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Conserved domains on  [gi|258596995|ref|XP_001347366|]
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26S protease regulatory subunit 4, putative [Plasmodium falciparum 3D7]

Protein Classification

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

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

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
PTZ00361 PTZ00361
26 proteosome regulatory subunit 4-like protein; Provisional
1-448 0e+00

26 proteosome regulatory subunit 4-like protein; Provisional


:

Pssm-ID: 185575 [Multi-domain]  Cd Length: 438  Bit Score: 811.31  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258596995   1 MGNTPGGMNNPygflgkkedkdKGKDKDKEKKKLESVPISHMGKKKKKNKGTSGHSKLPNVTPNTKCRLKLLKLERIKDY 80
Cdd:PTZ00361   1 MGNAQGQGNNQ-----------KDKNKKKEKKKKESPPPPHEIKRKKKRKGPDAASKLPKVTPNTKCRLRLLKLERIKDY 69
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258596995  81 LLLEEEYITNQEQIKSSDDKNYVKL-KIDDLRGSPVSVGTLEELIDENHGIIATSVGPEYYVNILSFVDKDLLEPGCSVL 159
Cdd:PTZ00361  70 LLLEEEFITNQEAQKPAQEKNEAELkKVDDLRGSPLSVGTLEEIIDENHAIVSSSVGPEYYVNILSFVDKEQLEPGCSVL 149
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258596995 160 LNNKTNSVVGILLDEVDPLVSVMKVEKAPLESYADIGGLESQIQEIKEAVELPLTHPELYEDIGIKPPKGVILYGPPGTG 239
Cdd:PTZ00361 150 LHNKTHSVVGILLDEVDPLVSVMKVDKAPLESYADIGGLEQQIQEIKEAVELPLTHPELYDDIGIKPPKGVILYGPPGTG 229
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258596995 240 KTLLAKAVANETSATFLRVVGSELIQKYLGDGPKLVREMFKVAEEHAPSIVFIDEIDAVGTKRYEATSGGEREIQRTMLE 319
Cdd:PTZ00361 230 KTLLAKAVANETSATFLRVVGSELIQKYLGDGPKLVRELFRVAEENAPSIVFIDEIDAIGTKRYDATSGGEKEIQRTMLE 309
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258596995 320 LLNQLDGFDSRGDVKVIMATNRIDSLDPALIRPGRIDRKIQLPNPDTKTKRRIFQIHTSKMTMSPDVDLEEFVMSKDELS 399
Cdd:PTZ00361 310 LLNQLDGFDSRGDVKVIMATNRIESLDPALIRPGRIDRKIEFPNPDEKTKRRIFEIHTSKMTLAEDVDLEEFIMAKDELS 389
                        410       420       430       440
                 ....*....|....*....|....*....|....*....|....*....
gi 258596995 400 GADIKAICTEAGLLALRERRMKITQADLRKARDKALFQKKGNIPEGLYL 448
Cdd:PTZ00361 390 GADIKAICTEAGLLALRERRMKVTQADFRKAKEKVLYRKKGNIPEGLYL 438
 
Name Accession Description Interval E-value
PTZ00361 PTZ00361
26 proteosome regulatory subunit 4-like protein; Provisional
1-448 0e+00

26 proteosome regulatory subunit 4-like protein; Provisional


Pssm-ID: 185575 [Multi-domain]  Cd Length: 438  Bit Score: 811.31  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258596995   1 MGNTPGGMNNPygflgkkedkdKGKDKDKEKKKLESVPISHMGKKKKKNKGTSGHSKLPNVTPNTKCRLKLLKLERIKDY 80
Cdd:PTZ00361   1 MGNAQGQGNNQ-----------KDKNKKKEKKKKESPPPPHEIKRKKKRKGPDAASKLPKVTPNTKCRLRLLKLERIKDY 69
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258596995  81 LLLEEEYITNQEQIKSSDDKNYVKL-KIDDLRGSPVSVGTLEELIDENHGIIATSVGPEYYVNILSFVDKDLLEPGCSVL 159
Cdd:PTZ00361  70 LLLEEEFITNQEAQKPAQEKNEAELkKVDDLRGSPLSVGTLEEIIDENHAIVSSSVGPEYYVNILSFVDKEQLEPGCSVL 149
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258596995 160 LNNKTNSVVGILLDEVDPLVSVMKVEKAPLESYADIGGLESQIQEIKEAVELPLTHPELYEDIGIKPPKGVILYGPPGTG 239
Cdd:PTZ00361 150 LHNKTHSVVGILLDEVDPLVSVMKVDKAPLESYADIGGLEQQIQEIKEAVELPLTHPELYDDIGIKPPKGVILYGPPGTG 229
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258596995 240 KTLLAKAVANETSATFLRVVGSELIQKYLGDGPKLVREMFKVAEEHAPSIVFIDEIDAVGTKRYEATSGGEREIQRTMLE 319
Cdd:PTZ00361 230 KTLLAKAVANETSATFLRVVGSELIQKYLGDGPKLVRELFRVAEENAPSIVFIDEIDAIGTKRYDATSGGEKEIQRTMLE 309
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258596995 320 LLNQLDGFDSRGDVKVIMATNRIDSLDPALIRPGRIDRKIQLPNPDTKTKRRIFQIHTSKMTMSPDVDLEEFVMSKDELS 399
Cdd:PTZ00361 310 LLNQLDGFDSRGDVKVIMATNRIESLDPALIRPGRIDRKIEFPNPDEKTKRRIFEIHTSKMTLAEDVDLEEFIMAKDELS 389
                        410       420       430       440
                 ....*....|....*....|....*....|....*....|....*....
gi 258596995 400 GADIKAICTEAGLLALRERRMKITQADLRKARDKALFQKKGNIPEGLYL 448
Cdd:PTZ00361 390 GADIKAICTEAGLLALRERRMKVTQADFRKAKEKVLYRKKGNIPEGLYL 438
26Sp45 TIGR01242
26S proteasome subunit P45 family; Many proteins may score above the trusted cutoff because an ...
65-435 3.83e-157

26S proteasome subunit P45 family; Many proteins may score above the trusted cutoff because an internal


Pssm-ID: 130309 [Multi-domain]  Cd Length: 364  Bit Score: 448.86  E-value: 3.83e-157
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258596995   65 TKCRLKLLKLEriKDYLLLEEEYITNQEQIKssddknYVKLKIDDLRGSPVSVGTLEELIDENHGIIATSVGPEYYVNIL 144
Cdd:TIGR01242   2 SELDVRIRKLE--DEKRSLEKEKIRLERELE------RLRSEIERLRSPPLIVGTVLEVLDDNRVVVKSSTGPNFVVNVS 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258596995  145 SFVDKDLLEPGCSVLLNNKTNSVVGILLDEVDPLVSVMKVEKAPLESYADIGGLESQIQEIKEAVELPLTHPELYEDIGI 224
Cdd:TIGR01242  74 AFIDRKSLKPGARVALNQQTLTIVDVLPTSKDPLVKGMEVEERPNVSYEDIGGLEEQIREIREAVELPLKHPELFEEVGI 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258596995  225 KPPKGVILYGPPGTGKTLLAKAVANETSATFLRVVGSELIQKYLGDGPKLVREMFKVAEEHAPSIVFIDEIDAVGTKRYE 304
Cdd:TIGR01242 154 EPPKGVLLYGPPGTGKTLLAKAVAHETNATFIRVVGSELVRKYIGEGARLVREIFELAKEKAPSIIFIDEIDAIAAKRTD 233
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258596995  305 ATSGGEREIQRTMLELLNQLDGFDSRGDVKVIMATNRIDSLDPALIRPGRIDRKIQLPNPDTKTKRRIFQIHTSKMTMSP 384
Cdd:TIGR01242 234 SGTSGDREVQRTLMQLLAELDGFDPRGNVKVIAATNRPDILDPALLRPGRFDRIIEVPLPDFEGRLEILKIHTRKMKLAE 313
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|.
gi 258596995  385 DVDLEEFVMSKDELSGADIKAICTEAGLLALRERRMKITQADLRKARDKAL 435
Cdd:TIGR01242 314 DVDLEAIAKMTEGASGADLKAICTEAGMFAIREERDYVTMDDFIKAVEKVL 364
RPT1 COG1222
ATP-dependent 26S proteasome regulatory subunit [Posttranslational modification, protein ...
182-433 4.38e-132

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


Pssm-ID: 440835 [Multi-domain]  Cd Length: 326  Bit Score: 383.59  E-value: 4.38e-132
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258596995 182 MKVEKAPLESYADIGGLESQIQEIKEAVELPLTHPELYEDIGIKPPKGVILYGPPGTGKTLLAKAVANETSATFLRVVGS 261
Cdd:COG1222   67 AVPAESPDVTFDDIGGLDEQIEEIREAVELPLKNPELFRKYGIEPPKGVLLYGPPGTGKTLLAKAVAGELGAPFIRVRGS 146
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258596995 262 ELIQKYLGDGPKLVREMFKVAEEHAPSIVFIDEIDAVGTKRYEATSGGerEIQRTMLELLNQLDGFDSRGDVKVIMATNR 341
Cdd:COG1222  147 ELVSKYIGEGARNVREVFELAREKAPSIIFIDEIDAIAARRTDDGTSG--EVQRTVNQLLAELDGFESRGDVLIIAATNR 224
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258596995 342 IDSLDPALIRPGRIDRKIQLPNPDTKTKRRIFQIHTSKMTMSPDVDLEEFVMSKDELSGADIKAICTEAGLLALRERRMK 421
Cdd:COG1222  225 PDLLDPALLRPGRFDRVIEVPLPDEEAREEILKIHLRDMPLADDVDLDKLAKLTEGFSGADLKAIVTEAGMFAIREGRDT 304
                        250
                 ....*....|..
gi 258596995 422 ITQADLRKARDK 433
Cdd:COG1222  305 VTMEDLEKAIEK 316
RecA-like_PAN_like cd19502
proteasome activating nucleotidase PAN and related proteasome subunits; This subfamily ...
191-360 2.38e-114

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: 332.76  E-value: 2.38e-114
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258596995 191 SYADIGGLESQIQEIKEAVELPLTHPELYEDIGIKPPKGVILYGPPGTGKTLLAKAVANETSATFLRVVGSELIQKYLGD 270
Cdd:cd19502    1 TYEDIGGLDEQIREIREVVELPLKHPELFEELGIEPPKGVLLYGPPGTGKTLLAKAVANHTDATFIRVVGSELVQKYIGE 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258596995 271 GPKLVREMFKVAEEHAPSIVFIDEIDAVGTKRYEATSGGEREIQRTMLELLNQLDGFDSRGDVKVIMATNRIDSLDPALI 350
Cdd:cd19502   81 GARLVRELFEMAREKAPSIIFIDEIDAIGAKRFDSGTGGDREVQRTMLELLNQLDGFDPRGNIKVIMATNRPDILDPALL 160
                        170
                 ....*....|
gi 258596995 351 RPGRIDRKIQ 360
Cdd:cd19502  161 RPGRFDRKIE 170
AAA pfam00004
ATPase family associated with various cellular activities (AAA); AAA family proteins often ...
230-362 3.45e-52

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: 171.62  E-value: 3.45e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258596995  230 VILYGPPGTGKTLLAKAVANETSATFLRVVGSELIQKYLGDGPKLVREMFKVAEEHAPSIVFIDEIDAVGTKRYeatSGG 309
Cdd:pfam00004   1 LLLYGPPGTGKTTLAKAVAKELGAPFIEISGSELVSKYVGESEKRLRELFEAAKKLAPCVIFIDEIDALAGSRG---SGG 77
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 258596995  310 EREIQRTMLELLNQLDGFDSR-GDVKVIMATNRIDSLDPALIrpGRIDRKIQLP 362
Cdd:pfam00004  78 DSESRRVVNQLLTELDGFTSSnSKVIVIAATNRPDKLDPALL--GRFDRIIEFP 129
AAA smart00382
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ...
226-365 6.83e-19

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: 83.19  E-value: 6.83e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258596995   226 PPKGVILYGPPGTGKTLLAKAVANETSATFLRVV-----------------GSELIQKYLGDGPKLVREMFKVAEEHAPS 288
Cdd:smart00382   1 PGEVILIVGPPGSGKTTLARALARELGPPGGGVIyidgedileevldqlllIIVGGKKASGSGELRLRLALALARKLKPD 80
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 258596995   289 IVFIDEIDAVGTKryeatsggEREIQRTMLELLNQLDGFDSRGDVKVIMATNRIDSLDPALIRPgRIDRKIQLPNPD 365
Cdd:smart00382  81 VLILDEITSLLDA--------EQEALLLLLEELRLLLLLKSEKNLTVILTTNDEKDLGPALLRR-RFDRRIVLLLIL 148
IS21_help_AAA NF038214
IS21-like element helper ATPase IstB; This protein family model resembles PF01695, but was ...
230-307 9.09e-05

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: 43.61  E-value: 9.09e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258596995 230 VILYGPPGTGKTLLAKAVANE-----TSATFLRVvgSELIQKYL---GDGpKLVREMFKVAeehAPSIVFIDEI-----D 296
Cdd:NF038214  93 VLLLGPPGTGKTHLAIALGYAacrqgYRVRFTTA--ADLVEQLAqarADG-RLGRLLRRLA---RYDLLIIDELgylpfS 166
                         90
                 ....*....|....*....
gi 258596995 297 AVGT--------KRYEATS 307
Cdd:NF038214 167 REGAnllfeliaDRYERGS 185
 
Name Accession Description Interval E-value
PTZ00361 PTZ00361
26 proteosome regulatory subunit 4-like protein; Provisional
1-448 0e+00

26 proteosome regulatory subunit 4-like protein; Provisional


Pssm-ID: 185575 [Multi-domain]  Cd Length: 438  Bit Score: 811.31  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258596995   1 MGNTPGGMNNPygflgkkedkdKGKDKDKEKKKLESVPISHMGKKKKKNKGTSGHSKLPNVTPNTKCRLKLLKLERIKDY 80
Cdd:PTZ00361   1 MGNAQGQGNNQ-----------KDKNKKKEKKKKESPPPPHEIKRKKKRKGPDAASKLPKVTPNTKCRLRLLKLERIKDY 69
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258596995  81 LLLEEEYITNQEQIKSSDDKNYVKL-KIDDLRGSPVSVGTLEELIDENHGIIATSVGPEYYVNILSFVDKDLLEPGCSVL 159
Cdd:PTZ00361  70 LLLEEEFITNQEAQKPAQEKNEAELkKVDDLRGSPLSVGTLEEIIDENHAIVSSSVGPEYYVNILSFVDKEQLEPGCSVL 149
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258596995 160 LNNKTNSVVGILLDEVDPLVSVMKVEKAPLESYADIGGLESQIQEIKEAVELPLTHPELYEDIGIKPPKGVILYGPPGTG 239
Cdd:PTZ00361 150 LHNKTHSVVGILLDEVDPLVSVMKVDKAPLESYADIGGLEQQIQEIKEAVELPLTHPELYDDIGIKPPKGVILYGPPGTG 229
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258596995 240 KTLLAKAVANETSATFLRVVGSELIQKYLGDGPKLVREMFKVAEEHAPSIVFIDEIDAVGTKRYEATSGGEREIQRTMLE 319
Cdd:PTZ00361 230 KTLLAKAVANETSATFLRVVGSELIQKYLGDGPKLVRELFRVAEENAPSIVFIDEIDAIGTKRYDATSGGEKEIQRTMLE 309
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258596995 320 LLNQLDGFDSRGDVKVIMATNRIDSLDPALIRPGRIDRKIQLPNPDTKTKRRIFQIHTSKMTMSPDVDLEEFVMSKDELS 399
Cdd:PTZ00361 310 LLNQLDGFDSRGDVKVIMATNRIESLDPALIRPGRIDRKIEFPNPDEKTKRRIFEIHTSKMTLAEDVDLEEFIMAKDELS 389
                        410       420       430       440
                 ....*....|....*....|....*....|....*....|....*....
gi 258596995 400 GADIKAICTEAGLLALRERRMKITQADLRKARDKALFQKKGNIPEGLYL 448
Cdd:PTZ00361 390 GADIKAICTEAGLLALRERRMKVTQADFRKAKEKVLYRKKGNIPEGLYL 438
PRK03992 PRK03992
proteasome-activating nucleotidase; Provisional
70-433 1.55e-178

proteasome-activating nucleotidase; Provisional


Pssm-ID: 179699 [Multi-domain]  Cd Length: 389  Bit Score: 503.98  E-value: 1.55e-178
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258596995  70 KLLKLERIKDYLLLEEEYITNqEQIKSSDDKNYVKLKIDDLRGSPVSVGTLEELIDENHGIIATSVGPEYYVNILSFVDK 149
Cdd:PRK03992   9 RNSELEEQIRQLELKLRDLEA-ENEKLERELERLKSELEKLKSPPLIVATVLEVLDDGRVVVKSSGGPQFLVNVSPFIDR 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258596995 150 DLLEPGCSVLLNNKTNSVVGILLDEVDPLVSVMKVEKAPLESYADIGGLESQIQEIKEAVELPLTHPELYEDIGIKPPKG 229
Cdd:PRK03992  88 EKLKPGARVALNQQSLAIVEVLPSEKDPRVQAMEVIESPNVTYEDIGGLEEQIREVREAVELPLKKPELFEEVGIEPPKG 167
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258596995 230 VILYGPPGTGKTLLAKAVANETSATFLRVVGSELIQKYLGDGPKLVREMFKVAEEHAPSIVFIDEIDAVGTKRYEATSGG 309
Cdd:PRK03992 168 VLLYGPPGTGKTLLAKAVAHETNATFIRVVGSELVQKFIGEGARLVRELFELAREKAPSIIFIDEIDAIAAKRTDSGTSG 247
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258596995 310 EREIQRTMLELLNQLDGFDSRGDVKVIMATNRIDSLDPALIRPGRIDRKIQLPNPDTKTKRRIFQIHTSKMTMSPDVDLE 389
Cdd:PRK03992 248 DREVQRTLMQLLAEMDGFDPRGNVKIIAATNRIDILDPAILRPGRFDRIIEVPLPDEEGRLEILKIHTRKMNLADDVDLE 327
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....
gi 258596995 390 EFVMSKDELSGADIKAICTEAGLLALRERRMKITQADLRKARDK 433
Cdd:PRK03992 328 ELAELTEGASGADLKAICTEAGMFAIRDDRTEVTMEDFLKAIEK 371
PTZ00454 PTZ00454
26S protease regulatory subunit 6B-like protein; Provisional
69-430 1.26e-162

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


Pssm-ID: 240423 [Multi-domain]  Cd Length: 398  Bit Score: 464.24  E-value: 1.26e-162
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258596995  69 LKLLKLERIKDYLLLEEEYI-TNQEQIKSSDDKnyVKLKIDDLRGSPVSVGTLEELIDENHGIIATSVGPEYYVNILSFV 147
Cdd:PTZ00454  22 EKLKELEKELEFLDIQEEYIkEEQKNLKRELIR--AKEEVKRIQSVPLVIGQFLEMIDSNYGIVSSTSGSNYYVRILSTL 99
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258596995 148 DKDLLEPGCSVLLNNKTNSVVGILLDEVDPLVSVMKVEKAPLESYADIGGLESQIQEIKEAVELPLTHPELYEDIGIKPP 227
Cdd:PTZ00454 100 NRELLKPNASVALHRHSHAVVDILPPEADSSIQLLQMSEKPDVTYSDIGGLDIQKQEIREAVELPLTCPELYEQIGIDPP 179
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258596995 228 KGVILYGPPGTGKTLLAKAVANETSATFLRVVGSELIQKYLGDGPKLVREMFKVAEEHAPSIVFIDEIDAVGTKRYEATS 307
Cdd:PTZ00454 180 RGVLLYGPPGTGKTMLAKAVAHHTTATFIRVVGSEFVQKYLGEGPRMVRDVFRLARENAPSIIFIDEVDSIATKRFDAQT 259
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258596995 308 GGEREIQRTMLELLNQLDGFDSRGDVKVIMATNRIDSLDPALIRPGRIDRKIQLPNPDTKTKRRIFQIHTSKMTMSPDVD 387
Cdd:PTZ00454 260 GADREVQRILLELLNQMDGFDQTTNVKVIMATNRADTLDPALLRPGRLDRKIEFPLPDRRQKRLIFQTITSKMNLSEEVD 339
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|...
gi 258596995 388 LEEFVMSKDELSGADIKAICTEAGLLALRERRMKITQADLRKA 430
Cdd:PTZ00454 340 LEDFVSRPEKISAADIAAICQEAGMQAVRKNRYVILPKDFEKG 382
26Sp45 TIGR01242
26S proteasome subunit P45 family; Many proteins may score above the trusted cutoff because an ...
65-435 3.83e-157

26S proteasome subunit P45 family; Many proteins may score above the trusted cutoff because an internal


Pssm-ID: 130309 [Multi-domain]  Cd Length: 364  Bit Score: 448.86  E-value: 3.83e-157
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258596995   65 TKCRLKLLKLEriKDYLLLEEEYITNQEQIKssddknYVKLKIDDLRGSPVSVGTLEELIDENHGIIATSVGPEYYVNIL 144
Cdd:TIGR01242   2 SELDVRIRKLE--DEKRSLEKEKIRLERELE------RLRSEIERLRSPPLIVGTVLEVLDDNRVVVKSSTGPNFVVNVS 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258596995  145 SFVDKDLLEPGCSVLLNNKTNSVVGILLDEVDPLVSVMKVEKAPLESYADIGGLESQIQEIKEAVELPLTHPELYEDIGI 224
Cdd:TIGR01242  74 AFIDRKSLKPGARVALNQQTLTIVDVLPTSKDPLVKGMEVEERPNVSYEDIGGLEEQIREIREAVELPLKHPELFEEVGI 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258596995  225 KPPKGVILYGPPGTGKTLLAKAVANETSATFLRVVGSELIQKYLGDGPKLVREMFKVAEEHAPSIVFIDEIDAVGTKRYE 304
Cdd:TIGR01242 154 EPPKGVLLYGPPGTGKTLLAKAVAHETNATFIRVVGSELVRKYIGEGARLVREIFELAKEKAPSIIFIDEIDAIAAKRTD 233
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258596995  305 ATSGGEREIQRTMLELLNQLDGFDSRGDVKVIMATNRIDSLDPALIRPGRIDRKIQLPNPDTKTKRRIFQIHTSKMTMSP 384
Cdd:TIGR01242 234 SGTSGDREVQRTLMQLLAELDGFDPRGNVKVIAATNRPDILDPALLRPGRFDRIIEVPLPDFEGRLEILKIHTRKMKLAE 313
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|.
gi 258596995  385 DVDLEEFVMSKDELSGADIKAICTEAGLLALRERRMKITQADLRKARDKAL 435
Cdd:TIGR01242 314 DVDLEAIAKMTEGASGADLKAICTEAGMFAIREERDYVTMDDFIKAVEKVL 364
RPT1 COG1222
ATP-dependent 26S proteasome regulatory subunit [Posttranslational modification, protein ...
182-433 4.38e-132

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


Pssm-ID: 440835 [Multi-domain]  Cd Length: 326  Bit Score: 383.59  E-value: 4.38e-132
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258596995 182 MKVEKAPLESYADIGGLESQIQEIKEAVELPLTHPELYEDIGIKPPKGVILYGPPGTGKTLLAKAVANETSATFLRVVGS 261
Cdd:COG1222   67 AVPAESPDVTFDDIGGLDEQIEEIREAVELPLKNPELFRKYGIEPPKGVLLYGPPGTGKTLLAKAVAGELGAPFIRVRGS 146
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258596995 262 ELIQKYLGDGPKLVREMFKVAEEHAPSIVFIDEIDAVGTKRYEATSGGerEIQRTMLELLNQLDGFDSRGDVKVIMATNR 341
Cdd:COG1222  147 ELVSKYIGEGARNVREVFELAREKAPSIIFIDEIDAIAARRTDDGTSG--EVQRTVNQLLAELDGFESRGDVLIIAATNR 224
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258596995 342 IDSLDPALIRPGRIDRKIQLPNPDTKTKRRIFQIHTSKMTMSPDVDLEEFVMSKDELSGADIKAICTEAGLLALRERRMK 421
Cdd:COG1222  225 PDLLDPALLRPGRFDRVIEVPLPDEEAREEILKIHLRDMPLADDVDLDKLAKLTEGFSGADLKAIVTEAGMFAIREGRDT 304
                        250
                 ....*....|..
gi 258596995 422 ITQADLRKARDK 433
Cdd:COG1222  305 VTMEDLEKAIEK 316
RecA-like_PAN_like cd19502
proteasome activating nucleotidase PAN and related proteasome subunits; This subfamily ...
191-360 2.38e-114

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: 332.76  E-value: 2.38e-114
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258596995 191 SYADIGGLESQIQEIKEAVELPLTHPELYEDIGIKPPKGVILYGPPGTGKTLLAKAVANETSATFLRVVGSELIQKYLGD 270
Cdd:cd19502    1 TYEDIGGLDEQIREIREVVELPLKHPELFEELGIEPPKGVLLYGPPGTGKTLLAKAVANHTDATFIRVVGSELVQKYIGE 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258596995 271 GPKLVREMFKVAEEHAPSIVFIDEIDAVGTKRYEATSGGEREIQRTMLELLNQLDGFDSRGDVKVIMATNRIDSLDPALI 350
Cdd:cd19502   81 GARLVRELFEMAREKAPSIIFIDEIDAIGAKRFDSGTGGDREVQRTMLELLNQLDGFDPRGNIKVIMATNRPDILDPALL 160
                        170
                 ....*....|
gi 258596995 351 RPGRIDRKIQ 360
Cdd:cd19502  161 RPGRFDRKIE 170
FtsH_fam TIGR01241
ATP-dependent metalloprotease FtsH; HflB(FtsH) is a pleiotropic protein required for correct ...
191-435 2.38e-84

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: 267.23  E-value: 2.38e-84
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258596995  191 SYADIGGLESQIQEIKEAVELpLTHPELYEDIGIKPPKGVILYGPPGTGKTLLAKAVANETSATFLRVVGSELIQKYLGD 270
Cdd:TIGR01241  53 TFKDVAGIDEAKEELMEIVDF-LKNPSKFTKLGAKIPKGVLLVGPPGTGKTLLAKAVAGEAGVPFFSISGSDFVEMFVGV 131
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258596995  271 GPKLVREMFKVAEEHAPSIVFIDEIDAVGTKRYEATSGGEREIQRTMLELLNQLDGFDSRGDVKVIMATNRIDSLDPALI 350
Cdd:TIGR01241 132 GASRVRDLFEQAKKNAPCIIFIDEIDAVGRQRGAGLGGGNDEREQTLNQLLVEMDGFGTNTGVIVIAATNRPDVLDPALL 211
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258596995  351 RPGRIDRKIQLPNPDTKTKRRIFQIHTSKMTMSPDVDLEEFVMSKDELSGADIKAICTEAGLLALRERRMKITQADLRKA 430
Cdd:TIGR01241 212 RPGRFDRQVVVDLPDIKGREEILKVHAKNKKLAPDVDLKAVARRTPGFSGADLANLLNEAALLAARKNKTEITMNDIEEA 291

                  ....*
gi 258596995  431 RDKAL 435
Cdd:TIGR01241 292 IDRVI 296
SpoVK COG0464
AAA+-type ATPase, SpoVK/Ycf46/Vps4 family [Cell wall/membrane/envelope biogenesis, Cell cycle ...
174-439 2.49e-83

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: 261.77  E-value: 2.49e-83
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258596995 174 EVDPLVSVMKVEKAPLESYADIGGLESQIQEIKEAVELPLTHPELYEDIGIKPPKGVILYGPPGTGKTLLAKAVANETSA 253
Cdd:COG0464  138 YEDIGGLEEELLELREAILDDLGGLEEVKEELRELVALPLKRPELREEYGLPPPRGLLLYGPPGTGKTLLARALAGELGL 217
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258596995 254 TFLRVVGSELIQKYLGDGPKLVREMFKVAEEHAPSIVFIDEIDAVGTKRyeaTSGGEREIQRTMLELLNQLDGFdsRGDV 333
Cdd:COG0464  218 PLIEVDLSDLVSKYVGETEKNLREVFDKARGLAPCVLFIDEADALAGKR---GEVGDGVGRRVVNTLLTEMEEL--RSDV 292
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258596995 334 KVIMATNRIDSLDPALIRpgRIDRKIQLPNPDTKTKRRIFQIHTSKMTMSPDVDLEEFVMSKDELSGADIKAICTEAGLL 413
Cdd:COG0464  293 VVIAATNRPDLLDPALLR--RFDEIIFFPLPDAEERLEIFRIHLRKRPLDEDVDLEELAEATEGLSGADIRNVVRRAALQ 370
                        250       260
                 ....*....|....*....|....*.
gi 258596995 414 ALRERRMKITQADLRKARDKALFQKK 439
Cdd:COG0464  371 ALRLGREPVTTEDLLEALEREDIFLK 396
CDC48 TIGR01243
AAA family ATPase, CDC48 subfamily; This subfamily of the AAA family ATPases includes two ...
179-416 3.40e-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: 3.40e-79
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258596995  179 VSVMKVEKAPLESYADIGGLESQIQEIKEAVELPLTHPELYEDIGIKPPKGVILYGPPGTGKTLLAKAVANETSATFLRV 258
Cdd:TIGR01243 164 VREEIERKVPKVTYEDIGGLKEAKEKIREMVELPMKHPELFEHLGIEPPKGVLLYGPPGTGKTLLAKAVANEAGAYFISI 243
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258596995  259 VGSELIQKYLGDGPKLVREMFKVAEEHAPSIVFIDEIDAVGTKRYEATsgGEREiQRTMLELLNQLDGFDSRGDVKVIMA 338
Cdd:TIGR01243 244 NGPEIMSKYYGESEERLREIFKEAEENAPSIIFIDEIDAIAPKREEVT--GEVE-KRVVAQLLTLMDGLKGRGRVIVIGA 320
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 258596995  339 TNRIDSLDPALIRPGRIDRKIQLPNPDTKTKRRIFQIHTSKMTMSPDVDLEEFVMSKDELSGADIKAICTEAGLLALR 416
Cdd:TIGR01243 321 TNRPDALDPALRRPGRFDREIVIRVPDKRARKEILKVHTRNMPLAEDVDLDKLAEVTHGFVGADLAALAKEAAMAALR 398
HflB COG0465
ATP-dependent Zn proteases [Posttranslational modification, protein turnover, chaperones];
182-433 9.43e-79

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


Pssm-ID: 440233 [Multi-domain]  Cd Length: 583  Bit Score: 255.35  E-value: 9.43e-79
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258596995 182 MKVEKAPLESYADIGGLESQIQEIKEAVELpLTHPELYEDIGIKPPKGVILYGPPGTGKTLLAKAVANETSATFLRVVGS 261
Cdd:COG0465  131 LYDEDKPKVTFDDVAGVDEAKEELQEIVDF-LKDPEKFTRLGAKIPKGVLLVGPPGTGKTLLAKAVAGEAGVPFFSISGS 209
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258596995 262 ELIQKYLGDGPKLVREMFKVAEEHAPSIVFIDEIDAVGTKRYEATSGG--EREiqRTmlelLNQL----DGFDSRGDVKV 335
Cdd:COG0465  210 DFVEMFVGVGASRVRDLFEQAKKNAPCIIFIDEIDAVGRQRGAGLGGGhdERE--QT----LNQLlvemDGFEGNEGVIV 283
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258596995 336 IMATNRIDSLDPALIRPGRIDRKIQLPNPDTKTKRRIFQIHTSKMTMSPDVDLEE-------FvmskdelSGADIKAICT 408
Cdd:COG0465  284 IAATNRPDVLDPALLRPGRFDRQVVVDLPDVKGREAILKVHARKKPLAPDVDLEViarrtpgF-------SGADLANLVN 356
                        250       260
                 ....*....|....*....|....*
gi 258596995 409 EAGLLALRERRMKITQADLRKARDK 433
Cdd:COG0465  357 EAALLAARRNKKAVTMEDFEEAIDR 381
CDC48 TIGR01243
AAA family ATPase, CDC48 subfamily; This subfamily of the AAA family ATPases includes two ...
188-417 1.53e-77

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: 255.60  E-value: 1.53e-77
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258596995  188 PLESYADIGGLESQIQEIKEAVELPLTHPELYEDIGIKPPKGVILYGPPGTGKTLLAKAVANETSATFLRVVGSELIQKY 267
Cdd:TIGR01243 448 PNVRWSDIGGLEEVKQELREAVEWPLKHPEIFEKMGIRPPKGVLLFGPPGTGKTLLAKAVATESGANFIAVRGPEILSKW 527
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258596995  268 LGDGPKLVREMFKVAEEHAPSIVFIDEIDAVGTKRyeATSGGEREIQRTMLELLNQLDGFDSRGDVKVIMATNRIDSLDP 347
Cdd:TIGR01243 528 VGESEKAIREIFRKARQAAPAIIFFDEIDAIAPAR--GARFDTSVTDRIVNQLLTEMDGIQELSNVVVIAATNRPDILDP 605
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258596995  348 ALIRPGRIDRKIQLPNPDTKTKRRIFQIHTSKMTMSPDVDLEEFVMSKDELSGADIKAICTEAGLLALRE 417
Cdd:TIGR01243 606 ALLRPGRFDRLILVPPPDEEARKEIFKIHTRSMPLAEDVDLEELAEMTEGYTGADIEAVCREAAMAALRE 675
RecA-like_CDC48_NLV2_r1-like cd19503
first of two ATPase domains of CDC48 and NLV2, and similar ATPase domains; CDC48 in yeast and ...
194-361 7.90e-73

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: 226.40  E-value: 7.90e-73
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258596995 194 DIGGLESQIQEIKEAVELPLTHPELYEDIGIKPPKGVILYGPPGTGKTLLAKAVANETSATFLRVVGSELIQKYLGDGPK 273
Cdd:cd19503    1 DIGGLDEQIASLKELIELPLKYPELFRALGLKPPRGVLLHGPPGTGKTLLARAVANEAGANFLSISGPSIVSKYLGESEK 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258596995 274 LVREMFKVAEEHAPSIVFIDEIDAVGTKRYEATSGGEReiqRTMLELLNQLDGFDSRGDVKVIMATNRIDSLDPALIRPG 353
Cdd:cd19503   81 NLREIFEEARSHAPSIIFIDEIDALAPKREEDQREVER---RVVAQLLTLMDGMSSRGKVVVIAATNRPDAIDPALRRPG 157

                 ....*...
gi 258596995 354 RIDRKIQL 361
Cdd:cd19503  158 RFDREVEI 165
RecA-like_FtsH cd19501
ATP-dependent zinc metalloprotease FtsH; FtsH ATPase is a processive, ATP-dependent zinc ...
191-360 1.77e-70

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: 220.57  E-value: 1.77e-70
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258596995 191 SYADIGGLESQIQEIKEAVELpLTHPELYEDIGIKPPKGVILYGPPGTGKTLLAKAVANETSATFLRVVGSELIQKYLGD 270
Cdd:cd19501    2 TFKDVAGCEEAKEELKEVVEF-LKNPEKFTKLGAKIPKGVLLVGPPGTGKTLLAKAVAGEAGVPFFSISGSDFVEMFVGV 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258596995 271 GPKLVREMFKVAEEHAPSIVFIDEIDAVGTKRYEATSGGEREIQRTMLELLNQLDGFDSRGDVKVIMATNRIDSLDPALI 350
Cdd:cd19501   81 GASRVRDLFEQAKKNAPCIVFIDEIDAVGRKRGAGLGGGHDEREQTLNQLLVEMDGFESNTGVIVIAATNRPDVLDPALL 160
                        170
                 ....*....|
gi 258596995 351 RPGRIDRKIQ 360
Cdd:cd19501  161 RPGRFDRQVY 170
RecA-like_CDC48_r1-like cd19519
first of two ATPase domains of CDC48 and similar ATPase domains; CDC48 in yeast and p97 or VCP ...
194-362 1.15e-68

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: 215.76  E-value: 1.15e-68
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258596995 194 DIGGLESQIQEIKEAVELPLTHPELYEDIGIKPPKGVILYGPPGTGKTLLAKAVANETSATFLRVVGSELIQKYLGDGPK 273
Cdd:cd19519    1 DIGGCRKQLAQIREMVELPLRHPELFKAIGIKPPRGILLYGPPGTGKTLIARAVANETGAFFFLINGPEIMSKLAGESES 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258596995 274 LVREMFKVAEEHAPSIVFIDEIDAVGTKRYEATSGGEReiqRTMLELLNQLDGFDSRGDVKVIMATNRIDSLDPALIRPG 353
Cdd:cd19519   81 NLRKAFEEAEKNAPAIIFIDEIDAIAPKREKTHGEVER---RIVSQLLTLMDGLKQRAHVIVMAATNRPNSIDPALRRFG 157

                 ....*....
gi 258596995 354 RIDRKIQLP 362
Cdd:cd19519  158 RFDREIDIG 166
pup_AAA TIGR03689
proteasome ATPase; In the Actinobacteria, as shown for Mycobacterium tuberculosis, some ...
119-426 2.95e-66

proteasome ATPase; In the Actinobacteria, as shown for Mycobacterium tuberculosis, some proteins are modified by ligation between an epsilon-amino group of a lysine side chain and the C-terminal carboxylate of the ubiquitin-like protein Pup. This modification leads to protein degradation by the archaeal-like proteasome found in the Actinobacteria. Members of this protein family belong to the AAA family of ATPases and tend to be clustered with the genes for Pup, the Pup ligase PafA, and structural components of the proteasome. This protein forms hexameric rings with ATPase activity. [Protein fate, Degradation of proteins, peptides, and glycopeptides]


Pssm-ID: 200312 [Multi-domain]  Cd Length: 512  Bit Score: 220.74  E-value: 2.95e-66
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258596995  119 TLEELIDENHGIIATSVGPEYYVNILSFVDKDLLEPGCSVLLNNKTN-SVVGILLDEVDPLVsvmkVEKAPLESYADIGG 197
Cdd:TIGR03689 111 TLKEVLDDGRALVTDRSGEERVVKLAGALADEGLRPGDTLLVDPRAGyAFEAIPRTEVEDLV----LEEVPDVTYADIGG 186
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258596995  198 LESQIQEIKEAVELPLTHPELYEDIGIKPPKGVILYGPPGTGKTLLAKAVANE----------TSATFLRVVGSELIQKY 267
Cdd:TIGR03689 187 LGSQIEQIRDAVELPFLHPELYREYGLKPPKGVLLYGPPGCGKTLIAKAVANSlaarigaeggGKSYFLNIKGPELLNKY 266
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258596995  268 LGDGPKLVREMFKVAEEHA----PSIVFIDEIDAVGTKRyeaTSGGEREIQRTML-ELLNQLDGFDSRGDVKVIMATNRI 342
Cdd:TIGR03689 267 VGETERQIRLIFQRAREKAsegrPVIVFFDEMDSLFRTR---GSGVSSDVETTVVpQLLAEIDGVESLDNVIVIGASNRE 343
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258596995  343 DSLDPALIRPGRIDRKIQLPNPDTKTKRRIFQIHtskmtMSPDVDLEEFVMSKDELSGADIKAICTEA--GLLALRERR- 419
Cdd:TIGR03689 344 DMIDPAILRPGRLDVKIRIERPDAEAAADIFAKY-----LTDDLPLPEDLAAHDGDREATAAALIQRVvdALYARSEANr 418

                  ....*...
gi 258596995  420 -MKITQAD 426
Cdd:TIGR03689 419 yVEVTYAN 426
ftsH CHL00176
cell division protein; Validated
191-433 7.43e-66

cell division protein; Validated


Pssm-ID: 214386 [Multi-domain]  Cd Length: 638  Bit Score: 222.62  E-value: 7.43e-66
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258596995 191 SYADIGGLESQIQEIKEAVELpLTHPELYEDIGIKPPKGVILYGPPGTGKTLLAKAVANETSATFLRVVGSELIQKYLGD 270
Cdd:CHL00176 181 TFRDIAGIEEAKEEFEEVVSF-LKKPERFTAVGAKIPKGVLLVGPPGTGKTLLAKAIAGEAEVPFFSISGSEFVEMFVGV 259
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258596995 271 GPKLVREMFKVAEEHAPSIVFIDEIDAVGTKRYEATSGGEREIQRTMLELLNQLDGFDSRGDVKVIMATNRIDSLDPALI 350
Cdd:CHL00176 260 GAARVRDLFKKAKENSPCIVFIDEIDAVGRQRGAGIGGGNDEREQTLNQLLTEMDGFKGNKGVIVIAATNRVDILDAALL 339
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258596995 351 RPGRIDRKIQLPNPDTKTKRRIFQIHTSKMTMSPDVDLEEFVMSKDELSGADIKAICTEAGLLALRERRMKITQADLRKA 430
Cdd:CHL00176 340 RPGRFDRQITVSLPDREGRLDILKVHARNKKLSPDVSLELIARRTPGFSGADLANLLNEAAILTARRKKATITMKEIDTA 419

                 ...
gi 258596995 431 RDK 433
Cdd:CHL00176 420 IDR 422
RecA-like_CDC48_r2-like cd19511
second of two ATPase domains of CDC48/p97, PEX1 and -6, VAT and NVL, and similar ATPase ...
203-359 6.37e-63

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: 200.59  E-value: 6.37e-63
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258596995 203 QEIKEAVELPLTHPELYEDIGIKPPKGVILYGPPGTGKTLLAKAVANETSATFLRVVGSELIQKYLGDGPKLVREMFKVA 282
Cdd:cd19511    3 RELKEAVEWPLKHPDAFKRLGIRPPKGVLLYGPPGCGKTLLAKALASEAGLNFISVKGPELFSKYVGESERAVREIFQKA 82
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 258596995 283 EEHAPSIVFIDEIDAVGTKRYEATSGGEREiqRTMLELLNQLDGFDSRGDVKVIMATNRIDSLDPALIRPGRIDRKI 359
Cdd:cd19511   83 RQAAPCIIFFDEIDSLAPRRGQSDSSGVTD--RVVSQLLTELDGIESLKGVVVIAATNRPDMIDPALLRPGRLDKLI 157
hflB PRK10733
ATP-dependent zinc metalloprotease FtsH;
182-435 1.20e-62

ATP-dependent zinc metalloprotease FtsH;


Pssm-ID: 182683 [Multi-domain]  Cd Length: 644  Bit Score: 214.13  E-value: 1.20e-62
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258596995 182 MKVEKAPLESYADIGGLESQIQEIKEAVELpLTHPELYEDIGIKPPKGVILYGPPGTGKTLLAKAVANETSATFLRVVGS 261
Cdd:PRK10733 141 MLTEDQIKTTFADVAGCDEAKEEVAELVEY-LREPSRFQKLGGKIPKGVLMVGPPGTGKTLLAKAIAGEAKVPFFTISGS 219
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258596995 262 ELIQKYLGDGPKLVREMFKVAEEHAPSIVFIDEIDAVGTKRYEATSGGEREIQRTMLELLNQLDGFDSRGDVKVIMATNR 341
Cdd:PRK10733 220 DFVEMFVGVGASRVRDMFEQAKKAAPCIIFIDEIDAVGRQRGAGLGGGHDEREQTLNQMLVEMDGFEGNEGIIVIAATNR 299
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258596995 342 IDSLDPALIRPGRIDRKIQLPNPDTKTKRRIFQIHTSKMTMSPDVDLEEFVMSKDELSGADIKAICTEAGLLALRERRMK 421
Cdd:PRK10733 300 PDVLDPALLRPGRFDRQVVVGLPDVRGREQILKVHMRRVPLAPDIDAAIIARGTPGFSGADLANLVNEAALFAARGNKRV 379
                        250
                 ....*....|....
gi 258596995 422 ITQADLRKARDKAL 435
Cdd:PRK10733 380 VSMVEFEKAKDKIM 393
RecA-like_VCP_r2 cd19529
second of two ATPase domains of Valosin-containing protein-like ATPase (VAT) and similar ...
203-361 3.76e-61

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: 196.18  E-value: 3.76e-61
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258596995 203 QEIKEAVELPLTHPELYEDIGIKPPKGVILYGPPGTGKTLLAKAVANETSATFLRVVGSELIQKYLGDGPKLVREMFKVA 282
Cdd:cd19529    3 QELKEAVEWPLLKPEVFKRLGIRPPKGILLYGPPGTGKTLLAKAVATESNANFISVKGPELLSKWVGESEKAIREIFRKA 82
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 258596995 283 EEHAPSIVFIDEIDAVGTKRyeATSGGEREIQRTMLELLNQLDGFDSRGDVKVIMATNRIDSLDPALIRPGRIDRKIQL 361
Cdd:cd19529   83 RQVAPCVIFFDEIDSIAPRR--GTTGDSGVTERVVNQLLTELDGLEEMNGVVVIAATNRPDIIDPALLRAGRFDRLIYI 159
RecA-like_protease cd19481
proteases similar to RecA; RecA-like NTPases. This family includes the NTP binding domain of ...
201-359 5.23e-60

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: 192.88  E-value: 5.23e-60
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258596995 201 QIQEIKEAVELPLTHPELYEDiGIKPPKGVILYGPPGTGKTLLAKAVANETSATFLRVVGSELIQKYLGDGPKLVREMFK 280
Cdd:cd19481    1 LKASLREAVEAPRRGSRLRRY-GLGLPKGILLYGPPGTGKTLLAKALAGELGLPLIVVKLSSLLSKYVGESEKNLRKIFE 79
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 258596995 281 VAEEHAPSIVFIDEIDAVGTKRyeATSGGEREIQRTMLELLNQLDGFDSRGDVKVIMATNRIDSLDPALIRPGRIDRKI 359
Cdd:cd19481   80 RARRLAPCILFIDEIDAIGRKR--DSSGESGELRRVLNQLLTELDGVNSRSKVLVIAATNRPDLLDPALLRPGRFDEVI 156
AAA pfam00004
ATPase family associated with various cellular activities (AAA); AAA family proteins often ...
230-362 3.45e-52

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: 171.62  E-value: 3.45e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258596995  230 VILYGPPGTGKTLLAKAVANETSATFLRVVGSELIQKYLGDGPKLVREMFKVAEEHAPSIVFIDEIDAVGTKRYeatSGG 309
Cdd:pfam00004   1 LLLYGPPGTGKTTLAKAVAKELGAPFIEISGSELVSKYVGESEKRLRELFEAAKKLAPCVIFIDEIDALAGSRG---SGG 77
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 258596995  310 EREIQRTMLELLNQLDGFDSR-GDVKVIMATNRIDSLDPALIrpGRIDRKIQLP 362
Cdd:pfam00004  78 DSESRRVVNQLLTELDGFTSSnSKVIVIAATNRPDKLDPALL--GRFDRIIEFP 129
RecA-like_CDC48_r2-like cd19528
second of two ATPase domains of CDC48 and similar ATPase domains; CDC48 in yeast and p97 or ...
203-359 2.26e-51

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: 170.77  E-value: 2.26e-51
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258596995 203 QEIKEAVELPLTHPELYEDIGIKPPKGVILYGPPGTGKTLLAKAVANETSATFLRVVGSELIQKYLGDGPKLVREMFKVA 282
Cdd:cd19528    3 RELQELVQYPVEHPDKFLKFGMTPSKGVLFYGPPGCGKTLLAKAIANECQANFISVKGPELLTMWFGESEANVRDIFDKA 82
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 258596995 283 EEHAPSIVFIDEIDAVGTKRYEATSGGEREIQRTMLELLNQLDGFDSRGDVKVIMATNRIDSLDPALIRPGRIDRKI 359
Cdd:cd19528   83 RAAAPCVLFFDELDSIAKARGGNIGDAGGAADRVINQILTEMDGMNTKKNVFIIGATNRPDIIDPAILRPGRLDQLI 159
RecA-like_NVL_r1-like cd19518
first of two ATPase domains of NVL (nuclear VCP-like protein) and similar ATPase domains; NVL ...
194-361 6.51e-50

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: 167.20  E-value: 6.51e-50
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258596995 194 DIGGLESQIQEIKEAVELPLTHPELYEDIGIKPPKGVILYGPPGTGKTLLAKAVANETSATFLRVVGSELIQKYLGDGPK 273
Cdd:cd19518    1 DIGGMDSTLKELCELLIHPILPPEYFQHLGVEPPRGVLLHGPPGCGKTMLANAIAGELKVPFLKISATEIVSGVSGESEE 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258596995 274 LVREMFKVAEEHAPSIVFIDEIDAVGTKRYEATSGGEReiqRTMLELLNQLDGF----DSRGDVKVIMATNRIDSLDPAL 349
Cdd:cd19518   81 KIRELFDQAISNAPCIVFIDEIDAITPKRESAQREMER---RIVSQLLTCMDELnnekTAGGPVLVIGATNRPDSLDPAL 157
                        170
                 ....*....|..
gi 258596995 350 IRPGRIDRKIQL 361
Cdd:cd19518  158 RRAGRFDREICL 169
RecA-like_Yta7-like cd19517
ATPase domain of Saccharomyces cerevisiae Yta7 and similar ATPase domains; Saccharomyces ...
194-358 2.67e-49

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: 165.76  E-value: 2.67e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258596995 194 DIGGLESQIQEIKEAVELPLTHPELYEDIGIKPPKGVILYGPPGTGKTLLAKAVANETSA-----TFLRVVGSELIQKYL 268
Cdd:cd19517    1 DIGGLSHYINQLKEMVFFPLLYPEVFAKFKITPPRGVLFHGPPGTGKTLMARALAAECSKggqkvSFFMRKGADCLSKWV 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258596995 269 GDGPKLVREMFKVAEEHAPSIVFIDEIDAVGTKRYEATSGGEREIQRTMLELlnqLDGFDSRGDVKVIMATNRIDSLDPA 348
Cdd:cd19517   81 GEAERQLRLLFEEAYRMQPSIIFFDEIDGLAPVRSSKQEQIHASIVSTLLAL---MDGLDNRGQVVVIGATNRPDALDPA 157
                        170
                 ....*....|
gi 258596995 349 LIRPGRIDRK 358
Cdd:cd19517  158 LRRPGRFDRE 167
RecA-like_VPS4-like cd19509
ATPase domain of VPS4, ATAD1, K, KTNA1, Spastin, FIGL-1 and similar ATPase domains; This ...
195-359 9.11e-49

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: 164.06  E-value: 9.11e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258596995 195 IGGLESQIQEIKEAVELPLTHPELYEDIgIKPPKGVILYGPPGTGKTLLAKAVANETSATFLRVVGSELIQKYLGDGPKL 274
Cdd:cd19509    1 IAGLDDAKEALKEAVILPSLRPDLFPGL-RGPPRGILLYGPPGTGKTLLARAVASESGSTFFSISASSLVSKWVGESEKI 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258596995 275 VREMFKVAEEHAPSIVFIDEIDAVGTKRYEATSGGEREIqRTmlELLNQLDGF--DSRGDVKVIMATNRIDSLDPALIRp 352
Cdd:cd19509   80 VRALFALARELQPSIIFIDEIDSLLSERGSGEHEASRRV-KT--EFLVQMDGVlnKPEDRVLVLGATNRPWELDEAFLR- 155

                 ....*..
gi 258596995 353 gRIDRKI 359
Cdd:cd19509  156 -RFEKRI 161
COG1223 COG1223
Predicted ATPase, AAA+ superfamily [General function prediction only];
194-430 6.04e-47

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


Pssm-ID: 440836 [Multi-domain]  Cd Length: 246  Bit Score: 161.98  E-value: 6.04e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258596995 194 DIGGLESQIQEIKEAVElPLTHPELYEDIGIKPPKGVILYGPPGTGKTLLAKAVANETSATFLRVVGSELIQKYLGDGPK 273
Cdd:COG1223    3 DVVGQEEAKKKLKLIIK-ELRRRENLRKFGLWPPRKILFYGPPGTGKTMLAEALAGELKLPLLTVRLDSLIGSYLGETAR 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258596995 274 LVREMFKVAEEhAPSIVFIDEIDAVGTKRYEATSGGerEIQRTMLELLNQLDGFDSrgDVKVIMATNRIDSLDPALIRpg 353
Cdd:COG1223   82 NLRKLFDFARR-APCVIFFDEFDAIAKDRGDQNDVG--EVKRVVNALLQELDGLPS--GSVVIAATNHPELLDSALWR-- 154
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 258596995 354 RIDRKIQLPNPDTKTKRRIFQIHTSKMTMSPDVDLEEFVMSKDELSGADIKAICTEAGLLALRERRMKITQADLRKA 430
Cdd:COG1223  155 RFDEVIEFPLPDKEERKEILELNLKKFPLPFELDLKKLAKKLEGLSGADIEKVLKTALKKAILEDREKVTKEDLEEA 231
RecA-like_NVL_r2-like cd19530
second of two ATPase domains of NVL (nuclear VCP-like protein) and similar ATPase domains; NVL ...
198-357 3.64e-46

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


Pssm-ID: 410938 [Multi-domain]  Cd Length: 161  Bit Score: 157.26  E-value: 3.64e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258596995 198 LESQIQEIKEAVELPLTHPELYEDIGIKPPKGVILYGPPGTGKTLLAKAVANETSATFLRVVGSELIQKYLGDGPKLVRE 277
Cdd:cd19530    1 LDHVREELTMSILRPIKRPDIYKALGIDLPTGVLLYGPPGCGKTLLAKAVANESGANFISVKGPELLNKYVGESERAVRQ 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258596995 278 MFKVAEEHAPSIVFIDEIDAVGTKR-YEATSGGEREIQrtmlELLNQLDGFDSRGDVKVIMATNRIDSLDPALIRPGRID 356
Cdd:cd19530   81 VFQRARASAPCVIFFDEVDALVPKRgDGGSWASERVVN----QLLTEMDGLEERSNVFVIAATNRPDIIDPAMLRPGRLD 156

                 .
gi 258596995 357 R 357
Cdd:cd19530  157 K 157
RecA-like_PEX6_r2 cd19527
second of two ATPase domains of Peroxisomal biogenesis factor 6 (PEX6); PEX6(also known as ...
204-361 1.49e-44

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: 153.05  E-value: 1.49e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258596995 204 EIKEAVELPLTHPELYEDiGIKPPKGVILYGPPGTGKTLLAKAVANETSATFLRVVGSELIQKYLGDGPKLVREMFKVAE 283
Cdd:cd19527    4 EILDTIQLPLEHPELFSS-GLRKRSGILLYGPPGTGKTLLAKAIATECSLNFLSVKGPELINMYIGESEANVREVFQKAR 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258596995 284 EHAPSIVFIDEIDAVGTKR-YEATSGGerEIQRTMLELLNQLDGF-DSRGDVKVIMATNRIDSLDPALIRPGRIDRKIQL 361
Cdd:cd19527   83 DAKPCVIFFDELDSLAPSRgNSGDSGG--VMDRVVSQLLAELDGMsSSGQDVFVIGATNRPDLLDPALLRPGRFDKLLYL 160
RecA-like_ATAD1 cd19520
ATPase domain of ATPase family AAA domain-containing protein 1 and similar ATPase domains; ...
194-351 3.29e-44

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: 152.19  E-value: 3.29e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258596995 194 DIGGLESQIQEIKEAVELPLTHPELYEDIGI-KPPKGVILYGPPGTGKTLLAKAVANETSATFLRVVGSELIQKYLGDGP 272
Cdd:cd19520    1 DIGGLDEVITELKELVILPLQRPELFDNSRLlQPPKGVLLYGPPGCGKTMLAKATAKEAGARFINLQVSSLTDKWYGESQ 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258596995 273 KLVREMFKVAEEHAPSIVFIDEIDAVGTKRyeatSGGEREIQRTM-LELLNQLDGFDSRGDVKVIM--ATNRIDSLDPAL 349
Cdd:cd19520   81 KLVAAVFSLASKLQPSIIFIDEIDSFLRQR----SSTDHEATAMMkAEFMSLWDGLSTDGNCRVIVmgATNRPQDLDEAI 156

                 ..
gi 258596995 350 IR 351
Cdd:cd19520  157 LR 158
RecA-like_VPS4 cd19521
ATPase domain of vacuolar protein sorting-associated protein 4; Vacuolar protein ...
188-359 6.31e-42

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: 146.16  E-value: 6.31e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258596995 188 PLESYADIGGLESQIQEIKEAVELPLTHPELYEDiGIKPPKGVILYGPPGTGKTLLAKAVANETSATFLRVVGSELIQKY 267
Cdd:cd19521    2 PNVKWEDVAGLEGAKEALKEAVILPVKFPHLFTG-NRKPWSGILLYGPPGTGKSYLAKAVATEANSTFFSVSSSDLVSKW 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258596995 268 LGDGPKLVREMFKVAEEHAPSIVFIDEIDAVGTKRYEATSGGEREIQRtmlELLNQLDGF--DSRGdVKVIMATNRIDSL 345
Cdd:cd19521   81 MGESEKLVKQLFAMARENKPSIIFIDEVDSLCGTRGEGESEASRRIKT---ELLVQMNGVgnDSQG-VLVLGATNIPWQL 156
                        170
                 ....*....|....
gi 258596995 346 DPALIRpgRIDRKI 359
Cdd:cd19521  157 DSAIRR--RFEKRI 168
RecA-like_PEX1_r2 cd19526
second of two ATPase domains of Peroxisomal biogenesis factor 1 (PEX1); PEX1(also known as ...
205-359 6.67e-41

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: 143.34  E-value: 6.67e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258596995 205 IKEAVELPLTHPELYEDIGIKPPKGVILYGPPGTGKTLLAKAVANETSATFLRVVGSELIQKYLGDGPKLVREMFKVAEE 284
Cdd:cd19526    5 LEETIEWPSKYPKIFASSPLRLRSGILLYGPPGCGKTLLASAIASECGLNFISVKGPELLNKYIGASEQNVRDLFSRAQS 84
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 258596995 285 HAPSIVFIDEIDAVGTKRYEATSGgerEIQRTMLELLNQLDGFDSRGDVKVIMATNRIDSLDPALIRPGRIDRKI 359
Cdd:cd19526   85 AKPCILFFDEFDSIAPKRGHDSTG---VTDRVVNQLLTQLDGVEGLDGVYVLAATSRPDLIDPALLRPGRLDKLV 156
RecA-like_spastin cd19524
ATPase domain of spastin; Spastin is an ATP-dependent microtubule-severing protein involved in ...
194-351 1.51e-40

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: 142.30  E-value: 1.51e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258596995 194 DIGGLESQIQEIKEAVELPLTHPELYedIGIK-PPKGVILYGPPGTGKTLLAKAVANETSATFLRVVGSELIQKYLGDGP 272
Cdd:cd19524    1 DIAGQDLAKQALQEMVILPSLRPELF--TGLRaPARGLLLFGPPGNGKTMLAKAVAAESNATFFNISAASLTSKYVGEGE 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258596995 273 KLVREMFKVAEEHAPSIVFIDEIDAVGTKRYEATSGGEReiqRTMLELLNQLDGFDSRGD--VKVIMATNRIDSLDPALI 350
Cdd:cd19524   79 KLVRALFAVARELQPSIIFIDEVDSLLSERSEGEHEASR---RLKTEFLIEFDGVQSNGDdrVLVMGATNRPQELDDAVL 155

                 .
gi 258596995 351 R 351
Cdd:cd19524  156 R 156
RecA-like_KTNA1 cd19522
Katanin p60 ATPase-containing subunit A1; Katanin p60 ATPase-containing subunit A1 (KTNA1) is ...
194-359 1.08e-39

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: 140.50  E-value: 1.08e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258596995 194 DIGGLESQIQEIKEAVELPLTHPELYEDIGiKPPKGVILYGPPGTGKTLLAKAVANETSATFLRVVGSELIQKYLGDGPK 273
Cdd:cd19522    1 DIADLEEAKKLLEEAVVLPMWMPEFFKGIR-RPWKGVLMVGPPGTGKTLLAKAVATECGTTFFNVSSSTLTSKYRGESEK 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258596995 274 LVREMFKVAEEHAPSIVFIDEIDAVGTKRyeATSGGEREIQRTMLELLNQLDGF-------DSRGDVKVIMATNRIDSLD 346
Cdd:cd19522   80 LVRLLFEMARFYAPTTIFIDEIDSICSRR--GTSEEHEASRRVKSELLVQMDGVggasendDPSKMVMVLAATNFPWDID 157
                        170
                 ....*....|...
gi 258596995 347 PALIRpgRIDRKI 359
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; ...
192-351 7.13e-39

ATPase domain of Fidgetin-Like 1 (FIGL-1); FIGL-1 may participate in DNA repair in the nucleus; it may be involved in DNA double-strand break repair via homologous recombination. Caenorhabditis elegans FIGL-1 is a nuclear protein and controls the mitotic progression in the germ line and mouse FIGL-1 may be involved in the control of male meiosis. human FIGL-1 has been shown to be a centrosome protein involved in ciliogenesis perhaps as a microtubule-severing protein. This subfamily belongs to the RecA-like NTPase family which includes the NTP binding domain of F1 and V1 H(+)ATPases, DnaB and related helicases as well as bacterial RecA and related eukaryotic and archaeal recombinases. The RecA-like NTPase family also includes bacterial conjugation proteins and related DNA transfer proteins involved in type II and type IV secretion.


Pssm-ID: 410933 [Multi-domain]  Cd Length: 186  Bit Score: 138.97  E-value: 7.13e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258596995 192 YADIGGLESQIQEIKEAVELPLTHPELYedIGIK-PPKGVILYGPPGTGKTLLAKAVANETSATFLRVVGSELIQKYLGD 270
Cdd:cd19525   21 WADIAGLEFAKKTIKEIVVWPMLRPDIF--TGLRgPPKGILLFGPPGTGKTLIGKCIASQSGATFFSISASSLTSKWVGE 98
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258596995 271 GPKLVREMFKVAEEHAPSIVFIDEIDAVGTKRYEATSGGEREIQRtmlELLNQLDGFDSRGDVKVIM--ATNRIDSLDPA 348
Cdd:cd19525   99 GEKMVRALFSVARCKQPAVIFIDEIDSLLSQRGEGEHESSRRIKT---EFLVQLDGATTSSEDRILVvgATNRPQEIDEA 175

                 ...
gi 258596995 349 LIR 351
Cdd:cd19525  176 ARR 178
RecA-like_NSF-SEC18_r1-like cd19504
first of two ATPase domains of NSF and SEC18, and similar ATPase domains; ...
195-361 1.20e-29

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: 113.74  E-value: 1.20e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258596995 195 IGGLESQIQEI-KEAVELPLTHPELYEDIGIKPPKGVILYGPPGTGKTLLAKAVANETSATFLRVV-GSELIQKYLGDGP 272
Cdd:cd19504    2 IGGLDKEFSDIfRRAFASRVFPPEIVEQLGCKHVKGILLYGPPGTGKTLMARQIGKMLNAREPKIVnGPEILNKYVGESE 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258596995 273 KLVREMFKVAEEHAPS--------IVFIDEIDAVGTKRyeATSGGEREIQRTML-ELLNQLDGFDSRGDVKVIMATNRID 343
Cdd:cd19504   82 ANIRKLFADAEEEQRRlgansglhIIIFDEIDAICKQR--GSMAGSTGVHDTVVnQLLSKIDGVEQLNNILVIGMTNRKD 159
                        170
                 ....*....|....*...
gi 258596995 344 SLDPALIRPGRIDRKIQL 361
Cdd:cd19504  160 LIDEALLRPGRLEVQMEI 177
RecA-like_fidgetin cd19523
ATPase domain of fidgetin; Fidgetin (FIGN) is a ATP-dependent microtubule severing protein. ...
194-351 3.51e-29

ATPase domain of fidgetin; Fidgetin (FIGN) is a ATP-dependent microtubule severing protein. This subfamily belongs to the RecA-like NTPase family which includes the NTP binding domain of F1 and V1 H(+)ATPases, DnaB and related helicases as well as bacterial RecA and related eukaryotic and archaeal recombinases. The RecA-like NTPase family also includes bacterial conjugation proteins and related DNA transfer proteins involved in type II and type IV secretion.


Pssm-ID: 410931 [Multi-domain]  Cd Length: 163  Bit Score: 111.90  E-value: 3.51e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258596995 194 DIGGLESQIQEIKEAVELPLTHPELYEDIgIKPPKGVILYGPPGTGKTLLAKAVANETSATFLRVVGSELIQKYLGDGPK 273
Cdd:cd19523    1 DIAGLGALKAAIKEEVLWPLLRPDAFSGL-LRLPRSILLFGPRGTGKTLLGRCLASQLGATFLRLRGSTLVAKWAGEGEK 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258596995 274 LVREMFKVAEEHAPSIVFIDEIDAVGTKRYEatsgGEREIQRTMLELLNQLDGFDSRGD--VKVIMATNRIDSLDPALIR 351
Cdd:cd19523   80 ILQASFLAARCRQPSVLFISDLDALLSSQDD----EASPVGRLQVELLAQLDGVLGSGEdgVLVVCTTSKPEEIDESLRR 155
AAA cd00009
The AAA+ (ATPases Associated with a wide variety of cellular Activities) superfamily ...
196-362 1.85e-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: 109.54  E-value: 1.85e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258596995 196 GGLESQIQEIKEAVELPlthpelyedigikPPKGVILYGPPGTGKTLLAKAVANET---SATFLRVVGSELIQKYLG--- 269
Cdd:cd00009    1 VGQEEAIEALREALELP-------------PPKNLLLYGPPGTGKTTLARAIANELfrpGAPFLYLNASDLLEGLVVael 67
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258596995 270 DGPKLVREMFKVAEEHAPSIVFIDEIDAVGtkryeatsggeREIQRTMLELLNQL-DGFDSRGDVKVIMATNRIDSLDPA 348
Cdd:cd00009   68 FGHFLVRLLFELAEKAKPGVLFIDEIDSLS-----------RGAQNALLRVLETLnDLRIDRENVRVIGATNRPLLGDLD 136
                        170
                 ....*....|....
gi 258596995 349 LIRPGRIDRKIQLP 362
Cdd:cd00009  137 RALYDRLDIRIVIP 150
RecA-like_Ycf46-like cd19507
ATPase domain of Ycf46 and similar ATPase domains; Ycf46 may play a role in the regulation of ...
223-357 8.38e-24

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: 97.05  E-value: 8.38e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258596995 223 GIKPPKGVILYGPPGTGKTLLAKAVANETSATFLRVVGSELIQKYLGDGPKLVREMFKVAEEHAPSIVFIDEID-AVGTK 301
Cdd:cd19507   27 GLPTPKGLLLVGIQGTGKSLTAKAIAGVWQLPLLRLDMGRLFGGLVGESESRLRQMIQTAEAIAPCVLWIDEIEkGFSNA 106
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 258596995 302 RYEATSGGEREIQRTMLELLNQldgfdSRGDVKVIMATNRIDSLDPALIRPGRIDR 357
Cdd:cd19507  107 DSKGDSGTSSRVLGTFLTWLQE-----KKKPVFVVATANNVQSLPPELLRKGRFDE 157
ycf46 CHL00195
Ycf46; Provisional
190-419 1.64e-23

Ycf46; Provisional


Pssm-ID: 177094 [Multi-domain]  Cd Length: 489  Bit Score: 102.79  E-value: 1.64e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258596995 190 ESYADIGGLESQIQEIKEAVElplTHPELYEDIGIKPPKGVILYGPPGTGKTLLAKAVANETSATFLRVVGSELIQKYLG 269
Cdd:CHL00195 225 EKISDIGGLDNLKDWLKKRST---SFSKQASNYGLPTPRGLLLVGIQGTGKSLTAKAIANDWQLPLLRLDVGKLFGGIVG 301
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258596995 270 DGPKLVREMFKVAEEHAPSIVFIDEIDAVGTKRYEAT-SGGEREIQRTMLELLNQldgfdSRGDVKVIMATNRIDSLDPA 348
Cdd:CHL00195 302 ESESRMRQMIRIAEALSPCILWIDEIDKAFSNSESKGdSGTTNRVLATFITWLSE-----KKSPVFVVATANNIDLLPLE 376
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 258596995 349 LIRPGRIDRKIQLPNPDTKTKRRIFQIHTSKmtMSPD----VDLEEFVMSKDELSGADIKAICTEAGLLALRERR 419
Cdd:CHL00195 377 ILRKGRFDEIFFLDLPSLEEREKIFKIHLQK--FRPKswkkYDIKKLSKLSNKFSGAEIEQSIIEAMYIAFYEKR 449
RecA-like_BCS1 cd19510
Mitochondrial chaperone BCS1; Mitochondrial chaperone BCS1 is necessary for the assembly of ...
205-359 3.95e-23

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: 95.11  E-value: 3.95e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258596995 205 IKEAVELPLTHPELYEDIGIKPPKGVILYGPPGTGKTLLAKAVANETSATFLRVvgsELIQKYLGDgpKLVREMFKVAEE 284
Cdd:cd19510    1 IIDDLKDFIKNEDWYNDRGIPYRRGYLLYGPPGTGKSSFIAALAGELDYDICDL---NLSEVVLTD--DRLNHLLNTAPK 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258596995 285 HapSIVFIDEIDAV-----GTKRYEATSGGEREIqrTMLELLNQLDGFDSRGDVKVIMATNRIDSLDPALIRPGRIDRKI 359
Cdd:cd19510   76 Q--SIILLEDIDAAfesreHNKKNPSAYGGLSRV--TFSGLLNALDGVASSEERIVFMTTNHIERLDPALIRPGRVDMKI 151
AAA smart00382
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ...
226-365 6.83e-19

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: 83.19  E-value: 6.83e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258596995   226 PPKGVILYGPPGTGKTLLAKAVANETSATFLRVV-----------------GSELIQKYLGDGPKLVREMFKVAEEHAPS 288
Cdd:smart00382   1 PGEVILIVGPPGSGKTTLARALARELGPPGGGVIyidgedileevldqlllIIVGGKKASGSGELRLRLALALARKLKPD 80
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 258596995   289 IVFIDEIDAVGTKryeatsggEREIQRTMLELLNQLDGFDSRGDVKVIMATNRIDSLDPALIRPgRIDRKIQLPNPD 365
Cdd:smart00382  81 VLILDEITSLLDA--------EQEALLLLLEELRLLLLLKSEKNLTVILTTNDEKDLGPALLRR-RFDRRIVLLLIL 148
RecA-like_Pch2-like cd19508
ATPase domain of Pachytene checkpoint 2 (Pch2) and similar ATPase domains; Pch2 (known as ...
230-350 1.37e-14

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: 72.09  E-value: 1.37e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258596995 230 VILYGPPGTGKTLLAKAVANETS---------ATFLRVVGSELIQKYLGDGPKLVREMFK-----VAEEHAPSIVFIDEI 295
Cdd:cd19508   55 VLLHGPPGTGKTSLCKALAQKLSirlssryryGQLIEINSHSLFSKWFSESGKLVTKMFQkiqelIDDKDALVFVLIDEV 134
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 258596995 296 DAVGTKRYEATSGGE-REIQRTMLELLNQLDGFDSRGDVKVIMATNRIDSLDPALI 350
Cdd:cd19508  135 ESLAAARSASSSGTEpSDAIRVVNAVLTQIDRIKRYHNNVILLTSNLLEKIDVAFV 190
AAA_lid_3 pfam17862
AAA+ lid domain; This entry represents the alpha helical AAA+ lid domain that is found to the ...
385-429 6.62e-11

AAA+ lid domain; This entry represents the alpha helical AAA+ lid domain that is found to the C-terminus of AAA domains.


Pssm-ID: 465537 [Multi-domain]  Cd Length: 45  Bit Score: 57.16  E-value: 6.62e-11
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 258596995  385 DVDLEEFVMSKDELSGADIKAICTEAGLLALRERRMKITQADLRK 429
Cdd:pfam17862   1 DVDLEELAERTEGFSGADLEALCREAALAALRRGLEAVTQEDLEE 45
Prot_ATP_ID_OB pfam16450
Proteasomal ATPase OB C-terminal domain; This is the interdomain (ID) or oligonucleotide ...
117-171 2.09e-10

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


Pssm-ID: 465118 [Multi-domain]  Cd Length: 56  Bit Score: 55.98  E-value: 2.09e-10
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 258596995  117 VGTLEELIDENHGIIATSVGPEYYVNILSFVDKDLLEPGCSVLLNNKTNSVVGIL 171
Cdd:pfam16450   1 VATVVEVLDDGRALVKSSGGEERVVRLAGSLDEEKLRPGDRVLLDPRSGYALEVL 55
RarA COG2256
Replication-associated recombination protein RarA (DNA-dependent ATPase) [Replication, ...
230-295 3.16e-10

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


Pssm-ID: 441857 [Multi-domain]  Cd Length: 439  Bit Score: 61.61  E-value: 3.16e-10
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 258596995 230 VILYGPPGTGKTLLAKAVANETSATFLRV--VGSeliqkylgdGPKLVREMFKVAEEHA----PSIVFIDEI 295
Cdd:COG2256   52 MILWGPPGTGKTTLARLIANATDAEFVALsaVTS---------GVKDIREVIEEARERRaygrRTILFVDEI 114
PRK13342 PRK13342
recombination factor protein RarA; Reviewed
230-295 9.82e-10

recombination factor protein RarA; Reviewed


Pssm-ID: 237355 [Multi-domain]  Cd Length: 413  Bit Score: 60.10  E-value: 9.82e-10
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258596995 230 VILYGPPGTGKTLLAKAVANETSATFLRVVGSEliqkylgDGPKLVREMFKVAEEHAPS----IVFIDEI 295
Cdd:PRK13342  39 MILWGPPGTGKTTLARIIAGATDAPFEALSAVT-------SGVKDLREVIEEARQRRSAgrrtILFIDEI 101
RecA-like_ATAD3-like cd19512
ATPase domains of ATPase AAA-domain protein 3A (ATAD3A), -3B, and -3C, and similar ATPase ...
198-360 4.93e-09

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: 54.84  E-value: 4.93e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258596995 198 LESQIQEIKEAVELPLTHPELYEDIgikppkgvILYGPPGTGKTLLAKAVANETSATFLRVVGSELIQkyLG-DGPKLVR 276
Cdd:cd19512    1 LEARVRDIAIATRNTKKNKGLYRNI--------LFYGPPGTGKTLFAKKLALHSGMDYAIMTGGDVAP--MGrEGVTAIH 70
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258596995 277 EMFKVAEEHAPS-IVFIDEIDAVGTKRyeaTSGGEREIQRTMLELLNQLDGFDSRgDVKVIMATNRIDSLDPALirPGRI 355
Cdd:cd19512   71 KVFDWANTSRRGlLLFVDEADAFLRKR---STEKISEDLRAALNAFLYRTGEQSN-KFMLVLASNQPEQFDWAI--NDRI 144

                 ....*
gi 258596995 356 DRKIQ 360
Cdd:cd19512  145 DEMVE 149
RecA-like_Ycf2 cd19505
ATPase domain of plant YCF2; Ycf2 is a chloroplast ATPase which has an essential function; ...
223-361 4.16e-08

ATPase domain of plant YCF2; Ycf2 is a chloroplast ATPase which has an essential function; however, its function remains unclear. The gene encoding YCF2 is the largest known plastid gene in angiosperms and has been used to predict phylogenetic relationships. This subfamily belongs to the RecA-like NTPase family which includes the NTP binding domain of F1 and V1 H(+)ATPases, DnaB and related helicases as well as bacterial RecA and related eukaryotic and archaeal recombinases. The RecA-like NTPase family also includes bacterial conjugation proteins and related DNA transfer proteins involved in type II and type IV secretion.


Pssm-ID: 410913 [Multi-domain]  Cd Length: 161  Bit Score: 52.38  E-value: 4.16e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258596995 223 GIKPPKGVILYGPPGTGKTLLAKAVANETSATFLRVVGSELIQ---KYLGDGPKLVREM-----------FKVAEEHAPS 288
Cdd:cd19505    8 GLSPSKGILLIGSIETGRSYLIKSLAANSYVPLIRISLNKLLYnkpDFGNDDWIDGMLIlkeslhrlnlqFELAKAMSPC 87
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 258596995 289 IVFIDEIDAVGTKRYEATSGGEReiqRTMLELLNQLDGFDSRGDVK----VIMATNRIDSLDPALIRPGRIDRKIQL 361
Cdd:cd19505   88 IIWIPNIHELNVNRSTQNLEEDP---KLLLGLLLNYLSRDFEKSSTrnilVIASTHIPQKVDPALIAPNRLDTCINI 161
AAA_5 pfam07728
AAA domain (dynein-related subfamily); This Pfam entry includes some of the AAA proteins not ...
229-351 4.67e-07

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: 48.83  E-value: 4.67e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258596995  229 GVILYGPPGTGKTLLAKAVANETS-ATFLRVVGS------ELIQKY--------LGDGPkLVREMFKvaeehaPSIVFID 293
Cdd:pfam07728   1 GVLLVGPPGTGKTELAERLAAALSnRPVFYVQLTrdtteeDLFGRRnidpggasWVDGP-LVRAARE------GEIAVLD 73
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 258596995  294 EIDAvgtkryeatsgGEREIQRTMLELLN-----QLDGF----DSRGDVKVIMATNRID----SLDPALIR 351
Cdd:pfam07728  74 EINR-----------ANPDVLNSLLSLLDerrllLPDGGelvkAAPDGFRLIATMNPLDrglnELSPALRS 133
TIGR02928 TIGR02928
orc1/cdc6 family replication initiation protein; Members of this protein family are found ...
226-434 1.15e-06

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: 50.32  E-value: 1.15e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258596995  226 PPKGVILYGPPGTGKTLLAKAVANE----TSATFLRV---------------VGSELIQKYLGDGP----------KLVR 276
Cdd:TIGR02928  39 RPSNVFIYGKTGTGKTAVTKYVMKEleeaAEDRDVRVvtvyvncqildtlyqVLVELANQLRGSGEevpttglstsEVFR 118
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258596995  277 EMFKVAEEHAPSIVFI-DEIDavgtkrYEATSGGEREIQRTMLELLNQLDGfdsrGDVKVIMATNRI---DSLDPAlIRP 352
Cdd:TIGR02928 119 RLYKELNERGDSLIIVlDEID------YLVGDDDDLLYQLSRARSNGDLDN----AKVGVIGISNDLkfrENLDPR-VKS 187
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258596995  353 GRIDRKIQLPNPDTKTKRRIFQiHTSKMTMSPDVDLEE---FVMSKDELSGADI-KAICT--EAGLLALRERRMKITQAD 426
Cdd:TIGR02928 188 SLCEEEIIFPPYDAEELRDILE-NRAEKAFYDGVLDDGvipLCAALAAQEHGDArKAIDLlrVAGEIAEREGAERVTEDH 266

                  ....*...
gi 258596995  427 LRKARDKA 434
Cdd:TIGR02928 267 VEKAQEKI 274
RecA-like_HslU cd19498
ATP-dependent protease ATPase subunit HslU; HslU is a component of the ATP-dependent protease ...
227-321 1.75e-06

ATP-dependent protease ATPase subunit HslU; HslU is a component of the ATP-dependent protease HslVU. In HslVU, HslU ATPase serves to unfold and translocate protein substrate, and the HslV protease degrades the unfolded proteins. This RecA-like_HslU subfamily belongs to the RecA-like NTPase family which includes the NTP binding domain of F1 and V1 H(+)ATPases, DnaB and related helicases as well as bacterial RecA and related eukaryotic and archaeal recombinases. The RecA-like NTPase family also includes bacterial conjugation proteins and related DNA transfer proteins involved in type II and type IV secretion.


Pssm-ID: 410906 [Multi-domain]  Cd Length: 183  Bit Score: 48.14  E-value: 1.75e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258596995 227 PKGVILYGPPGTGKTLLAKAVANETSATFLRVVGSELIQ-KYLG-DGPKLVREMFKvaeehapSIVFIDEIDAVGTKRYE 304
Cdd:cd19498   46 PKNILMIGPTGVGKTEIARRLAKLAGAPFIKVEATKFTEvGYVGrDVESIIRDLVE-------GIVFIDEIDKIAKRGGS 118
                         90
                 ....*....|....*...
gi 258596995 305 ATSGGERE-IQRTMLELL 321
Cdd:cd19498  119 SGPDVSREgVQRDLLPIV 136
McrB COG1401
5-methylcytosine-specific restriction endonuclease McrBC, GTP-binding regulatory subunit McrB ...
68-295 3.87e-06

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


Pssm-ID: 441011 [Multi-domain]  Cd Length: 477  Bit Score: 49.00  E-value: 3.87e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258596995  68 RLKLLKLERIKDYLLLEEEYITNQEQIKSSDDKNYVKLKIDDLRGSPVSVGTLEELIDENHGIIATSVGPEYYVNILSFV 147
Cdd:COG1401   49 RLSEELLRADRAARATELVEELSAALEVVVLLLDLEKVELNEKLALSEAAVAIEELYELEADSEIEAVGLLLELAERSDA 128
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258596995 148 DKDLLEPGCSVLLNNKTNSVVGILLDEVDPLVSVMKVEKAPLESYADIGGLESQIQEIKEAVELPLTHPELYEDIG---- 223
Cdd:COG1401  129 LEALERARLLLELADLEERAALETEVLEALEAELEELLAAPEDLSADALAAELSAAEELYSEDLESEDDYLKDLLRekfe 208
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258596995 224 ---------IKPPKGVILYGPPGTGKTLLAKAVANETSAT----FLRVV------GSELIQKY---LGDG-----PKLVR 276
Cdd:COG1401  209 etleaflaaLKTKKNVILAGPPGTGKTYLARRLAEALGGEdngrIEFVQfhpswsYEDFLLGYrpsLDEGkyeptPGIFL 288
                        250       260
                 ....*....|....*....|.
gi 258596995 277 EMFKVAEEH--APSIVFIDEI 295
Cdd:COG1401  289 RFCLKAEKNpdKPYVLIIDEI 309
DUF815 pfam05673
Protein of unknown function (DUF815); This family consists of several bacterial proteins of ...
178-293 4.87e-06

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


Pssm-ID: 428578 [Multi-domain]  Cd Length: 250  Bit Score: 47.91  E-value: 4.87e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258596995  178 LVSVMKVEKAPLEsyaDIGGLESQIQEIKEAVELPLTHpelyedigiKPPKGVILYGPPGTGKTLLAKAVANETSATFLR 257
Cdd:pfam05673  16 LEPVPHPDPVRLD---DLVGIERQKEALIRNTRRFLAG---------LPANNVLLWGARGTGKSSLVKALLNEYADQGLR 83
                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 258596995  258 VVgsELIQKYLGDGPKLVREmfkVAEEHAPSIVFID 293
Cdd:pfam05673  84 LI--EVDKEDLGDLPDLVDL---LRDRPYRFILFCD 114
PRK13341 PRK13341
AAA family ATPase;
231-295 6.45e-06

AAA family ATPase;


Pssm-ID: 237354 [Multi-domain]  Cd Length: 725  Bit Score: 48.51  E-value: 6.45e-06
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258596995 231 ILYGPPGTGKTLLAKAVANETSATFLrVVGSELiqkylgDGPKLVREMFKVAEEHAP-----SIVFIDEI 295
Cdd:PRK13341  56 ILYGPPGVGKTTLARIIANHTRAHFS-SLNAVL------AGVKDLRAEVDRAKERLErhgkrTILFIDEV 118
PRK04195 PRK04195
replication factor C large subunit; Provisional
225-313 6.52e-06

replication factor C large subunit; Provisional


Pssm-ID: 235250 [Multi-domain]  Cd Length: 482  Bit Score: 48.38  E-value: 6.52e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258596995 225 KPPKGVILYGPPGTGKTLLAKAVANE--------------TSATFLRVVGSELIQKYLGDGPKlvremfkvaeehapSIV 290
Cdd:PRK04195  37 KPKKALLLYGPPGVGKTSLAHALANDygwevielnasdqrTADVIERVAGEAATSGSLFGARR--------------KLI 102
                         90       100
                 ....*....|....*....|...
gi 258596995 291 FIDEIDAVGTKryeATSGGEREI 313
Cdd:PRK04195 103 LLDEVDGIHGN---EDRGGARAI 122
RecA-like_ClpB_Hsp104-like cd19499
Chaperone protein ClpB/Hsp104 subfamily; Bacterial Caseinolytic peptidase B (ClpB) and ...
225-359 6.77e-06

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: 46.40  E-value: 6.77e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258596995 225 KPPKGVILYGPPGTGKTLLAKAVA---NETSATFLRVVGSELIQKY-----LGDGPKLV--REMFKVAEE---HAPSIVF 291
Cdd:cd19499   39 RPIGSFLFLGPTGVGKTELAKALAellFGDEDNLIRIDMSEYMEKHsvsrlIGAPPGYVgyTEGGQLTEAvrrKPYSVVL 118
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 258596995 292 IDEIDAVgtkryeatsggEREIQRTMLELLNqlDGF--DSRG---DVK---VIMATNRidsLDPALIrpGRIDRKI 359
Cdd:cd19499  119 LDEIEKA-----------HPDVQNLLLQVLD--DGRltDSHGrtvDFKntiIIMTSNH---FRPEFL--NRIDEIV 176
T7SS_EccA TIGR03922
type VII secretion AAA-ATPase EccA; This model represents the AAA family ATPase, EccA, of the ...
186-362 7.70e-06

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


Pssm-ID: 188437 [Multi-domain]  Cd Length: 557  Bit Score: 48.30  E-value: 7.70e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258596995  186 KAPLESYADIGGLESQIQEIKEAVELPLTHPELyediGIKPP---KGVILYGPPGTGKTLLAKAVANETSA-TFLR---- 257
Cdd:TIGR03922 272 EAELAEQIGLERVKRQVAALKSSTAMALARAER----GLPVAqtsNHMLFAGPPGTGKTTIARVVAKIYCGlGVLRkplv 347
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258596995  258 --VVGSELIQKYLGDGPKLVREMFKVAEEhapSIVFIDEIDAVGTKRYEATSGGEREIQRTMLELLNqldgfDSRGDVKV 335
Cdd:TIGR03922 348 reVSRADLIGQYIGESEAKTNEIIDSALG---GVLFLDEAYTLVETGYGQKDPFGLEAIDTLLARME-----NDRDRLVV 419
                         170       180       190
                  ....*....|....*....|....*....|.
gi 258596995  336 IMATNRiDSLDPAL-IRPG---RIDRKIQLP 362
Cdd:TIGR03922 420 IGAGYR-KDLDKFLeVNEGlrsRFTRVIEFP 449
ruvB PRK00080
Holliday junction branch migration DNA helicase RuvB;
230-295 8.07e-06

Holliday junction branch migration DNA helicase RuvB;


Pssm-ID: 234619 [Multi-domain]  Cd Length: 328  Bit Score: 47.43  E-value: 8.07e-06
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 258596995 230 VILYGPPGTGKTLLAKAVANETSATfLRVVGSELIQKyLGDgpkLVReMFKVAEEHapSIVFIDEI 295
Cdd:PRK00080  54 VLLYGPPGLGKTTLANIIANEMGVN-IRITSGPALEK-PGD---LAA-ILTNLEEG--DVLFIDEI 111
AAA_2 pfam07724
AAA domain (Cdc48 subfamily); This Pfam entry includes some of the AAA proteins not detected ...
227-321 1.01e-05

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


Pssm-ID: 400187 [Multi-domain]  Cd Length: 168  Bit Score: 45.65  E-value: 1.01e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258596995  227 PKGVILY-GPPGTGKTLLAKAVANE---TSATFLRVVGSELIQKYL-----GDGPKLVR--EMFKVAE---EHAPSIVFI 292
Cdd:pfam07724   2 PIGSFLFlGPTGVGKTELAKALAELlfgDERALIRIDMSEYMEEHSvsrliGAPPGYVGyeEGGQLTEavrRKPYSIVLI 81
                          90       100
                  ....*....|....*....|....*....
gi 258596995  293 DEIDavgtkryEATSGgereIQRTMLELL 321
Cdd:pfam07724  82 DEIE-------KAHPG----VQNDLLQIL 99
CDC6 COG1474
Cdc6-related protein, AAA superfamily ATPase [Replication, recombination and repair];
199-434 1.50e-05

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


Pssm-ID: 441083 [Multi-domain]  Cd Length: 389  Bit Score: 47.15  E-value: 1.50e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258596995 199 ESQIQEIKEAVElPLTHPElyedigikPPKGVILYGPPGTGKTLLAKAVANE---------TSATFLRV----------V 259
Cdd:COG1474   32 EEEIEELASALR-PALRGE--------RPSNVLIYGPTGTGKTAVAKYVLEEleeeaeergVDVRVVYVncrqastryrV 102
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258596995 260 GSELIQKyLGDGP----------KLVREMFKVAEEHAPSIVFI-DEIDAVGTKRYEatsggerEIQRTMLELLNQLDGfd 328
Cdd:COG1474  103 LSRILEE-LGSGEdipstglstdELFDRLYEALDERDGVLVVVlDEIDYLVDDEGD-------DLLYQLLRANEELEG-- 172
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258596995 329 srGDVKVIMATNRI---DSLDPALIRPGRiDRKIQLPnPDTKT------KRRIfqihtskmtmspDVDLEEFVMSKD--- 396
Cdd:COG1474  173 --ARVGVIGISNDLeflENLDPRVKSSLG-EEEIVFP-PYDADelrdilEDRA------------ELAFYDGVLSDEvip 236
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*..
gi 258596995 397 ---ELSGADI----KAICT--EAGLLALRERRMKITQADLRKARDKA 434
Cdd:COG1474  237 liaALAAQEHgdarKAIDLlrVAGEIAEREGSDRVTEEHVREAREKI 283
MoxR COG0714
MoxR-like ATPase [General function prediction only]; MoxR-like ATPase is part of the Pathway ...
230-296 2.43e-05

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


Pssm-ID: 440478 [Multi-domain]  Cd Length: 292  Bit Score: 45.93  E-value: 2.43e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258596995 230 VILYGPPGTGKTLLAKAVANETSATFLRV-----------VGSELIQKYLGD-----GPklvreMFKvaeehapSIVFID 293
Cdd:COG0714   34 LLLEGVPGVGKTTLAKALARALGLPFIRIqftpdllpsdiLGTYIYDQQTGEfefrpGP-----LFA-------NVLLAD 101

                 ...
gi 258596995 294 EID 296
Cdd:COG0714  102 EIN 104
RecA-like_IQCA1 cd19506
ATPase domain of IQ and AAA domain-containing protein 1 (IQCA1); IQCA1 (also known as dynein ...
228-294 4.01e-05

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: 43.67  E-value: 4.01e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 258596995 228 KGVILYGPPGTGKTLLAKAVANETSATFLRVVGSELIQKYLG-DGPKLVREM-FKVAEEHAPSIVFIDE 294
Cdd:cd19506   27 KSLLLAGPSGVGKKMLVHAICTETGANLFNLSPSNIAGKYPGkNGLQMMLHLvLKVARQLQPSVIWIGD 95
ruvB TIGR00635
Holliday junction DNA helicase, RuvB subunit; All proteins in this family for which functions ...
230-299 6.41e-05

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: 44.60  E-value: 6.41e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258596995  230 VILYGPPGTGKTLLAKAVANETSaTFLRVVGSELIQKylgdgPKLVREMFKVAEEHapSIVFIDEIDAVG 299
Cdd:TIGR00635  33 LLLYGPPGLGKTTLAHIIANEMG-VNLKITSGPALEK-----PGDLAAILTNLEEG--DVLFIDEIHRLS 94
DnaC COG1484
DNA replication protein DnaC [Replication, recombination and repair];
224-307 6.64e-05

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


Pssm-ID: 441093 [Multi-domain]  Cd Length: 242  Bit Score: 44.39  E-value: 6.64e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258596995 224 IKPPKGVILYGPPGTGKTLLAKAVANE-----TSATFLRVvgSELIQKY---LGDGpKLVREMFKVAeehAPSIVFIDEI 295
Cdd:COG1484   96 IERGENLILLGPPGTGKTHLAIALGHEacragYRVRFTTA--PDLVNELkeaRADG-RLERLLKRLA---KVDLLILDEL 169
                         90       100
                 ....*....|....*....|....*
gi 258596995 296 -----DAVGT--------KRYEATS 307
Cdd:COG1484  170 gylplDAEGAellfelisDRYERRS 194
IS21_help_AAA NF038214
IS21-like element helper ATPase IstB; This protein family model resembles PF01695, but was ...
230-307 9.09e-05

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: 43.61  E-value: 9.09e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258596995 230 VILYGPPGTGKTLLAKAVANE-----TSATFLRVvgSELIQKYL---GDGpKLVREMFKVAeehAPSIVFIDEI-----D 296
Cdd:NF038214  93 VLLLGPPGTGKTHLAIALGYAacrqgYRVRFTTA--ADLVEQLAqarADG-RLGRLLRRLA---RYDLLIIDELgylpfS 166
                         90
                 ....*....|....*....
gi 258596995 297 AVGT--------KRYEATS 307
Cdd:NF038214 167 REGAnllfeliaDRYERGS 185
RecA-like_superfamily cd01120
RecA-like_NTPases; RecA-like NTPases. This superfamily includes the NTP binding domain of F1 ...
230-346 1.17e-04

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


Pssm-ID: 410865 [Multi-domain]  Cd Length: 119  Bit Score: 41.72  E-value: 1.17e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258596995 230 VILYGPPGTGKTLLAKAVANETSATFLRVVGSELIQKYLgdgpklvREMFKVAEEHAPSIVFIDEIDAVGTKRYEATSGG 309
Cdd:cd01120    1 ILITGPPGSGKTTLLLQFAEQALLSDEPVIFISFLDTIL-------EAIEDLIEEKKLDIIIIDSLSSLARASQGDRSSE 73
                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 258596995 310 EREIQRTMLELLNQLDgfdsrgdvKVIMATNRIDSLD 346
Cdd:cd01120   74 LLEDLAKLLRAARNTG--------ITVIATIHSDKFD 102
RuvB_N pfam05496
Holliday junction DNA helicase RuvB P-loop domain; The RuvB protein makes up part of the ...
230-295 1.54e-04

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: 42.10  E-value: 1.54e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 258596995  230 VILYGPPGTGKTLLAKAVANETSATFlRVVGSELIQKyLGDGPKLVREMfkvaEEHapSIVFIDEI 295
Cdd:pfam05496  36 VLLYGPPGLGKTTLANIIANEMGVNI-RITSGPAIER-PGDLAAILTNL----EPG--DVLFIDEI 93
44 PHA02544
clamp loader, small subunit; Provisional
231-349 2.14e-04

clamp loader, small subunit; Provisional


Pssm-ID: 222866 [Multi-domain]  Cd Length: 316  Bit Score: 43.05  E-value: 2.14e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258596995 231 ILYGP-PGTGKTLLAKAVANETSATFLRVVGSEliqkylgDGPKLVREMFK-----VAEEHAPSIVFIDEIDAVGTKrye 304
Cdd:PHA02544  46 LLHSPsPGTGKTTVAKALCNEVGAEVLFVNGSD-------CRIDFVRNRLTrfastVSLTGGGKVIIIDEFDRLGLA--- 115
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 258596995 305 atsggerEIQRTMLELLNQLDgfdsrGDVKVIMATNRIDSLDPAL 349
Cdd:PHA02544 116 -------DAQRHLRSFMEAYS-----KNCSFIITANNKNGIIEPL 148
RecA-like_Lon cd19500
lon protease homolog 2 peroxisomal; Lon protease (also known as Lon peptidase) is an ...
228-299 2.14e-04

lon protease homolog 2 peroxisomal; Lon protease (also known as Lon peptidase) is an evolutionarily conserved ATP-dependent serine protease, present in bacteria and eukaryotic mitochondria and peroxisomes, which mediates the selective degradation of mutant and abnormal proteins as well as certain short-lived regulatory proteins. Lon protease is both an ATP-dependent peptidase and a protein-activated ATPase. This RecA-like Lon domain subfamily belongs to the RecA-like NTPase family which includes the NTP binding domain of F1 and V1 H(+)ATPases, DnaB and related helicases as well as bacterial RecA and related eukaryotic and archaeal recombinases. The RecA-like NTPase family also includes bacterial conjugation proteins and related DNA transfer proteins involved in type II and type IV secretion.


Pssm-ID: 410908 [Multi-domain]  Cd Length: 182  Bit Score: 42.16  E-value: 2.14e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258596995 228 KGVIL--YGPPGTGKTLLAKAVANETSATFLRV-VG-----SELI---QKYLGDGP-KLVREMfKVAEEHAPSIVfIDEI 295
Cdd:cd19500   36 KGPILclVGPPGVGKTSLGKSIARALGRKFVRIsLGgvrdeAEIRghrRTYVGAMPgRIIQAL-KKAGTNNPVFL-LDEI 113

                 ....
gi 258596995 296 DAVG 299
Cdd:cd19500  114 DKIG 117
AAA_22 pfam13401
AAA domain;
230-338 2.68e-04

AAA domain;


Pssm-ID: 379165 [Multi-domain]  Cd Length: 129  Bit Score: 40.79  E-value: 2.68e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258596995  230 VILYGPPGTGKTLLAKAVANE-----------------TSATFLRVVGSELIQKYLGDGPK--LVREMFKVAEEHAPSIV 290
Cdd:pfam13401   8 LVLTGESGTGKTTLLRRLLEQlpevrdsvvfvdlpsgtSPKDLLRALLRALGLPLSGRLSKeeLLAALQQLLLALAVAVV 87
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 258596995  291 F-IDEIDAvgtkryeatsggereIQRTMLELLNQLDGFdSRGDVKVIMA 338
Cdd:pfam13401  88 LiIDEAQH---------------LSLEALEELRDLLNL-SSKLLQLILV 120
PRK08116 PRK08116
hypothetical protein; Validated
229-259 4.43e-04

hypothetical protein; Validated


Pssm-ID: 236153 [Multi-domain]  Cd Length: 268  Bit Score: 41.93  E-value: 4.43e-04
                         10        20        30
                 ....*....|....*....|....*....|.
gi 258596995 229 GVILYGPPGTGKTLLAKAVANETSATFLRVV 259
Cdd:PRK08116 116 GLLLWGSVGTGKTYLAACIANELIEKGVPVI 146
COG0645 COG0645
Predicted kinase, contains AAA domain [General function prediction only];
230-302 7.28e-04

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


Pssm-ID: 440410 [Multi-domain]  Cd Length: 164  Bit Score: 40.28  E-value: 7.28e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258596995 230 VILYGPPGTGKTLLAKAVANETSATFLR--VVGSEL-------IQKYLGDGPKLVREMFKVAEEHA---PSIVfideIDA 297
Cdd:COG0645    2 ILVCGLPGSGKSTLARALAERLGAVRLRsdVVRKRLfgaglapLERSPEATARTYARLLALARELLaagRSVI----LDA 77

                 ....*
gi 258596995 298 VGTKR 302
Cdd:COG0645   78 TFLRR 82
RecA-like_ClpX cd19497
ATP-dependent Clp protease ATP-binding subunit ClpX; ClpX is a component of the ATP-dependent ...
230-301 8.43e-04

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


Pssm-ID: 410905 [Multi-domain]  Cd Length: 251  Bit Score: 41.05  E-value: 8.43e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258596995 230 VILYGPPGTGKTLLAK----------AVANETSATFLRVVGSE---LIQKYLGDGpklvreMFKVaEEHAPSIVFIDEID 296
Cdd:cd19497   53 ILLIGPTGSGKTLLAQtlakildvpfAIADATTLTEAGYVGEDvenILLKLLQAA------DYDV-ERAQRGIVYIDEID 125

                 ....*
gi 258596995 297 AVGTK 301
Cdd:cd19497  126 KIARK 130
COG2842 COG2842
Bacteriophage DNA transposition protein, AAA+ family ATPase [Mobilome: prophages, transposons]; ...
230-296 8.68e-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: 8.68e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258596995 230 VILYGPPGTGKTLLAKAVANE-------------TSATFLRVVGSELiqkYLGDGPKLVREMFKVAEEH---APSIVFID 293
Cdd:COG2842   53 GVVYGESGVGKTTAAREYANRnpnviyvtaspswTSKELLEELAEEL---GIPAPPGTIADLRDRILERlagTGRLLIID 129

                 ...
gi 258596995 294 EID 296
Cdd:COG2842  130 EAD 132
recomb_radB TIGR02237
DNA repair and recombination protein RadB; This family consists exclusively of archaeal RadB ...
228-285 9.55e-04

DNA repair and recombination protein RadB; This family consists exclusively of archaeal RadB protein, a homolog of bacterial RecA (TIGR02012), eukaryotic RAD51 (TIGR02239) and DMC1 (TIGR02238), and archaeal RadA (TIGR02236).


Pssm-ID: 274047 [Multi-domain]  Cd Length: 209  Bit Score: 40.48  E-value: 9.55e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 258596995  228 KGVI--LYGPPGTGKTLLAKAVANETSATFLRVV-------GSELIQKYLGDGPKLVREMFKVAEEH 285
Cdd:TIGR02237  11 RGTItqIYGPPGSGKTNICMILAVNAARQGKKVVyidteglSPERFKQIAEDRPERALSNFIVFEVF 77
AAA_16 pfam13191
AAA ATPase domain; This family of domains contain a P-loop motif that is characteriztic of the ...
197-348 2.15e-03

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: 38.64  E-value: 2.15e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258596995  197 GLESQIQEIKEAvelplthpelYEDIGIKPPKGVILYGPPGTGKTLLAKAV---ANETSATFLRVVGSELIQkYLGDGPK 273
Cdd:pfam13191   4 GREEELEQLLDA----------LDRVRSGRPPSVLLTGEAGTGKTTLLRELlraLERDGGYFLRGKCDENLP-YSPLLEA 72
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 258596995  274 LVREMFKVAEEHAPSIVFIDEIDAVGTKRYEATSGGEREIQRTMLELLNQLDGFDSRGDVKVIMATNRIDSLDPA 348
Cdd:pfam13191  73 LTREGLLRQLLDELESSLLEAWRAALLEALAPVPELPGDLAERLLDLLLRLLDLLARGERPLVLVLDDLQWADEA 147
TIP49 COG1224
DNA helicase TIP49, TBP-interacting protein [Transcription];
228-263 3.75e-03

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


Pssm-ID: 440837 [Multi-domain]  Cd Length: 452  Bit Score: 39.57  E-value: 3.75e-03
                         10        20        30
                 ....*....|....*....|....*....|....*...
gi 258596995 228 KGVILYGPPGTGKTLLAKAVANETSA--TFLRVVGSEL 263
Cdd:COG1224   65 KGILIVGPPGTGKTALAVAIARELGEdtPFVAISGSEI 102
RNA_helicase pfam00910
RNA helicase; This family includes RNA helicases thought to be involved in duplex unwinding ...
230-261 4.33e-03

RNA helicase; This family includes RNA helicases thought to be involved in duplex unwinding during viral RNA replication. Members of this family are found in a variety of single stranded RNA viruses.


Pssm-ID: 459992  Cd Length: 102  Bit Score: 36.43  E-value: 4.33e-03
                          10        20        30
                  ....*....|....*....|....*....|..
gi 258596995  230 VILYGPPGTGKTLLAKAVANETSATFLRVVGS 261
Cdd:pfam00910   1 IWLYGPPGCGKSTLAKYLARALLKKLGLPKDS 32
TIP49 pfam06068
TIP49 P-loop domain; This family consists of the C-terminal region of several eukaryotic and ...
228-263 4.52e-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: 39.21  E-value: 4.52e-03
                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 258596995  228 KGVILYGPPGTGKTLLAKAVANE--TSATFLRVVGSEL 263
Cdd:pfam06068  51 RAVLIAGPPGTGKTALAIAISKElgEDTPFTSISGSEV 88
RuvB COG2255
Holliday junction resolvasome RuvABC, ATP-dependent DNA helicase subunit RuvB [Replication, ...
230-295 5.01e-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: 38.91  E-value: 5.01e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 258596995 230 VILYGPPGTGKTLLAKAVANETSATfLRVVGSELIQKyLGDgpklvremfkVA------EEHapSIVFIDEI 295
Cdd:COG2255   57 VLLYGPPGLGKTTLAHIIANEMGVN-IRITSGPAIEK-PGD----------LAailtnlEEG--DVLFIDEI 114
 
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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