Bit Score: 37.09  E-value: 6.26e-03
                          10        20
                  ....*....|....*....|
gi 1148885657 196 VLLYGPPGTGKTLLARAVAH 215
Cdd:pfam05496  36 VLLYGPPGLGKTTLANIIAN 55
Mg_chelatase pfam01078
Magnesium chelatase, subunit ChlI; Magnesium-chelatase is a three-component enzyme that ...
187-212 6.54e-03

Magnesium chelatase, subunit ChlI; Magnesium-chelatase is a three-component enzyme that catalyzes the insertion of Mg2+ into protoporphyrin IX. This is the first unique step in the synthesis of (bacterio)chlorophyll. Due to this, it is thought that Mg-chelatase has an important role in channelling inter- mediates into the (bacterio)chlorophyll branch in response to conditions suitable for photosynthetic growth. ChlI and BchD have molecular weight between 38-42 kDa.


Pssm-ID: 426032 [Multi-domain]  Cd Length: 207  Bit Score: 37.51  E-value: 6.54e-03
                          10        20
                  ....*....|....*....|....*...
gi 1148885657 187 ALGIAQPKG--VLLYGPPGTGKTLLARA 212
Cdd:pfam01078  14 ALEIAAAGGhnLLMIGPPGSGKTMLAKR 41
RuvB COG2255
Holliday junction resolvasome RuvABC, ATP-dependent DNA helicase subunit RuvB [Replication, ...
196-215 6.76e-03

Holliday junction resolvasome RuvABC, ATP-dependent DNA helicase subunit RuvB [Replication, recombination and repair];


Pssm-ID: 441856 [Multi-domain]  Cd Length: 337  Bit Score: 38.14  E-value: 6.76e-03
                          10        20
                  ....*....|....*....|
gi 1148885657 196 VLLYGPPGTGKTLLARAVAH 215
Cdd:COG2255    57 VLLYGPPGLGKTTLAHIIAN 76
PRK08116 PRK08116
hypothetical protein; Validated
195-216 6.89e-03

hypothetical protein; Validated


Pssm-ID: 236153 [Multi-domain]  Cd Length: 268  Bit Score: 38.08  E-value: 6.89e-03
                          10        20
                  ....*....|....*....|..
gi 1148885657 195 GVLLYGPPGTGKTLLARAVAHH 216
Cdd:PRK08116  116 GLLLWGSVGTGKTYLAACIANE 137
COG0645 COG0645
Predicted kinase, contains AAA domain [General function prediction only];
196-224 8.33e-03

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


Pssm-ID: 440410 [Multi-domain]  Cd Length: 164  Bit Score: 36.81  E-value: 8.33e-03
                          10        20
                  ....*....|....*....|....*....
gi 1148885657 196 VLLYGPPGTGKTLLARAVAHHTDCTFIRV 224
Cdd:COG0645     2 ILVCGLPGSGKSTLARALAERLGAVRLRS 30
RecA-like_superfamily cd01120
RecA-like_NTPases; RecA-like NTPases. This superfamily includes the NTP binding domain of F1 ...
196-312 8.58e-03

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


Pssm-ID: 410865 [Multi-domain]  Cd Length: 119  Bit Score: 35.94  E-value: 8.58e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148885657 196 VLLYGPPGTGKTLLARAVAH---HTDCTFIRVSGSElvqkfigegaRMVRELFVMAREHAPSIIFmdeIDSIGSSRLEGG 272
Cdd:cd01120     1 ILITGPPGSGKTTLLLQFAEqalLSDEPVIFISFLD----------TILEAIEDLIEEKKLDIII---IDSLSSLARASQ 67
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 1148885657 273 SGGDSEVQRTMLELLNQldgfeATKNIKVIMATNRIDILD 312
Cdd:cd01120    68 GDRSSELLEDLAKLLRA-----ARNTGITVIATIHSDKFD 102
IS21_help_AAA NF038214
IS21-like element helper ATPase IstB; This protein family model resembles PF01695, but was ...
190-215 9.22e-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: 37.45  E-value: 9.22e-03
                          10        20
                  ....*....|....*....|....*.
gi 1148885657 190 IAQPKGVLLYGPPGTGKTLLARAVAH 215
Cdd:NF038214   87 IERAENVLLLGPPGTGKTHLAIALGY 112
 
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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