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Conserved domains on  [gi|6679501|ref|NP_032973|]
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26S proteasome regulatory subunit 4 [Mus musculus]

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
 1-440 0e+00

26 proteosome regulatory subunit 4-like protein; Provisional


:

Pssm-ID: 185575 [Multi-domain]  Cd Length: 438  Bit Score: 791.28  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6679501     1 MGQSQSGGHGPGGGKKDDKDKKkkYEPPVPTRVGKKKKKTKGPDAASKLPLVTPHTQCRLKLLKLERIKDYLLMEEEFIR 80
Cdd:PTZ00361   1 MGNAQGQGNNQKDKNKKKEKKK--KESPPPPHEIKRKKKRKGPDAASKLPKVTPNTKCRLRLLKLERIKDYLLLEEEFIT 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6679501    81 NQEQMKPLEEKQEEERSKVDDLRGTPMSVGTLEEIIDDNHAIVSTSVGSEHYVSILSFVDKDLLEPGCSVLLNHKVHAVI 160
Cdd:PTZ00361  79 NQEAQKPAQEKNEAELKKVDDLRGSPLSVGTLEEIIDENHAIVSSSVGPEYYVNILSFVDKEQLEPGCSVLLHNKTHSVV 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6679501   161 GVLMDDTDPLVTVMKVEKAPQETYADIGGLDNQIQEIKESVELPLTHPEYYEEMGIKPPKGVILYGPPGTGKTLLAKAVA 240
Cdd:PTZ00361 159 GILLDEVDPLVSVMKVDKAPLESYADIGGLEQQIQEIKEAVELPLTHPELYDDIGIKPPKGVILYGPPGTGKTLLAKAVA 238

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6679501   241 NQTSATFLRVVGSELIQKYLGDGPKLVRELFRVAEEHAPSIVFIDEIDAIGTKRYDSNSGGEREIQRTMLELLNQLDGFD 320
Cdd:PTZ00361 239 NETSATFLRVVGSELIQKYLGDGPKLVRELFRVAEENAPSIVFIDEIDAIGTKRYDATSGGEKEIQRTMLELLNQLDGFD 318

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6679501   321 SRGDVKVIMATNRIETLDPALIRPGRIDRKIEFPLPDEKTKKRIFQIHTSRMTLADDVTLDDLIMAKDDLSGADIKAICT 400
Cdd:PTZ00361 319 SRGDVKVIMATNRIESLDPALIRPGRIDRKIEFPNPDEKTKRRIFEIHTSKMTLAEDVDLEEFIMAKDELSGADIKAICT 398

                        410       420       430       440
                 ....*....|....*....|....*....|....*....|
gi 6679501   401 EAGLMALRERRMKVTNEDFKKSKENVLYKKQEGTPEGLYL 440
Cdd:PTZ00361 399 EAGLLALRERRMKVTQADFRKAKEKVLYRKKGNIPEGLYL 438
 
Name Accession Description Interval E-value
PTZ00361 PTZ00361
26 proteosome regulatory subunit 4-like protein; Provisional
 1-440 0e+00

26 proteosome regulatory subunit 4-like protein; Provisional


Pssm-ID: 185575 [Multi-domain]  Cd Length: 438  Bit Score: 791.28  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6679501     1 MGQSQSGGHGPGGGKKDDKDKKkkYEPPVPTRVGKKKKKTKGPDAASKLPLVTPHTQCRLKLLKLERIKDYLLMEEEFIR 80
Cdd:PTZ00361   1 MGNAQGQGNNQKDKNKKKEKKK--KESPPPPHEIKRKKKRKGPDAASKLPKVTPNTKCRLRLLKLERIKDYLLLEEEFIT 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6679501    81 NQEQMKPLEEKQEEERSKVDDLRGTPMSVGTLEEIIDDNHAIVSTSVGSEHYVSILSFVDKDLLEPGCSVLLNHKVHAVI 160
Cdd:PTZ00361  79 NQEAQKPAQEKNEAELKKVDDLRGSPLSVGTLEEIIDENHAIVSSSVGPEYYVNILSFVDKEQLEPGCSVLLHNKTHSVV 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6679501   161 GVLMDDTDPLVTVMKVEKAPQETYADIGGLDNQIQEIKESVELPLTHPEYYEEMGIKPPKGVILYGPPGTGKTLLAKAVA 240
Cdd:PTZ00361 159 GILLDEVDPLVSVMKVDKAPLESYADIGGLEQQIQEIKEAVELPLTHPELYDDIGIKPPKGVILYGPPGTGKTLLAKAVA 238

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6679501   241 NQTSATFLRVVGSELIQKYLGDGPKLVRELFRVAEEHAPSIVFIDEIDAIGTKRYDSNSGGEREIQRTMLELLNQLDGFD 320
Cdd:PTZ00361 239 NETSATFLRVVGSELIQKYLGDGPKLVRELFRVAEENAPSIVFIDEIDAIGTKRYDATSGGEKEIQRTMLELLNQLDGFD 318

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6679501   321 SRGDVKVIMATNRIETLDPALIRPGRIDRKIEFPLPDEKTKKRIFQIHTSRMTLADDVTLDDLIMAKDDLSGADIKAICT 400
Cdd:PTZ00361 319 SRGDVKVIMATNRIESLDPALIRPGRIDRKIEFPNPDEKTKRRIFEIHTSKMTLAEDVDLEEFIMAKDELSGADIKAICT 398

                        410       420       430       440
                 ....*....|....*....|....*....|....*....|
gi 6679501   401 EAGLMALRERRMKVTNEDFKKSKENVLYKKQEGTPEGLYL 440
Cdd:PTZ00361 399 EAGLLALRERRMKVTQADFRKAKEKVLYRKKGNIPEGLYL 438
26Sp45 TIGR01242
26S proteasome subunit P45 family; Many proteins may score above the trusted cutoff because an ...
 55-427 1.06e-152

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: 437.31  E-value: 1.06e-152
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6679501     55 HTQCRLKLLKLEriKDYLLMEEEFIRNQEQMKPLeekqeeeRSKVDDLRGTPMSVGTLEEIIDDNHAIVSTSVGSEHYVS 134
Cdd:TIGR01242   1 ISELDVRIRKLE--DEKRSLEKEKIRLERELERL-------RSEIERLRSPPLIVGTVLEVLDDNRVVVKSSTGPNFVVN 71

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6679501    135 ILSFVDKDLLEPGCSVLLNHKVHAVIGVLMDDTDPLVTVMKVEKAPQETYADIGGLDNQIQEIKESVELPLTHPEYYEEM 214
Cdd:TIGR01242  72 VSAFIDRKSLKPGARVALNQQTLTIVDVLPTSKDPLVKGMEVEERPNVSYEDIGGLEEQIREIREAVELPLKHPELFEEV 151

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6679501    215 GIKPPKGVILYGPPGTGKTLLAKAVANQTSATFLRVVGSELIQKYLGDGPKLVRELFRVAEEHAPSIVFIDEIDAIGTKR 294
Cdd:TIGR01242 152 GIEPPKGVLLYGPPGTGKTLLAKAVAHETNATFIRVVGSELVRKYIGEGARLVREIFELAKEKAPSIIFIDEIDAIAAKR 231

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6679501    295 YDSNSGGEREIQRTMLELLNQLDGFDSRGDVKVIMATNRIETLDPALIRPGRIDRKIEFPLPDEKTKKRIFQIHTSRMTL 374
Cdd:TIGR01242 232 TDSGTSGDREVQRTLMQLLAELDGFDPRGNVKVIAATNRPDILDPALLRPGRFDRIIEVPLPDFEGRLEILKIHTRKMKL 311

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|...
gi 6679501    375 ADDVTLDDLIMAKDDLSGADIKAICTEAGLMALRERRMKVTNEDFKKSKENVL 427
Cdd:TIGR01242 312 AEDVDLEAIAKMTEGASGADLKAICTEAGMFAIREERDYVTMDDFIKAVEKVL 364
RPT1 COG1222
ATP-dependent 26S proteasome regulatory subunit [Posttranslational modification, protein ...
 165-435 7.23e-134

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


Pssm-ID: 440835 [Multi-domain]  Cd Length: 326  Bit Score: 387.82  E-value: 7.23e-134
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6679501  165 DDTDPLVTVMKVEKAPQETYADIGGLDNQIQEIKESVELPLTHPEYYEEMGIKPPKGVILYGPPGTGKTLLAKAVANQTS 244
Cdd:COG1222  58 KRLGTPRGTAVPAESPDVTFDDIGGLDEQIEEIREAVELPLKNPELFRKYGIEPPKGVLLYGPPGTGKTLLAKAVAGELG 137

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6679501  245 ATFLRVVGSELIQKYLGDGPKLVRELFRVAEEHAPSIVFIDEIDAIGTKRYDSNSGGerEIQRTMLELLNQLDGFDSRGD 324
Cdd:COG1222 138 APFIRVRGSELVSKYIGEGARNVREVFELAREKAPSIIFIDEIDAIAARRTDDGTSG--EVQRTVNQLLAELDGFESRGD 215

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6679501  325 VKVIMATNRIETLDPALIRPGRIDRKIEFPLPDEKTKKRIFQIHTSRMTLADDVTLDDLIMAKDDLSGADIKAICTEAGL 404
Cdd:COG1222 216 VLIIAATNRPDLLDPALLRPGRFDRVIEVPLPDEEAREEILKIHLRDMPLADDVDLDKLAKLTEGFSGADLKAIVTEAGM 295

                       250       260       270
                ....*....|....*....|....*....|.
gi 6679501  405 MALRERRMKVTNEDFKKSKENVLYKKQEGTP 435
Cdd:COG1222 296 FAIREGRDTVTMEDLEKAIEKVKKKTETATN 326
RecA-like_PAN_like cd19502
proteasome activating nucleotidase PAN and related proteasome subunits; This subfamily ...
 183-353 5.41e-118

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: 341.62  E-value: 5.41e-118
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6679501  183 TYADIGGLDNQIQEIKESVELPLTHPEYYEEMGIKPPKGVILYGPPGTGKTLLAKAVANQTSATFLRVVGSELIQKYLGD 262
Cdd:cd19502   1 TYEDIGGLDEQIREIREVVELPLKHPELFEELGIEPPKGVLLYGPPGTGKTLLAKAVANHTDATFIRVVGSELVQKYIGE 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6679501  263 GPKLVRELFRVAEEHAPSIVFIDEIDAIGTKRYDSNSGGEREIQRTMLELLNQLDGFDSRGDVKVIMATNRIETLDPALI 342
Cdd:cd19502  81 GARLVRELFEMAREKAPSIIFIDEIDAIGAKRFDSGTGGDREVQRTMLELLNQLDGFDPRGNIKVIMATNRPDILDPALL 160

                       170
                ....*....|.
gi 6679501  343 RPGRIDRKIEF 353
Cdd:cd19502 161 RPGRFDRKIEF 171
AAA pfam00004
ATPase family associated with various cellular activities (AAA); AAA family proteins often ...
 222-355 4.53e-54

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: 176.24  E-value: 4.53e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6679501    222 VILYGPPGTGKTLLAKAVANQTSATFLRVVGSELIQKYLGDGPKLVRELFRVAEEHAPSIVFIDEIDAIGTKRydsNSGG 301
Cdd:pfam00004   1 LLLYGPPGTGKTTLAKAVAKELGAPFIEISGSELVSKYVGESEKRLRELFEAAKKLAPCVIFIDEIDALAGSR---GSGG 77

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 6679501    302 EREIQRTMLELLNQLDGFDSR-GDVKVIMATNRIETLDPALIrpGRIDRKIEFPL 355
Cdd:pfam00004  78 DSESRRVVNQLLTELDGFTSSnSKVIVIAATNRPDKLDPALL--GRFDRIIEFPL 130
AAA smart00382
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ...
 218-357 3.82e-20

ATPases associated with a variety of cellular activities; AAA - ATPases associated with a variety of cellular activities. This profile/alignment only detects a fraction of this vast family. The poorly conserved N-terminal helix is missing from the alignment.


Pssm-ID: 214640 [Multi-domain]  Cd Length: 148  Bit Score: 86.66  E-value: 3.82e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6679501     218 PPKGVILYGPPGTGKTLLAKAVANQTSATFLRVV-----------------GSELIQKYLGDGPKLVRELFRVAEEHAPS 280
Cdd:smart00382   1 PGEVILIVGPPGSGKTTLARALARELGPPGGGVIyidgedileevldqlllIIVGGKKASGSGELRLRLALALARKLKPD 80

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 6679501     281 IVFIDEIDAIGTKrydsnsggEREIQRTMLELLNQLDGFDSRGDVKVIMATNRIETLDPALIRPgRIDRKIEFPLPD 357
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 ...
 222-287 3.49e-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: 3.49e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 6679501   222 VILYGPPGTGKTLLAKAVANQ-----TSATFLRVvgSELIQKYL---GDGpKLVRELFRVAeehAPSIVFIDEI 287
Cdd:NF038214  93 VLLLGPPGTGKTHLAIALGYAacrqgYRVRFTTA--ADLVEQLAqarADG-RLGRLLRRLA---RYDLLIIDEL 160
 
Name Accession Description Interval E-value
PTZ00361 PTZ00361
26 proteosome regulatory subunit 4-like protein; Provisional
 1-440 0e+00

26 proteosome regulatory subunit 4-like protein; Provisional


Pssm-ID: 185575 [Multi-domain]  Cd Length: 438  Bit Score: 791.28  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6679501     1 MGQSQSGGHGPGGGKKDDKDKKkkYEPPVPTRVGKKKKKTKGPDAASKLPLVTPHTQCRLKLLKLERIKDYLLMEEEFIR 80
Cdd:PTZ00361   1 MGNAQGQGNNQKDKNKKKEKKK--KESPPPPHEIKRKKKRKGPDAASKLPKVTPNTKCRLRLLKLERIKDYLLLEEEFIT 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6679501    81 NQEQMKPLEEKQEEERSKVDDLRGTPMSVGTLEEIIDDNHAIVSTSVGSEHYVSILSFVDKDLLEPGCSVLLNHKVHAVI 160
Cdd:PTZ00361  79 NQEAQKPAQEKNEAELKKVDDLRGSPLSVGTLEEIIDENHAIVSSSVGPEYYVNILSFVDKEQLEPGCSVLLHNKTHSVV 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6679501   161 GVLMDDTDPLVTVMKVEKAPQETYADIGGLDNQIQEIKESVELPLTHPEYYEEMGIKPPKGVILYGPPGTGKTLLAKAVA 240
Cdd:PTZ00361 159 GILLDEVDPLVSVMKVDKAPLESYADIGGLEQQIQEIKEAVELPLTHPELYDDIGIKPPKGVILYGPPGTGKTLLAKAVA 238

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6679501   241 NQTSATFLRVVGSELIQKYLGDGPKLVRELFRVAEEHAPSIVFIDEIDAIGTKRYDSNSGGEREIQRTMLELLNQLDGFD 320
Cdd:PTZ00361 239 NETSATFLRVVGSELIQKYLGDGPKLVRELFRVAEENAPSIVFIDEIDAIGTKRYDATSGGEKEIQRTMLELLNQLDGFD 318

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6679501   321 SRGDVKVIMATNRIETLDPALIRPGRIDRKIEFPLPDEKTKKRIFQIHTSRMTLADDVTLDDLIMAKDDLSGADIKAICT 400
Cdd:PTZ00361 319 SRGDVKVIMATNRIESLDPALIRPGRIDRKIEFPNPDEKTKRRIFEIHTSKMTLAEDVDLEEFIMAKDELSGADIKAICT 398

                        410       420       430       440
                 ....*....|....*....|....*....|....*....|
gi 6679501   401 EAGLMALRERRMKVTNEDFKKSKENVLYKKQEGTPEGLYL 440
Cdd:PTZ00361 399 EAGLLALRERRMKVTQADFRKAKEKVLYRKKGNIPEGLYL 438
PRK03992 PRK03992
proteasome-activating nucleotidase; Provisional
 71-436 3.68e-176

proteasome-activating nucleotidase; Provisional


Pssm-ID: 179699 [Multi-domain]  Cd Length: 389  Bit Score: 497.82  E-value: 3.68e-176
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6679501    71 YLLMEEEFIRNQEQMKPLEEKQEEERSKVDDLRGTPMSVGTLEEIIDDNHAIVSTSVGSEHYVSILSFVDKDLLEPGCSV 150
Cdd:PRK03992  17 IRQLELKLRDLEAENEKLERELERLKSELEKLKSPPLIVATVLEVLDDGRVVVKSSGGPQFLVNVSPFIDREKLKPGARV 96

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6679501   151 LLNHKVHAVIGVLMDDTDPLVTVMKVEKAPQETYADIGGLDNQIQEIKESVELPLTHPEYYEEMGIKPPKGVILYGPPGT 230
Cdd:PRK03992  97 ALNQQSLAIVEVLPSEKDPRVQAMEVIESPNVTYEDIGGLEEQIREVREAVELPLKKPELFEEVGIEPPKGVLLYGPPGT 176

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6679501   231 GKTLLAKAVANQTSATFLRVVGSELIQKYLGDGPKLVRELFRVAEEHAPSIVFIDEIDAIGTKRYDSNSGGEREIQRTML 310
Cdd:PRK03992 177 GKTLLAKAVAHETNATFIRVVGSELVQKFIGEGARLVRELFELAREKAPSIIFIDEIDAIAAKRTDSGTSGDREVQRTLM 256

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6679501   311 ELLNQLDGFDSRGDVKVIMATNRIETLDPALIRPGRIDRKIEFPLPDEKTKKRIFQIHTSRMTLADDVTLDDLIMAKDDL 390
Cdd:PRK03992 257 QLLAEMDGFDPRGNVKIIAATNRIDILDPAILRPGRFDRIIEVPLPDEEGRLEILKIHTRKMNLADDVDLEELAELTEGA 336

                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....*.
gi 6679501   391 SGADIKAICTEAGLMALRERRMKVTNEDFKKSKENVLYKKQEGTPE 436
Cdd:PRK03992 337 SGADLKAICTEAGMFAIRDDRTEVTMEDFLKAIEKVMGKEEKDSME 382
PTZ00454 PTZ00454
26S protease regulatory subunit 6B-like protein; Provisional
 44-432 8.19e-162

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


Pssm-ID: 240423 [Multi-domain]  Cd Length: 398  Bit Score: 461.93  E-value: 8.19e-162
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6679501    44 DAASKLPLVTPHTQCRL--KLLKLERIKDYLLMEEEFIRnqEQMKPLeeKQEEERSK--VDDLRGTPMSVGTLEEIIDDN 119
Cdd:PTZ00454   4 TAAAAVASSTTHTERDLyeKLKELEKELEFLDIQEEYIK--EEQKNL--KRELIRAKeeVKRIQSVPLVIGQFLEMIDSN 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6679501   120 HAIVSTSVGSEHYVSILSFVDKDLLEPGCSVLLNHKVHAVIGVLMDDTDPLVTVMKVEKAPQETYADIGGLDNQIQEIKE 199
Cdd:PTZ00454  80 YGIVSSTSGSNYYVRILSTLNRELLKPNASVALHRHSHAVVDILPPEADSSIQLLQMSEKPDVTYSDIGGLDIQKQEIRE 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6679501   200 SVELPLTHPEYYEEMGIKPPKGVILYGPPGTGKTLLAKAVANQTSATFLRVVGSELIQKYLGDGPKLVRELFRVAEEHAP 279
Cdd:PTZ00454 160 AVELPLTCPELYEQIGIDPPRGVLLYGPPGTGKTMLAKAVAHHTTATFIRVVGSEFVQKYLGEGPRMVRDVFRLARENAP 239

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6679501   280 SIVFIDEIDAIGTKRYDSNSGGEREIQRTMLELLNQLDGFDSRGDVKVIMATNRIETLDPALIRPGRIDRKIEFPLPDEK 359
Cdd:PTZ00454 240 SIIFIDEVDSIATKRFDAQTGADREVQRILLELLNQMDGFDQTTNVKVIMATNRADTLDPALLRPGRLDRKIEFPLPDRR 319

                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 6679501   360 TKKRIFQIHTSRMTLADDVTLDDLIMAKDDLSGADIKAICTEAGLMALRERRMKVTNEDFKKSKENVLYKKQE 432
Cdd:PTZ00454 320 QKRLIFQTITSKMNLSEEVDLEDFVSRPEKISAADIAAICQEAGMQAVRKNRYVILPKDFEKGYKTVVRKTDR 392
26Sp45 TIGR01242
26S proteasome subunit P45 family; Many proteins may score above the trusted cutoff because an ...
 55-427 1.06e-152

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: 437.31  E-value: 1.06e-152
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6679501     55 HTQCRLKLLKLEriKDYLLMEEEFIRNQEQMKPLeekqeeeRSKVDDLRGTPMSVGTLEEIIDDNHAIVSTSVGSEHYVS 134
Cdd:TIGR01242   1 ISELDVRIRKLE--DEKRSLEKEKIRLERELERL-------RSEIERLRSPPLIVGTVLEVLDDNRVVVKSSTGPNFVVN 71

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6679501    135 ILSFVDKDLLEPGCSVLLNHKVHAVIGVLMDDTDPLVTVMKVEKAPQETYADIGGLDNQIQEIKESVELPLTHPEYYEEM 214
Cdd:TIGR01242  72 VSAFIDRKSLKPGARVALNQQTLTIVDVLPTSKDPLVKGMEVEERPNVSYEDIGGLEEQIREIREAVELPLKHPELFEEV 151

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6679501    215 GIKPPKGVILYGPPGTGKTLLAKAVANQTSATFLRVVGSELIQKYLGDGPKLVRELFRVAEEHAPSIVFIDEIDAIGTKR 294
Cdd:TIGR01242 152 GIEPPKGVLLYGPPGTGKTLLAKAVAHETNATFIRVVGSELVRKYIGEGARLVREIFELAKEKAPSIIFIDEIDAIAAKR 231

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6679501    295 YDSNSGGEREIQRTMLELLNQLDGFDSRGDVKVIMATNRIETLDPALIRPGRIDRKIEFPLPDEKTKKRIFQIHTSRMTL 374
Cdd:TIGR01242 232 TDSGTSGDREVQRTLMQLLAELDGFDPRGNVKVIAATNRPDILDPALLRPGRFDRIIEVPLPDFEGRLEILKIHTRKMKL 311

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|...
gi 6679501    375 ADDVTLDDLIMAKDDLSGADIKAICTEAGLMALRERRMKVTNEDFKKSKENVL 427
Cdd:TIGR01242 312 AEDVDLEAIAKMTEGASGADLKAICTEAGMFAIREERDYVTMDDFIKAVEKVL 364
RPT1 COG1222
ATP-dependent 26S proteasome regulatory subunit [Posttranslational modification, protein ...
 165-435 7.23e-134

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


Pssm-ID: 440835 [Multi-domain]  Cd Length: 326  Bit Score: 387.82  E-value: 7.23e-134
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6679501  165 DDTDPLVTVMKVEKAPQETYADIGGLDNQIQEIKESVELPLTHPEYYEEMGIKPPKGVILYGPPGTGKTLLAKAVANQTS 244
Cdd:COG1222  58 KRLGTPRGTAVPAESPDVTFDDIGGLDEQIEEIREAVELPLKNPELFRKYGIEPPKGVLLYGPPGTGKTLLAKAVAGELG 137

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6679501  245 ATFLRVVGSELIQKYLGDGPKLVRELFRVAEEHAPSIVFIDEIDAIGTKRYDSNSGGerEIQRTMLELLNQLDGFDSRGD 324
Cdd:COG1222 138 APFIRVRGSELVSKYIGEGARNVREVFELAREKAPSIIFIDEIDAIAARRTDDGTSG--EVQRTVNQLLAELDGFESRGD 215

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6679501  325 VKVIMATNRIETLDPALIRPGRIDRKIEFPLPDEKTKKRIFQIHTSRMTLADDVTLDDLIMAKDDLSGADIKAICTEAGL 404
Cdd:COG1222 216 VLIIAATNRPDLLDPALLRPGRFDRVIEVPLPDEEAREEILKIHLRDMPLADDVDLDKLAKLTEGFSGADLKAIVTEAGM 295

                       250       260       270
                ....*....|....*....|....*....|.
gi 6679501  405 MALRERRMKVTNEDFKKSKENVLYKKQEGTP 435
Cdd:COG1222 296 FAIREGRDTVTMEDLEKAIEKVKKKTETATN 326
RecA-like_PAN_like cd19502
proteasome activating nucleotidase PAN and related proteasome subunits; This subfamily ...
 183-353 5.41e-118

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: 341.62  E-value: 5.41e-118
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6679501  183 TYADIGGLDNQIQEIKESVELPLTHPEYYEEMGIKPPKGVILYGPPGTGKTLLAKAVANQTSATFLRVVGSELIQKYLGD 262
Cdd:cd19502   1 TYEDIGGLDEQIREIREVVELPLKHPELFEELGIEPPKGVLLYGPPGTGKTLLAKAVANHTDATFIRVVGSELVQKYIGE 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6679501  263 GPKLVRELFRVAEEHAPSIVFIDEIDAIGTKRYDSNSGGEREIQRTMLELLNQLDGFDSRGDVKVIMATNRIETLDPALI 342
Cdd:cd19502  81 GARLVRELFEMAREKAPSIIFIDEIDAIGAKRFDSGTGGDREVQRTMLELLNQLDGFDPRGNIKVIMATNRPDILDPALL 160

                       170
                ....*....|.
gi 6679501  343 RPGRIDRKIEF 353
Cdd:cd19502 161 RPGRFDRKIEF 171
SpoVK COG0464
AAA+-type ATPase, SpoVK/Ycf46/Vps4 family [Cell wall/membrane/envelope biogenesis, Cell cycle ...
 168-421 1.25e-81

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: 257.15  E-value: 1.25e-81
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6679501  168 DPLVTVMKVEKAPQETYADIGGLDNQIQEIKESVELPLTHPEYYEEMGIKPPKGVILYGPPGTGKTLLAKAVANQTSATF 247
Cdd:COG0464 140 DIGGLEEELLELREAILDDLGGLEEVKEELRELVALPLKRPELREEYGLPPPRGLLLYGPPGTGKTLLARALAGELGLPL 219

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6679501  248 LRVVGSELIQKYLGDGPKLVRELFRVAEEHAPSIVFIDEIDAIGTKRYDSNSGGEREIQRTmleLLNQLDGFdsRGDVKV 327
Cdd:COG0464 220 IEVDLSDLVSKYVGETEKNLREVFDKARGLAPCVLFIDEADALAGKRGEVGDGVGRRVVNT---LLTEMEEL--RSDVVV 294

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6679501  328 IMATNRIETLDPALIRpgRIDRKIEFPLPDEKTKKRIFQIHTSRMTLADDVTLDDLIMAKDDLSGADIKAICTEAGLMAL 407
Cdd:COG0464 295 IAATNRPDLLDPALLR--RFDEIIFFPLPDAEERLEIFRIHLRKRPLDEDVDLEELAEATEGLSGADIRNVVRRAALQAL 372

                       250
                ....*....|....
gi 6679501  408 RERRMKVTNEDFKK 421
Cdd:COG0464 373 RLGREPVTTEDLLE 386
FtsH_fam TIGR01241
ATP-dependent metalloprotease FtsH; HflB(FtsH) is a pleiotropic protein required for correct ...
 177-428 6.34e-81

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: 257.98  E-value: 6.34e-81
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6679501    177 EKAPQETYADIGGLDNQIQEIKESVELpLTHPEYYEEMGIKPPKGVILYGPPGTGKTLLAKAVANQTSATFLRVVGSELI 256
Cdd:TIGR01241  47 EEKPKVTFKDVAGIDEAKEELMEIVDF-LKNPSKFTKLGAKIPKGVLLVGPPGTGKTLLAKAVAGEAGVPFFSISGSDFV 125

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6679501    257 QKYLGDGPKLVRELFRVAEEHAPSIVFIDEIDAIGTKRYDSNSGGEREIQRTMLELLNQLDGFDSRGDVKVIMATNRIET 336
Cdd:TIGR01241 126 EMFVGVGASRVRDLFEQAKKNAPCIIFIDEIDAVGRQRGAGLGGGNDEREQTLNQLLVEMDGFGTNTGVIVIAATNRPDV 205

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6679501    337 LDPALIRPGRIDRKIEFPLPDEKTKKRIFQIHTSRMTLADDVTLDDLIMAKDDLSGADIKAICTEAGLMALRERRMKVTN 416
Cdd:TIGR01241 206 LDPALLRPGRFDRQVVVDLPDIKGREEILKVHAKNKKLAPDVDLKAVARRTPGFSGADLANLLNEAALLAARKNKTEITM 285

                         250
                  ....*....|..
gi 6679501    417 EDFKKSKENVLY 428
Cdd:TIGR01241 286 NDIEEAIDRVIA 297
CDC48 TIGR01243
AAA family ATPase, CDC48 subfamily; This subfamily of the AAA family ATPases includes two ...
 171-426 1.45e-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: 252.91  E-value: 1.45e-76
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6679501    171 VTVMKVEKAPQETYADIGGLDNQIQEIKESVELPLTHPEYYEEMGIKPPKGVILYGPPGTGKTLLAKAVANQTSATFLRV 250
Cdd:TIGR01243 164 VREEIERKVPKVTYEDIGGLKEAKEKIREMVELPMKHPELFEHLGIEPPKGVLLYGPPGTGKTLLAKAVANEAGAYFISI 243

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6679501    251 VGSELIQKYLGDGPKLVRELFRVAEEHAPSIVFIDEIDAIGTKRYDSNsgGEREiQRTMLELLNQLDGFDSRGDVKVIMA 330
Cdd:TIGR01243 244 NGPEIMSKYYGESEERLREIFKEAEENAPSIIFIDEIDAIAPKREEVT--GEVE-KRVVAQLLTLMDGLKGRGRVIVIGA 320

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6679501    331 TNRIETLDPALIRPGRIDRKIEFPLPDEKTKKRIFQIHTSRMTLADDVTLDDLIMAKDDLSGADIKAICTEAGLMALRE- 409
Cdd:TIGR01243 321 TNRPDALDPALRRPGRFDREIVIRVPDKRARKEILKVHTRNMPLAEDVDLDKLAEVTHGFVGADLAALAKEAAMAALRRf 400

                         250       260       270
                  ....*....|....*....|....*....|....*
gi 6679501    410 ------------------RRMKVTNEDFKKSKENV 426
Cdd:TIGR01243 401 iregkinfeaeeipaevlKELKVTMKDFMEALKMV 435
CDC48 TIGR01243
AAA family ATPase, CDC48 subfamily; This subfamily of the AAA family ATPases includes two ...
 180-429 1.56e-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: 252.91  E-value: 1.56e-76
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6679501    180 PQETYADIGGLDNQIQEIKESVELPLTHPEYYEEMGIKPPKGVILYGPPGTGKTLLAKAVANQTSATFLRVVGSELIQKY 259
Cdd:TIGR01243 448 PNVRWSDIGGLEEVKQELREAVEWPLKHPEIFEKMGIRPPKGVLLFGPPGTGKTLLAKAVATESGANFIAVRGPEILSKW 527

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6679501    260 LGDGPKLVRELFRVAEEHAPSIVFIDEIDAIGTKRydSNSGGEREIQRTMLELLNQLDGFDSRGDVKVIMATNRIETLDP 339
Cdd:TIGR01243 528 VGESEKAIREIFRKARQAAPAIIFFDEIDAIAPAR--GARFDTSVTDRIVNQLLTEMDGIQELSNVVVIAATNRPDILDP 605

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6679501    340 ALIRPGRIDRKIEFPLPDEKTKKRIFQIHTSRMTLADDVTLDDLIMAKDDLSGADIKAICTEAGLMALRERRMKVTNEDF 419
Cdd:TIGR01243 606 ALLRPGRFDRLILVPPPDEEARKEIFKIHTRSMPLAEDVDLEELAEMTEGYTGADIEAVCREAAMAALRESIGSPAKEKL 685

                         250
                  ....*....|
gi 6679501    420 KKSKENVLYK 429
Cdd:TIGR01243 686 EVGEEEFLKD 695
HflB COG0465
ATP-dependent Zn proteases [Posttranslational modification, protein turnover, chaperones];
174-427 2.33e-75

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


Pssm-ID: 440233 [Multi-domain]  Cd Length: 583  Bit Score: 246.10  E-value: 2.33e-75
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6679501  174 MKVEKAPQETYADIGGLDNQIQEIKESVELpLTHPEYYEEMGIKPPKGVILYGPPGTGKTLLAKAVANQTSATFLRVVGS 253
Cdd:COG0465 131 LYDEDKPKVTFDDVAGVDEAKEELQEIVDF-LKDPEKFTRLGAKIPKGVLLVGPPGTGKTLLAKAVAGEAGVPFFSISGS 209

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6679501  254 ELIQKYLGDGPKLVRELFRVAEEHAPSIVFIDEIDAIGTKRyDSNSGG---EREiqRTmlelLNQL----DGFDSRGDVK 326
Cdd:COG0465 210 DFVEMFVGVGASRVRDLFEQAKKNAPCIIFIDEIDAVGRQR-GAGLGGghdERE--QT----LNQLlvemDGFEGNEGVI 282

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6679501  327 VIMATNRIETLDPALIRPGRIDRKIEFPLPDEKTKKRIFQIHTSRMTLADDVTLDDLIMAKDDLSGADIKAICTEAGLMA 406
Cdd:COG0465 283 VIAATNRPDVLDPALLRPGRFDRQVVVDLPDVKGREAILKVHARKKPLAPDVDLEVIARRTPGFSGADLANLVNEAALLA 362

                       250       260
                ....*....|....*....|.
gi 6679501  407 LRERRMKVTNEDFKKSKENVL 427
Cdd:COG0465 363 ARRNKKAVTMEDFEEAIDRVI 383
RecA-like_CDC48_NLV2_r1-like cd19503
first of two ATPase domains of CDC48 and NLV2, and similar ATPase domains; CDC48 in yeast and ...
 186-353 1.37e-71

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: 222.94  E-value: 1.37e-71
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6679501  186 DIGGLDNQIQEIKESVELPLTHPEYYEEMGIKPPKGVILYGPPGTGKTLLAKAVANQTSATFLRVVGSELIQKYLGDGPK 265
Cdd:cd19503   1 DIGGLDEQIASLKELIELPLKYPELFRALGLKPPRGVLLHGPPGTGKTLLARAVANEAGANFLSISGPSIVSKYLGESEK 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6679501  266 LVRELFRVAEEHAPSIVFIDEIDAIGTKRYDSNSGGEReiqRTMLELLNQLDGFDSRGDVKVIMATNRIETLDPALIRPG 345
Cdd:cd19503  81 NLREIFEEARSHAPSIIFIDEIDALAPKREEDQREVER---RVVAQLLTLMDGMSSRGKVVVIAATNRPDAIDPALRRPG 157


                ....*...
gi 6679501  346 RIDRKIEF 353
Cdd:cd19503 158 RFDREVEI 165
RecA-like_FtsH cd19501
ATP-dependent zinc metalloprotease FtsH; FtsH ATPase is a processive, ATP-dependent zinc ...
 183-351 5.86e-69

ATP-dependent zinc metalloprotease FtsH; FtsH ATPase is a processive, ATP-dependent zinc metallopeptidase for both cytoplasmic and membrane proteins. It is anchored to the cytoplasmic membrane such that the amino- and carboxy-termini are exposed to the cytoplasm. It presents a membrane-bound hexameric structure that is able to unfold and degrade protein substrates. It is comprised of an N-terminal transmembrane region and the larger C-terminal cytoplasmic region, which consists of an ATPase domain and a protease domain. This RecA-Like FTsH subfamily represents the ATPase domain, and belongs to the RecA-like NTPase family which includes the NTP binding domain of F1 and V1 H(+)ATPases, DnaB and related helicases as well as bacterial RecA and related eukaryotic and archaeal recombinases. The RecA-like NTPase family also includes bacterial conjugation proteins and related DNA transfer proteins involved in type II and type IV secretion.


Pssm-ID: 410909 [Multi-domain]  Cd Length: 171  Bit Score: 216.33  E-value: 5.86e-69
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6679501  183 TYADIGGLDNQIQEIKESVELpLTHPEYYEEMGIKPPKGVILYGPPGTGKTLLAKAVANQTSATFLRVVGSELIQKYLGD 262
Cdd:cd19501   2 TFKDVAGCEEAKEELKEVVEF-LKNPEKFTKLGAKIPKGVLLVGPPGTGKTLLAKAVAGEAGVPFFSISGSDFVEMFVGV 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6679501  263 GPKLVRELFRVAEEHAPSIVFIDEIDAIGTKRYDSNSGGEREIQRTMLELLNQLDGFDSRGDVKVIMATNRIETLDPALI 342
Cdd:cd19501  81 GASRVRDLFEQAKKNAPCIVFIDEIDAVGRKRGAGLGGGHDEREQTLNQLLVEMDGFESNTGVIVIAATNRPDVLDPALL 160


                ....*....
gi 6679501  343 RPGRIDRKI 351
Cdd:cd19501 161 RPGRFDRQV 169
pup_AAA TIGR03689
proteasome ATPase; In the Actinobacteria, as shown for Mycobacterium tuberculosis, some ...
 111-398 4.20e-67

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: 222.66  E-value: 4.20e-67
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6679501    111 TLEEIIDDNHAIVSTSVGSEHYVSILSFVDKDLLEPGCSVLLNHKV-HAVIGVLMDDTDPLVtvmkVEKAPQETYADIGG 189
Cdd:TIGR03689 111 TLKEVLDDGRALVTDRSGEERVVKLAGALADEGLRPGDTLLVDPRAgYAFEAIPRTEVEDLV----LEEVPDVTYADIGG 186

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6679501    190 LDNQIQEIKESVELPLTHPEYYEEMGIKPPKGVILYGPPGTGKTLLAKAVAN----------QTSATFLRVVGSELIQKY 259
Cdd:TIGR03689 187 LGSQIEQIRDAVELPFLHPELYREYGLKPPKGVLLYGPPGCGKTLIAKAVANslaarigaegGGKSYFLNIKGPELLNKY 266

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6679501    260 LGDGPKLVRELFRVAEEHA----PSIVFIDEIDAIGTKRydsNSGGEREIQRTML-ELLNQLDGFDSRGDVKVIMATNRI 334
Cdd:TIGR03689 267 VGETERQIRLIFQRAREKAsegrPVIVFFDEMDSLFRTR---GSGVSSDVETTVVpQLLAEIDGVESLDNVIVIGASNRE 343

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 6679501    335 ETLDPALIRPGRIDRKIEFPLPDEKTKKRIFQIHtsrmtLADDVTLDDLIMAKDDLSGADIKAI 398
Cdd:TIGR03689 344 DMIDPAILRPGRLDVKIRIERPDAEAAADIFAKY-----LTDDLPLPEDLAAHDGDREATAAAL 402
ftsH CHL00176
cell division protein; Validated
 183-435 4.37e-67

cell division protein; Validated


Pssm-ID: 214386 [Multi-domain]  Cd Length: 638  Bit Score: 225.70  E-value: 4.37e-67
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6679501   183 TYADIGGLDNQIQEIKESVELpLTHPEYYEEMGIKPPKGVILYGPPGTGKTLLAKAVANQTSATFLRVVGSELIQKYLGD 262
Cdd:CHL00176 181 TFRDIAGIEEAKEEFEEVVSF-LKKPERFTAVGAKIPKGVLLVGPPGTGKTLLAKAIAGEAEVPFFSISGSEFVEMFVGV 259

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6679501   263 GPKLVRELFRVAEEHAPSIVFIDEIDAIGTKRYDSNSGGEREIQRTMLELLNQLDGFDSRGDVKVIMATNRIETLDPALI 342
Cdd:CHL00176 260 GAARVRDLFKKAKENSPCIVFIDEIDAVGRQRGAGIGGGNDEREQTLNQLLTEMDGFKGNKGVIVIAATNRVDILDAALL 339

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6679501   343 RPGRIDRKIEFPLPDEKTKKRIFQIHTSRMTLADDVTLddLIMAKDD--LSGADIKAICTEAGLMALRERRMKVTNEDFK 420
Cdd:CHL00176 340 RPGRFDRQITVSLPDREGRLDILKVHARNKKLSPDVSL--ELIARRTpgFSGADLANLLNEAAILTARRKKATITMKEID 417

                        250
                 ....*....|....*
gi 6679501   421 KSKENVLyKKQEGTP 435
Cdd:CHL00176 418 TAIDRVI-AGLEGTP 431
RecA-like_CDC48_r1-like cd19519
first of two ATPase domains of CDC48 and similar ATPase domains; CDC48 in yeast and p97 or VCP ...
 186-354 1.32e-65

first of two ATPase domains of CDC48 and similar ATPase domains; CDC48 in yeast and p97 or VCP metazoans is an ATP-dependent molecular chaperone which plays an essential role in many cellular processes, by segregating polyubiquitinated proteins from complexes or membranes. Cdc48/p97 consists of an N-terminal domain and two ATPase domains; this subfamily represents the first of the two ATPase domains. CDC48's roles include in the fragmentation of Golgi stacks during mitosis and for their reassembly after mitosis, and in the formation of the nuclear envelope, and of the transitional endoplasmic reticulum (tER). This RecA-like_cdc48_r1-like subfamily belongs to the RecA-like family which includes the NTP binding domain of F1 and V1 H(+)ATPases, DnaB and related helicases as well as bacterial RecA and related eukaryotic and archaeal recombinases. The RecA-like NTPase family also includes bacterial conjugation proteins and related DNA transfer proteins involved in type II and type IV secretion.


Pssm-ID: 410927 [Multi-domain]  Cd Length: 166  Bit Score: 207.67  E-value: 1.32e-65
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6679501  186 DIGGLDNQIQEIKESVELPLTHPEYYEEMGIKPPKGVILYGPPGTGKTLLAKAVANQTSATFLRVVGSELIQKYLGDGPK 265
Cdd:cd19519   1 DIGGCRKQLAQIREMVELPLRHPELFKAIGIKPPRGILLYGPPGTGKTLIARAVANETGAFFFLINGPEIMSKLAGESES 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6679501  266 LVRELFRVAEEHAPSIVFIDEIDAIGTKRYDSNSGGEReiqRTMLELLNQLDGFDSRGDVKVIMATNRIETLDPALIRPG 345
Cdd:cd19519  81 NLRKAFEEAEKNAPAIIFIDEIDAIAPKREKTHGEVER---RIVSQLLTLMDGLKQRAHVIVMAATNRPNSIDPALRRFG 157


                ....*....
gi 6679501  346 RIDRKIEFP 354
Cdd:cd19519 158 RFDREIDIG 166
RecA-like_CDC48_r2-like cd19511
second of two ATPase domains of CDC48/p97, PEX1 and -6, VAT and NVL, and similar ATPase ...
 195-351 1.28e-63

second of two ATPase domains of CDC48/p97, PEX1 and -6, VAT and NVL, and similar ATPase domains; This subfamily includes the second of two ATPase domains of the molecular chaperone CDC48 in yeast and p97 or VCP in metazoans, Peroxisomal biogenesis factor 1 (PEX1) and -6 (PEX6), Valosin-containing protein-like ATPase (VAT), and nuclear VCP-like protein (NVL). This subfamily belongs to the RecA-like NTPase family which includes the NTP binding domain of F1 and V1 H(+)ATPases, DnaB and related helicases as well as bacterial RecA and related eukaryotic and archaeal recombinases. The RecA-like NTPase family also includes bacterial conjugation proteins and related DNA transfer proteins involved in type II and type IV secretion.


Pssm-ID: 410919 [Multi-domain]  Cd Length: 159  Bit Score: 202.13  E-value: 1.28e-63
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6679501  195 QEIKESVELPLTHPEYYEEMGIKPPKGVILYGPPGTGKTLLAKAVANQTSATFLRVVGSELIQKYLGDGPKLVRELFRVA 274
Cdd:cd19511   3 RELKEAVEWPLKHPDAFKRLGIRPPKGVLLYGPPGCGKTLLAKALASEAGLNFISVKGPELFSKYVGESERAVREIFQKA 82

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 6679501  275 EEHAPSIVFIDEIDAIGTKRYDSNSGGEREiqRTMLELLNQLDGFDSRGDVKVIMATNRIETLDPALIRPGRIDRKI 351
Cdd:cd19511  83 RQAAPCIIFFDEIDSLAPRRGQSDSSGVTD--RVVSQLLTELDGIESLKGVVVIAATNRPDMIDPALLRPGRLDKLI 157
RecA-like_protease cd19481
proteases similar to RecA; RecA-like NTPases. This family includes the NTP binding domain of ...
 193-353 1.68e-61

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: 196.73  E-value: 1.68e-61
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6679501  193 QIQEIKESVELPLTHPEYyEEMGIKPPKGVILYGPPGTGKTLLAKAVANQTSATFLRVVGSELIQKYLGDGPKLVRELFR 272
Cdd:cd19481   1 LKASLREAVEAPRRGSRL-RRYGLGLPKGILLYGPPGTGKTLLAKALAGELGLPLIVVKLSSLLSKYVGESEKNLRKIFE 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6679501  273 VAEEHAPSIVFIDEIDAIGTKRydSNSGGEREIQRTMLELLNQLDGFDSRGDVKVIMATNRIETLDPALIRPGRIDRKIE 352
Cdd:cd19481  80 RARRLAPCILFIDEIDAIGRKR--DSSGESGELRRVLNQLLTELDGVNSRSKVLVIAATNRPDLLDPALLRPGRFDEVIE 157


                .
gi 6679501  353 F 353
Cdd:cd19481 158 F 158
hflB PRK10733
ATP-dependent zinc metalloprotease FtsH;
174-427 4.83e-61

ATP-dependent zinc metalloprotease FtsH;


Pssm-ID: 182683 [Multi-domain]  Cd Length: 644  Bit Score: 209.51  E-value: 4.83e-61
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6679501   174 MKVEKAPQETYADIGGLDNQIQEIKESVELpLTHPEYYEEMGIKPPKGVILYGPPGTGKTLLAKAVANQTSATFLRVVGS 253
Cdd:PRK10733 141 MLTEDQIKTTFADVAGCDEAKEEVAELVEY-LREPSRFQKLGGKIPKGVLMVGPPGTGKTLLAKAIAGEAKVPFFTISGS 219

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6679501   254 ELIQKYLGDGPKLVRELFRVAEEHAPSIVFIDEIDAIGTKRYDSNSGGEREIQRTMLELLNQLDGFDSRGDVKVIMATNR 333
Cdd:PRK10733 220 DFVEMFVGVGASRVRDMFEQAKKAAPCIIFIDEIDAVGRQRGAGLGGGHDEREQTLNQMLVEMDGFEGNEGIIVIAATNR 299

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6679501   334 IETLDPALIRPGRIDRKIEFPLPDEKTKKRIFQIHTSRMTLADDVTLDDLIMAKDDLSGADIKAICTEAGLMALRERRMK 413
Cdd:PRK10733 300 PDVLDPALLRPGRFDRQVVVGLPDVRGREQILKVHMRRVPLAPDIDAAIIARGTPGFSGADLANLVNEAALFAARGNKRV 379

                        250
                 ....*....|....
gi 6679501   414 VTNEDFKKSKENVL 427
Cdd:PRK10733 380 VSMVEFEKAKDKIM 393
RecA-like_VCP_r2 cd19529
second of two ATPase domains of Valosin-containing protein-like ATPase (VAT) and similar ...
 195-351 2.92e-60

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: 193.48  E-value: 2.92e-60
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6679501  195 QEIKESVELPLTHPEYYEEMGIKPPKGVILYGPPGTGKTLLAKAVANQTSATFLRVVGSELIQKYLGDGPKLVRELFRVA 274
Cdd:cd19529   3 QELKEAVEWPLLKPEVFKRLGIRPPKGILLYGPPGTGKTLLAKAVATESNANFISVKGPELLSKWVGESEKAIREIFRKA 82

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 6679501  275 EEHAPSIVFIDEIDAIGTKRYDSNSGGEREiqRTMLELLNQLDGFDSRGDVKVIMATNRIETLDPALIRPGRIDRKI 351
Cdd:cd19529  83 RQVAPCVIFFDEIDSIAPRRGTTGDSGVTE--RVVNQLLTELDGLEEMNGVVVIAATNRPDIIDPALLRAGRFDRLI 157
AAA pfam00004
ATPase family associated with various cellular activities (AAA); AAA family proteins often ...
 222-355 4.53e-54

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: 176.24  E-value: 4.53e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6679501    222 VILYGPPGTGKTLLAKAVANQTSATFLRVVGSELIQKYLGDGPKLVRELFRVAEEHAPSIVFIDEIDAIGTKRydsNSGG 301
Cdd:pfam00004   1 LLLYGPPGTGKTTLAKAVAKELGAPFIEISGSELVSKYVGESEKRLRELFEAAKKLAPCVIFIDEIDALAGSR---GSGG 77

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 6679501    302 EREIQRTMLELLNQLDGFDSR-GDVKVIMATNRIETLDPALIrpGRIDRKIEFPL 355
Cdd:pfam00004  78 DSESRRVVNQLLTELDGFTSSnSKVIVIAATNRPDKLDPALL--GRFDRIIEFPL 130
COG1223 COG1223
Predicted ATPase, AAA+ superfamily [General function prediction only];
196-437 1.48e-52

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


Pssm-ID: 440836 [Multi-domain]  Cd Length: 246  Bit Score: 176.61  E-value: 1.48e-52
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6679501  196 EIKESVEL---PLTHPEYYEEMGIKPPKGVILYGPPGTGKTLLAKAVANQTSATFLRVVGSELIQKYLGDGPKLVRELFR 272
Cdd:COG1223   9 EAKKKLKLiikELRRRENLRKFGLWPPRKILFYGPPGTGKTMLAEALAGELKLPLLTVRLDSLIGSYLGETARNLRKLFD 88

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6679501  273 VAEEhAPSIVFIDEIDAIGTKRYDSNSGGerEIQRTMLELLNQLDGFDSrgDVKVIMATNRIETLDPALIRpgRIDRKIE 352
Cdd:COG1223  89 FARR-APCVIFFDEFDAIAKDRGDQNDVG--EVKRVVNALLQELDGLPS--GSVVIAATNHPELLDSALWR--RFDEVIE 161

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6679501  353 FPLPDEKTKKRIFQIHTSRMTLADDVTLDDLIMAKDDLSGADIKAICTEAGLMALRERRMKVTNEDFKKSKENVLYKKQE 432
Cdd:COG1223 162 FPLPDKEERKEILELNLKKFPLPFELDLKKLAKKLEGLSGADIEKVLKTALKKAILEDREKVTKEDLEEALKQRKERKKE 241


                ....*
gi 6679501  433 GTPEG 437
Cdd:COG1223 242 PKKEG 246
RecA-like_CDC48_r2-like cd19528
second of two ATPase domains of CDC48 and similar ATPase domains; CDC48 in yeast and p97 or ...
 195-351 6.44e-52

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: 171.92  E-value: 6.44e-52
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6679501  195 QEIKESVELPLTHPEYYEEMGIKPPKGVILYGPPGTGKTLLAKAVANQTSATFLRVVGSELIQKYLGDGPKLVRELFRVA 274
Cdd:cd19528   3 RELQELVQYPVEHPDKFLKFGMTPSKGVLFYGPPGCGKTLLAKAIANECQANFISVKGPELLTMWFGESEANVRDIFDKA 82

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 6679501  275 EEHAPSIVFIDEIDAIGTKRYDSNSGGEREIQRTMLELLNQLDGFDSRGDVKVIMATNRIETLDPALIRPGRIDRKI 351
Cdd:cd19528  83 RAAAPCVLFFDELDSIAKARGGNIGDAGGAADRVINQILTEMDGMNTKKNVFIIGATNRPDIIDPAILRPGRLDQLI 159
RecA-like_VPS4-like cd19509
ATPase domain of VPS4, ATAD1, K, KTNA1, Spastin, FIGL-1 and similar ATPase domains; This ...
 187-351 2.85e-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: 2.85e-49
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6679501  187 IGGLDNQIQEIKESVELPLTHPEYYEeMGIKPPKGVILYGPPGTGKTLLAKAVANQTSATFLRVVGSELIQKYLGDGPKL 266
Cdd:cd19509   1 IAGLDDAKEALKEAVILPSLRPDLFP-GLRGPPRGILLYGPPGTGKTLLARAVASESGSTFFSISASSLVSKWVGESEKI 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6679501  267 VRELFRVAEEHAPSIVFIDEIDAIGTKRYDSNSGGEREIqRTmlELLNQLDGF--DSRGDVKVIMATNRIETLDPALIRp 344
Cdd:cd19509  80 VRALFALARELQPSIIFIDEIDSLLSERGSGEHEASRRV-KT--EFLVQMDGVlnKPEDRVLVLGATNRPWELDEAFLR- 155


                ....*..
gi 6679501  345 gRIDRKI 351
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 ...
 186-351 4.15e-49

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: 164.89  E-value: 4.15e-49
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6679501  186 DIGGLDNQIQEIKESVELPLTHPEYYEEMGIKPPKGVILYGPPGTGKTLLAKAVANQTSATFLRVVGSELIQKYLGDGPK 265
Cdd:cd19518   1 DIGGMDSTLKELCELLIHPILPPEYFQHLGVEPPRGVLLHGPPGCGKTMLANAIAGELKVPFLKISATEIVSGVSGESEE 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6679501  266 LVRELFRVAEEHAPSIVFIDEIDAIGTKRydsnSGGEREIQRTML-ELLNQLDGF----DSRGDVKVIMATNRIETLDPA 340
Cdd:cd19518  81 KIRELFDQAISNAPCIVFIDEIDAITPKR----ESAQREMERRIVsQLLTCMDELnnekTAGGPVLVIGATNRPDSLDPA 156

                       170
                ....*....|.
gi 6679501  341 LIRPGRIDRKI 351
Cdd:cd19518 157 LRRAGRFDREI 167
RecA-like_Yta7-like cd19517
ATPase domain of Saccharomyces cerevisiae Yta7 and similar ATPase domains; Saccharomyces ...
 186-353 4.33e-49

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


Pssm-ID: 410925 [Multi-domain]  Cd Length: 170  Bit Score: 164.99  E-value: 4.33e-49
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6679501  186 DIGGLDNQIQEIKESVELPLTHPEYYEEMGIKPPKGVILYGPPGTGKTLLAKAVANQTSA-----TFLRVVGSELIQKYL 260
Cdd:cd19517   1 DIGGLSHYINQLKEMVFFPLLYPEVFAKFKITPPRGVLFHGPPGTGKTLMARALAAECSKggqkvSFFMRKGADCLSKWV 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6679501  261 GDGPKLVRELFRVAEEHAPSIVFIDEIDAIGTKRYDSNSGGEREIQRTMLELlnqLDGFDSRGDVKVIMATNRIETLDPA 340
Cdd:cd19517  81 GEAERQLRLLFEEAYRMQPSIIFFDEIDGLAPVRSSKQEQIHASIVSTLLAL---MDGLDNRGQVVVIGATNRPDALDPA 157

                       170
                ....*....|...
gi 6679501  341 LIRPGRIDRKIEF 353
Cdd:cd19517 158 LRRPGRFDREFYF 170
RecA-like_NVL_r2-like cd19530
second of two ATPase domains of NVL (nuclear VCP-like protein) and similar ATPase domains; NVL ...
 190-349 4.77e-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: 156.49  E-value: 4.77e-46
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6679501  190 LDNQIQEIKESVELPLTHPEYYEEMGIKPPKGVILYGPPGTGKTLLAKAVANQTSATFLRVVGSELIQKYLGDGPKLVRE 269
Cdd:cd19530   1 LDHVREELTMSILRPIKRPDIYKALGIDLPTGVLLYGPPGCGKTLLAKAVANESGANFISVKGPELLNKYVGESERAVRQ 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6679501  270 LFRVAEEHAPSIVFIDEIDAIGTKRYDSNSGGereIQRTMLELLNQLDGFDSRGDVKVIMATNRIETLDPALIRPGRIDR 349
Cdd:cd19530  81 VFQRARASAPCVIFFDEVDALVPKRGDGGSWA---SERVVNQLLTEMDGLEERSNVFVIAATNRPDIIDPAMLRPGRLDK 157
RecA-like_ATAD1 cd19520
ATPase domain of ATPase family AAA domain-containing protein 1 and similar ATPase domains; ...
 186-343 3.50e-44

ATPase domain of ATPase family AAA domain-containing protein 1 and similar ATPase domains; ATPase family AAA domain-containing protein 1 (ATAD1, also known as Thorase) is an ATPase that plays a critical role in regulating the surface expression of alpha-amino-3-hydroxy-5-methyl-4-isoxazolepropionic acid (AMPA) receptors, thereby regulating synaptic plasticity, learning and memory. This subfamily belongs to the RecA-like NTPase family which includes the NTP binding domain of F1 and V1 H(+)ATPases, DnaB and related helicases as well as bacterial RecA and related eukaryotic and archaeal recombinases. The RecA-like NTPase family also includes bacterial conjugation proteins and related DNA transfer proteins involved in type II and type IV secretion.


Pssm-ID: 410928 [Multi-domain]  Cd Length: 166  Bit Score: 151.81  E-value: 3.50e-44
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6679501  186 DIGGLDNQIQEIKESVELPLTHPEYYEEMGI-KPPKGVILYGPPGTGKTLLAKAVANQTSATFLRVVGSELIQKYLGDGP 264
Cdd:cd19520   1 DIGGLDEVITELKELVILPLQRPELFDNSRLlQPPKGVLLYGPPGCGKTMLAKATAKEAGARFINLQVSSLTDKWYGESQ 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6679501  265 KLVRELFRVAEEHAPSIVFIDEIDAIGTKRydsnSGGEREIQRTM-LELLNQLDGFDSRGDVKVIM--ATNRIETLDPAL 341
Cdd:cd19520  81 KLVAAVFSLASKLQPSIIFIDEIDSFLRQR----SSTDHEATAMMkAEFMSLWDGLSTDGNCRVIVmgATNRPQDLDEAI 156


                ..
gi 6679501  342 IR 343
Cdd:cd19520 157 LR 158
RecA-like_PEX6_r2 cd19527
second of two ATPase domains of Peroxisomal biogenesis factor 6 (PEX6); PEX6(also known as ...
 196-349 6.68e-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: 148.43  E-value: 6.68e-43
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6679501  196 EIKESVELPLTHPEYYEEmGIKPPKGVILYGPPGTGKTLLAKAVANQTSATFLRVVGSELIQKYLGDGPKLVRELFRVAE 275
Cdd:cd19527   4 EILDTIQLPLEHPELFSS-GLRKRSGILLYGPPGTGKTLLAKAIATECSLNFLSVKGPELINMYIGESEANVREVFQKAR 82

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 6679501  276 EHAPSIVFIDEIDAIGTKRYDS-NSGGerEIQRTMLELLNQLDGF-DSRGDVKVIMATNRIETLDPALIRPGRIDR 349
Cdd:cd19527  83 DAKPCVIFFDELDSLAPSRGNSgDSGG--VMDRVVSQLLAELDGMsSSGQDVFVIGATNRPDLLDPALLRPGRFDK 156
RecA-like_VPS4 cd19521
ATPase domain of vacuolar protein sorting-associated protein 4; Vacuolar protein ...
 180-351 1.14e-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: 145.39  E-value: 1.14e-41
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6679501  180 PQETYADIGGLDNQIQEIKESVELPLTHPEYYEEmGIKPPKGVILYGPPGTGKTLLAKAVANQTSATFLRVVGSELIQKY 259
Cdd:cd19521   2 PNVKWEDVAGLEGAKEALKEAVILPVKFPHLFTG-NRKPWSGILLYGPPGTGKSYLAKAVATEANSTFFSVSSSDLVSKW 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6679501  260 LGDGPKLVRELFRVAEEHAPSIVFIDEIDAIGTKRYDSNSGGEREIQRtmlELLNQLDGF--DSRGdVKVIMATNRIETL 337
Cdd:cd19521  81 MGESEKLVKQLFAMARENKPSIIFIDEVDSLCGTRGEGESEASRRIKT---ELLVQMNGVgnDSQG-VLVLGATNIPWQL 156

                       170
                ....*....|....
gi 6679501  338 DPALIRpgRIDRKI 351
Cdd:cd19521 157 DSAIRR--RFEKRI 168
RecA-like_PEX1_r2 cd19526
second of two ATPase domains of Peroxisomal biogenesis factor 1 (PEX1); PEX1(also known as ...
 197-352 2.06e-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: 144.49  E-value: 2.06e-41
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6679501  197 IKESVELPLTHPEYYEEMGIKPPKGVILYGPPGTGKTLLAKAVANQTSATFLRVVGSELIQKYLGDGPKLVRELFRVAEE 276
Cdd:cd19526   5 LEETIEWPSKYPKIFASSPLRLRSGILLYGPPGCGKTLLASAIASECGLNFISVKGPELLNKYIGASEQNVRDLFSRAQS 84

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 6679501  277 HAPSIVFIDEIDAIGTKRYDSNSGgerEIQRTMLELLNQLDGFDSRGDVKVIMATNRIETLDPALIRPGRIDRKIE 352
Cdd:cd19526  85 AKPCILFFDEFDSIAPKRGHDSTG---VTDRVVNQLLTQLDGVEGLDGVYVLAATSRPDLIDPALLRPGRLDKLVY 157
RecA-like_spastin cd19524
ATPase domain of spastin; Spastin is an ATP-dependent microtubule-severing protein involved in ...
 186-343 5.39e-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: 143.45  E-value: 5.39e-41
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6679501  186 DIGGLDNQIQEIKESVELPLTHPEYYeeMGIK-PPKGVILYGPPGTGKTLLAKAVANQTSATFLRVVGSELIQKYLGDGP 264
Cdd:cd19524   1 DIAGQDLAKQALQEMVILPSLRPELF--TGLRaPARGLLLFGPPGNGKTMLAKAVAAESNATFFNISAASLTSKYVGEGE 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6679501  265 KLVRELFRVAEEHAPSIVFIDEIDAIGTKRYDSNSGGEReiqRTMLELLNQLDGFDSRGD--VKVIMATNRIETLDPALI 342
Cdd:cd19524  79 KLVRALFAVARELQPSIIFIDEVDSLLSERSEGEHEASR---RLKTEFLIEFDGVQSNGDdrVLVMGATNRPQELDDAVL 155


                .
gi 6679501  343 R 343
Cdd:cd19524 156 R 156
RecA-like_KTNA1 cd19522
Katanin p60 ATPase-containing subunit A1; Katanin p60 ATPase-containing subunit A1 (KTNA1) is ...
 186-351 7.20e-40

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


Pssm-ID: 410930 [Multi-domain]  Cd Length: 170  Bit Score: 140.89  E-value: 7.20e-40
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6679501  186 DIGGLDNQIQEIKESVELPLTHPEYYEemGIKPP-KGVILYGPPGTGKTLLAKAVANQTSATFLRVVGSELIQKYLGDGP 264
Cdd:cd19522   1 DIADLEEAKKLLEEAVVLPMWMPEFFK--GIRRPwKGVLMVGPPGTGKTLLAKAVATECGTTFFNVSSSTLTSKYRGESE 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6679501  265 KLVRELFRVAEEHAPSIVFIDEIDAIGTKRydsNSGGEREI-QRTMLELLNQLDGF-------DSRGDVKVIMATNRIET 336
Cdd:cd19522  79 KLVRLLFEMARFYAPTTIFIDEIDSICSRR---GTSEEHEAsRRVKSELLVQMDGVggasendDPSKMVMVLAATNFPWD 155

                       170
                ....*....|....*
gi 6679501  337 LDPALIRpgRIDRKI 351
Cdd:cd19522 156 IDEALRR--RLEKRI 168
RecA-like_Figl-1 cd19525
ATPase domain of Fidgetin-Like 1 (FIGL-1); FIGL-1 may participate in DNA repair in the nucleus; ...
 180-343 1.04e-39

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


Pssm-ID: 410933 [Multi-domain]  Cd Length: 186  Bit Score: 140.89  E-value: 1.04e-39
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6679501  180 PQETYADIGGLDNQIQEIKESVELPLTHPEYYeeMGIK-PPKGVILYGPPGTGKTLLAKAVANQTSATFLRVVGSELIQK 258
Cdd:cd19525  17 PPINWADIAGLEFAKKTIKEIVVWPMLRPDIF--TGLRgPPKGILLFGPPGTGKTLIGKCIASQSGATFFSISASSLTSK 94

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6679501  259 YLGDGPKLVRELFRVAEEHAPSIVFIDEIDAIGTKRYDSNSGGEREIQRtmlELLNQLDGFDSRGDVKVIM--ATNRIET 336
Cdd:cd19525  95 WVGEGEKMVRALFSVARCKQPAVIFIDEIDSLLSQRGEGEHESSRRIKT---EFLVQLDGATTSSEDRILVvgATNRPQE 171


                ....*..
gi 6679501  337 LDPALIR 343
Cdd:cd19525 172 IDEAARR 178
RecA-like_NSF-SEC18_r1-like cd19504
first of two ATPase domains of NSF and SEC18, and similar ATPase domains; ...
 187-352 2.09e-30

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: 115.66  E-value: 2.09e-30
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6679501  187 IGGLDNQIQEI-KESVELPLTHPEYYEEMGIKPPKGVILYGPPGTGKTLLAKAVANQTSATFLRVV-GSELIQKYLGDGP 264
Cdd:cd19504   2 IGGLDKEFSDIfRRAFASRVFPPEIVEQLGCKHVKGILLYGPPGTGKTLMARQIGKMLNAREPKIVnGPEILNKYVGESE 81

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6679501  265 KLVRELFRVAEEHAPS--------IVFIDEIDAIGTKRyDSNSGGEREIQRTMLELLNQLDGFDSRGDVKVIMATNRIET 336
Cdd:cd19504  82 ANIRKLFADAEEEQRRlgansglhIIIFDEIDAICKQR-GSMAGSTGVHDTVVNQLLSKIDGVEQLNNILVIGMTNRKDL 160

                       170
                ....*....|....*.
gi 6679501  337 LDPALIRPGRIDRKIE 352
Cdd:cd19504 161 IDEALLRPGRLEVQME 176
RecA-like_fidgetin cd19523
ATPase domain of fidgetin; Fidgetin (FIGN) is a ATP-dependent microtubule severing protein. ...
 186-343 3.19e-30

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


Pssm-ID: 410931 [Multi-domain]  Cd Length: 163  Bit Score: 114.60  E-value: 3.19e-30
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6679501  186 DIGGLDNQIQEIKESVELPLTHPEYYEEMgIKPPKGVILYGPPGTGKTLLAKAVANQTSATFLRVVGSELIQKYLGDGPK 265
Cdd:cd19523   1 DIAGLGALKAAIKEEVLWPLLRPDAFSGL-LRLPRSILLFGPRGTGKTLLGRCLASQLGATFLRLRGSTLVAKWAGEGEK 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6679501  266 LVRELFRVAEEHAPSIVFIDEIDAIGTKRYDsnsgGEREIQRTMLELLNQLDGFDSRGD--VKVIMATNRIETLDPALIR 343
Cdd:cd19523  80 ILQASFLAARCRQPSVLFISDLDALLSSQDD----EASPVGRLQVELLAQLDGVLGSGEdgVLVVCTTSKPEEIDESLRR 155
AAA cd00009
The AAA+ (ATPases Associated with a wide variety of cellular Activities) superfamily ...
 188-355 1.10e-28

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


Pssm-ID: 99707 [Multi-domain]  Cd Length: 151  Bit Score: 110.31  E-value: 1.10e-28
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6679501  188 GGLDNQIQEIKESVELPlthpeyyeemgikPPKGVILYGPPGTGKTLLAKAVANQT---SATFLRVVGSELIQKYLG--- 261
Cdd:cd00009   1 VGQEEAIEALREALELP-------------PPKNLLLYGPPGTGKTTLARAIANELfrpGAPFLYLNASDLLEGLVVael 67

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6679501  262 DGPKLVRELFRVAEEHAPSIVFIDEIDAIGtkrydsnsggeREIQRTMLELLNQL-DGFDSRGDVKVIMATNRIETLDPA 340
Cdd:cd00009  68 FGHFLVRLLFELAEKAKPGVLFIDEIDSLS-----------RGAQNALLRVLETLnDLRIDRENVRVIGATNRPLLGDLD 136

                       170
                ....*....|....*
gi 6679501  341 LIRPGRIDRKIEFPL 355
Cdd:cd00009 137 RALYDRLDIRIVIPL 151
RecA-like_BCS1 cd19510
Mitochondrial chaperone BCS1; Mitochondrial chaperone BCS1 is necessary for the assembly of ...
 197-353 2.48e-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: 100.89  E-value: 2.48e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6679501  197 IKESVELPLTHPEYYEEMGIKPPKGVILYGPPGTGKTLLAKAVANqtsatFLR--VVGSELIQKYLGDgpKLVRELFRVA 274
Cdd:cd19510   1 IIDDLKDFIKNEDWYNDRGIPYRRGYLLYGPPGTGKSSFIAALAG-----ELDydICDLNLSEVVLTD--DRLNHLLNTA 73

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6679501  275 EEHapSIVFIDEIDA-----IGTKRYDSNSGGEREIqrTMLELLNQLDGFDSRGDVKVIMATNRIETLDPALIRPGRIDR 349
Cdd:cd19510  74 PKQ--SIILLEDIDAafesrEHNKKNPSAYGGLSRV--TFSGLLNALDGVASSEERIVFMTTNHIERLDPALIRPGRVDM 149


                ....
gi 6679501  350 KIEF 353
Cdd:cd19510 150 KIYM 153
ycf46 CHL00195
Ycf46; Provisional
 179-427 1.54e-24

Ycf46; Provisional


Pssm-ID: 177094 [Multi-domain]  Cd Length: 489  Bit Score: 105.49  E-value: 1.54e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6679501   179 APQETYADIGGLDNQIQEIKESVElplTHPEYYEEMGIKPPKGVILYGPPGTGKTLLAKAVANQTSATFLRVVGSELIQK 258
Cdd:CHL00195 222 SVNEKISDIGGLDNLKDWLKKRST---SFSKQASNYGLPTPRGLLLVGIQGTGKSLTAKAIANDWQLPLLRLDVGKLFGG 298

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6679501   259 YLGDGPKLVRELFRVAEEHAPSIVFIDEIDAIGTKRYDSN-SGGEREIQRTMLELLNQldgfdSRGDVKVIMATNRIETL 337
Cdd:CHL00195 299 IVGESESRMRQMIRIAEALSPCILWIDEIDKAFSNSESKGdSGTTNRVLATFITWLSE-----KKSPVFVVATANNIDLL 373

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6679501   338 DPALIRPGRIDRKIEFPLPDEKTKKRIFQIHTSRMTLADDVTLDDLIMAK--DDLSGADIKAICTEAGLMALRERRmKVT 415
Cdd:CHL00195 374 PLEILRKGRFDEIFFLDLPSLEEREKIFKIHLQKFRPKSWKKYDIKKLSKlsNKFSGAEIEQSIIEAMYIAFYEKR-EFT 452

                        250
                 ....*....|..
gi 6679501   416 NEDFKKSKENVL 427
Cdd:CHL00195 453 TDDILLALKQFI 464
RecA-like_Ycf46-like cd19507
ATPase domain of Ycf46 and similar ATPase domains; Ycf46 may play a role in the regulation of ...
 186-349 1.24e-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: 96.67  E-value: 1.24e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6679501  186 DIGGLDNqiqeIKESVEL--PLTHPEYyEEMGIKPPKGVILYGPPGTGKTLLAKAVANQTSATFLRVVGSELIQKYLGDG 263
Cdd:cd19507   1 DVGGLDN----LKDWLKKrkAAFSKQA-SAYGLPTPKGLLLVGIQGTGKSLTAKAIAGVWQLPLLRLDMGRLFGGLVGES 75

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6679501  264 PKLVRELFRVAEEHAPSIVFIDEID-AIGTKRYDSNSGGEREIQRTMLELLNQldgfdSRGDVKVIMATNRIETLDPALI 342
Cdd:cd19507  76 ESRLRQMIQTAEAIAPCVLWIDEIEkGFSNADSKGDSGTSSRVLGTFLTWLQE-----KKKPVFVVATANNVQSLPPELL 150


                ....*..
gi 6679501  343 RPGRIDR 349
Cdd:cd19507 151 RKGRFDE 157
AAA smart00382
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ...
 218-357 3.82e-20

ATPases associated with a variety of cellular activities; AAA - ATPases associated with a variety of cellular activities. This profile/alignment only detects a fraction of this vast family. The poorly conserved N-terminal helix is missing from the alignment.


Pssm-ID: 214640 [Multi-domain]  Cd Length: 148  Bit Score: 86.66  E-value: 3.82e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6679501     218 PPKGVILYGPPGTGKTLLAKAVANQTSATFLRVV-----------------GSELIQKYLGDGPKLVRELFRVAEEHAPS 280
Cdd:smart00382   1 PGEVILIVGPPGSGKTTLARALARELGPPGGGVIyidgedileevldqlllIIVGGKKASGSGELRLRLALALARKLKPD 80

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 6679501     281 IVFIDEIDAIGTKrydsnsggEREIQRTMLELLNQLDGFDSRGDVKVIMATNRIETLDPALIRPgRIDRKIEFPLPD 357
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 ...
 222-342 2.32e-14

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


Pssm-ID: 410916 [Multi-domain]  Cd Length: 199  Bit Score: 71.32  E-value: 2.32e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6679501  222 VILYGPPGTGKTLLAKAVANQTS---------ATFLRVVGSELIQKYLGDGPKLVRELFR-----VAEEHAPSIVFIDEI 287
Cdd:cd19508  55 VLLHGPPGTGKTSLCKALAQKLSirlssryryGQLIEINSHSLFSKWFSESGKLVTKMFQkiqelIDDKDALVFVLIDEV 134

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 6679501  288 DAIGTKRYDSNSGGE-REIQRTMLELLNQLDGFDSRGDVKVIMATNRIETLDPALI 342
Cdd:cd19508 135 ESLAAARSASSSGTEpSDAIRVVNAVLTQIDRIKRYHNNVILLTSNLLEKIDVAFV 190
RecA-like_ATAD3-like cd19512
ATPase domains of ATPase AAA-domain protein 3A (ATAD3A), -3B, and -3C, and similar ATPase ...
 220-353 2.64e-11

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


Pssm-ID: 410920 [Multi-domain]  Cd Length: 150  Bit Score: 61.39  E-value: 2.64e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6679501  220 KGVILYGPPGTGKTLLAKAVANQTSATFLRVVGSELIQkyLG-DGPKLVRELFRVAEEHAPS-IVFIDEIDAIGTKRyds 297
Cdd:cd19512  23 RNILFYGPPGTGKTLFAKKLALHSGMDYAIMTGGDVAP--MGrEGVTAIHKVFDWANTSRRGlLLFVDEADAFLRKR--- 97

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 6679501  298 NSGGEREIQRTMLELLNQLDGFDSRgDVKVIMATNRIETLDPALirPGRIDRKIEF 353
Cdd:cd19512  98 STEKISEDLRAALNAFLYRTGEQSN-KFMLVLASNQPEQFDWAI--NDRIDEMVEF 150
AAA_lid_3 pfam17862
AAA+ lid domain; This entry represents the alpha helical AAA+ lid domain that is found to the ...
 377-421 4.42e-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: 54.85  E-value: 4.42e-10
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 6679501    377 DVTLDDLIMAKDDLSGADIKAICTEAGLMALRERRMKVTNEDFKK 421
Cdd:pfam17862   1 DVDLEELAERTEGFSGADLEALCREAALAALRRGLEAVTQEDLEE 45
RarA COG2256
Replication-associated recombination protein RarA (DNA-dependent ATPase) [Replication, ...
 222-287 6.76e-10

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


Pssm-ID: 441857 [Multi-domain]  Cd Length: 439  Bit Score: 60.84  E-value: 6.76e-10
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 6679501  222 VILYGPPGTGKTLLAKAVANQTSATFLRV--VGSeliqkylgdGPKLVRELFRVAEEHA----PSIVFIDEI 287
Cdd:COG2256  52 MILWGPPGTGKTTLARLIANATDAEFVALsaVTS---------GVKDIREVIEEARERRaygrRTILFVDEI 114
RecA-like_Ycf2 cd19505
ATPase domain of plant YCF2; Ycf2 is a chloroplast ATPase which has an essential function; ...
 213-353 2.61e-09

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: 55.84  E-value: 2.61e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6679501  213 EMGIKPPKGVILYGPPGTGKTLLAKAVANQTSATFLRVVGSELIQKYLGDGPKLVR--------------ELFRVAEEHA 278
Cdd:cd19505   6 RLGLSPSKGILLIGSIETGRSYLIKSLAANSYVPLIRISLNKLLYNKPDFGNDDWIdgmlilkeslhrlnLQFELAKAMS 85

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 6679501  279 PSIVFIDEIDAIGTKRYDSNSGGEReiqRTMLELLNQLDGFDSRGDVK----VIMATNRIETLDPALIRPGRIDRKIEF 353
Cdd:cd19505  86 PCIIWIPNIHELNVNRSTQNLEEDP---KLLLGLLLNYLSRDFEKSSTrnilVIASTHIPQKVDPALIAPNRLDTCINI 161
Prot_ATP_ID_OB pfam16450
Proteasomal ATPase OB C-terminal domain; This is the interdomain (ID) or oligonucleotide ...
 109-163 4.71e-09

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


Pssm-ID: 465118 [Multi-domain]  Cd Length: 56  Bit Score: 52.12  E-value: 4.71e-09
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 6679501    109 VGTLEEIIDDNHAIVSTSVGSEHYVSILSFVDKDLLEPGCSVLLNHKVHAVIGVL 163
Cdd:pfam16450   1 VATVVEVLDDGRALVKSSGGEERVVRLAGSLDEEKLRPGDRVLLDPRSGYALEVL 55
PRK13342 PRK13342
recombination factor protein RarA; Reviewed
 222-287 5.95e-09

recombination factor protein RarA; Reviewed


Pssm-ID: 237355 [Multi-domain]  Cd Length: 413  Bit Score: 57.79  E-value: 5.95e-09
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6679501   222 VILYGPPGTGKTLLAKAVANQTSATFLRVVGSEliqkylgDGPKLVRELFRVAEEHAPS----IVFIDEI 287
Cdd:PRK13342  39 MILWGPPGTGKTTLARIIAGATDAPFEALSAVT-------SGVKDLREVIEEARQRRSAgrrtILFIDEI 101
T7SS_EccA TIGR03922
type VII secretion AAA-ATPase EccA; This model represents the AAA family ATPase, EccA, of the ...
 189-390 2.30e-08

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: 56.01  E-value: 2.30e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6679501    189 GLD---NQIQEIKESVELPLTHpeyyEEMGIKPP---KGVILYGPPGTGKTLLAKAVANQTSA-TFLR------VVGSEL 255
Cdd:TIGR03922 280 GLErvkRQVAALKSSTAMALAR----AERGLPVAqtsNHMLFAGPPGTGKTTIARVVAKIYCGlGVLRkplvreVSRADL 355

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6679501    256 IQKYLGDGPKLVRELFrvaEEHAPSIVFIDEIDAIGTKRYDSNSGGEREIQRTMLELLNqldgfDSRGDVKVIMA----- 330
Cdd:TIGR03922 356 IGQYIGESEAKTNEII---DSALGGVLFLDEAYTLVETGYGQKDPFGLEAIDTLLARME-----NDRDRLVVIGAgyrkd 427

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 6679501    331 TNRIETLDPALirPGRIDRKIEFP--LPDEktkkrIFQIhTSRMTLADDVTLDDliMAKDDL 390
Cdd:TIGR03922 428 LDKFLEVNEGL--RSRFTRVIEFPsySPDE-----LVEI-ARRMATERDSVLDD--AAADAL 479
TIGR02928 TIGR02928
orc1/cdc6 family replication initiation protein; Members of this protein family are found ...
 218-426 3.25e-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: 55.33  E-value: 3.25e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6679501    218 PPKGVILYGPPGTGKTLLAKAVANQ----TSATFLRV---------------VGSELIQKYLGDGP----------KLVR 268
Cdd:TIGR02928  39 RPSNVFIYGKTGTGKTAVTKYVMKEleeaAEDRDVRVvtvyvncqildtlyqVLVELANQLRGSGEevpttglstsEVFR 118

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6679501    269 ELFRVAEEHAPSIVFI-DEIDAIgtkrydSNSGGEREIQRTMLELLNQLDGfdsrGDVKVIMATNRI---ETLDPAlIRP 344
Cdd:TIGR02928 119 RLYKELNERGDSLIIVlDEIDYL------VGDDDDLLYQLSRARSNGDLDN----AKVGVIGISNDLkfrENLDPR-VKS 187

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6679501    345 GRIDRKIEFPLPDEktkKRIFQIHTSRMTLA--DDVTLDDLI------MAKDdlSGADIKAICT--EAGLMALRERRMKV 414
Cdd:TIGR02928 188 SLCEEEIIFPPYDA---EELRDILENRAEKAfyDGVLDDGVIplcaalAAQE--HGDARKAIDLlrVAGEIAEREGAERV 262

                         250
                  ....*....|..
gi 6679501    415 TNEDFKKSKENV 426
Cdd:TIGR02928 263 TEDHVEKAQEKI 274
RecA-like_HslU cd19498
ATP-dependent protease ATPase subunit HslU; HslU is a component of the ATP-dependent protease ...
 219-313 1.47e-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: 51.23  E-value: 1.47e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6679501  219 PKGVILYGPPGTGKTLLAKAVANQTSATFLRVVGSELIQ-KYLG-DGPKLVRELfrvaeehAPSIVFIDEIDAIGTKRYD 296
Cdd:cd19498  46 PKNILMIGPTGVGKTEIARRLAKLAGAPFIKVEATKFTEvGYVGrDVESIIRDL-------VEGIVFIDEIDKIAKRGGS 118

                        90
                ....*....|....*...
gi 6679501  297 SNSGGERE-IQRTMLELL 313
Cdd:cd19498 119 SGPDVSREgVQRDLLPIV 136
RecA-like_ClpB_Hsp104-like cd19499
Chaperone protein ClpB/Hsp104 subfamily; Bacterial Caseinolytic peptidase B (ClpB) and ...
 217-353 6.11e-07

Chaperone protein ClpB/Hsp104 subfamily; Bacterial Caseinolytic peptidase B (ClpB) and eukaryotic Heat shock protein 104 (Hsp104) are ATP-dependent molecular chaperones and essential proteins of the heat-shock response. ClpB/Hsp104 ATPases, in concert with the DnaK/Hsp70 chaperone system, disaggregate and reactivate aggregated proteins. This RecA-like_ClpB_Hsp104_like subfamily belongs to the RecA-like NTPase family which includes the NTP binding domain of F1 and V1 H(+)ATPases, DnaB and related helicases as well as bacterial RecA and related eukaryotic and archaeal recombinases. The RecA-like NTPase family also includes bacterial conjugation proteins and related DNA transfer proteins involved in type II and type IV secretion.


Pssm-ID: 410907 [Multi-domain]  Cd Length: 178  Bit Score: 49.48  E-value: 6.11e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6679501  217 KPPKGVILYGPPGTGKTLLAKAVA---NQTSATFLRVVGSELIQKY-----LGDGPKLV--RELFRVAEE---HAPSIVF 283
Cdd:cd19499  39 RPIGSFLFLGPTGVGKTELAKALAellFGDEDNLIRIDMSEYMEKHsvsrlIGAPPGYVgyTEGGQLTEAvrrKPYSVVL 118

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 6679501  284 IDEIDAigtkrydsnsgGEREIQRTMLELLNqlDGF--DSRG---DVK---VIMATNrieTLDPALIrpGRIDRKIEF 353
Cdd:cd19499 119 LDEIEK-----------AHPDVQNLLLQVLD--DGRltDSHGrtvDFKntiIIMTSN---HFRPEFL--NRIDEIVVF 178
AAA_2 pfam07724
AAA domain (Cdc48 subfamily); This Pfam entry includes some of the AAA proteins not detected ...
 219-313 1.12e-06

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: 48.35  E-value: 1.12e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6679501    219 PKGVILY-GPPGTGKTLLAKAVANQ---TSATFLRVVGSELIQKYL-----GDGPKLVR-----ELFRVAEEHAPSIVFI 284
Cdd:pfam07724   2 PIGSFLFlGPTGVGKTELAKALAELlfgDERALIRIDMSEYMEEHSvsrliGAPPGYVGyeeggQLTEAVRRKPYSIVLI 81

                          90       100
                  ....*....|....*....|....*....
gi 6679501    285 DEIDAIGtkrydsnsggeREIQRTMLELL 313
Cdd:pfam07724  82 DEIEKAH-----------PGVQNDLLQIL 99
CDC6 COG1474
Cdc6-related protein, AAA superfamily ATPase [Replication, recombination and repair];
191-438 1.34e-06

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


Pssm-ID: 441083 [Multi-domain]  Cd Length: 389  Bit Score: 50.23  E-value: 1.34e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6679501  191 DNQIQEIKESVElPLTHPEyyeemgikPPKGVILYGPPGTGKTLLAKAVANQ---------TSATFLRV----------V 251
Cdd:COG1474  32 EEEIEELASALR-PALRGE--------RPSNVLIYGPTGTGKTAVAKYVLEEleeeaeergVDVRVVYVncrqastryrV 102

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6679501  252 GSELIQKyLGDGP----------KLVRELFRVAEEHAPSIVFI-DEIDAIGTKRYDsnsggerEIQRTMLELLNQLDGfd 320
Cdd:COG1474 103 LSRILEE-LGSGEdipstglstdELFDRLYEALDERDGVLVVVlDEIDYLVDDEGD-------DLLYQLLRANEELEG-- 172

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6679501  321 srGDVKVIMATNRI---ETLDPALIRPGRiDRKIEFPlP---DEktkkrIFQIHTSR--MTLADDVTLDDLI--MAkdDL 390
Cdd:COG1474 173 --ARVGVIGISNDLeflENLDPRVKSSLG-EEEIVFP-PydaDE-----LRDILEDRaeLAFYDGVLSDEVIplIA--AL 241

                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....
gi 6679501  391 SGADI----KAICT--EAGLMALRERRMKVTNEDFKKSKENVLYKKQEGTPEGL 438
Cdd:COG1474 242 AAQEHgdarKAIDLlrVAGEIAEREGSDRVTEEHVREAREKIERDRLLEVLRGL 295
AAA_5 pfam07728
AAA domain (dynein-related subfamily); This Pfam entry includes some of the AAA proteins not ...
 221-343 1.92e-06

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


Pssm-ID: 400191 [Multi-domain]  Cd Length: 135  Bit Score: 46.90  E-value: 1.92e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6679501    221 GVILYGPPGTGKTLLAKAVANQTS-ATFLRVVGS------ELIQKYL--GDGPKLV-RELFRVAEEhaPSIVFIDEIDAI 290
Cdd:pfam07728   1 GVLLVGPPGTGKTELAERLAAALSnRPVFYVQLTrdtteeDLFGRRNidPGGASWVdGPLVRAARE--GEIAVLDEINRA 78

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 6679501    291 gtkrydsnsggEREIQRTMLELLN-----QLDGF----DSRGDVKVIMATNRIET----LDPALIR 343
Cdd:pfam07728  79 -----------NPDVLNSLLSLLDerrllLPDGGelvkAAPDGFRLIATMNPLDRglneLSPALRS 133
PRK04195 PRK04195
replication factor C large subunit; Provisional
 217-305 5.31e-06

replication factor C large subunit; Provisional


Pssm-ID: 235250 [Multi-domain]  Cd Length: 482  Bit Score: 48.38  E-value: 5.31e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6679501   217 KPPKGVILYGPPGTGKTLLAKAVAN-------------QTSATFL-RVVGSELIQKYLGDGPKlvrelfrvaeehapSIV 282
Cdd:PRK04195  37 KPKKALLLYGPPGVGKTSLAHALANdygwevielnasdQRTADVIeRVAGEAATSGSLFGARR--------------KLI 102

                         90       100
                 ....*....|....*....|...
gi 6679501   283 FIDEIDAIgTKRYDsnSGGEREI 305
Cdd:PRK04195 103 LLDEVDGI-HGNED--RGGARAI 122
MoxR COG0714
MoxR-like ATPase [General function prediction only]; MoxR-like ATPase is part of the Pathway ...
 222-288 1.28e-05

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


Pssm-ID: 440478 [Multi-domain]  Cd Length: 292  Bit Score: 46.70  E-value: 1.28e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6679501  222 VILYGPPGTGKTLLAKAVANQTSATFLRV-----------VGSELIQKYLGD-----GPklvreLFRvaeehapSIVFID 285
Cdd:COG0714  34 LLLEGVPGVGKTTLAKALARALGLPFIRIqftpdllpsdiLGTYIYDQQTGEfefrpGP-----LFA-------NVLLAD 101


                ...
gi 6679501  286 EID 288
Cdd:COG0714 102 EIN 104
DUF815 pfam05673
Protein of unknown function (DUF815); This family consists of several bacterial proteins of ...
 185-285 1.49e-05

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


Pssm-ID: 428578 [Multi-domain]  Cd Length: 250  Bit Score: 46.37  E-value: 1.49e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6679501    185 ADIGGLDNQIQEIKESVELPLTHpeyyeemgiKPPKGVILYGPPGTGKTLLAKAVANQTSATFLRVVgsELIQKYLGDGP 264
Cdd:pfam05673  28 DDLVGIERQKEALIRNTRRFLAG---------LPANNVLLWGARGTGKSSLVKALLNEYADQGLRLI--EVDKEDLGDLP 96

                          90       100
                  ....*....|....*....|.
gi 6679501    265 KLVRELFRVAEEHapsIVFID 285
Cdd:pfam05673  97 DLVDLLRDRPYRF---ILFCD 114
McrB COG1401
5-methylcytosine-specific restriction endonuclease McrBC, GTP-binding regulatory subunit McrB ...
 176-287 2.12e-05

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


Pssm-ID: 441011 [Multi-domain]  Cd Length: 477  Bit Score: 46.69  E-value: 2.12e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6679501  176 VEKAPQETYADIGGLDNQIQEIKESVELPLTHPEYYEEMG-------------IKPPKGVILYGPPGTGKTLLAKAVANQ 242
Cdd:COG1401 165 LLAAPEDLSADALAAELSAAEELYSEDLESEDDYLKDLLRekfeetleaflaaLKTKKNVILAGPPGTGKTYLARRLAEA 244

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 6679501  243 TSAT----FLRVV------GSELIQKY---LGDG-----PKLVRELFRVAEEH--APSIVFIDEI 287
Cdd:COG1401 245 LGGEdngrIEFVQfhpswsYEDFLLGYrpsLDEGkyeptPGIFLRFCLKAEKNpdKPYVLIIDEI 309
RecA-like_superfamily cd01120
RecA-like_NTPases; RecA-like NTPases. This superfamily includes the NTP binding domain of F1 ...
 222-338 2.43e-05

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


Pssm-ID: 410865 [Multi-domain]  Cd Length: 119  Bit Score: 43.65  E-value: 2.43e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6679501  222 VILYGPPGTGKTLLAKAVANQTSATFLRVVGSELIQKYLgdgpklvRELFRVAEEHAPSIVFIDEIDAIGTKRYDSNSGG 301
Cdd:cd01120   1 ILITGPPGSGKTTLLLQFAEQALLSDEPVIFISFLDTIL-------EAIEDLIEEKKLDIIIIDSLSSLARASQGDRSSE 73

                        90       100       110
                ....*....|....*....|....*....|....*..
gi 6679501  302 EREIQRTMLELLNQLDgfdsrgdvKVIMATNRIETLD 338
Cdd:cd01120  74 LLEDLAKLLRAARNTG--------ITVIATIHSDKFD 102
PRK13341 PRK13341
AAA family ATPase;
223-287 3.61e-05

AAA family ATPase;


Pssm-ID: 237354 [Multi-domain]  Cd Length: 725  Bit Score: 46.20  E-value: 3.61e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6679501   223 ILYGPPGTGKTLLAKAVANQTSATFLrVVGSELiqkylgDGPKLVRELFRVAEEHAP-----SIVFIDEI 287
Cdd:PRK13341  56 ILYGPPGVGKTTLARIIANHTRAHFS-SLNAVL------AGVKDLRAEVDRAKERLErhgkrTILFIDEV 118
AAA_22 pfam13401
AAA domain;
222-330 5.25e-05

AAA domain;


Pssm-ID: 379165 [Multi-domain]  Cd Length: 129  Bit Score: 42.71  E-value: 5.25e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6679501    222 VILYGPPGTGKTLLAKAVANQ-----------------TSATFLRVVGSELIQKYLGDGPK--LVRELFRVAEEHAPSIV 282
Cdd:pfam13401   8 LVLTGESGTGKTTLLRRLLEQlpevrdsvvfvdlpsgtSPKDLLRALLRALGLPLSGRLSKeeLLAALQQLLLALAVAVV 87

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 6679501    283 F-IDEIDAigtkrydsnsggereIQRTMLELLNQLDGFdSRGDVKVIMA 330
Cdd:pfam13401  88 LiIDEAQH---------------LSLEALEELRDLLNL-SSKLLQLILV 120
RecA-like_Lon cd19500
lon protease homolog 2 peroxisomal; Lon protease (also known as Lon peptidase) is an ...
 220-291 5.75e-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: 43.70  E-value: 5.75e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6679501  220 KGVIL--YGPPGTGKTLLAKAVANQTSATFLRV-VG-----SELI---QKYLGDGPKLVRELFRVAEEHAPSIVfIDEID 288
Cdd:cd19500  36 KGPILclVGPPGVGKTSLGKSIARALGRKFVRIsLGgvrdeAEIRghrRTYVGAMPGRIIQALKKAGTNNPVFL-LDEID 114


                ...
gi 6679501  289 AIG 291
Cdd:cd19500 115 KIG 117
ruvB PRK00080
Holliday junction branch migration DNA helicase RuvB;
222-287 6.17e-05

Holliday junction branch migration DNA helicase RuvB;


Pssm-ID: 234619 [Multi-domain]  Cd Length: 328  Bit Score: 44.74  E-value: 6.17e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 6679501   222 VILYGPPGTGKTLLAKAVANQTSATfLRVVGSELIQKyLGDgpkLVReLFRVAEEHapSIVFIDEI 287
Cdd:PRK00080  54 VLLYGPPGLGKTTLANIIANEMGVN-IRITSGPALEK-PGD---LAA-ILTNLEEG--DVLFIDEI 111
DnaC COG1484
DNA replication protein DnaC [Replication, recombination and repair];
216-270 9.07e-05

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


Pssm-ID: 441093 [Multi-domain]  Cd Length: 242  Bit Score: 43.62  E-value: 9.07e-05
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 6679501  216 IKPPKGVILYGPPGTGKTLLAKAVANQ-----TSATFLRVvgseliqkylgdgPKLVREL 270
Cdd:COG1484  96 IERGENLILLGPPGTGKTHLAIALGHEacragYRVRFTTA-------------PDLVNEL 142
COG2842 COG2842
Bacteriophage DNA transposition protein, AAA+ family ATPase [Mobilome: prophages, transposons]; ...
 222-421 1.01e-04

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


Pssm-ID: 442090 [Multi-domain]  Cd Length: 254  Bit Score: 43.79  E-value: 1.01e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6679501  222 VILYGPPGTGKTLLAKAVANQ-------------TSATFLRVVGSELiqkYLGDGPKLVRELFRVAEEH---APSIVFID 285
Cdd:COG2842  53 GVVYGESGVGKTTAAREYANRnpnviyvtaspswTSKELLEELAEEL---GIPAPPGTIADLRDRILERlagTGRLLIID 129

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6679501  286 EIDAIGTKrydsnsggereiqrtMLELLNQLdgFDsRGDVKVIMATNriETLDPALIRPGRIDRKIEFPLPDEKTKKRIF 365
Cdd:COG2842 130 EADHLKPK---------------ALEELRDI--HD-ETGVGVVLIGM--ERLPAKLKRYEQLYSRIGFWVEFKPLSLEDV 189

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 6679501  366 QIhtsrmtLAD---DVTLDDLIMAKDDLSGADIKAICT---EAGLMALRERRMKVTNEDFKK 421
Cdd:COG2842 190 RA------LAEawgELTDPDLLELLHRITRGNLRRLDRtlrLAARAAKRNGLTKITLDHVRA 245
44 PHA02544
clamp loader, small subunit; Provisional
 223-367 1.29e-04

clamp loader, small subunit; Provisional


Pssm-ID: 222866 [Multi-domain]  Cd Length: 316  Bit Score: 43.83  E-value: 1.29e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6679501   223 ILYGP-PGTGKTLLAKAVANQTSATFLRVVGSEliqkylgDGPKLVR-ELFRVAE----EHAPSIVFIDEIDAIGTKryd 296
Cdd:PHA02544  46 LLHSPsPGTGKTTVAKALCNEVGAEVLFVNGSD-------CRIDFVRnRLTRFAStvslTGGGKVIIIDEFDRLGLA--- 115

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 6679501   297 snsggerEIQRTMLELLNQLDgfdsrGDVKVIMATNRIETLDPALIrpGRIdRKIEFPLPDEKTK--------KRIFQI 367
Cdd:PHA02544 116 -------DAQRHLRSFMEAYS-----KNCSFIITANNKNGIIEPLR--SRC-RVIDFGVPTKEEQiemmkqmiVRCKGI 179
RecA-like_ClpX cd19497
ATP-dependent Clp protease ATP-binding subunit ClpX; ClpX is a component of the ATP-dependent ...
 222-293 1.95e-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: 42.97  E-value: 1.95e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6679501  222 VILYGPPGTGKTLLAK----------AVANQTSATFLRVVG-------SELIQKYLGDGPKlvrelfrvAEEhapSIVFI 284
Cdd:cd19497  53 ILLIGPTGSGKTLLAQtlakildvpfAIADATTLTEAGYVGedvenilLKLLQAADYDVER--------AQR---GIVYI 121


                ....*....
gi 6679501  285 DEIDAIGTK 293
Cdd:cd19497 122 DEIDKIARK 130
IS21_help_AAA NF038214
IS21-like element helper ATPase IstB; This protein family model resembles PF01695, but was ...
 222-287 3.49e-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: 3.49e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 6679501   222 VILYGPPGTGKTLLAKAVANQ-----TSATFLRVvgSELIQKYL---GDGpKLVRELFRVAeehAPSIVFIDEI 287
Cdd:NF038214  93 VLLLGPPGTGKTHLAIALGYAacrqgYRVRFTTA--ADLVEQLAqarADG-RLGRLLRRLA---RYDLLIIDEL 160
RuvB_N pfam05496
Holliday junction DNA helicase RuvB P-loop domain; The RuvB protein makes up part of the ...
 222-287 3.70e-04

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


Pssm-ID: 398900 [Multi-domain]  Cd Length: 159  Bit Score: 40.95  E-value: 3.70e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 6679501    222 VILYGPPGTGKTLLAKAVANQTSATFlRVVGSELIQKyLGDGPKLVRELfrvaEEHapSIVFIDEI 287
Cdd:pfam05496  36 VLLYGPPGLGKTTLANIIANEMGVNI-RITSGPAIER-PGDLAAILTNL----EPG--DVLFIDEI 93
RecA-like_IQCA1 cd19506
ATPase domain of IQ and AAA domain-containing protein 1 (IQCA1); IQCA1 (also known as dynein ...
 220-286 5.51e-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: 40.59  E-value: 5.51e-04
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 6679501  220 KGVILYGPPGTGKTLLAKAVANQTSATFLRVVGSELIQKYLGDG--PKLVRELFRVAEEHAPSIVFIDE 286
Cdd:cd19506  27 KSLLLAGPSGVGKKMLVHAICTETGANLFNLSPSNIAGKYPGKNglQMMLHLVLKVARQLQPSVIWIGD 95
PRK08116 PRK08116
hypothetical protein; Validated
 211-251 5.55e-04

hypothetical protein; Validated


Pssm-ID: 236153 [Multi-domain]  Cd Length: 268  Bit Score: 41.54  E-value: 5.55e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|.
gi 6679501   211 YEEMGiKPPKGVILYGPPGTGKTLLAKAVANQTSATFLRVV 251
Cdd:PRK08116 107 FEEMK-KENVGLLLWGSVGTGKTYLAACIANELIEKGVPVI 146
RecA-like cd01393
RecA family; RecA is a bacterial enzyme which has roles in homologous recombination, DNA ...
 224-344 7.47e-04

RecA family; RecA is a bacterial enzyme which has roles in homologous recombination, DNA repair, and the induction of the SOS response. RecA couples ATP hydrolysis to DNA strand exchange. While prokaryotes have a single RecA protein, eukaryotes have multiple RecA homologs such as Rad51, DMC1 and Rad55/57. Archaea have the RecA-like homologs RadA and RadB.


Pssm-ID: 410881 [Multi-domain]  Cd Length: 185  Bit Score: 40.41  E-value: 7.47e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6679501  224 LYGPPGTGKTLLA-KAVAN-----------QTSATF---------LRVVGSELIQKYLGDGPKLVR-----ELFRVAEEH 277
Cdd:cd01393   6 IYGPPGSGKTQLAlQLAANalllgggvvwiDTEGAFppsrlvqilEASPSSELELAEALSRLLYFRppdtlAHLLALDSL 85

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6679501  278 AP--------SIVFIDEIDAIGTKRYDSNSGGEREI---QRTMLELLNQLDGFDSRGDVKVI----MATNRIETLDPALI 342
Cdd:cd01393  86 PEslfpppntSLVVVDSVSALFRKAFPRGGDGDSSSslrARLLSQLARALQKLAAQFNLAVVvtnqVTTKIRGGSGASLV 165


                ..
gi 6679501  343 RP 344
Cdd:cd01393 166 PP 167
ruvB TIGR00635
Holliday junction DNA helicase, RuvB subunit; All proteins in this family for which functions ...
 222-291 8.24e-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: 41.13  E-value: 8.24e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6679501    222 VILYGPPGTGKTLLAKAVANQTSaTFLRVVGSELIQKylgdgPKLVRELFRVAEEHapSIVFIDEIDAIG 291
Cdd:TIGR00635  33 LLLYGPPGLGKTTLAHIIANEMG-VNLKITSGPALEK-----PGDLAAILTNLEEG--DVLFIDEIHRLS 94
ExeA COG3267
Type II secretory pathway ATPase component GspA/ExeA/MshM [Intracellular trafficking, ...
 215-286 3.42e-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: 39.00  E-value: 3.42e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6679501  215 GIKPPKGVI-LYGPPGTGKTLLAKAVANQ---------------TSATFLRVVGSELIQKYLGDGPK-----LVRELFRV 273
Cdd:COG3267  38 ALAQGGGFVvLTGEVGTGKTTLLRRLLERlpddvkvayipnpqlSPAELLRAIADELGLEPKGASKAdllrqLQEFLLEL 117

                        90
                ....*....|...
gi 6679501  274 AEEHAPSIVFIDE 286
Cdd:COG3267 118 AAAGRRVVLIIDE 130
ycf2 CHL00206
Ycf2; Provisional
 213-318 3.99e-03

Ycf2; Provisional


Pssm-ID: 214396 [Multi-domain]  Cd Length: 2281  Bit Score: 39.89  E-value: 3.99e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6679501    213 EMGIKPPKGVILYGPPGTGKTLLAKAVANQTSATFLRVvgseLIQKYLGDGPKLvrelfrvaeehapsiVFIDEIDAIGT 292
Cdd:CHL00206 1624 RLALSPSRGILVIGSIGTGRSYLVKYLATNSYVPFITV----FLNKFLDNKPKG---------------FLIDDIDIDDS 1684

                          90       100
                  ....*....|....*....|....*.
gi 6679501    293 KRYDSNSGGEREIQRTMLELLNQLDG 318
Cdd:CHL00206 1685 DDIDDSDDIDRDLDTELLTMMNALTM 1710
COG0645 COG0645
Predicted kinase, contains AAA domain [General function prediction only];
222-278 4.06e-03

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


Pssm-ID: 440410 [Multi-domain]  Cd Length: 164  Bit Score: 37.97  E-value: 4.06e-03
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 6679501  222 VILYGPPGTGKTLLAKAVANQTSATFLR--VVGSEL-------IQKYLGDGPKLVRELFRVAEEHA 278
Cdd:COG0645   2 ILVCGLPGSGKSTLARALAERLGAVRLRsdVVRKRLfgaglapLERSPEATARTYARLLALARELL 67
DnaA COG0593
Chromosomal replication initiation ATPase DnaA [Replication, recombination and repair];
224-378 4.41e-03

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


Pssm-ID: 440358 [Multi-domain]  Cd Length: 303  Bit Score: 39.02  E-value: 4.41e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6679501  224 LYGPPGTGKTLLAKAVANQTSATF--LRVV-------GSELIQKYLGDGPKLVRELFRvaeehAPSIVFIDEIDAIGTKR 294
Cdd:COG0593  39 LYGGVGLGKTHLLHAIGNEALENNpgARVVyltaeefTNDFINAIRNNTIEEFKEKYR-----SVDVLLIDDIQFLAGKE 113

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6679501  295 YDsnsggereiQRTMLELLNQLdgFDSRGdvKVIMATNR----IETLDPAL-----------IRPgridrkiefplPDEK 359
Cdd:COG0593 114 AT---------QEEFFHTFNAL--REAGK--QIVLTSDRppkeLPGLEERLrsrlewglvvdIQP-----------PDLE 169

                       170       180
                ....*....|....*....|.
gi 6679501  360 TKKRIFQ--IHTSRMTLADDV 378
Cdd:COG0593 170 TRIAILRkkAADRGLELPDEV 190
recomb_radB TIGR02237
DNA repair and recombination protein RadB; This family consists exclusively of archaeal RadB ...
 220-344 4.90e-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: 38.17  E-value: 4.90e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6679501    220 KGVI--LYGPPGTGKTLLAKAVANQTSATFLRVV-------GSELIQKYLGDGPKLV-------------------RELF 271
Cdd:TIGR02237  11 RGTItqIYGPPGSGKTNICMILAVNAARQGKKVVyidteglSPERFKQIAEDRPERAlsnfivfevfdfdeqgvaiQKTS 90

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 6679501    272 RVAEEHAPSIVFIDEIDAI-GTKRYDSNSGGEREIQRTMLELLnqldGFDSRGDVKVIMaTNRI-ETLDPALIRP 344
Cdd:TIGR02237  91 KFIDRDSASLVVVDSFTALyRLELSDDRISRNRELARQLTLLL----SLARKKNLAVVI-TNQVyTDVNNGTLRP 160
RNA_helicase pfam00910
RNA helicase; This family includes RNA helicases thought to be involved in duplex unwinding ...
 222-253 7.24e-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: 36.04  E-value: 7.24e-03
                          10        20        30
                  ....*....|....*....|....*....|..
gi 6679501    222 VILYGPPGTGKTLLAKAVANQTSATFLRVVGS 253
Cdd:pfam00910   1 IWLYGPPGCGKSTLAKYLARALLKKLGLPKDS 32
 
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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