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Conserved domains on  [gi|1098423980|gb|OII72254|]
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26s proteasome regulatory subunit S4 like AAA ATPase [Cryptosporidium ubiquitum]

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
 1-445 0e+00

26 proteosome regulatory subunit 4-like protein; Provisional


:

Pssm-ID: 185575 [Multi-domain]  Cd Length: 438  Bit Score: 852.14  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1098423980   1 MGNSHGVLgeggmknNRKSRNNGKDEKKKLESAPPPMEMKRKRKQKGPPQYARLPTVLPNAKCRLRLLKYERIKDYLMME 80
Cdd:PTZ00361    1 MGNAQGQG-------NNQKDKNKKKEKKKKESPPPPHEIKRKKKRKGPDAASKLPKVTPNTKCRLRLLKLERIKDYLLLE 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1098423980  81 QEFITSMESVKPSAETAEEEHNKVDDLRGSPMNIGTLEEIIDENHAIVSSSVGSEYYVNILSFVDKNQLEPGSSVLLHNK 160
Cdd:PTZ00361   74 EEFITNQEAQKPAQEKNEAELKKVDDLRGSPLSVGTLEEIIDENHAIVSSSVGPEYYVNILSFVDKEQLEPGCSVLLHNK 153

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1098423980 161 VYSVVGIMNDEVDPLVSVMKVDKAPLESYADIGGLEQQIQEIKEAVEIPLTHPELYDDIGIKPPKGVILYGPPGTGKTLL 240
Cdd:PTZ00361  154 THSVVGILLDEVDPLVSVMKVDKAPLESYADIGGLEQQIQEIKEAVELPLTHPELYDDIGIKPPKGVILYGPPGTGKTLL 233

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1098423980 241 AKAVANETSATFLRVVGSELIQKYLGDGPKLVRELFRVAEENAPSIVFIDEIDAVGTKRHDSQSGGERDIQRTMLELLNQ 320
Cdd:PTZ00361  234 AKAVANETSATFLRVVGSELIQKYLGDGPKLVRELFRVAEENAPSIVFIDEIDAIGTKRYDATSGGEKEIQRTMLELLNQ 313

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1098423980 321 LDGFEARGDVKVIMATNKIESLDPALIRPGRIDRKIELPNPDCKTKRRIFQIHTSKMTLSEDVDLEEFIMAKDDISGADI 400
Cdd:PTZ00361  314 LDGFDSRGDVKVIMATNRIESLDPALIRPGRIDRKIEFPNPDEKTKRRIFEIHTSKMTLAEDVDLEEFIMAKDELSGADI 393

                         410       420       430       440
                  ....*....|....*....|....*....|....*....|....*
gi 1098423980 401 KAICTEAGLLALRERRMRVTQEDLRKAKEKALYRKKGGIPEGLYL 445
Cdd:PTZ00361  394 KAICTEAGLLALRERRMKVTQADFRKAKEKVLYRKKGNIPEGLYL 438
 
Name Accession Description Interval E-value
PTZ00361 PTZ00361
26 proteosome regulatory subunit 4-like protein; Provisional
 1-445 0e+00

26 proteosome regulatory subunit 4-like protein; Provisional


Pssm-ID: 185575 [Multi-domain]  Cd Length: 438  Bit Score: 852.14  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1098423980   1 MGNSHGVLgeggmknNRKSRNNGKDEKKKLESAPPPMEMKRKRKQKGPPQYARLPTVLPNAKCRLRLLKYERIKDYLMME 80
Cdd:PTZ00361    1 MGNAQGQG-------NNQKDKNKKKEKKKKESPPPPHEIKRKKKRKGPDAASKLPKVTPNTKCRLRLLKLERIKDYLLLE 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1098423980  81 QEFITSMESVKPSAETAEEEHNKVDDLRGSPMNIGTLEEIIDENHAIVSSSVGSEYYVNILSFVDKNQLEPGSSVLLHNK 160
Cdd:PTZ00361   74 EEFITNQEAQKPAQEKNEAELKKVDDLRGSPLSVGTLEEIIDENHAIVSSSVGPEYYVNILSFVDKEQLEPGCSVLLHNK 153

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1098423980 161 VYSVVGIMNDEVDPLVSVMKVDKAPLESYADIGGLEQQIQEIKEAVEIPLTHPELYDDIGIKPPKGVILYGPPGTGKTLL 240
Cdd:PTZ00361  154 THSVVGILLDEVDPLVSVMKVDKAPLESYADIGGLEQQIQEIKEAVELPLTHPELYDDIGIKPPKGVILYGPPGTGKTLL 233

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1098423980 241 AKAVANETSATFLRVVGSELIQKYLGDGPKLVRELFRVAEENAPSIVFIDEIDAVGTKRHDSQSGGERDIQRTMLELLNQ 320
Cdd:PTZ00361  234 AKAVANETSATFLRVVGSELIQKYLGDGPKLVRELFRVAEENAPSIVFIDEIDAIGTKRYDATSGGEKEIQRTMLELLNQ 313

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1098423980 321 LDGFEARGDVKVIMATNKIESLDPALIRPGRIDRKIELPNPDCKTKRRIFQIHTSKMTLSEDVDLEEFIMAKDDISGADI 400
Cdd:PTZ00361  314 LDGFDSRGDVKVIMATNRIESLDPALIRPGRIDRKIEFPNPDEKTKRRIFEIHTSKMTLAEDVDLEEFIMAKDELSGADI 393

                         410       420       430       440
                  ....*....|....*....|....*....|....*....|....*
gi 1098423980 401 KAICTEAGLLALRERRMRVTQEDLRKAKEKALYRKKGGIPEGLYL 445
Cdd:PTZ00361  394 KAICTEAGLLALRERRMKVTQADFRKAKEKVLYRKKGNIPEGLYL 438
26Sp45 TIGR01242
26S proteasome subunit P45 family; Many proteins may score above the trusted cutoff because an ...
 60-432 1.55e-149

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: 429.60  E-value: 1.55e-149
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1098423980  60 NAKCRLRLLKyeriKDYLMMEQEFITSMESVkpsaetaEEEHNKVDDLRGSPMNIGTLEEIIDENHAIVSSSVGSEYYVN 139
Cdd:TIGR01242   3 ELDVRIRKLE----DEKRSLEKEKIRLEREL-------ERLRSEIERLRSPPLIVGTVLEVLDDNRVVVKSSTGPNFVVN 71

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1098423980 140 ILSFVDKNQLEPGSSVLLHNKVYSVVGIMNDEVDPLVSVMKVDKAPLESYADIGGLEQQIQEIKEAVEIPLTHPELYDDI 219
Cdd:TIGR01242  72 VSAFIDRKSLKPGARVALNQQTLTIVDVLPTSKDPLVKGMEVEERPNVSYEDIGGLEEQIREIREAVELPLKHPELFEEV 151

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1098423980 220 GIKPPKGVILYGPPGTGKTLLAKAVANETSATFLRVVGSELIQKYLGDGPKLVRELFRVAEENAPSIVFIDEIDAVGTKR 299
Cdd:TIGR01242 152 GIEPPKGVLLYGPPGTGKTLLAKAVAHETNATFIRVVGSELVRKYIGEGARLVREIFELAKEKAPSIIFIDEIDAIAAKR 231

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1098423980 300 HDSQSGGERDIQRTMLELLNQLDGFEARGDVKVIMATNKIESLDPALIRPGRIDRKIELPNPDCKTKRRIFQIHTSKMTL 379
Cdd:TIGR01242 232 TDSGTSGDREVQRTLMQLLAELDGFDPRGNVKVIAATNRPDILDPALLRPGRFDRIIEVPLPDFEGRLEILKIHTRKMKL 311

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1098423980 380 SEDVDLEEFIMAKDDISGADIKAICTEAGLLALRERRMRVTQEDLRKAKEKAL 432
Cdd:TIGR01242 312 AEDVDLEAIAKMTEGASGADLKAICTEAGMFAIREERDYVTMDDFIKAVEKVL 364
RPT1 COG1222
ATP-dependent 26S proteasome regulatory subunit [Posttranslational modification, protein ...
 179-430 6.93e-131

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


Pssm-ID: 440835 [Multi-domain]  Cd Length: 326  Bit Score: 380.51  E-value: 6.93e-131
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1098423980 179 MKVDKAPLESYADIGGLEQQIQEIKEAVEIPLTHPELYDDIGIKPPKGVILYGPPGTGKTLLAKAVANETSATFLRVVGS 258
Cdd:COG1222    67 AVPAESPDVTFDDIGGLDEQIEEIREAVELPLKNPELFRKYGIEPPKGVLLYGPPGTGKTLLAKAVAGELGAPFIRVRGS 146

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1098423980 259 ELIQKYLGDGPKLVRELFRVAEENAPSIVFIDEIDAVGTKRHDSQSGGErdIQRTMLELLNQLDGFEARGDVKVIMATNK 338
Cdd:COG1222   147 ELVSKYIGEGARNVREVFELAREKAPSIIFIDEIDAIAARRTDDGTSGE--VQRTVNQLLAELDGFESRGDVLIIAATNR 224

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1098423980 339 IESLDPALIRPGRIDRKIELPNPDCKTKRRIFQIHTSKMTLSEDVDLEEFIMAKDDISGADIKAICTEAGLLALRERRMR 418
Cdd:COG1222   225 PDLLDPALLRPGRFDRVIEVPLPDEEAREEILKIHLRDMPLADDVDLDKLAKLTEGFSGADLKAIVTEAGMFAIREGRDT 304

                         250
                  ....*....|..
gi 1098423980 419 VTQEDLRKAKEK 430
Cdd:COG1222   305 VTMEDLEKAIEK 316
RecA-like_PAN_like cd19502
proteasome activating nucleotidase PAN and related proteasome subunits; This subfamily ...
 188-357 1.90e-110

proteasome activating nucleotidase PAN and related proteasome subunits; This subfamily contains ATPase subunits of the eukaryotic 26S proteasome, and of the archaeal proteasome which carry out ATP-dependent degradation of substrates of the ubiquitin-proteasome pathway. The eukaryotic 26S proteasome consists of a proteolytic 20S core particle (CP), and a 19S regulatory particle (RP) which provides the ATP-dependence and the specificity for ubiquitinated proteins. In the archaea the RP is a homohexameric complex of proteasome-activating nucleotidase (PAN). This subfamily also includes various eukaryotic 26S subunits including, proteasome 26S subunit, ATPase 2 (PSMC2, also known as S7 and MSS1) which is a member of the 19S RP and has a chaperone like activity; and proteasome 20S subunit alpha 6 (PSMA6, also known as IOTA, p27K, and PROS27) which is a member of the 20S CP. This RecA-like_PAN subfamily belongs to the RecA-like NTPase family which includes the NTP binding domain of F1 and V1 H(+)ATPases, DnaB and related helicases as well as bacterial RecA and related eukaryotic and archaeal recombinases. The RecA-like NTPase family also includes bacterial conjugation proteins and related DNA transfer proteins involved in type II and type IV secretion.


Pssm-ID: 410910 [Multi-domain]  Cd Length: 171  Bit Score: 322.75  E-value: 1.90e-110
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1098423980 188 SYADIGGLEQQIQEIKEAVEIPLTHPELYDDIGIKPPKGVILYGPPGTGKTLLAKAVANETSATFLRVVGSELIQKYLGD 267
Cdd:cd19502     1 TYEDIGGLDEQIREIREVVELPLKHPELFEELGIEPPKGVLLYGPPGTGKTLLAKAVANHTDATFIRVVGSELVQKYIGE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1098423980 268 GPKLVRELFRVAEENAPSIVFIDEIDAVGTKRHDSQSGGERDIQRTMLELLNQLDGFEARGDVKVIMATNKIESLDPALI 347
Cdd:cd19502    81 GARLVRELFEMAREKAPSIIFIDEIDAIGAKRFDSGTGGDREVQRTMLELLNQLDGFDPRGNIKVIMATNRPDILDPALL 160

                         170
                  ....*....|
gi 1098423980 348 RPGRIDRKIE 357
Cdd:cd19502   161 RPGRFDRKIE 170
AAA pfam00004
ATPase family associated with various cellular activities (AAA); AAA family proteins often ...
 227-359 3.39e-51

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


Pssm-ID: 459627 [Multi-domain]  Cd Length: 130  Bit Score: 168.93  E-value: 3.39e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1098423980 227 VILYGPPGTGKTLLAKAVANETSATFLRVVGSELIQKYLGDGPKLVRELFRVAEENAPSIVFIDEIDAVGTKRhdsQSGG 306
Cdd:pfam00004   1 LLLYGPPGTGKTTLAKAVAKELGAPFIEISGSELVSKYVGESEKRLRELFEAAKKLAPCVIFIDEIDALAGSR---GSGG 77

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1098423980 307 ERDIQRTMLELLNQLDGFEAR-GDVKVIMATNKIESLDPALIrpGRIDRKIELP 359
Cdd:pfam00004  78 DSESRRVVNQLLTELDGFTSSnSKVIVIAATNRPDKLDPALL--GRFDRIIEFP 129
AAA smart00382
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ...
 223-362 4.37e-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: 83.58  E-value: 4.37e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1098423980  223 PPKGVILYGPPGTGKTLLAKAVANETSATFLRVV-----------------GSELIQKYLGDGPKLVRELFRVAEENAPS 285
Cdd:smart00382   1 PGEVILIVGPPGSGKTTLARALARELGPPGGGVIyidgedileevldqlllIIVGGKKASGSGELRLRLALALARKLKPD 80

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1098423980  286 IVFIDEIDAVGTKrhdsqsggERDIQRTMLELLNQLDGFEARGDVKVIMATNKIESLDPALIRPgRIDRKIELPNPD 362
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 ...
 227-292 3.48e-04

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: 42.07  E-value: 3.48e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1098423980 227 VILYGPPGTGKTLLAKAVANE-----TSATFLRVvgSELIQKYL---GDGpKLVRELFRVAeenAPSIVFIDEI 292
Cdd:NF038214   93 VLLLGPPGTGKTHLAIALGYAacrqgYRVRFTTA--ADLVEQLAqarADG-RLGRLLRRLA---RYDLLIIDEL 160
 
Name Accession Description Interval E-value
PTZ00361 PTZ00361
26 proteosome regulatory subunit 4-like protein; Provisional
 1-445 0e+00

26 proteosome regulatory subunit 4-like protein; Provisional


Pssm-ID: 185575 [Multi-domain]  Cd Length: 438  Bit Score: 852.14  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1098423980   1 MGNSHGVLgeggmknNRKSRNNGKDEKKKLESAPPPMEMKRKRKQKGPPQYARLPTVLPNAKCRLRLLKYERIKDYLMME 80
Cdd:PTZ00361    1 MGNAQGQG-------NNQKDKNKKKEKKKKESPPPPHEIKRKKKRKGPDAASKLPKVTPNTKCRLRLLKLERIKDYLLLE 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1098423980  81 QEFITSMESVKPSAETAEEEHNKVDDLRGSPMNIGTLEEIIDENHAIVSSSVGSEYYVNILSFVDKNQLEPGSSVLLHNK 160
Cdd:PTZ00361   74 EEFITNQEAQKPAQEKNEAELKKVDDLRGSPLSVGTLEEIIDENHAIVSSSVGPEYYVNILSFVDKEQLEPGCSVLLHNK 153

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1098423980 161 VYSVVGIMNDEVDPLVSVMKVDKAPLESYADIGGLEQQIQEIKEAVEIPLTHPELYDDIGIKPPKGVILYGPPGTGKTLL 240
Cdd:PTZ00361  154 THSVVGILLDEVDPLVSVMKVDKAPLESYADIGGLEQQIQEIKEAVELPLTHPELYDDIGIKPPKGVILYGPPGTGKTLL 233

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1098423980 241 AKAVANETSATFLRVVGSELIQKYLGDGPKLVRELFRVAEENAPSIVFIDEIDAVGTKRHDSQSGGERDIQRTMLELLNQ 320
Cdd:PTZ00361  234 AKAVANETSATFLRVVGSELIQKYLGDGPKLVRELFRVAEENAPSIVFIDEIDAIGTKRYDATSGGEKEIQRTMLELLNQ 313

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1098423980 321 LDGFEARGDVKVIMATNKIESLDPALIRPGRIDRKIELPNPDCKTKRRIFQIHTSKMTLSEDVDLEEFIMAKDDISGADI 400
Cdd:PTZ00361  314 LDGFDSRGDVKVIMATNRIESLDPALIRPGRIDRKIEFPNPDEKTKRRIFEIHTSKMTLAEDVDLEEFIMAKDELSGADI 393

                         410       420       430       440
                  ....*....|....*....|....*....|....*....|....*
gi 1098423980 401 KAICTEAGLLALRERRMRVTQEDLRKAKEKALYRKKGGIPEGLYL 445
Cdd:PTZ00361  394 KAICTEAGLLALRERRMKVTQADFRKAKEKVLYRKKGNIPEGLYL 438
PRK03992 PRK03992
proteasome-activating nucleotidase; Provisional
 69-441 3.81e-171

proteasome-activating nucleotidase; Provisional


Pssm-ID: 179699 [Multi-domain]  Cd Length: 389  Bit Score: 485.11  E-value: 3.81e-171
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1098423980  69 KYERIKDYLMMEQEFITSMESVKPSAETAEEEHNK--------VDDLRGSPMNIGTLEEIIDENHAIVSSSVGSEYYVNI 140
Cdd:PRK03992    2 RLEALEERNSELEEQIRQLELKLRDLEAENEKLERelerlkseLEKLKSPPLIVATVLEVLDDGRVVVKSSGGPQFLVNV 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1098423980 141 LSFVDKNQLEPGSSVLLHNKVYSVVGIMNDEVDPLVSVMKVDKAPLESYADIGGLEQQIQEIKEAVEIPLTHPELYDDIG 220
Cdd:PRK03992   82 SPFIDREKLKPGARVALNQQSLAIVEVLPSEKDPRVQAMEVIESPNVTYEDIGGLEEQIREVREAVELPLKKPELFEEVG 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1098423980 221 IKPPKGVILYGPPGTGKTLLAKAVANETSATFLRVVGSELIQKYLGDGPKLVRELFRVAEENAPSIVFIDEIDAVGTKRH 300
Cdd:PRK03992  162 IEPPKGVLLYGPPGTGKTLLAKAVAHETNATFIRVVGSELVQKFIGEGARLVRELFELAREKAPSIIFIDEIDAIAAKRT 241

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1098423980 301 DSQSGGERDIQRTMLELLNQLDGFEARGDVKVIMATNKIESLDPALIRPGRIDRKIELPNPDCKTKRRIFQIHTSKMTLS 380
Cdd:PRK03992  242 DSGTSGDREVQRTLMQLLAEMDGFDPRGNVKIIAATNRIDILDPAILRPGRFDRIIEVPLPDEEGRLEILKIHTRKMNLA 321

                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1098423980 381 EDVDLEEFIMAKDDISGADIKAICTEAGLLALRERRMRVTQEDLRKAKEKALYRKKGGIPE 441
Cdd:PRK03992  322 DDVDLEELAELTEGASGADLKAICTEAGMFAIRDDRTEVTMEDFLKAIEKVMGKEEKDSME 382
PTZ00454 PTZ00454
26S protease regulatory subunit 6B-like protein; Provisional
 65-436 1.33e-159

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


Pssm-ID: 240423 [Multi-domain]  Cd Length: 398  Bit Score: 456.53  E-value: 1.33e-159
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1098423980  65 LRLLKYERIKDYLMMEQEFI-TSMESVKPSAETAEEEhnkVDDLRGSPMNIGTLEEIIDENHAIVSSSVGSEYYVNILSF 143
Cdd:PTZ00454   22 EKLKELEKELEFLDIQEEYIkEEQKNLKRELIRAKEE---VKRIQSVPLVIGQFLEMIDSNYGIVSSTSGSNYYVRILST 98

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1098423980 144 VDKNQLEPGSSVLLHNKVYSVVGIMNDEVDPLVSVMKVDKAPLESYADIGGLEQQIQEIKEAVEIPLTHPELYDDIGIKP 223
Cdd:PTZ00454   99 LNRELLKPNASVALHRHSHAVVDILPPEADSSIQLLQMSEKPDVTYSDIGGLDIQKQEIREAVELPLTCPELYEQIGIDP 178

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1098423980 224 PKGVILYGPPGTGKTLLAKAVANETSATFLRVVGSELIQKYLGDGPKLVRELFRVAEENAPSIVFIDEIDAVGTKRHDSQ 303
Cdd:PTZ00454  179 PRGVLLYGPPGTGKTMLAKAVAHHTTATFIRVVGSEFVQKYLGEGPRMVRDVFRLARENAPSIIFIDEVDSIATKRFDAQ 258

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1098423980 304 SGGERDIQRTMLELLNQLDGFEARGDVKVIMATNKIESLDPALIRPGRIDRKIELPNPDCKTKRRIFQIHTSKMTLSEDV 383
Cdd:PTZ00454  259 TGADREVQRILLELLNQMDGFDQTTNVKVIMATNRADTLDPALLRPGRLDRKIEFPLPDRRQKRLIFQTITSKMNLSEEV 338

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1098423980 384 DLEEFIMAKDDISGADIKAICTEAGLLALRERRMRVTQEDLRKAKeKALYRKK 436
Cdd:PTZ00454  339 DLEDFVSRPEKISAADIAAICQEAGMQAVRKNRYVILPKDFEKGY-KTVVRKT 390
26Sp45 TIGR01242
26S proteasome subunit P45 family; Many proteins may score above the trusted cutoff because an ...
 60-432 1.55e-149

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: 429.60  E-value: 1.55e-149
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1098423980  60 NAKCRLRLLKyeriKDYLMMEQEFITSMESVkpsaetaEEEHNKVDDLRGSPMNIGTLEEIIDENHAIVSSSVGSEYYVN 139
Cdd:TIGR01242   3 ELDVRIRKLE----DEKRSLEKEKIRLEREL-------ERLRSEIERLRSPPLIVGTVLEVLDDNRVVVKSSTGPNFVVN 71

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1098423980 140 ILSFVDKNQLEPGSSVLLHNKVYSVVGIMNDEVDPLVSVMKVDKAPLESYADIGGLEQQIQEIKEAVEIPLTHPELYDDI 219
Cdd:TIGR01242  72 VSAFIDRKSLKPGARVALNQQTLTIVDVLPTSKDPLVKGMEVEERPNVSYEDIGGLEEQIREIREAVELPLKHPELFEEV 151

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1098423980 220 GIKPPKGVILYGPPGTGKTLLAKAVANETSATFLRVVGSELIQKYLGDGPKLVRELFRVAEENAPSIVFIDEIDAVGTKR 299
Cdd:TIGR01242 152 GIEPPKGVLLYGPPGTGKTLLAKAVAHETNATFIRVVGSELVRKYIGEGARLVREIFELAKEKAPSIIFIDEIDAIAAKR 231

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1098423980 300 HDSQSGGERDIQRTMLELLNQLDGFEARGDVKVIMATNKIESLDPALIRPGRIDRKIELPNPDCKTKRRIFQIHTSKMTL 379
Cdd:TIGR01242 232 TDSGTSGDREVQRTLMQLLAELDGFDPRGNVKVIAATNRPDILDPALLRPGRFDRIIEVPLPDFEGRLEILKIHTRKMKL 311

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1098423980 380 SEDVDLEEFIMAKDDISGADIKAICTEAGLLALRERRMRVTQEDLRKAKEKAL 432
Cdd:TIGR01242 312 AEDVDLEAIAKMTEGASGADLKAICTEAGMFAIREERDYVTMDDFIKAVEKVL 364
RPT1 COG1222
ATP-dependent 26S proteasome regulatory subunit [Posttranslational modification, protein ...
 179-430 6.93e-131

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


Pssm-ID: 440835 [Multi-domain]  Cd Length: 326  Bit Score: 380.51  E-value: 6.93e-131
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1098423980 179 MKVDKAPLESYADIGGLEQQIQEIKEAVEIPLTHPELYDDIGIKPPKGVILYGPPGTGKTLLAKAVANETSATFLRVVGS 258
Cdd:COG1222    67 AVPAESPDVTFDDIGGLDEQIEEIREAVELPLKNPELFRKYGIEPPKGVLLYGPPGTGKTLLAKAVAGELGAPFIRVRGS 146

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1098423980 259 ELIQKYLGDGPKLVRELFRVAEENAPSIVFIDEIDAVGTKRHDSQSGGErdIQRTMLELLNQLDGFEARGDVKVIMATNK 338
Cdd:COG1222   147 ELVSKYIGEGARNVREVFELAREKAPSIIFIDEIDAIAARRTDDGTSGE--VQRTVNQLLAELDGFESRGDVLIIAATNR 224

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1098423980 339 IESLDPALIRPGRIDRKIELPNPDCKTKRRIFQIHTSKMTLSEDVDLEEFIMAKDDISGADIKAICTEAGLLALRERRMR 418
Cdd:COG1222   225 PDLLDPALLRPGRFDRVIEVPLPDEEAREEILKIHLRDMPLADDVDLDKLAKLTEGFSGADLKAIVTEAGMFAIREGRDT 304

                         250
                  ....*....|..
gi 1098423980 419 VTQEDLRKAKEK 430
Cdd:COG1222   305 VTMEDLEKAIEK 316
RecA-like_PAN_like cd19502
proteasome activating nucleotidase PAN and related proteasome subunits; This subfamily ...
 188-357 1.90e-110

proteasome activating nucleotidase PAN and related proteasome subunits; This subfamily contains ATPase subunits of the eukaryotic 26S proteasome, and of the archaeal proteasome which carry out ATP-dependent degradation of substrates of the ubiquitin-proteasome pathway. The eukaryotic 26S proteasome consists of a proteolytic 20S core particle (CP), and a 19S regulatory particle (RP) which provides the ATP-dependence and the specificity for ubiquitinated proteins. In the archaea the RP is a homohexameric complex of proteasome-activating nucleotidase (PAN). This subfamily also includes various eukaryotic 26S subunits including, proteasome 26S subunit, ATPase 2 (PSMC2, also known as S7 and MSS1) which is a member of the 19S RP and has a chaperone like activity; and proteasome 20S subunit alpha 6 (PSMA6, also known as IOTA, p27K, and PROS27) which is a member of the 20S CP. This RecA-like_PAN subfamily belongs to the RecA-like NTPase family which includes the NTP binding domain of F1 and V1 H(+)ATPases, DnaB and related helicases as well as bacterial RecA and related eukaryotic and archaeal recombinases. The RecA-like NTPase family also includes bacterial conjugation proteins and related DNA transfer proteins involved in type II and type IV secretion.


Pssm-ID: 410910 [Multi-domain]  Cd Length: 171  Bit Score: 322.75  E-value: 1.90e-110
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1098423980 188 SYADIGGLEQQIQEIKEAVEIPLTHPELYDDIGIKPPKGVILYGPPGTGKTLLAKAVANETSATFLRVVGSELIQKYLGD 267
Cdd:cd19502     1 TYEDIGGLDEQIREIREVVELPLKHPELFEELGIEPPKGVLLYGPPGTGKTLLAKAVANHTDATFIRVVGSELVQKYIGE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1098423980 268 GPKLVRELFRVAEENAPSIVFIDEIDAVGTKRHDSQSGGERDIQRTMLELLNQLDGFEARGDVKVIMATNKIESLDPALI 347
Cdd:cd19502    81 GARLVRELFEMAREKAPSIIFIDEIDAIGAKRFDSGTGGDREVQRTMLELLNQLDGFDPRGNIKVIMATNRPDILDPALL 160

                         170
                  ....*....|
gi 1098423980 348 RPGRIDRKIE 357
Cdd:cd19502   161 RPGRFDRKIE 170
SpoVK COG0464
AAA+-type ATPase, SpoVK/Ycf46/Vps4 family [Cell wall/membrane/envelope biogenesis, Cell cycle ...
 171-427 4.36e-80

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: 253.29  E-value: 4.36e-80
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1098423980 171 EVDPLVSVMKVDKAPLESYADIGGLEQQIQEIKEAVEIPLTHPELYDDIGIKPPKGVILYGPPGTGKTLLAKAVANETSA 250
Cdd:COG0464   138 YEDIGGLEEELLELREAILDDLGGLEEVKEELRELVALPLKRPELREEYGLPPPRGLLLYGPPGTGKTLLARALAGELGL 217

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1098423980 251 TFLRVVGSELIQKYLGDGPKLVRELFRVAEENAPSIVFIDEIDAVGTKRhdsQSGGERDIQRTMLELLNQLDGFeaRGDV 330
Cdd:COG0464   218 PLIEVDLSDLVSKYVGETEKNLREVFDKARGLAPCVLFIDEADALAGKR---GEVGDGVGRRVVNTLLTEMEEL--RSDV 292

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1098423980 331 KVIMATNKIESLDPALIRpgRIDRKIELPNPDCKTKRRIFQIHTSKMTLSEDVDLEEFIMAKDDISGADIKAICTEAGLL 410
Cdd:COG0464   293 VVIAATNRPDLLDPALLR--RFDEIIFFPLPDAEERLEIFRIHLRKRPLDEDVDLEELAEATEGLSGADIRNVVRRAALQ 370

                         250
                  ....*....|....*..
gi 1098423980 411 ALRERRMRVTQEDLRKA 427
Cdd:COG0464   371 ALRLGREPVTTEDLLEA 387
FtsH_fam TIGR01241
ATP-dependent metalloprotease FtsH; HflB(FtsH) is a pleiotropic protein required for correct ...
 188-437 1.12e-78

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: 252.59  E-value: 1.12e-78
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1098423980 188 SYADIGGLEQQIQEIKEAVEIpLTHPELYDDIGIKPPKGVILYGPPGTGKTLLAKAVANETSATFLRVVGSELIQKYLGD 267
Cdd:TIGR01241  53 TFKDVAGIDEAKEELMEIVDF-LKNPSKFTKLGAKIPKGVLLVGPPGTGKTLLAKAVAGEAGVPFFSISGSDFVEMFVGV 131

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1098423980 268 GPKLVRELFRVAEENAPSIVFIDEIDAVGTKRHDSQSGGERDIQRTMLELLNQLDGFEARGDVKVIMATNKIESLDPALI 347
Cdd:TIGR01241 132 GASRVRDLFEQAKKNAPCIIFIDEIDAVGRQRGAGLGGGNDEREQTLNQLLVEMDGFGTNTGVIVIAATNRPDVLDPALL 211

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1098423980 348 RPGRIDRKIELPNPDCKTKRRIFQIHTSKMTLSEDVDLEEFIMAKDDISGADIKAICTEAGLLALRERRMRVTQEDLRKA 427
Cdd:TIGR01241 212 RPGRFDRQVVVDLPDIKGREEILKVHAKNKKLAPDVDLKAVARRTPGFSGADLANLLNEAALLAARKNKTEITMNDIEEA 291

                         250
                  ....*....|..
gi 1098423980 428 KEKALY--RKKG 437
Cdd:TIGR01241 292 IDRVIAgpEKKS 303
CDC48 TIGR01243
AAA family ATPase, CDC48 subfamily; This subfamily of the AAA family ATPases includes two ...
 185-436 2.71e-76

AAA family ATPase, CDC48 subfamily; This subfamily of the AAA family ATPases includes two members each from three archaeal species. It also includes yeast CDC48 (cell division control protein 48) and the human ortholog, transitional endoplasmic reticulum ATPase (valosin-containing protein). These proteins in eukaryotes are involved in the budding and transfer of membrane from the transitional endoplasmic reticulum to the Golgi apparatus.


Pssm-ID: 273521 [Multi-domain]  Cd Length: 733  Bit Score: 252.14  E-value: 2.71e-76
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1098423980 185 PLESYADIGGLEQQIQEIKEAVEIPLTHPELYDDIGIKPPKGVILYGPPGTGKTLLAKAVANETSATFLRVVGSELIQKY 264
Cdd:TIGR01243 448 PNVRWSDIGGLEEVKQELREAVEWPLKHPEIFEKMGIRPPKGVLLFGPPGTGKTLLAKAVATESGANFIAVRGPEILSKW 527

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1098423980 265 LGDGPKLVRELFRVAEENAPSIVFIDEIDAVGTKRHDSQSGGERDiqRTMLELLNQLDGFEARGDVKVIMATNKIESLDP 344
Cdd:TIGR01243 528 VGESEKAIREIFRKARQAAPAIIFFDEIDAIAPARGARFDTSVTD--RIVNQLLTEMDGIQELSNVVVIAATNRPDILDP 605

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1098423980 345 ALIRPGRIDRKIELPNPDCKTKRRIFQIHTSKMTLSEDVDLEEFIMAKDDISGADIKAICTEAGLLALRERRMRVTQEDL 424
Cdd:TIGR01243 606 ALLRPGRFDRLILVPPPDEEARKEIFKIHTRSMPLAEDVDLEELAEMTEGYTGADIEAVCREAAMAALRESIGSPAKEKL 685

                         250
                  ....*....|..
gi 1098423980 425 RKAKEKALYRKK 436
Cdd:TIGR01243 686 EVGEEEFLKDLK 697
CDC48 TIGR01243
AAA family ATPase, CDC48 subfamily; This subfamily of the AAA family ATPases includes two ...
 176-413 5.67e-75

AAA family ATPase, CDC48 subfamily; This subfamily of the AAA family ATPases includes two members each from three archaeal species. It also includes yeast CDC48 (cell division control protein 48) and the human ortholog, transitional endoplasmic reticulum ATPase (valosin-containing protein). These proteins in eukaryotes are involved in the budding and transfer of membrane from the transitional endoplasmic reticulum to the Golgi apparatus.


Pssm-ID: 273521 [Multi-domain]  Cd Length: 733  Bit Score: 248.67  E-value: 5.67e-75
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1098423980 176 VSVMKVDKAPLESYADIGGLEQQIQEIKEAVEIPLTHPELYDDIGIKPPKGVILYGPPGTGKTLLAKAVANETSATFLRV 255
Cdd:TIGR01243 164 VREEIERKVPKVTYEDIGGLKEAKEKIREMVELPMKHPELFEHLGIEPPKGVLLYGPPGTGKTLLAKAVANEAGAYFISI 243

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1098423980 256 VGSELIQKYLGDGPKLVRELFRVAEENAPSIVFIDEIDAVGTKRHDSQSGGERdiqRTMLELLNQLDGFEARGDVKVIMA 335
Cdd:TIGR01243 244 NGPEIMSKYYGESEERLREIFKEAEENAPSIIFIDEIDAIAPKREEVTGEVEK---RVVAQLLTLMDGLKGRGRVIVIGA 320

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1098423980 336 TNKIESLDPALIRPGRIDRKIELPNPDCKTKRRIFQIHTSKMTLSEDVDLEEFIMAKDDISGADIKAICTEAGLLALR 413
Cdd:TIGR01243 321 TNRPDALDPALRRPGRFDREIVIRVPDKRARKEILKVHTRNMPLAEDVDLDKLAEVTHGFVGADLAALAKEAAMAALR 398
HflB COG0465
ATP-dependent Zn proteases [Posttranslational modification, protein turnover, chaperones];
190-430 4.68e-73

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


Pssm-ID: 440233 [Multi-domain]  Cd Length: 583  Bit Score: 239.94  E-value: 4.68e-73
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1098423980 190 ADIGGLEQQIQEIKEAVEIpLTHPELYDDIGIKPPKGVILYGPPGTGKTLLAKAVANETSATFLRVVGSELIQKYLGDGP 269
Cdd:COG0465   142 DDVAGVDEAKEELQEIVDF-LKDPEKFTRLGAKIPKGVLLVGPPGTGKTLLAKAVAGEAGVPFFSISGSDFVEMFVGVGA 220

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1098423980 270 KLVRELFRVAEENAPSIVFIDEIDAVGTKRHDSQSGG--ERDiqRTmlelLNQL----DGFEARGDVKVIMATNKIESLD 343
Cdd:COG0465   221 SRVRDLFEQAKKNAPCIIFIDEIDAVGRQRGAGLGGGhdERE--QT----LNQLlvemDGFEGNEGVIVIAATNRPDVLD 294

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1098423980 344 PALIRPGRIDRKIELPNPDCKTKRRIFQIHTSKMTLSEDVDLEE-------FimakddiSGADIKAICTEAGLLALRERR 416
Cdd:COG0465   295 PALLRPGRFDRQVVVDLPDVKGREAILKVHARKKPLAPDVDLEViarrtpgF-------SGADLANLVNEAALLAARRNK 367

                         250
                  ....*....|....
gi 1098423980 417 MRVTQEDLRKAKEK 430
Cdd:COG0465   368 KAVTMEDFEEAIDR 381
RecA-like_CDC48_NLV2_r1-like cd19503
first of two ATPase domains of CDC48 and NLV2, and similar ATPase domains; CDC48 in yeast and ...
 191-358 6.47e-70

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: 218.70  E-value: 6.47e-70
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1098423980 191 DIGGLEQQIQEIKEAVEIPLTHPELYDDIGIKPPKGVILYGPPGTGKTLLAKAVANETSATFLRVVGSELIQKYLGDGPK 270
Cdd:cd19503     1 DIGGLDEQIASLKELIELPLKYPELFRALGLKPPRGVLLHGPPGTGKTLLARAVANEAGANFLSISGPSIVSKYLGESEK 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1098423980 271 LVRELFRVAEENAPSIVFIDEIDAVGTKRHDSQSGGERdiqRTMLELLNQLDGFEARGDVKVIMATNKIESLDPALIRPG 350
Cdd:cd19503    81 NLREIFEEARSHAPSIIFIDEIDALAPKREEDQREVER---RVVAQLLTLMDGMSSRGKVVVIAATNRPDAIDPALRRPG 157


                  ....*...
gi 1098423980 351 RIDRKIEL 358
Cdd:cd19503   158 RFDREVEI 165
pup_AAA TIGR03689
proteasome ATPase; In the Actinobacteria, as shown for Mycobacterium tuberculosis, some ...
 87-423 7.07e-68

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: 224.59  E-value: 7.07e-68
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1098423980  87 MESVKPSAETAEEEHNKVDDLRGSPM--NIGTLEEIIDENHAIVSSSVGSEYYVNILSFVDKNQLEPGSSVLLHNKV-YS 163
Cdd:TIGR03689  80 AAELVPGQTVRLNEALQVVEACDFERtgEIVTLKEVLDDGRALVTDRSGEERVVKLAGALADEGLRPGDTLLVDPRAgYA 159

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1098423980 164 VVGIMNDEVDPLVsvmkVDKAPLESYADIGGLEQQIQEIKEAVEIPLTHPELYDDIGIKPPKGVILYGPPGTGKTLLAKA 243
Cdd:TIGR03689 160 FEAIPRTEVEDLV----LEEVPDVTYADIGGLGSQIEQIRDAVELPFLHPELYREYGLKPPKGVLLYGPPGCGKTLIAKA 235

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1098423980 244 VANE----------TSATFLRVVGSELIQKYLGDGPKLVRELF----RVAEENAPSIVFIDEIDAVGTKRhdsQSGGERD 309
Cdd:TIGR03689 236 VANSlaarigaeggGKSYFLNIKGPELLNKYVGETERQIRLIFqrarEKASEGRPVIVFFDEMDSLFRTR---GSGVSSD 312

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1098423980 310 IQRTML-ELLNQLDGFEARGDVKVIMATNKIESLDPALIRPGRIDRKIELPNPDCKTKRRIFQIHtskmtLSEDVDLEEF 388
Cdd:TIGR03689 313 VETTVVpQLLAEIDGVESLDNVIVIGASNREDMIDPAILRPGRLDVKIRIERPDAEAAADIFAKY-----LTDDLPLPED 387

                         330       340       350
                  ....*....|....*....|....*....|....*....
gi 1098423980 389 IMAKDDISGADIKAICTEA--GLLALRERR--MRVTQED 423
Cdd:TIGR03689 388 LAAHDGDREATAAALIQRVvdALYARSEANryVEVTYAN 426
RecA-like_CDC48_r1-like cd19519
first of two ATPase domains of CDC48 and similar ATPase domains; CDC48 in yeast and p97 or VCP ...
 191-359 3.86e-67

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: 211.53  E-value: 3.86e-67
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1098423980 191 DIGGLEQQIQEIKEAVEIPLTHPELYDDIGIKPPKGVILYGPPGTGKTLLAKAVANETSATFLRVVGSELIQKYLGDGPK 270
Cdd:cd19519     1 DIGGCRKQLAQIREMVELPLRHPELFKAIGIKPPRGILLYGPPGTGKTLIARAVANETGAFFFLINGPEIMSKLAGESES 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1098423980 271 LVRELFRVAEENAPSIVFIDEIDAVGTKRHDSQSGGERdiqRTMLELLNQLDGFEARGDVKVIMATNKIESLDPALIRPG 350
Cdd:cd19519    81 NLRKAFEEAEKNAPAIIFIDEIDAIAPKREKTHGEVER---RIVSQLLTLMDGLKQRAHVIVMAATNRPNSIDPALRRFG 157


                  ....*....
gi 1098423980 351 RIDRKIELP 359
Cdd:cd19519   158 RFDREIDIG 166
RecA-like_FtsH cd19501
ATP-dependent zinc metalloprotease FtsH; FtsH ATPase is a processive, ATP-dependent zinc ...
 188-356 1.05e-66

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: 210.55  E-value: 1.05e-66
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1098423980 188 SYADIGGLEQQIQEIKEAVEIpLTHPELYDDIGIKPPKGVILYGPPGTGKTLLAKAVANETSATFLRVVGSELIQKYLGD 267
Cdd:cd19501     2 TFKDVAGCEEAKEELKEVVEF-LKNPEKFTKLGAKIPKGVLLVGPPGTGKTLLAKAVAGEAGVPFFSISGSDFVEMFVGV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1098423980 268 GPKLVRELFRVAEENAPSIVFIDEIDAVGTKRHDSQSGGERDIQRTMLELLNQLDGFEARGDVKVIMATNKIESLDPALI 347
Cdd:cd19501    81 GASRVRDLFEQAKKNAPCIVFIDEIDAVGRKRGAGLGGGHDEREQTLNQLLVEMDGFESNTGVIVIAATNRPDVLDPALL 160


                  ....*....
gi 1098423980 348 RPGRIDRKI 356
Cdd:cd19501   161 RPGRFDRQV 169
RecA-like_CDC48_r2-like cd19511
second of two ATPase domains of CDC48/p97, PEX1 and -6, VAT and NVL, and similar ATPase ...
 200-356 8.18e-64

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: 202.90  E-value: 8.18e-64
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1098423980 200 QEIKEAVEIPLTHPELYDDIGIKPPKGVILYGPPGTGKTLLAKAVANETSATFLRVVGSELIQKYLGDGPKLVRELFRVA 279
Cdd:cd19511     3 RELKEAVEWPLKHPDAFKRLGIRPPKGVLLYGPPGCGKTLLAKALASEAGLNFISVKGPELFSKYVGESERAVREIFQKA 82

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1098423980 280 EENAPSIVFIDEIDAVGTKRHDSQSGGERDiqRTMLELLNQLDGFEARGDVKVIMATNKIESLDPALIRPGRIDRKI 356
Cdd:cd19511    83 RQAAPCIIFFDEIDSLAPRRGQSDSSGVTD--RVVSQLLTELDGIESLKGVVVIAATNRPDMIDPALLRPGRLDKLI 157
ftsH CHL00176
cell division protein; Validated
 179-430 5.22e-63

cell division protein; Validated


Pssm-ID: 214386 [Multi-domain]  Cd Length: 638  Bit Score: 214.91  E-value: 5.22e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1098423980 179 MKVDKAPleSYADIGGLEQQIQEIKEAVEIpLTHPELYDDIGIKPPKGVILYGPPGTGKTLLAKAVANETSATFLRVVGS 258
Cdd:CHL00176  174 MEADTGI--TFRDIAGIEEAKEEFEEVVSF-LKKPERFTAVGAKIPKGVLLVGPPGTGKTLLAKAIAGEAEVPFFSISGS 250

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1098423980 259 ELIQKYLGDGPKLVRELFRVAEENAPSIVFIDEIDAVGTKRHDSQSGGERDIQRTMLELLNQLDGFEARGDVKVIMATNK 338
Cdd:CHL00176  251 EFVEMFVGVGAARVRDLFKKAKENSPCIVFIDEIDAVGRQRGAGIGGGNDEREQTLNQLLTEMDGFKGNKGVIVIAATNR 330

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1098423980 339 IESLDPALIRPGRIDRKIELPNPDCKTKRRIFQIHTSKMTLSEDVDLEefIMAKDDI--SGADIKAICTEAGLLALRERR 416
Cdd:CHL00176  331 VDILDAALLRPGRFDRQITVSLPDREGRLDILKVHARNKKLSPDVSLE--LIARRTPgfSGADLANLLNEAAILTARRKK 408

                         250
                  ....*....|....
gi 1098423980 417 MRVTQEDLRKAKEK 430
Cdd:CHL00176  409 ATITMKEIDTAIDR 422
RecA-like_VCP_r2 cd19529
second of two ATPase domains of Valosin-containing protein-like ATPase (VAT) and similar ...
 200-356 5.84e-59

second of two ATPase domains of Valosin-containing protein-like ATPase (VAT) and similar ATPase domains; The Valosin-containing protein-like ATPase of Thermoplasma acidophilum (VAT), is an archaeal homolog of the ubiquitous Cdc48/p97. It is a protein unfoldase that functions in concert with the 20S proteasome by unfolding proteasome substrates and passing them on for degradation. VAT forms a homohexamer, each monomer contains two tandem ATPase domains, referred to as D1 and D2, and an N-terminal domain. This subfamily belongs to the RecA-like NTPase family which includes the NTP binding domain of F1 and V1 H(+)ATPases, DnaB and related helicases as well as bacterial RecA and related eukaryotic and archaeal recombinases. The RecA-like NTPase family also includes bacterial conjugation proteins and related DNA transfer proteins involved in type II and type IV secretion.


Pssm-ID: 410937 [Multi-domain]  Cd Length: 159  Bit Score: 190.40  E-value: 5.84e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1098423980 200 QEIKEAVEIPLTHPELYDDIGIKPPKGVILYGPPGTGKTLLAKAVANETSATFLRVVGSELIQKYLGDGPKLVRELFRVA 279
Cdd:cd19529     3 QELKEAVEWPLLKPEVFKRLGIRPPKGILLYGPPGTGKTLLAKAVATESNANFISVKGPELLSKWVGESEKAIREIFRKA 82

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1098423980 280 EENAPSIVFIDEIDAVGTKRhdSQSGGERDIQRTMLELLNQLDGFEARGDVKVIMATNKIESLDPALIRPGRIDRKI 356
Cdd:cd19529    83 RQVAPCVIFFDEIDSIAPRR--GTTGDSGVTERVVNQLLTELDGLEEMNGVVVIAATNRPDIIDPALLRAGRFDRLI 157
RecA-like_protease cd19481
proteases similar to RecA; RecA-like NTPases. This family includes the NTP binding domain of ...
 198-358 6.84e-59

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: 190.19  E-value: 6.84e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1098423980 198 QIQEIKEAVEIPLTHPELYDDiGIKPPKGVILYGPPGTGKTLLAKAVANETSATFLRVVGSELIQKYLGDGPKLVRELFR 277
Cdd:cd19481     1 LKASLREAVEAPRRGSRLRRY-GLGLPKGILLYGPPGTGKTLLAKALAGELGLPLIVVKLSSLLSKYVGESEKNLRKIFE 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1098423980 278 VAEENAPSIVFIDEIDAVGTKRHDSQSGGERdiQRTMLELLNQLDGFEARGDVKVIMATNKIESLDPALIRPGRIDRKIE 357
Cdd:cd19481    80 RARRLAPCILFIDEIDAIGRKRDSSGESGEL--RRVLNQLLTELDGVNSRSKVLVIAATNRPDLLDPALLRPGRFDEVIE 157


                  .
gi 1098423980 358 L 358
Cdd:cd19481   158 F 158
hflB PRK10733
ATP-dependent zinc metalloprotease FtsH;
188-432 2.34e-58

ATP-dependent zinc metalloprotease FtsH;


Pssm-ID: 182683 [Multi-domain]  Cd Length: 644  Bit Score: 202.57  E-value: 2.34e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1098423980 188 SYADIGGLEQQIQEIKEAVEIpLTHPELYDDIGIKPPKGVILYGPPGTGKTLLAKAVANETSATFLRVVGSELIQKYLGD 267
Cdd:PRK10733  150 TFADVAGCDEAKEEVAELVEY-LREPSRFQKLGGKIPKGVLMVGPPGTGKTLLAKAIAGEAKVPFFTISGSDFVEMFVGV 228

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1098423980 268 GPKLVRELFRVAEENAPSIVFIDEIDAVGTKRHDSQSGGERDIQRTMLELLNQLDGFEARGDVKVIMATNKIESLDPALI 347
Cdd:PRK10733  229 GASRVRDMFEQAKKAAPCIIFIDEIDAVGRQRGAGLGGGHDEREQTLNQMLVEMDGFEGNEGIIVIAATNRPDVLDPALL 308

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1098423980 348 RPGRIDRKIELPNPDCKTKRRIFQIHTSKMTLSEDVDLEEFIMAKDDISGADIKAICTEAGLLALRERRMRVTQEDLRKA 427
Cdd:PRK10733  309 RPGRFDRQVVVGLPDVRGREQILKVHMRRVPLAPDIDAAIIARGTPGFSGADLANLVNEAALFAARGNKRVVSMVEFEKA 388


                  ....*
gi 1098423980 428 KEKAL 432
Cdd:PRK10733  389 KDKIM 393
AAA pfam00004
ATPase family associated with various cellular activities (AAA); AAA family proteins often ...
 227-359 3.39e-51

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


Pssm-ID: 459627 [Multi-domain]  Cd Length: 130  Bit Score: 168.93  E-value: 3.39e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1098423980 227 VILYGPPGTGKTLLAKAVANETSATFLRVVGSELIQKYLGDGPKLVRELFRVAEENAPSIVFIDEIDAVGTKRhdsQSGG 306
Cdd:pfam00004   1 LLLYGPPGTGKTTLAKAVAKELGAPFIEISGSELVSKYVGESEKRLRELFEAAKKLAPCVIFIDEIDALAGSR---GSGG 77

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1098423980 307 ERDIQRTMLELLNQLDGFEAR-GDVKVIMATNKIESLDPALIrpGRIDRKIELP 359
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 ...
 200-356 3.97e-50

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: 167.30  E-value: 3.97e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1098423980 200 QEIKEAVEIPLTHPELYDDIGIKPPKGVILYGPPGTGKTLLAKAVANETSATFLRVVGSELIQKYLGDGPKLVRELFRVA 279
Cdd:cd19528     3 RELQELVQYPVEHPDKFLKFGMTPSKGVLFYGPPGCGKTLLAKAIANECQANFISVKGPELLTMWFGESEANVRDIFDKA 82

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1098423980 280 EENAPSIVFIDEIDAVGTKRHDSQSGGERDIQRTMLELLNQLDGFEARGDVKVIMATNKIESLDPALIRPGRIDRKI 356
Cdd:cd19528    83 RAAAPCVLFFDELDSIAKARGGNIGDAGGAADRVINQILTEMDGMNTKKNVFIIGATNRPDIIDPAILRPGRLDQLI 159
COG1223 COG1223
Predicted ATPase, AAA+ superfamily [General function prediction only];
191-442 7.82e-50

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


Pssm-ID: 440836 [Multi-domain]  Cd Length: 246  Bit Score: 169.68  E-value: 7.82e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1098423980 191 DIGGLEQQIQEIKEAVEiPLTHPELYDDIGIKPPKGVILYGPPGTGKTLLAKAVANETSATFLRVVGSELIQKYLGDGPK 270
Cdd:COG1223     3 DVVGQEEAKKKLKLIIK-ELRRRENLRKFGLWPPRKILFYGPPGTGKTMLAEALAGELKLPLLTVRLDSLIGSYLGETAR 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1098423980 271 LVRELFRVAEEnAPSIVFIDEIDAVGTKRHDSQSGGErdIQRTMLELLNQLDGFeaRGDVKVIMATNKIESLDPALIRpg 350
Cdd:COG1223    82 NLRKLFDFARR-APCVIFFDEFDAIAKDRGDQNDVGE--VKRVVNALLQELDGL--PSGSVVIAATNHPELLDSALWR-- 154

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1098423980 351 RIDRKIELPNPDCKTKRRIFQIHTSKMTLSEDVDLEEFIMAKDDISGADIKAICTEAGLLALRERRMRVTQEDLRKAKEK 430
Cdd:COG1223   155 RFDEVIEFPLPDKEERKEILELNLKKFPLPFELDLKKLAKKLEGLSGADIEKVLKTALKKAILEDREKVTKEDLEEALKQ 234

                         250
                  ....*....|..
gi 1098423980 431 ALYRKKGGIPEG 442
Cdd:COG1223   235 RKERKKEPKKEG 246
RecA-like_VPS4-like cd19509
ATPase domain of VPS4, ATAD1, K, KTNA1, Spastin, FIGL-1 and similar ATPase domains; This ...
 192-356 2.92e-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: 165.22  E-value: 2.92e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1098423980 192 IGGLEQQIQEIKEAVEIPLTHPELYDDIgIKPPKGVILYGPPGTGKTLLAKAVANETSATFLRVVGSELIQKYLGDGPKL 271
Cdd:cd19509     1 IAGLDDAKEALKEAVILPSLRPDLFPGL-RGPPRGILLYGPPGTGKTLLARAVASESGSTFFSISASSLVSKWVGESEKI 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1098423980 272 VRELFRVAEENAPSIVFIDEIDAVGTKRHDSQSGGERdiqRTMLELLNQLDGFEARGD--VKVIMATNKIESLDPALIRp 349
Cdd:cd19509    80 VRALFALARELQPSIIFIDEIDSLLSERGSGEHEASR---RVKTEFLVQMDGVLNKPEdrVLVLGATNRPWELDEAFLR- 155


                  ....*..
gi 1098423980 350 gRIDRKI 356
Cdd:cd19509   156 -RFEKRI 161
RecA-like_NVL_r1-like cd19518
first of two ATPase domains of NVL (nuclear VCP-like protein) and similar ATPase domains; NVL ...
 191-358 1.55e-48

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: 163.73  E-value: 1.55e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1098423980 191 DIGGLEQQIQEIKEAVEIPLTHPELYDDIGIKPPKGVILYGPPGTGKTLLAKAVANETSATFLRVVGSELIQKYLGDGPK 270
Cdd:cd19518     1 DIGGMDSTLKELCELLIHPILPPEYFQHLGVEPPRGVLLHGPPGCGKTMLANAIAGELKVPFLKISATEIVSGVSGESEE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1098423980 271 LVRELFRVAEENAPSIVFIDEIDAVGTKRHDSQSGGERdiqRTMLELLNQLDGFEARGD----VKVIMATNKIESLDPAL 346
Cdd:cd19518    81 KIRELFDQAISNAPCIVFIDEIDAITPKRESAQREMER---RIVSQLLTCMDELNNEKTaggpVLVIGATNRPDSLDPAL 157

                         170
                  ....*....|..
gi 1098423980 347 IRPGRIDRKIEL 358
Cdd:cd19518   158 RRAGRFDREICL 169
RecA-like_Yta7-like cd19517
ATPase domain of Saccharomyces cerevisiae Yta7 and similar ATPase domains; Saccharomyces ...
 191-355 4.69e-47

ATPase domain of Saccharomyces cerevisiae Yta7 and similar ATPase domains; Saccharomyces cerevisiae Yta7 is a chromatin-associated AAA-ATPase involved in regulation of chromatin dynamics. Its human ortholog ANCCA/ATAD2 transcriptionally activates pathways of malignancy in a broad range of cancers. The RecA-like_Yta7 subfamily belongs to the RecA-like NTPase family which includes the NTP binding domain of F1 and V1 H(+)ATPases, DnaB and related helicases as well as bacterial RecA and related eukaryotic and archaeal recombinases. The RecA-like NTPase family also includes bacterial conjugation proteins and related DNA transfer proteins involved in type II and type IV secretion.


Pssm-ID: 410925 [Multi-domain]  Cd Length: 170  Bit Score: 159.60  E-value: 4.69e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1098423980 191 DIGGLEQQIQEIKEAVEIPLTHPELYDDIGIKPPKGVILYGPPGTGKTLLAKAVANETSA-----TFLRVVGSELIQKYL 265
Cdd:cd19517     1 DIGGLSHYINQLKEMVFFPLLYPEVFAKFKITPPRGVLFHGPPGTGKTLMARALAAECSKggqkvSFFMRKGADCLSKWV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1098423980 266 GDGPKLVRELFRVAEENAPSIVFIDEIDAVGTKRHDSQSGGERDIQRTMLELlnqLDGFEARGDVKVIMATNKIESLDPA 345
Cdd:cd19517    81 GEAERQLRLLFEEAYRMQPSIIFFDEIDGLAPVRSSKQEQIHASIVSTLLAL---MDGLDNRGQVVVIGATNRPDALDPA 157

                         170
                  ....*....|
gi 1098423980 346 LIRPGRIDRK 355
Cdd:cd19517   158 LRRPGRFDRE 167
RecA-like_NVL_r2-like cd19530
second of two ATPase domains of NVL (nuclear VCP-like protein) and similar ATPase domains; NVL ...
 195-354 2.86e-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: 2.86e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1098423980 195 LEQQIQEIKEAVEIPLTHPELYDDIGIKPPKGVILYGPPGTGKTLLAKAVANETSATFLRVVGSELIQKYLGDGPKLVRE 274
Cdd:cd19530     1 LDHVREELTMSILRPIKRPDIYKALGIDLPTGVLLYGPPGCGKTLLAKAVANESGANFISVKGPELLNKYVGESERAVRQ 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1098423980 275 LFRVAEENAPSIVFIDEIDAVGTKRHDSQSGGerdIQRTMLELLNQLDGFEARGDVKVIMATNKIESLDPALIRPGRIDR 354
Cdd:cd19530    81 VFQRARASAPCVIFFDEVDALVPKRGDGGSWA---SERVVNQLLTEMDGLEERSNVFVIAATNRPDIIDPAMLRPGRLDK 157
RecA-like_PEX6_r2 cd19527
second of two ATPase domains of Peroxisomal biogenesis factor 6 (PEX6); PEX6(also known as ...
 201-354 3.31e-43

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: 149.20  E-value: 3.31e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1098423980 201 EIKEAVEIPLTHPELYDDiGIKPPKGVILYGPPGTGKTLLAKAVANETSATFLRVVGSELIQKYLGDGPKLVRELFRVAE 280
Cdd:cd19527     4 EILDTIQLPLEHPELFSS-GLRKRSGILLYGPPGTGKTLLAKAIATECSLNFLSVKGPELINMYIGESEANVREVFQKAR 82

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1098423980 281 ENAPSIVFIDEIDAVGTKRHDS-QSGGERDiqRTMLELLNQLDGFEARG-DVKVIMATNKIESLDPALIRPGRIDR 354
Cdd:cd19527    83 DAKPCVIFFDELDSLAPSRGNSgDSGGVMD--RVVSQLLAELDGMSSSGqDVFVIGATNRPDLLDPALLRPGRFDK 156
RecA-like_VPS4 cd19521
ATPase domain of vacuolar protein sorting-associated protein 4; Vacuolar protein ...
 185-356 2.26e-41

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: 144.62  E-value: 2.26e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1098423980 185 PLESYADIGGLEQQIQEIKEAVEIPLTHPELYDDiGIKPPKGVILYGPPGTGKTLLAKAVANETSATFLRVVGSELIQKY 264
Cdd:cd19521     2 PNVKWEDVAGLEGAKEALKEAVILPVKFPHLFTG-NRKPWSGILLYGPPGTGKSYLAKAVATEANSTFFSVSSSDLVSKW 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1098423980 265 LGDGPKLVRELFRVAEENAPSIVFIDEIDAVGTKRHDSQSGGERDIQRtmlELLNQLDGFEARGD-VKVIMATNKIESLD 343
Cdd:cd19521    81 MGESEKLVKQLFAMARENKPSIIFIDEVDSLCGTRGEGESEASRRIKT---ELLVQMNGVGNDSQgVLVLGATNIPWQLD 157

                         170
                  ....*....|...
gi 1098423980 344 PALIRpgRIDRKI 356
Cdd:cd19521   158 SAIRR--RFEKRI 168
RecA-like_PEX1_r2 cd19526
second of two ATPase domains of Peroxisomal biogenesis factor 1 (PEX1); PEX1(also known as ...
 202-357 4.61e-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: 143.72  E-value: 4.61e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1098423980 202 IKEAVEIPLTHPELYDDIGIKPPKGVILYGPPGTGKTLLAKAVANETSATFLRVVGSELIQKYLGDGPKLVRELFRVAEE 281
Cdd:cd19526     5 LEETIEWPSKYPKIFASSPLRLRSGILLYGPPGCGKTLLASAIASECGLNFISVKGPELLNKYIGASEQNVRDLFSRAQS 84

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1098423980 282 NAPSIVFIDEIDAVGTKR-HDSQsgGERDiqRTMLELLNQLDGFEARGDVKVIMATNKIESLDPALIRPGRIDRKIE 357
Cdd:cd19526    85 AKPCILFFDEFDSIAPKRgHDST--GVTD--RVVNQLLTQLDGVEGLDGVYVLAATSRPDLIDPALLRPGRLDKLVY 157
RecA-like_ATAD1 cd19520
ATPase domain of ATPase family AAA domain-containing protein 1 and similar ATPase domains; ...
 191-348 5.08e-41

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: 143.72  E-value: 5.08e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1098423980 191 DIGGLEQQIQEIKEAVEIPLTHPELYDDIGI-KPPKGVILYGPPGTGKTLLAKAVANETSATFLRVVGSELIQKYLGDGP 269
Cdd:cd19520     1 DIGGLDEVITELKELVILPLQRPELFDNSRLlQPPKGVLLYGPPGCGKTMLAKATAKEAGARFINLQVSSLTDKWYGESQ 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1098423980 270 KLVRELFRVAEENAPSIVFIDEIDAVGTKRhdsqSGGERDIQRTM-LELLNQLDGFEARGDVKVIM--ATNKIESLDPAL 346
Cdd:cd19520    81 KLVAAVFSLASKLQPSIIFIDEIDSFLRQR----SSTDHEATAMMkAEFMSLWDGLSTDGNCRVIVmgATNRPQDLDEAI 156


                  ..
gi 1098423980 347 IR 348
Cdd:cd19520   157 LR 158
RecA-like_spastin cd19524
ATPase domain of spastin; Spastin is an ATP-dependent microtubule-severing protein involved in ...
 191-348 9.68e-41

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: 143.07  E-value: 9.68e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1098423980 191 DIGGLEQQIQEIKEAVEIPLTHPELYddIGIK-PPKGVILYGPPGTGKTLLAKAVANETSATFLRVVGSELIQKYLGDGP 269
Cdd:cd19524     1 DIAGQDLAKQALQEMVILPSLRPELF--TGLRaPARGLLLFGPPGNGKTMLAKAVAAESNATFFNISAASLTSKYVGEGE 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1098423980 270 KLVRELFRVAEENAPSIVFIDEIDAVGTKRHDSQSGGERdiqRTMLELLNQLDGFEARGD--VKVIMATNKIESLDPALI 347
Cdd:cd19524    79 KLVRALFAVARELQPSIIFIDEVDSLLSERSEGEHEASR---RLKTEFLIEFDGVQSNGDdrVLVMGATNRPQELDDAVL 155


                  .
gi 1098423980 348 R 348
Cdd:cd19524   156 R 156
RecA-like_Figl-1 cd19525
ATPase domain of Fidgetin-Like 1 (FIGL-1); FIGL-1 may participate in DNA repair in the nucleus; ...
 181-348 1.43e-38

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: 137.81  E-value: 1.43e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1098423980 181 VDKAPLESYADIGGLEQQIQEIKEAVEIPLTHPELYddIGIK-PPKGVILYGPPGTGKTLLAKAVANETSATFLRVVGSE 259
Cdd:cd19525    13 MDHGPPINWADIAGLEFAKKTIKEIVVWPMLRPDIF--TGLRgPPKGILLFGPPGTGKTLIGKCIASQSGATFFSISASS 90

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1098423980 260 LIQKYLGDGPKLVRELFRVAEENAPSIVFIDEIDAVGTKRHDSQSGGERDIQRtmlELLNQLDGFEARGDVKVIM--ATN 337
Cdd:cd19525    91 LTSKWVGEGEKMVRALFSVARCKQPAVIFIDEIDSLLSQRGEGEHESSRRIKT---EFLVQLDGATTSSEDRILVvgATN 167

                         170
                  ....*....|.
gi 1098423980 338 KIESLDPALIR 348
Cdd:cd19525   168 RPQEIDEAARR 178
RecA-like_KTNA1 cd19522
Katanin p60 ATPase-containing subunit A1; Katanin p60 ATPase-containing subunit A1 (KTNA1) is ...
 191-356 1.34e-37

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: 134.73  E-value: 1.34e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1098423980 191 DIGGLEQQIQEIKEAVEIPLTHPELYDDIGiKPPKGVILYGPPGTGKTLLAKAVANETSATFLRVVGSELIQKYLGDGPK 270
Cdd:cd19522     1 DIADLEEAKKLLEEAVVLPMWMPEFFKGIR-RPWKGVLMVGPPGTGKTLLAKAVATECGTTFFNVSSSTLTSKYRGESEK 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1098423980 271 LVRELFRVAEENAPSIVFIDEIDAVGTKRhdsQSGGERDI-QRTMLELLNQLDGF-------EARGDVKVIMATNKIESL 342
Cdd:cd19522    80 LVRLLFEMARFYAPTTIFIDEIDSICSRR---GTSEEHEAsRRVKSELLVQMDGVggasendDPSKMVMVLAATNFPWDI 156

                         170
                  ....*....|....
gi 1098423980 343 DPALIRpgRIDRKI 356
Cdd:cd19522   157 DEALRR--RLEKRI 168
RecA-like_fidgetin cd19523
ATPase domain of fidgetin; Fidgetin (FIGN) is a ATP-dependent microtubule severing protein. ...
 191-348 1.50e-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: 113.06  E-value: 1.50e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1098423980 191 DIGGLEQQIQEIKEAVEIPLTHPELYDDIgIKPPKGVILYGPPGTGKTLLAKAVANETSATFLRVVGSELIQKYLGDGPK 270
Cdd:cd19523     1 DIAGLGALKAAIKEEVLWPLLRPDAFSGL-LRLPRSILLFGPRGTGKTLLGRCLASQLGATFLRLRGSTLVAKWAGEGEK 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1098423980 271 LVRELFRVAEENAPSIVFIDEIDAVGTKRHDSQSGGerdiQRTMLELLNQLDGFEARGD--VKVIMATNKIESLDPALIR 348
Cdd:cd19523    80 ILQASFLAARCRQPSVLFISDLDALLSSQDDEASPV----GRLQVELLAQLDGVLGSGEdgVLVVCTTSKPEEIDESLRR 155
RecA-like_NSF-SEC18_r1-like cd19504
first of two ATPase domains of NSF and SEC18, and similar ATPase domains; ...
 192-358 1.02e-27

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: 108.35  E-value: 1.02e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1098423980 192 IGGLEQQIQEI-KEAVEIPLTHPELYDDIGIKPPKGVILYGPPGTGKTLLAKAVANETSATFLRVV-GSELIQKYLGDGP 269
Cdd:cd19504     2 IGGLDKEFSDIfRRAFASRVFPPEIVEQLGCKHVKGILLYGPPGTGKTLMARQIGKMLNAREPKIVnGPEILNKYVGESE 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1098423980 270 KLVRELFRVAEENAPS--------IVFIDEIDAVGTKRhdSQSGGERDIQRTML-ELLNQLDGFEARGDVKVIMATNKIE 340
Cdd:cd19504    82 ANIRKLFADAEEEQRRlgansglhIIIFDEIDAICKQR--GSMAGSTGVHDTVVnQLLSKIDGVEQLNNILVIGMTNRKD 159

                         170
                  ....*....|....*...
gi 1098423980 341 SLDPALIRPGRIDRKIEL 358
Cdd:cd19504   160 LIDEALLRPGRLEVQMEI 177
AAA cd00009
The AAA+ (ATPases Associated with a wide variety of cellular Activities) superfamily ...
 193-359 1.56e-27

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


Pssm-ID: 99707 [Multi-domain]  Cd Length: 151  Bit Score: 107.23  E-value: 1.56e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1098423980 193 GGLEQQIQEIKEAVEIPlthpelyddigikPPKGVILYGPPGTGKTLLAKAVANET---SATFLRVVGSELIQKYLG--- 266
Cdd:cd00009     1 VGQEEAIEALREALELP-------------PPKNLLLYGPPGTGKTTLARAIANELfrpGAPFLYLNASDLLEGLVVael 67

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1098423980 267 DGPKLVRELFRVAEENAPSIVFIDEIDAVGtkrhdsqsggeRDIQRTMLELLNQL-DGFEARGDVKVIMATNKIESLDPA 345
Cdd:cd00009    68 FGHFLVRLLFELAEKAKPGVLFIDEIDSLS-----------RGAQNALLRVLETLnDLRIDRENVRVIGATNRPLLGDLD 136

                         170
                  ....*....|....
gi 1098423980 346 LIRPGRIDRKIELP 359
Cdd:cd00009   137 RALYDRLDIRIVIP 150
RecA-like_BCS1 cd19510
Mitochondrial chaperone BCS1; Mitochondrial chaperone BCS1 is necessary for the assembly of ...
 202-358 4.22e-25

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: 100.50  E-value: 4.22e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1098423980 202 IKEAVEIPLTHPELYDDIGIKPPKGVILYGPPGTGKTLLAKAVANETSATFLRVvgsELIQKYLGDgpKLVRELFRVAEE 281
Cdd:cd19510     1 IIDDLKDFIKNEDWYNDRGIPYRRGYLLYGPPGTGKSSFIAALAGELDYDICDL---NLSEVVLTD--DRLNHLLNTAPK 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1098423980 282 NapSIVFIDEIDA--VGTKRHDSQSGGERDIQR-TMLELLNQLDGFEARGDVKVIMATNKIESLDPALIRPGRIDRKIEL 358
Cdd:cd19510    76 Q--SIILLEDIDAafESREHNKKNPSAYGGLSRvTFSGLLNALDGVASSEERIVFMTTNHIERLDPALIRPGRVDMKIYM 153
ycf46 CHL00195
Ycf46; Provisional
 187-430 2.71e-24

Ycf46; Provisional


Pssm-ID: 177094 [Multi-domain]  Cd Length: 489  Bit Score: 105.10  E-value: 2.71e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1098423980 187 ESYADIGGLEQQIQEIKEAVEIPLTHPELYddiGIKPPKGVILYGPPGTGKTLLAKAVANETSATFLRVVGSELIQKYLG 266
Cdd:CHL00195  225 EKISDIGGLDNLKDWLKKRSTSFSKQASNY---GLPTPRGLLLVGIQGTGKSLTAKAIANDWQLPLLRLDVGKLFGGIVG 301

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1098423980 267 DGPKLVRELFRVAEENAPSIVFIDEIDAVGTKRHDS-QSGGERDIQRTMLELLNqldgfEARGDVKVIMATNKIESLDPA 345
Cdd:CHL00195  302 ESESRMRQMIRIAEALSPCILWIDEIDKAFSNSESKgDSGTTNRVLATFITWLS-----EKKSPVFVVATANNIDLLPLE 376

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1098423980 346 LIRPGRIDRKIELPNPDCKTKRRIFQIHTSKMTLS--EDVDLEEFIMAKDDISGADIKAICTEAGLLALRERRmRVTQED 423
Cdd:CHL00195  377 ILRKGRFDEIFFLDLPSLEEREKIFKIHLQKFRPKswKKYDIKKLSKLSNKFSGAEIEQSIIEAMYIAFYEKR-EFTTDD 455


                  ....*..
gi 1098423980 424 LRKAKEK 430
Cdd:CHL00195  456 ILLALKQ 462
RecA-like_Ycf46-like cd19507
ATPase domain of Ycf46 and similar ATPase domains; Ycf46 may play a role in the regulation of ...
 220-354 4.85e-23

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


Pssm-ID: 410915 [Multi-domain]  Cd Length: 161  Bit Score: 95.13  E-value: 4.85e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1098423980 220 GIKPPKGVILYGPPGTGKTLLAKAVANETSATFLRVVGSELIQKYLGDGPKLVRELFRVAEENAPSIVFIDEID-AVGTK 298
Cdd:cd19507    27 GLPTPKGLLLVGIQGTGKSLTAKAIAGVWQLPLLRLDMGRLFGGLVGESESRLRQMIQTAEAIAPCVLWIDEIEkGFSNA 106

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1098423980 299 RHDSQSGGERDIQRTMLELLNqldgfEARGDVKVIMATNKIESLDPALIRPGRIDR 354
Cdd:cd19507   107 DSKGDSGTSSRVLGTFLTWLQ-----EKKKPVFVVATANNVQSLPPELLRKGRFDE 157
AAA smart00382
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ...
 223-362 4.37e-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: 83.58  E-value: 4.37e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1098423980  223 PPKGVILYGPPGTGKTLLAKAVANETSATFLRVV-----------------GSELIQKYLGDGPKLVRELFRVAEENAPS 285
Cdd:smart00382   1 PGEVILIVGPPGSGKTTLARALARELGPPGGGVIyidgedileevldqlllIIVGGKKASGSGELRLRLALALARKLKPD 80

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1098423980  286 IVFIDEIDAVGTKrhdsqsggERDIQRTMLELLNQLDGFEARGDVKVIMATNKIESLDPALIRPgRIDRKIELPNPD 362
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 ...
 227-347 7.22e-16

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: 75.95  E-value: 7.22e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1098423980 227 VILYGPPGTGKTLLAKAVANETS---------ATFLRVVGSELIQKYLGDGPKLVRELFR-----VAEENAPSIVFIDEI 292
Cdd:cd19508    55 VLLHGPPGTGKTSLCKALAQKLSirlssryryGQLIEINSHSLFSKWFSESGKLVTKMFQkiqelIDDKDALVFVLIDEV 134

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1098423980 293 DAVGTKRHDSQSGGE-RDIQRTMLELLNQLDGFEARGDVKVIMATNKIESLDPALI 347
Cdd:cd19508   135 ESLAAARSASSSGTEpSDAIRVVNAVLTQIDRIKRYHNNVILLTSNLLEKIDVAFV 190
Prot_ATP_ID_OB pfam16450
Proteasomal ATPase OB C-terminal domain; This is the interdomain (ID) or oligonucleotide ...
 114-167 6.82e-11

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: 57.52  E-value: 6.82e-11
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1098423980 114 IGTLEEIIDENHAIVSSSVGSEYYVNILSFVDKNQLEPGSSVLLHNKVYSVVGI 167
Cdd:pfam16450   1 VATVVEVLDDGRALVKSSGGEERVVRLAGSLDEEKLRPGDRVLLDPRSGYALEV 54
AAA_lid_3 pfam17862
AAA+ lid domain; This entry represents the alpha helical AAA+ lid domain that is found to the ...
 382-426 1.57e-10

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


Pssm-ID: 465537 [Multi-domain]  Cd Length: 45  Bit Score: 56.01  E-value: 1.57e-10
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 1098423980 382 DVDLEEFIMAKDDISGADIKAICTEAGLLALRERRMRVTQEDLRK 426
Cdd:pfam17862   1 DVDLEELAERTEGFSGADLEALCREAALAALRRGLEAVTQEDLEE 45
RarA COG2256
Replication-associated recombination protein RarA (DNA-dependent ATPase) [Replication, ...
 227-292 6.62e-10

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


Pssm-ID: 441857 [Multi-domain]  Cd Length: 439  Bit Score: 60.84  E-value: 6.62e-10
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1098423980 227 VILYGPPGTGKTLLAKAVANETSATFLRV--VGSeliqkylgdGPKLVRELFRVAEENA----PSIVFIDEI 292
Cdd:COG2256    52 MILWGPPGTGKTTLARLIANATDAEFVALsaVTS---------GVKDIREVIEEARERRaygrRTILFVDEI 114
RecA-like_ATAD3-like cd19512
ATPase domains of ATPase AAA-domain protein 3A (ATAD3A), -3B, and -3C, and similar ATPase ...
 195-357 3.11e-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: 55.61  E-value: 3.11e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1098423980 195 LEQQIQEIKEAVEIPLTHPELYddigikppKGVILYGPPGTGKTLLAKAVANETSATFLRVVGSELIQkyLG-DGPKLVR 273
Cdd:cd19512     1 LEARVRDIAIATRNTKKNKGLY--------RNILFYGPPGTGKTLFAKKLALHSGMDYAIMTGGDVAP--MGrEGVTAIH 70

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1098423980 274 ELFRVAEE-NAPSIVFIDEIDAVGTKRhdSQSGGERDIQRTMLELLNQLDgfEARGDVKVIMATNKIESLDPALirPGRI 352
Cdd:cd19512    71 KVFDWANTsRRGLLLFVDEADAFLRKR--STEKISEDLRAALNAFLYRTG--EQSNKFMLVLASNQPEQFDWAI--NDRI 144


                  ....*
gi 1098423980 353 DRKIE 357
Cdd:cd19512   145 DEMVE 149
PRK13342 PRK13342
recombination factor protein RarA; Reviewed
 227-292 3.16e-09

recombination factor protein RarA; Reviewed


Pssm-ID: 237355 [Multi-domain]  Cd Length: 413  Bit Score: 58.56  E-value: 3.16e-09
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1098423980 227 VILYGPPGTGKTLLAKAVANETSATFLRVVGSEliqkylgDGPKLVRELFRVAEENAPS----IVFIDEI 292
Cdd:PRK13342   39 MILWGPPGTGKTTLARIIAGATDAPFEALSAVT-------SGVKDLREVIEEARQRRSAgrrtILFIDEI 101
TIGR02928 TIGR02928
orc1/cdc6 family replication initiation protein; Members of this protein family are found ...
 223-431 1.14e-08

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: 56.49  E-value: 1.14e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1098423980 223 PPKGVILYGPPGTGKTLLAKAVANE----TSATFLRV---------------VGSELIQKYLGDGP----------KLVR 273
Cdd:TIGR02928  39 RPSNVFIYGKTGTGKTAVTKYVMKEleeaAEDRDVRVvtvyvncqildtlyqVLVELANQLRGSGEevpttglstsEVFR 118

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1098423980 274 ELFRVAEENAPSIVFI-DEIDAVgtKRHDSqsggerdiqrtmlELLNQLDGFEARGD-----VKVIMATNKI---ESLDP 344
Cdd:TIGR02928 119 RLYKELNERGDSLIIVlDEIDYL--VGDDD-------------DLLYQLSRARSNGDldnakVGVIGISNDLkfrENLDP 183

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1098423980 345 AlIRPGRIDRKIELPNPDCKTKRRIFQiHTSKMTLSEDVDLEEFI------MAKDdiSGADIKAICT--EAGLLALRERR 416
Cdd:TIGR02928 184 R-VKSSLCEEEIIFPPYDAEELRDILE-NRAEKAFYDGVLDDGVIplcaalAAQE--HGDARKAIDLlrVAGEIAEREGA 259

                         250
                  ....*....|....*
gi 1098423980 417 MRVTQEDLRKAKEKA 431
Cdd:TIGR02928 260 ERVTEDHVEKAQEKI 274
RecA-like_Ycf2 cd19505
ATPase domain of plant YCF2; Ycf2 is a chloroplast ATPase which has an essential function; ...
 220-356 5.09e-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: 5.09e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1098423980 220 GIKPPKGVILYGPPGTGKTLLAKAVANETSATFLRVVGSELIQKYLGDGPKLVR--------------ELFRVAEENAPS 285
Cdd:cd19505     8 GLSPSKGILLIGSIETGRSYLIKSLAANSYVPLIRISLNKLLYNKPDFGNDDWIdgmlilkeslhrlnLQFELAKAMSPC 87

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1098423980 286 IVFIDEIDAVGTKRHDSQSGGERDiqrTMLELLNQL--DGFEARG--DVKVIMATNKIESLDPALIRPGRIDRKI 356
Cdd:cd19505    88 IIWIPNIHELNVNRSTQNLEEDPK---LLLGLLLNYlsRDFEKSStrNILVIASTHIPQKVDPALIAPNRLDTCI 159
AAA_2 pfam07724
AAA domain (Cdc48 subfamily); This Pfam entry includes some of the AAA proteins not detected ...
 224-318 1.00e-07

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: 51.43  E-value: 1.00e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1098423980 224 PKGVILY-GPPGTGKTLLAKAVANE---TSATFLRVVGSELIQKYL-----GDGPKLVR-----ELFRVAEENAPSIVFI 289
Cdd:pfam07724   2 PIGSFLFlGPTGVGKTELAKALAELlfgDERALIRIDMSEYMEEHSvsrliGAPPGYVGyeeggQLTEAVRRKPYSIVLI 81

                          90       100
                  ....*....|....*....|....*....
gi 1098423980 290 DEIDavgtKRHdsqsggeRDIQRTMLELL 318
Cdd:pfam07724  82 DEIE----KAH-------PGVQNDLLQIL 99
AAA_5 pfam07728
AAA domain (dynein-related subfamily); This Pfam entry includes some of the AAA proteins not ...
 226-348 1.32e-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: 50.37  E-value: 1.32e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1098423980 226 GVILYGPPGTGKTLLAKAVANETS-ATFLRVVGS------ELIQKYL--GDGPKLV-RELFRVAEEnaPSIVFIDEIDAv 295
Cdd:pfam07728   1 GVLLVGPPGTGKTELAERLAAALSnRPVFYVQLTrdtteeDLFGRRNidPGGASWVdGPLVRAARE--GEIAVLDEINR- 77

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1098423980 296 gtkrhdsqsgGERDIQRTMLELLN-----QLDGFE----ARGDVKVIMATN----KIESLDPALIR 348
Cdd:pfam07728  78 ----------ANPDVLNSLLSLLDerrllLPDGGElvkaAPDGFRLIATMNpldrGLNELSPALRS 133
CDC6 COG1474
Cdc6-related protein, AAA superfamily ATPase [Replication, recombination and repair];
196-431 1.78e-07

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


Pssm-ID: 441083 [Multi-domain]  Cd Length: 389  Bit Score: 52.93  E-value: 1.78e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1098423980 196 EQQIQEIKEAVEiPLTHPElyddigikPPKGVILYGPPGTGKTLLAKAVANE---------TSATFLRV----------V 256
Cdd:COG1474    32 EEEIEELASALR-PALRGE--------RPSNVLIYGPTGTGKTAVAKYVLEEleeeaeergVDVRVVYVncrqastryrV 102

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1098423980 257 GSELIQKyLGDGPKLVR------ELF-----RVAEENAPSIVFIDEIDAVGTKRHDsqsggerDIQRTMLELLNQLDGfe 325
Cdd:COG1474   103 LSRILEE-LGSGEDIPStglstdELFdrlyeALDERDGVLVVVLDEIDYLVDDEGD-------DLLYQLLRANEELEG-- 172

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1098423980 326 arGDVKVIMATNKI---ESLDPALIRPGRiDRKIELPNPDcktKRRIFQI--HTSKMTLSEDV---DLEEFImAkdDISG 397
Cdd:COG1474   173 --ARVGVIGISNDLeflENLDPRVKSSLG-EEEIVFPPYD---ADELRDIleDRAELAFYDGVlsdEVIPLI-A--ALAA 243

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|
gi 1098423980 398 ADI----KAICT--EAGLLALRERRMRVTQEDLRKAKEKA 431
Cdd:COG1474   244 QEHgdarKAIDLlrVAGEIAEREGSDRVTEEHVREAREKI 283
DUF815 pfam05673
Protein of unknown function (DUF815); This family consists of several bacterial proteins of ...
 175-290 3.86e-07

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: 51.00  E-value: 3.86e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1098423980 175 LVSVMKVDKAPLEsyaDIGGLEQQIQEIKEAVEIPLTHpelyddigiKPPKGVILYGPPGTGKTLLAKAVANETSATFLR 254
Cdd:pfam05673  16 LEPVPHPDPVRLD---DLVGIERQKEALIRNTRRFLAG---------LPANNVLLWGARGTGKSSLVKALLNEYADQGLR 83

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 1098423980 255 VVgsELIQKYLGDGPKLVRELfrvAEENAPSIVFID 290
Cdd:pfam05673  84 LI--EVDKEDLGDLPDLVDLL---RDRPYRFILFCD 114
RecA-like_HslU cd19498
ATP-dependent protease ATPase subunit HslU; HslU is a component of the ATP-dependent protease ...
 200-310 4.76e-07

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: 49.69  E-value: 4.76e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1098423980 200 QEIKEAVEIPLTH--------PELYDDIgikPPKGVILYGPPGTGKTLLAKAVANETSATFLRVVGSELIQ-KYLG-DGP 269
Cdd:cd19498    17 DEAKRAVAIALRNrwrrmqlpEELRDEV---TPKNILMIGPTGVGKTEIARRLAKLAGAPFIKVEATKFTEvGYVGrDVE 93

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 1098423980 270 KLVRELfrvaeenAPSIVFIDEIDAV----GTKRHD-SQSGGERDI 310
Cdd:cd19498    94 SIIRDL-------VEGIVFIDEIDKIakrgGSSGPDvSREGVQRDL 132
MoxR COG0714
MoxR-like ATPase [General function prediction only]; MoxR-like ATPase is part of the Pathway ...
 227-293 2.52e-06

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


Pssm-ID: 440478 [Multi-domain]  Cd Length: 292  Bit Score: 49.01  E-value: 2.52e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1098423980 227 VILYGPPGTGKTLLAKAVANETSATFLRV-----------VGSELIQKYLGD-----GPklvreLFRvaeenapSIVFID 290
Cdd:COG0714    34 LLLEGVPGVGKTTLAKALARALGLPFIRIqftpdllpsdiLGTYIYDQQTGEfefrpGP-----LFA-------NVLLAD 101


                  ...
gi 1098423980 291 EID 293
Cdd:COG0714   102 EIN 104
ruvB PRK00080
Holliday junction branch migration DNA helicase RuvB;
227-292 3.71e-06

Holliday junction branch migration DNA helicase RuvB;


Pssm-ID: 234619 [Multi-domain]  Cd Length: 328  Bit Score: 48.59  E-value: 3.71e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1098423980 227 VILYGPPGTGKTLLAKAVANETSATfLRVVGSELIQKyLGDgpkLVReLFRVAEENapSIVFIDEI 292
Cdd:PRK00080   54 VLLYGPPGLGKTTLANIIANEMGVN-IRITSGPALEK-PGD---LAA-ILTNLEEG--DVLFIDEI 111
RecA-like_ClpB_Hsp104-like cd19499
Chaperone protein ClpB/Hsp104 subfamily; Bacterial Caseinolytic peptidase B (ClpB) and ...
 222-356 7.45e-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: 46.02  E-value: 7.45e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1098423980 222 KPPKGVILYGPPGTGKTLLAKAVA---NETSATFLRVVGSELIQKY-----LGDGPKLV--RELFRVAEE---NAPSIVF 288
Cdd:cd19499    39 RPIGSFLFLGPTGVGKTELAKALAellFGDEDNLIRIDMSEYMEKHsvsrlIGAPPGYVgyTEGGQLTEAvrrKPYSVVL 118

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1098423980 289 IDEIDavgtKRHdsqsggeRDIQRTMLELLNqlDGF--EARG---DVK---VIMATNkieSLDPALIrpGRIDRKI 356
Cdd:cd19499   119 LDEIE----KAH-------PDVQNLLLQVLD--DGRltDSHGrtvDFKntiIIMTSN---HFRPEFL--NRIDEIV 176
PRK04195 PRK04195
replication factor C large subunit; Provisional
 222-247 1.33e-05

replication factor C large subunit; Provisional


Pssm-ID: 235250 [Multi-domain]  Cd Length: 482  Bit Score: 47.22  E-value: 1.33e-05
                          10        20
                  ....*....|....*....|....*.
gi 1098423980 222 KPPKGVILYGPPGTGKTLLAKAVANE 247
Cdd:PRK04195   37 KPKKALLLYGPPGVGKTSLAHALAND 62
McrB COG1401
5-methylcytosine-specific restriction endonuclease McrBC, GTP-binding regulatory subunit McrB ...
 181-292 1.50e-05

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


Pssm-ID: 441011 [Multi-domain]  Cd Length: 477  Bit Score: 47.07  E-value: 1.50e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1098423980 181 VDKAPLESYADIGGLEQQIQEIKEAVEIPLTHPELYDDIG-------------IKPPKGVILYGPPGTGKTLLAKAVANE 247
Cdd:COG1401   165 LLAAPEDLSADALAAELSAAEELYSEDLESEDDYLKDLLRekfeetleaflaaLKTKKNVILAGPPGTGKTYLARRLAEA 244

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1098423980 248 TSAT----FLRVV------GSELIQKY---LGDG-----PKLVRELFRVAEEN--APSIVFIDEI 292
Cdd:COG1401   245 LGGEdngrIEFVQfhpswsYEDFLLGYrpsLDEGkyeptPGIFLRFCLKAEKNpdKPYVLIIDEI 309
PRK13341 PRK13341
AAA family ATPase;
228-292 1.70e-05

AAA family ATPase;


Pssm-ID: 237354 [Multi-domain]  Cd Length: 725  Bit Score: 47.36  E-value: 1.70e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1098423980 228 ILYGPPGTGKTLLAKAVANETSATFLrVVGSELiqkylgDGPKLVRELFRVAEE-----NAPSIVFIDEI 292
Cdd:PRK13341   56 ILYGPPGVGKTTLARIIANHTRAHFS-SLNAVL------AGVKDLRAEVDRAKErlerhGKRTILFIDEV 118
RecA-like_Lon cd19500
lon protease homolog 2 peroxisomal; Lon protease (also known as Lon peptidase) is an ...
 225-318 2.28e-05

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: 44.86  E-value: 2.28e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1098423980 225 KGVIL--YGPPGTGKTLLAKAVANETSATFLRV-VG-----SELI---QKYLGDGPKLVRELFRVAEENAPSIVfIDEID 293
Cdd:cd19500    36 KGPILclVGPPGVGKTSLGKSIARALGRKFVRIsLGgvrdeAEIRghrRTYVGAMPGRIIQALKKAGTNNPVFL-LDEID 114

                          90       100
                  ....*....|....*....|....*
gi 1098423980 294 AVGTKRHDSQSGGerdiqrtMLELL 318
Cdd:cd19500   115 KIGSSFRGDPASA-------LLEVL 132
RuvB_N pfam05496
Holliday junction DNA helicase RuvB P-loop domain; The RuvB protein makes up part of the ...
 227-292 3.47e-05

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: 44.03  E-value: 3.47e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1098423980 227 VILYGPPGTGKTLLAKAVANETSATFlRVVGSELIQKyLGDGPKLVRELfrvaEENapSIVFIDEI 292
Cdd:pfam05496  36 VLLYGPPGLGKTTLANIIANEMGVNI-RITSGPAIER-PGDLAAILTNL----EPG--DVLFIDEI 93
44 PHA02544
clamp loader, small subunit; Provisional
 228-346 4.05e-05

clamp loader, small subunit; Provisional


Pssm-ID: 222866 [Multi-domain]  Cd Length: 316  Bit Score: 45.37  E-value: 4.05e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1098423980 228 ILYGP-PGTGKTLLAKAVANETSATFLRVVGSEliqkylgDGPKLVR-ELFRVAE----ENAPSIVFIDEIDAVGTkrHD 301
Cdd:PHA02544   46 LLHSPsPGTGKTTVAKALCNEVGAEVLFVNGSD-------CRIDFVRnRLTRFAStvslTGGGKVIIIDEFDRLGL--AD 116

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 1098423980 302 SQsggerDIQRTMLEllnqldgfEARGDVKVIMATNKIESLDPAL 346
Cdd:PHA02544  117 AQ-----RHLRSFME--------AYSKNCSFIITANNKNGIIEPL 148
AAA_16 pfam13191
AAA ATPase domain; This family of domains contain a P-loop motif that is characteriztic of the ...
 194-345 4.07e-05

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: 44.03  E-value: 4.07e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1098423980 194 GLEQQIQEIKEAveiplthpelYDDIGIKPPKGVILYGPPGTGKTLLAKAV---ANETSATFLRVVGSELIQkYLGDGPK 270
Cdd:pfam13191   4 GREEELEQLLDA----------LDRVRSGRPPSVLLTGEAGTGKTTLLRELlraLERDGGYFLRGKCDENLP-YSPLLEA 72

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1098423980 271 LVRELFRVAEENAPSIVFIDEIDAVGTKRHDSQSGGERDIQRTMLELLNQLDGFEARGDVKVIMATNKIESLDPA 345
Cdd:pfam13191  73 LTREGLLRQLLDELESSLLEAWRAALLEALAPVPELPGDLAERLLDLLLRLLDLLARGERPLVLVLDDLQWADEA 147
DnaC COG1484
DNA replication protein DnaC [Replication, recombination and repair];
221-275 6.46e-05

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


Pssm-ID: 441093 [Multi-domain]  Cd Length: 242  Bit Score: 44.39  E-value: 6.46e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1098423980 221 IKPPKGVILYGPPGTGKTLLAKAVANE-----TSATFLRVvgseliqkylgdgPKLVREL 275
Cdd:COG1484    96 IERGENLILLGPPGTGKTHLAIALGHEacragYRVRFTTA-------------PDLVNEL 142
RecA-like_superfamily cd01120
RecA-like_NTPases; RecA-like NTPases. This superfamily includes the NTP binding domain of F1 ...
 227-321 1.08e-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: 1.08e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1098423980 227 VILYGPPGTGKTLLAKAVANETSATFLRVVGSELIQKYLgdgpklvRELFRVAEENAPSIVFIDEIDAVGTKRHDSQSGG 306
Cdd:cd01120     1 ILITGPPGSGKTTLLLQFAEQALLSDEPVIFISFLDTIL-------EAIEDLIEEKKLDIIIIDSLSSLARASQGDRSSE 73

                          90
                  ....*....|....*
gi 1098423980 307 ERDIQRTMLELLNQL 321
Cdd:cd01120    74 LLEDLAKLLRAARNT 88
T7SS_EccA TIGR03922
type VII secretion AAA-ATPase EccA; This model represents the AAA family ATPase, EccA, of the ...
 183-359 1.31e-04

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


Pssm-ID: 188437 [Multi-domain]  Cd Length: 557  Bit Score: 44.45  E-value: 1.31e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1098423980 183 KAPLESYADIGGLEQQIQEIKEAVEIPLTHPELyddiGIKPP---KGVILYGPPGTGKTLLAKAVANETSA-TFLR---- 254
Cdd:TIGR03922 272 EAELAEQIGLERVKRQVAALKSSTAMALARAER----GLPVAqtsNHMLFAGPPGTGKTTIARVVAKIYCGlGVLRkplv 347

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1098423980 255 --VVGSELIQKYLGDGPKLVRELFrvaEENAPSIVFIDEIDAVgtkrHDSQSGGERDIQrtmLELLNQ-LDGFEA-RGDV 330
Cdd:TIGR03922 348 reVSRADLIGQYIGESEAKTNEII---DSALGGVLFLDEAYTL----VETGYGQKDPFG---LEAIDTlLARMENdRDRL 417

                         170       180       190
                  ....*....|....*....|....*....|....
gi 1098423980 331 KVIMA-----TNKIESLDPALirPGRIDRKIELP 359
Cdd:TIGR03922 418 VVIGAgyrkdLDKFLEVNEGL--RSRFTRVIEFP 449
RecA-like_IQCA1 cd19506
ATPase domain of IQ and AAA domain-containing protein 1 (IQCA1); IQCA1 (also known as dynein ...
 225-291 2.05e-04

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


Pssm-ID: 410914 [Multi-domain]  Cd Length: 160  Bit Score: 41.74  E-value: 2.05e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1098423980 225 KGVILYGPPGTGKTLLAKAVANETSATFLRVVGSELIQKYLGDG--PKLVRELFRVAEENAPSIVFIDE 291
Cdd:cd19506    27 KSLLLAGPSGVGKKMLVHAICTETGANLFNLSPSNIAGKYPGKNglQMMLHLVLKVARQLQPSVIWIGD 95
IS21_help_AAA NF038214
IS21-like element helper ATPase IstB; This protein family model resembles PF01695, but was ...
 227-292 3.48e-04

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: 42.07  E-value: 3.48e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1098423980 227 VILYGPPGTGKTLLAKAVANE-----TSATFLRVvgSELIQKYL---GDGpKLVRELFRVAeenAPSIVFIDEI 292
Cdd:NF038214   93 VLLLGPPGTGKTHLAIALGYAacrqgYRVRFTTA--ADLVEQLAqarADG-RLGRLLRRLA---RYDLLIIDEL 160
COG0645 COG0645
Predicted kinase, contains AAA domain [General function prediction only];
227-301 3.69e-04

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


Pssm-ID: 440410 [Multi-domain]  Cd Length: 164  Bit Score: 41.05  E-value: 3.69e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1098423980 227 VILYGPPGTGKTLLAKAVANETSATFLR--VVGSEL-------IQKYLGDGPKLVRELFRVAEENA---PSIVfideIDA 294
Cdd:COG0645     2 ILVCGLPGSGKSTLARALAERLGAVRLRsdVVRKRLfgaglapLERSPEATARTYARLLALARELLaagRSVI----LDA 77


                  ....*..
gi 1098423980 295 VGTKRHD 301
Cdd:COG0645    78 TFLRRAQ 84
RecA-like_ClpX cd19497
ATP-dependent Clp protease ATP-binding subunit ClpX; ClpX is a component of the ATP-dependent ...
 210-318 3.74e-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: 41.82  E-value: 3.74e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1098423980 210 LTHPELYDDIGIKPPKG-VILYGPPGTGKTLLAK----------AVANETSATFLRVVG-------SELIQKYLGDGPKl 271
Cdd:cd19497    35 IRNNLKQKDDDVELEKSnILLIGPTGSGKTLLAQtlakildvpfAIADATTLTEAGYVGedvenilLKLLQAADYDVER- 113

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1098423980 272 vrelfrvAEEnapSIVFIDEIDAVGTKrHDSQSgGERD-----IQRTMLELL 318
Cdd:cd19497   114 -------AQR---GIVYIDEIDKIARK-SENPS-ITRDvsgegVQQALLKIL 153
ruvB TIGR00635
Holliday junction DNA helicase, RuvB subunit; All proteins in this family for which functions ...
 227-296 4.75e-04

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: 41.90  E-value: 4.75e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1098423980 227 VILYGPPGTGKTLLAKAVANETSaTFLRVVGSELIQKYlGDGPKLVRELfrvaeeNAPSIVFIDEIDAVG 296
Cdd:TIGR00635  33 LLLYGPPGLGKTTLAHIIANEMG-VNLKITSGPALEKP-GDLAAILTNL------EEGDVLFIDEIHRLS 94
COG2842 COG2842
Bacteriophage DNA transposition protein, AAA+ family ATPase [Mobilome: prophages, transposons]; ...
 227-293 4.87e-04

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


Pssm-ID: 442090 [Multi-domain]  Cd Length: 254  Bit Score: 41.48  E-value: 4.87e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1098423980 227 VILYGPPGTGKTLLAKAVANE-------------TSATFLRVVGSELiqkYLGDGPKLVRELFRVAEE---NAPSIVFID 290
Cdd:COG2842    53 GVVYGESGVGKTTAAREYANRnpnviyvtaspswTSKELLEELAEEL---GIPAPPGTIADLRDRILErlaGTGRLLIID 129


                  ...
gi 1098423980 291 EID 293
Cdd:COG2842   130 EAD 132
PRK08116 PRK08116
hypothetical protein; Validated
 226-299 6.63e-04

hypothetical protein; Validated


Pssm-ID: 236153 [Multi-domain]  Cd Length: 268  Bit Score: 41.16  E-value: 6.63e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1098423980 226 GVILYGPPGTGKTLLAKAVANETSATFLRVVG---SEL---IQKYLGDGPKLVRELFRVAEENAPSIVfideIDAVGTKR 299
Cdd:PRK08116  116 GLLLWGSVGTGKTYLAACIANELIEKGVPVIFvnfPQLlnrIKSTYKSSGKEDENEIIRSLVNADLLI----LDDLGAER 191
AAA_22 pfam13401
AAA domain;
227-335 8.33e-04

AAA domain;


Pssm-ID: 379165 [Multi-domain]  Cd Length: 129  Bit Score: 39.25  E-value: 8.33e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1098423980 227 VILYGPPGTGKTLLAKAVANE-----------------TSATFLRVVGSELIQKylGDGPKLVRELFR-----VAEENAP 284
Cdd:pfam13401   8 LVLTGESGTGKTTLLRRLLEQlpevrdsvvfvdlpsgtSPKDLLRALLRALGLP--LSGRLSKEELLAalqqlLLALAVA 85

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1098423980 285 SIVFIDEIDAvgtkrhdsqsggerdIQRTMLELLNQLDGFeARGDVKVIMA 335
Cdd:pfam13401  86 VVLIIDEAQH---------------LSLEALEELRDLLNL-SSKLLQLILV 120
cdc6 PRK00411
ORC1-type DNA replication protein;
196-433 1.81e-03

ORC1-type DNA replication protein;


Pssm-ID: 234751 [Multi-domain]  Cd Length: 394  Bit Score: 40.22  E-value: 1.81e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1098423980 196 EQQIQEIKEAVEiPLTHpelyddiGIKPPKgVILYGPPGTGKTLLAKAVANETSATFLRV---------------VGSEL 260
Cdd:PRK00411   36 EEQIEELAFALR-PALR-------GSRPLN-VLIYGPPGTGKTTTVKKVFEELEEIAVKVvyvyincqidrtryaIFSEI 106

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1098423980 261 IQKYLGDGPKLV----RELF-----RVAEENAPSIVFIDEIDAVGTKRHDsqsggerDIQRTMLELLNQLDGfeARGDVK 331
Cdd:PRK00411  107 ARQLFGHPPPSSglsfDELFdkiaeYLDERDRVLIVALDDINYLFEKEGN-------DVLYSLLRAHEEYPG--ARIGVI 177

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1098423980 332 VIMA-TNKIESLDP---ALIRPgridRKIELPnPdcKTKRRIFQIHTS--KMTLSEDV---DLEEFIMAKDDISGADI-K 401
Cdd:PRK00411  178 GISSdLTFLYILDPrvkSVFRP----EEIYFP-P--YTADEIFDILKDrvEEGFYPGVvddEVLDLIADLTAREHGDArV 250

                         250       260       270
                  ....*....|....*....|....*....|....
gi 1098423980 402 AICT--EAGLLALRERRMRVTQEDLRKAKEKALY 433
Cdd:PRK00411  251 AIDLlrRAGLIAEREGSRKVTEEDVRKAYEKSEI 284
ExeA COG3267
Type II secretory pathway ATPase component GspA/ExeA/MshM [Intracellular trafficking, ...
 220-291 1.89e-03

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


Pssm-ID: 442498 [Multi-domain]  Cd Length: 261  Bit Score: 39.77  E-value: 1.89e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1098423980 220 GIKPPKGVI-LYGPPGTGKTLLAKAVANE---------------TSATFLRVVGSELIQKYLGDGPK-----LVRELFRV 278
Cdd:COG3267    38 ALAQGGGFVvLTGEVGTGKTTLLRRLLERlpddvkvayipnpqlSPAELLRAIADELGLEPKGASKAdllrqLQEFLLEL 117

                          90
                  ....*....|...
gi 1098423980 279 AEENAPSIVFIDE 291
Cdd:COG3267   118 AAAGRRVVLIIDE 130
ycf2 CHL00206
Ycf2; Provisional
 219-323 2.41e-03

Ycf2; Provisional


Pssm-ID: 214396 [Multi-domain]  Cd Length: 2281  Bit Score: 40.66  E-value: 2.41e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1098423980  219 IGIKPPKGVILYGPPGTGKTLLAKAVANETSATFLRVvgseLIQKYLGDGPKLvrelfrvaeenapsiVFIDEIDAVGTK 298
Cdd:CHL00206  1625 LALSPSRGILVIGSIGTGRSYLVKYLATNSYVPFITV----FLNKFLDNKPKG---------------FLIDDIDIDDSD 1685

                           90       100
                   ....*....|....*....|....*
gi 1098423980  299 RHDSQSGGERDIQRTMLELLNQLDG 323
Cdd:CHL00206  1686 DIDDSDDIDRDLDTELLTMMNALTM 1710
recomb_radB TIGR02237
DNA repair and recombination protein RadB; This family consists exclusively of archaeal RadB ...
 225-349 3.82e-03

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: 38.55  E-value: 3.82e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1098423980 225 KGVI--LYGPPGTGKTLLAKAVANETSATFLRVV-------GSELIQKYLGDGPKLV-------------------RELF 276
Cdd:TIGR02237  11 RGTItqIYGPPGSGKTNICMILAVNAARQGKKVVyidteglSPERFKQIAEDRPERAlsnfivfevfdfdeqgvaiQKTS 90

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1098423980 277 RVAEENAPSIVFIDEIDAVgtkrhdSQSGGERDIQRTMLELLNQ---LDGFEARGDVKVIMaTNKI-ESLDPALIRP 349
Cdd:TIGR02237  91 KFIDRDSASLVVVDSFTAL------YRLELSDDRISRNRELARQltlLLSLARKKNLAVVI-TNQVyTDVNNGTLRP 160
RNA_helicase pfam00910
RNA helicase; This family includes RNA helicases thought to be involved in duplex unwinding ...
 227-258 4.30e-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: 4.30e-03
                          10        20        30
                  ....*....|....*....|....*....|..
gi 1098423980 227 VILYGPPGTGKTLLAKAVANETSATFLRVVGS 258
Cdd:pfam00910   1 IWLYGPPGCGKSTLAKYLARALLKKLGLPKDS 32
RuvB COG2255
Holliday junction resolvasome RuvABC, ATP-dependent DNA helicase subunit RuvB [Replication, ...
 227-292 4.39e-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: 4.39e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1098423980 227 VILYGPPGTGKTLLAKAVANETSATfLRVVGSELIQKyLGDGPKLVRELfrvaEENapSIVFIDEI 292
Cdd:COG2255    57 VLLYGPPGLGKTTLAHIIANEMGVN-IRITSGPAIEK-PGDLAAILTNL----EEG--DVLFIDEI 114
TIP49 pfam06068
TIP49 P-loop domain; This family consists of the C-terminal region of several eukaryotic and ...
 225-260 5.43e-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: 38.83  E-value: 5.43e-03
                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 1098423980 225 KGVILYGPPGTGKTLLAKAVANE--TSATFLRVVGSEL 260
Cdd:pfam06068  51 RAVLIAGPPGTGKTALAIAISKElgEDTPFTSISGSEV 88
TIP49 COG1224
DNA helicase TIP49, TBP-interacting protein [Transcription];
225-260 5.95e-03

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


Pssm-ID: 440837 [Multi-domain]  Cd Length: 452  Bit Score: 38.80  E-value: 5.95e-03
                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 1098423980 225 KGVILYGPPGTGKTLLAKAVANETSA--TFLRVVGSEL 260
Cdd:COG1224    65 KGILIVGPPGTGKTALAVAIARELGEdtPFVAISGSEI 102
NACHT pfam05729
NACHT domain; This NTPase domain is found in apoptosis proteins as well as those involved in ...
 227-319 7.38e-03

NACHT domain; This NTPase domain is found in apoptosis proteins as well as those involved in MHC transcription activation. This family is closely related to pfam00931.


Pssm-ID: 428606 [Multi-domain]  Cd Length: 166  Bit Score: 37.28  E-value: 7.38e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1098423980 227 VILYGPPGTGKTLLAKAVA---------NETSATFLRVVGS-----------ELIQKYLGDGPKLVRELFRVAEENAPSI 286
Cdd:pfam05729   3 VILQGEAGSGKTTLLQKLAllwaqgklpQGFDFVFFLPCRElsrsgnarslaDLLFSQWPEPAAPVSEVWAVILELPERL 82

                          90       100       110
                  ....*....|....*....|....*....|....
gi 1098423980 287 VFI-DEIDavGTKRHDSQSGGERDIQRTMLELLN 319
Cdd:pfam05729  83 LLIlDGLD--ELVSDLGQLDGPCPVLTLLSSLLR 114
IstB_IS21 pfam01695
IstB-like ATP binding protein; This protein contains an ATP/GTP binding P-loop motif. It is ...
 227-292 9.20e-03

IstB-like ATP binding protein; This protein contains an ATP/GTP binding P-loop motif. It is found associated with IS21 family insertion sequences. The function of this protein is unknown, but it may perform a transposase function.


Pssm-ID: 426385 [Multi-domain]  Cd Length: 238  Bit Score: 37.81  E-value: 9.20e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1098423980 227 VILYGPPGTGKTLLAKAVANET-----SATFLRVVG-SELIQKYLGDGpKLVRELFRVAeenAPSIVFIDEI 292
Cdd:pfam01695  95 VVLLGPPGVGKTHLAIALGVEAcragySVRFTSAADlVNQLKRAHGDG-KLTRKLQQLL---KPDVLILDEW 162
Prot_ATP_OB_N pfam17758
Proteasomal ATPase OB N-terminal domain; This is N-terminal oligonucleotide binding (OB) ...
 114-166 9.74e-03

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


Pssm-ID: 436018  Cd Length: 62  Bit Score: 34.45  E-value: 9.74e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1098423980 114 IGTLEEIIDENHAIVSSSVGSEYYVNILSFVDKNQLEPGSSVLLhNKVYSVVG 166
Cdd:pfam17758   2 YGTFLRVDDDDGTADVSVGGRRMRVAVSPTVDASELRPGQQVRL-NEALVVVG 53
 
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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