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Conserved domains on  [gi|1056850158|ref|NP_001317141|]
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26S proteasome regulatory subunit 4 isoform b [Homo sapiens]

Protein Classification

26S proteasome regulatory subunit 4( domain architecture ID 1002609)

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

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
PTZ00361 super family cl33178
26 proteosome regulatory subunit 4-like protein; Provisional
1-367 0e+00

26 proteosome regulatory subunit 4-like protein; Provisional


The actual alignment was detected with superfamily member PTZ00361:

Pssm-ID: 185575 [Multi-domain]  Cd Length: 438  Bit Score: 726.18  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1056850158   1 MEEEFIRNQEQMKPLEEKQEEERSKVDDLRGTPMSVGTLEEIIDDNHAIVSTSVGSEHYVSILSFVDKDLLEPGCSVLLN 80
Cdd:PTZ00361   72 LEEEFITNQEAQKPAQEKNEAELKKVDDLRGSPLSVGTLEEIIDENHAIVSSSVGPEYYVNILSFVDKEQLEPGCSVLLH 151
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1056850158  81 HKVHAVIGVLMDDTDPLVTVMKVEKAPQETYADIGGLDNQIQEIKESVELPLTHPEYYEEMGIKPPKGVILYGPPGTGKT 160
Cdd:PTZ00361  152 NKTHSVVGILLDEVDPLVSVMKVDKAPLESYADIGGLEQQIQEIKEAVELPLTHPELYDDIGIKPPKGVILYGPPGTGKT 231
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1056850158 161 LLAKAVANQTSATFLRVVGSELIQKYLGDGPKLVRELFRVAEEHAPSIVFIDEIDAIGTKRYDSNSGGEREIQRTMLELL 240
Cdd:PTZ00361  232 LLAKAVANETSATFLRVVGSELIQKYLGDGPKLVRELFRVAEENAPSIVFIDEIDAIGTKRYDATSGGEKEIQRTMLELL 311
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1056850158 241 NQLDGFDSRGDVKVIMATNRIETLDPALIRPGRIDRKIEFPLPDEKTKKRIFQIHTSRMTLADDVTLDDLIMAKDDLSGA 320
Cdd:PTZ00361  312 NQLDGFDSRGDVKVIMATNRIESLDPALIRPGRIDRKIEFPNPDEKTKRRIFEIHTSKMTLAEDVDLEEFIMAKDELSGA 391
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*..
gi 1056850158 321 DIKAICTEAGLMALRERRMKVTNEDFKKSKENVLYKKQEGTPEGLYL 367
Cdd:PTZ00361  392 DIKAICTEAGLLALRERRMKVTQADFRKAKEKVLYRKKGNIPEGLYL 438
 
Name Accession Description Interval E-value
PTZ00361 PTZ00361
26 proteosome regulatory subunit 4-like protein; Provisional
1-367 0e+00

26 proteosome regulatory subunit 4-like protein; Provisional


Pssm-ID: 185575 [Multi-domain]  Cd Length: 438  Bit Score: 726.18  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1056850158   1 MEEEFIRNQEQMKPLEEKQEEERSKVDDLRGTPMSVGTLEEIIDDNHAIVSTSVGSEHYVSILSFVDKDLLEPGCSVLLN 80
Cdd:PTZ00361   72 LEEEFITNQEAQKPAQEKNEAELKKVDDLRGSPLSVGTLEEIIDENHAIVSSSVGPEYYVNILSFVDKEQLEPGCSVLLH 151
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1056850158  81 HKVHAVIGVLMDDTDPLVTVMKVEKAPQETYADIGGLDNQIQEIKESVELPLTHPEYYEEMGIKPPKGVILYGPPGTGKT 160
Cdd:PTZ00361  152 NKTHSVVGILLDEVDPLVSVMKVDKAPLESYADIGGLEQQIQEIKEAVELPLTHPELYDDIGIKPPKGVILYGPPGTGKT 231
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1056850158 161 LLAKAVANQTSATFLRVVGSELIQKYLGDGPKLVRELFRVAEEHAPSIVFIDEIDAIGTKRYDSNSGGEREIQRTMLELL 240
Cdd:PTZ00361  232 LLAKAVANETSATFLRVVGSELIQKYLGDGPKLVRELFRVAEENAPSIVFIDEIDAIGTKRYDATSGGEKEIQRTMLELL 311
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1056850158 241 NQLDGFDSRGDVKVIMATNRIETLDPALIRPGRIDRKIEFPLPDEKTKKRIFQIHTSRMTLADDVTLDDLIMAKDDLSGA 320
Cdd:PTZ00361  312 NQLDGFDSRGDVKVIMATNRIESLDPALIRPGRIDRKIEFPNPDEKTKRRIFEIHTSKMTLAEDVDLEEFIMAKDELSGA 391
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*..
gi 1056850158 321 DIKAICTEAGLMALRERRMKVTNEDFKKSKENVLYKKQEGTPEGLYL 367
Cdd:PTZ00361  392 DIKAICTEAGLLALRERRMKVTQADFRKAKEKVLYRKKGNIPEGLYL 438
26Sp45 TIGR01242
26S proteasome subunit P45 family; Many proteins may score above the trusted cutoff because an ...
15-354 5.07e-151

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


Pssm-ID: 130309 [Multi-domain]  Cd Length: 364  Bit Score: 429.99  E-value: 5.07e-151
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1056850158  15 LEEKQEEERSKVDDLRGTPMSVGTLEEIIDDNHAIVSTSVGSEHYVSILSFVDKDLLEPGCSVLLNHKVHAVIGVLMDDT 94
Cdd:TIGR01242  25 LERELERLRSEIERLRSPPLIVGTVLEVLDDNRVVVKSSTGPNFVVNVSAFIDRKSLKPGARVALNQQTLTIVDVLPTSK 104
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1056850158  95 DPLVTVMKVEKAPQETYADIGGLDNQIQEIKESVELPLTHPEYYEEMGIKPPKGVILYGPPGTGKTLLAKAVANQTSATF 174
Cdd:TIGR01242 105 DPLVKGMEVEERPNVSYEDIGGLEEQIREIREAVELPLKHPELFEEVGIEPPKGVLLYGPPGTGKTLLAKAVAHETNATF 184
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1056850158 175 LRVVGSELIQKYLGDGPKLVRELFRVAEEHAPSIVFIDEIDAIGTKRYDSNSGGEREIQRTMLELLNQLDGFDSRGDVKV 254
Cdd:TIGR01242 185 IRVVGSELVRKYIGEGARLVREIFELAKEKAPSIIFIDEIDAIAAKRTDSGTSGDREVQRTLMQLLAELDGFDPRGNVKV 264
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1056850158 255 IMATNRIETLDPALIRPGRIDRKIEFPLPDEKTKKRIFQIHTSRMTLADDVTLDDLIMAKDDLSGADIKAICTEAGLMAL 334
Cdd:TIGR01242 265 IAATNRPDILDPALLRPGRFDRIIEVPLPDFEGRLEILKIHTRKMKLAEDVDLEAIAKMTEGASGADLKAICTEAGMFAI 344
                         330       340
                  ....*....|....*....|
gi 1056850158 335 RERRMKVTNEDFKKSKENVL 354
Cdd:TIGR01242 345 REERDYVTMDDFIKAVEKVL 364
RPT1 COG1222
ATP-dependent 26S proteasome regulatory subunit [Posttranslational modification, protein ...
92-362 1.26e-133

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


Pssm-ID: 440835 [Multi-domain]  Cd Length: 326  Bit Score: 384.36  E-value: 1.26e-133
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1056850158  92 DDTDPLVTVMKVEKAPQETYADIGGLDNQIQEIKESVELPLTHPEYYEEMGIKPPKGVILYGPPGTGKTLLAKAVANQTS 171
Cdd:COG1222    58 KRLGTPRGTAVPAESPDVTFDDIGGLDEQIEEIREAVELPLKNPELFRKYGIEPPKGVLLYGPPGTGKTLLAKAVAGELG 137
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1056850158 172 ATFLRVVGSELIQKYLGDGPKLVRELFRVAEEHAPSIVFIDEIDAIGTKRYDSNSGGerEIQRTMLELLNQLDGFDSRGD 251
Cdd:COG1222   138 APFIRVRGSELVSKYIGEGARNVREVFELAREKAPSIIFIDEIDAIAARRTDDGTSG--EVQRTVNQLLAELDGFESRGD 215
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1056850158 252 VKVIMATNRIETLDPALIRPGRIDRKIEFPLPDEKTKKRIFQIHTSRMTLADDVTLDDLIMAKDDLSGADIKAICTEAGL 331
Cdd:COG1222   216 VLIIAATNRPDLLDPALLRPGRFDRVIEVPLPDEEAREEILKIHLRDMPLADDVDLDKLAKLTEGFSGADLKAIVTEAGM 295
                         250       260       270
                  ....*....|....*....|....*....|.
gi 1056850158 332 MALRERRMKVTNEDFKKSKENVLYKKQEGTP 362
Cdd:COG1222   296 FAIREGRDTVTMEDLEKAIEKVKKKTETATN 326
RecA-like_PAN_like cd19502
proteasome activating nucleotidase PAN and related proteasome subunits; This subfamily ...
110-280 1.67e-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: 340.08  E-value: 1.67e-118
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1056850158 110 TYADIGGLDNQIQEIKESVELPLTHPEYYEEMGIKPPKGVILYGPPGTGKTLLAKAVANQTSATFLRVVGSELIQKYLGD 189
Cdd:cd19502     1 TYEDIGGLDEQIREIREVVELPLKHPELFEELGIEPPKGVLLYGPPGTGKTLLAKAVANHTDATFIRVVGSELVQKYIGE 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1056850158 190 GPKLVRELFRVAEEHAPSIVFIDEIDAIGTKRYDSNSGGEREIQRTMLELLNQLDGFDSRGDVKVIMATNRIETLDPALI 269
Cdd:cd19502    81 GARLVRELFEMAREKAPSIIFIDEIDAIGAKRFDSGTGGDREVQRTMLELLNQLDGFDPRGNIKVIMATNRPDILDPALL 160
                         170
                  ....*....|.
gi 1056850158 270 RPGRIDRKIEF 280
Cdd:cd19502   161 RPGRFDRKIEF 171
AAA pfam00004
ATPase family associated with various cellular activities (AAA); AAA family proteins often ...
149-282 1.93e-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: 175.47  E-value: 1.93e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1056850158 149 VILYGPPGTGKTLLAKAVANQTSATFLRVVGSELIQKYLGDGPKLVRELFRVAEEHAPSIVFIDEIDAIGTKRydsNSGG 228
Cdd:pfam00004   1 LLLYGPPGTGKTTLAKAVAKELGAPFIEISGSELVSKYVGESEKRLRELFEAAKKLAPCVIFIDEIDALAGSR---GSGG 77
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1056850158 229 EREIQRTMLELLNQLDGFDSR-GDVKVIMATNRIETLDPALIrpGRIDRKIEFPL 282
Cdd:pfam00004  78 DSESRRVVNQLLTELDGFTSSnSKVIVIAATNRPDKLDPALL--GRFDRIIEFPL 130
AAA smart00382
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ...
145-284 5.00e-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: 85.50  E-value: 5.00e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1056850158  145 PPKGVILYGPPGTGKTLLAKAVANQTSATFLRVV-----------------GSELIQKYLGDGPKLVRELFRVAEEHAPS 207
Cdd:smart00382   1 PGEVILIVGPPGSGKTTLARALARELGPPGGGVIyidgedileevldqlllIIVGGKKASGSGELRLRLALALARKLKPD 80
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1056850158  208 IVFIDEIDAIGTKrydsnsggEREIQRTMLELLNQLDGFDSRGDVKVIMATNRIETLDPALIRPgRIDRKIEFPLPD 284
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 ...
149-214 2.84e-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: 41.69  E-value: 2.84e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1056850158 149 VILYGPPGTGKTLLAKAVANQ-----TSATFLRVvgSELIQKYL---GDGpKLVRELFRVAeehAPSIVFIDEI 214
Cdd:NF038214   93 VLLLGPPGTGKTHLAIALGYAacrqgYRVRFTTA--ADLVEQLAqarADG-RLGRLLRRLA---RYDLLIIDEL 160
 
Name Accession Description Interval E-value
PTZ00361 PTZ00361
26 proteosome regulatory subunit 4-like protein; Provisional
1-367 0e+00

26 proteosome regulatory subunit 4-like protein; Provisional


Pssm-ID: 185575 [Multi-domain]  Cd Length: 438  Bit Score: 726.18  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1056850158   1 MEEEFIRNQEQMKPLEEKQEEERSKVDDLRGTPMSVGTLEEIIDDNHAIVSTSVGSEHYVSILSFVDKDLLEPGCSVLLN 80
Cdd:PTZ00361   72 LEEEFITNQEAQKPAQEKNEAELKKVDDLRGSPLSVGTLEEIIDENHAIVSSSVGPEYYVNILSFVDKEQLEPGCSVLLH 151
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1056850158  81 HKVHAVIGVLMDDTDPLVTVMKVEKAPQETYADIGGLDNQIQEIKESVELPLTHPEYYEEMGIKPPKGVILYGPPGTGKT 160
Cdd:PTZ00361  152 NKTHSVVGILLDEVDPLVSVMKVDKAPLESYADIGGLEQQIQEIKEAVELPLTHPELYDDIGIKPPKGVILYGPPGTGKT 231
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1056850158 161 LLAKAVANQTSATFLRVVGSELIQKYLGDGPKLVRELFRVAEEHAPSIVFIDEIDAIGTKRYDSNSGGEREIQRTMLELL 240
Cdd:PTZ00361  232 LLAKAVANETSATFLRVVGSELIQKYLGDGPKLVRELFRVAEENAPSIVFIDEIDAIGTKRYDATSGGEKEIQRTMLELL 311
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1056850158 241 NQLDGFDSRGDVKVIMATNRIETLDPALIRPGRIDRKIEFPLPDEKTKKRIFQIHTSRMTLADDVTLDDLIMAKDDLSGA 320
Cdd:PTZ00361  312 NQLDGFDSRGDVKVIMATNRIESLDPALIRPGRIDRKIEFPNPDEKTKRRIFEIHTSKMTLAEDVDLEEFIMAKDELSGA 391
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*..
gi 1056850158 321 DIKAICTEAGLMALRERRMKVTNEDFKKSKENVLYKKQEGTPEGLYL 367
Cdd:PTZ00361  392 DIKAICTEAGLLALRERRMKVTQADFRKAKEKVLYRKKGNIPEGLYL 438
PRK03992 PRK03992
proteasome-activating nucleotidase; Provisional
1-363 1.85e-175

proteasome-activating nucleotidase; Provisional


Pssm-ID: 179699 [Multi-domain]  Cd Length: 389  Bit Score: 492.81  E-value: 1.85e-175
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1056850158   1 MEEEFIRNQEQMKPLEEKQEEERSKVDDLRGTPMSVGTLEEIIDDNHAIVSTSVGSEHYVSILSFVDKDLLEPGCSVLLN 80
Cdd:PRK03992   20 LELKLRDLEAENEKLERELERLKSELEKLKSPPLIVATVLEVLDDGRVVVKSSGGPQFLVNVSPFIDREKLKPGARVALN 99
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1056850158  81 HKVHAVIGVLMDDTDPLVTVMKVEKAPQETYADIGGLDNQIQEIKESVELPLTHPEYYEEMGIKPPKGVILYGPPGTGKT 160
Cdd:PRK03992  100 QQSLAIVEVLPSEKDPRVQAMEVIESPNVTYEDIGGLEEQIREVREAVELPLKKPELFEEVGIEPPKGVLLYGPPGTGKT 179
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1056850158 161 LLAKAVANQTSATFLRVVGSELIQKYLGDGPKLVRELFRVAEEHAPSIVFIDEIDAIGTKRYDSNSGGEREIQRTMLELL 240
Cdd:PRK03992  180 LLAKAVAHETNATFIRVVGSELVQKFIGEGARLVRELFELAREKAPSIIFIDEIDAIAAKRTDSGTSGDREVQRTLMQLL 259
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1056850158 241 NQLDGFDSRGDVKVIMATNRIETLDPALIRPGRIDRKIEFPLPDEKTKKRIFQIHTSRMTLADDVTLDDLIMAKDDLSGA 320
Cdd:PRK03992  260 AEMDGFDPRGNVKIIAATNRIDILDPAILRPGRFDRIIEVPLPDEEGRLEILKIHTRKMNLADDVDLEELAELTEGASGA 339
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|...
gi 1056850158 321 DIKAICTEAGLMALRERRMKVTNEDFKKSKENVLYKKQEGTPE 363
Cdd:PRK03992  340 DLKAICTEAGMFAIRDDRTEVTMEDFLKAIEKVMGKEEKDSME 382
PTZ00454 PTZ00454
26S protease regulatory subunit 6B-like protein; Provisional
1-359 2.43e-159

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


Pssm-ID: 240423 [Multi-domain]  Cd Length: 398  Bit Score: 452.68  E-value: 2.43e-159
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1056850158   1 MEEEFIRnqEQMKPLeeKQEEERSK--VDDLRGTPMSVGTLEEIIDDNHAIVSTSVGSEHYVSILSFVDKDLLEPGCSVL 78
Cdd:PTZ00454   36 IQEEYIK--EEQKNL--KRELIRAKeeVKRIQSVPLVIGQFLEMIDSNYGIVSSTSGSNYYVRILSTLNRELLKPNASVA 111
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1056850158  79 LNHKVHAVIGVLMDDTDPLVTVMKVEKAPQETYADIGGLDNQIQEIKESVELPLTHPEYYEEMGIKPPKGVILYGPPGTG 158
Cdd:PTZ00454  112 LHRHSHAVVDILPPEADSSIQLLQMSEKPDVTYSDIGGLDIQKQEIREAVELPLTCPELYEQIGIDPPRGVLLYGPPGTG 191
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1056850158 159 KTLLAKAVANQTSATFLRVVGSELIQKYLGDGPKLVRELFRVAEEHAPSIVFIDEIDAIGTKRYDSNSGGEREIQRTMLE 238
Cdd:PTZ00454  192 KTMLAKAVAHHTTATFIRVVGSEFVQKYLGEGPRMVRDVFRLARENAPSIIFIDEVDSIATKRFDAQTGADREVQRILLE 271
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1056850158 239 LLNQLDGFDSRGDVKVIMATNRIETLDPALIRPGRIDRKIEFPLPDEKTKKRIFQIHTSRMTLADDVTLDDLIMAKDDLS 318
Cdd:PTZ00454  272 LLNQMDGFDQTTNVKVIMATNRADTLDPALLRPGRLDRKIEFPLPDRRQKRLIFQTITSKMNLSEEVDLEDFVSRPEKIS 351
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|.
gi 1056850158 319 GADIKAICTEAGLMALRERRMKVTNEDFKKSKENVLYKKQE 359
Cdd:PTZ00454  352 AADIAAICQEAGMQAVRKNRYVILPKDFEKGYKTVVRKTDR 392
26Sp45 TIGR01242
26S proteasome subunit P45 family; Many proteins may score above the trusted cutoff because an ...
15-354 5.07e-151

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


Pssm-ID: 130309 [Multi-domain]  Cd Length: 364  Bit Score: 429.99  E-value: 5.07e-151
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1056850158  15 LEEKQEEERSKVDDLRGTPMSVGTLEEIIDDNHAIVSTSVGSEHYVSILSFVDKDLLEPGCSVLLNHKVHAVIGVLMDDT 94
Cdd:TIGR01242  25 LERELERLRSEIERLRSPPLIVGTVLEVLDDNRVVVKSSTGPNFVVNVSAFIDRKSLKPGARVALNQQTLTIVDVLPTSK 104
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1056850158  95 DPLVTVMKVEKAPQETYADIGGLDNQIQEIKESVELPLTHPEYYEEMGIKPPKGVILYGPPGTGKTLLAKAVANQTSATF 174
Cdd:TIGR01242 105 DPLVKGMEVEERPNVSYEDIGGLEEQIREIREAVELPLKHPELFEEVGIEPPKGVLLYGPPGTGKTLLAKAVAHETNATF 184
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1056850158 175 LRVVGSELIQKYLGDGPKLVRELFRVAEEHAPSIVFIDEIDAIGTKRYDSNSGGEREIQRTMLELLNQLDGFDSRGDVKV 254
Cdd:TIGR01242 185 IRVVGSELVRKYIGEGARLVREIFELAKEKAPSIIFIDEIDAIAAKRTDSGTSGDREVQRTLMQLLAELDGFDPRGNVKV 264
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1056850158 255 IMATNRIETLDPALIRPGRIDRKIEFPLPDEKTKKRIFQIHTSRMTLADDVTLDDLIMAKDDLSGADIKAICTEAGLMAL 334
Cdd:TIGR01242 265 IAATNRPDILDPALLRPGRFDRIIEVPLPDFEGRLEILKIHTRKMKLAEDVDLEAIAKMTEGASGADLKAICTEAGMFAI 344
                         330       340
                  ....*....|....*....|
gi 1056850158 335 RERRMKVTNEDFKKSKENVL 354
Cdd:TIGR01242 345 REERDYVTMDDFIKAVEKVL 364
RPT1 COG1222
ATP-dependent 26S proteasome regulatory subunit [Posttranslational modification, protein ...
92-362 1.26e-133

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


Pssm-ID: 440835 [Multi-domain]  Cd Length: 326  Bit Score: 384.36  E-value: 1.26e-133
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1056850158  92 DDTDPLVTVMKVEKAPQETYADIGGLDNQIQEIKESVELPLTHPEYYEEMGIKPPKGVILYGPPGTGKTLLAKAVANQTS 171
Cdd:COG1222    58 KRLGTPRGTAVPAESPDVTFDDIGGLDEQIEEIREAVELPLKNPELFRKYGIEPPKGVLLYGPPGTGKTLLAKAVAGELG 137
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1056850158 172 ATFLRVVGSELIQKYLGDGPKLVRELFRVAEEHAPSIVFIDEIDAIGTKRYDSNSGGerEIQRTMLELLNQLDGFDSRGD 251
Cdd:COG1222   138 APFIRVRGSELVSKYIGEGARNVREVFELAREKAPSIIFIDEIDAIAARRTDDGTSG--EVQRTVNQLLAELDGFESRGD 215
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1056850158 252 VKVIMATNRIETLDPALIRPGRIDRKIEFPLPDEKTKKRIFQIHTSRMTLADDVTLDDLIMAKDDLSGADIKAICTEAGL 331
Cdd:COG1222   216 VLIIAATNRPDLLDPALLRPGRFDRVIEVPLPDEEAREEILKIHLRDMPLADDVDLDKLAKLTEGFSGADLKAIVTEAGM 295
                         250       260       270
                  ....*....|....*....|....*....|.
gi 1056850158 332 MALRERRMKVTNEDFKKSKENVLYKKQEGTP 362
Cdd:COG1222   296 FAIREGRDTVTMEDLEKAIEKVKKKTETATN 326
RecA-like_PAN_like cd19502
proteasome activating nucleotidase PAN and related proteasome subunits; This subfamily ...
110-280 1.67e-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: 340.08  E-value: 1.67e-118
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1056850158 110 TYADIGGLDNQIQEIKESVELPLTHPEYYEEMGIKPPKGVILYGPPGTGKTLLAKAVANQTSATFLRVVGSELIQKYLGD 189
Cdd:cd19502     1 TYEDIGGLDEQIREIREVVELPLKHPELFEELGIEPPKGVLLYGPPGTGKTLLAKAVANHTDATFIRVVGSELVQKYIGE 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1056850158 190 GPKLVRELFRVAEEHAPSIVFIDEIDAIGTKRYDSNSGGEREIQRTMLELLNQLDGFDSRGDVKVIMATNRIETLDPALI 269
Cdd:cd19502    81 GARLVRELFEMAREKAPSIIFIDEIDAIGAKRFDSGTGGDREVQRTMLELLNQLDGFDPRGNIKVIMATNRPDILDPALL 160
                         170
                  ....*....|.
gi 1056850158 270 RPGRIDRKIEF 280
Cdd:cd19502   161 RPGRFDRKIEF 171
SpoVK COG0464
AAA+-type ATPase, SpoVK/Ycf46/Vps4 family [Cell wall/membrane/envelope biogenesis, Cell cycle ...
95-348 1.00e-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: 254.84  E-value: 1.00e-81
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1056850158  95 DPLVTVMKVEKAPQETYADIGGLDNQIQEIKESVELPLTHPEYYEEMGIKPPKGVILYGPPGTGKTLLAKAVANQTSATF 174
Cdd:COG0464   140 DIGGLEEELLELREAILDDLGGLEEVKEELRELVALPLKRPELREEYGLPPPRGLLLYGPPGTGKTLLARALAGELGLPL 219
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1056850158 175 LRVVGSELIQKYLGDGPKLVRELFRVAEEHAPSIVFIDEIDAIGTKRYDSNSGGEREIQRTmleLLNQLDGFdsRGDVKV 254
Cdd:COG0464   220 IEVDLSDLVSKYVGETEKNLREVFDKARGLAPCVLFIDEADALAGKRGEVGDGVGRRVVNT---LLTEMEEL--RSDVVV 294
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1056850158 255 IMATNRIETLDPALIRpgRIDRKIEFPLPDEKTKKRIFQIHTSRMTLADDVTLDDLIMAKDDLSGADIKAICTEAGLMAL 334
Cdd:COG0464   295 IAATNRPDLLDPALLR--RFDEIIFFPLPDAEERLEIFRIHLRKRPLDEDVDLEELAEATEGLSGADIRNVVRRAALQAL 372
                         250
                  ....*....|....
gi 1056850158 335 RERRMKVTNEDFKK 348
Cdd:COG0464   373 RLGREPVTTEDLLE 386
FtsH_fam TIGR01241
ATP-dependent metalloprotease FtsH; HflB(FtsH) is a pleiotropic protein required for correct ...
104-355 3.32e-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: 256.44  E-value: 3.32e-81
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1056850158 104 EKAPQETYADIGGLDNQIQEIKESVELpLTHPEYYEEMGIKPPKGVILYGPPGTGKTLLAKAVANQTSATFLRVVGSELI 183
Cdd:TIGR01241  47 EEKPKVTFKDVAGIDEAKEELMEIVDF-LKNPSKFTKLGAKIPKGVLLVGPPGTGKTLLAKAVAGEAGVPFFSISGSDFV 125
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1056850158 184 QKYLGDGPKLVRELFRVAEEHAPSIVFIDEIDAIGTKRYDSNSGGEREIQRTMLELLNQLDGFDSRGDVKVIMATNRIET 263
Cdd:TIGR01241 126 EMFVGVGASRVRDLFEQAKKNAPCIIFIDEIDAVGRQRGAGLGGGNDEREQTLNQLLVEMDGFGTNTGVIVIAATNRPDV 205
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1056850158 264 LDPALIRPGRIDRKIEFPLPDEKTKKRIFQIHTSRMTLADDVTLDDLIMAKDDLSGADIKAICTEAGLMALRERRMKVTN 343
Cdd:TIGR01241 206 LDPALLRPGRFDRQVVVDLPDIKGREEILKVHAKNKKLAPDVDLKAVARRTPGFSGADLANLLNEAALLAARKNKTEITM 285
                         250
                  ....*....|..
gi 1056850158 344 EDFKKSKENVLY 355
Cdd:TIGR01241 286 NDIEEAIDRVIA 297
CDC48 TIGR01243
AAA family ATPase, CDC48 subfamily; This subfamily of the AAA family ATPases includes two ...
107-356 3.90e-77

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


Pssm-ID: 273521 [Multi-domain]  Cd Length: 733  Bit Score: 251.75  E-value: 3.90e-77
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1056850158 107 PQETYADIGGLDNQIQEIKESVELPLTHPEYYEEMGIKPPKGVILYGPPGTGKTLLAKAVANQTSATFLRVVGSELIQKY 186
Cdd:TIGR01243 448 PNVRWSDIGGLEEVKQELREAVEWPLKHPEIFEKMGIRPPKGVLLFGPPGTGKTLLAKAVATESGANFIAVRGPEILSKW 527
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1056850158 187 LGDGPKLVRELFRVAEEHAPSIVFIDEIDAIGTKRydSNSGGEREIQRTMLELLNQLDGFDSRGDVKVIMATNRIETLDP 266
Cdd:TIGR01243 528 VGESEKAIREIFRKARQAAPAIIFFDEIDAIAPAR--GARFDTSVTDRIVNQLLTEMDGIQELSNVVVIAATNRPDILDP 605
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1056850158 267 ALIRPGRIDRKIEFPLPDEKTKKRIFQIHTSRMTLADDVTLDDLIMAKDDLSGADIKAICTEAGLMALRERRMKVTNEDF 346
Cdd:TIGR01243 606 ALLRPGRFDRLILVPPPDEEARKEIFKIHTRSMPLAEDVDLEELAEMTEGYTGADIEAVCREAAMAALRESIGSPAKEKL 685
                         250
                  ....*....|
gi 1056850158 347 KKSKENVLYK 356
Cdd:TIGR01243 686 EVGEEEFLKD 695
CDC48 TIGR01243
AAA family ATPase, CDC48 subfamily; This subfamily of the AAA family ATPases includes two ...
98-353 4.10e-77

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


Pssm-ID: 273521 [Multi-domain]  Cd Length: 733  Bit Score: 251.75  E-value: 4.10e-77
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1056850158  98 VTVMKVEKAPQETYADIGGLDNQIQEIKESVELPLTHPEYYEEMGIKPPKGVILYGPPGTGKTLLAKAVANQTSATFLRV 177
Cdd:TIGR01243 164 VREEIERKVPKVTYEDIGGLKEAKEKIREMVELPMKHPELFEHLGIEPPKGVLLYGPPGTGKTLLAKAVANEAGAYFISI 243
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1056850158 178 VGSELIQKYLGDGPKLVRELFRVAEEHAPSIVFIDEIDAIGTKRYDSNsgGEREiQRTMLELLNQLDGFDSRGDVKVIMA 257
Cdd:TIGR01243 244 NGPEIMSKYYGESEERLREIFKEAEENAPSIIFIDEIDAIAPKREEVT--GEVE-KRVVAQLLTLMDGLKGRGRVIVIGA 320
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1056850158 258 TNRIETLDPALIRPGRIDRKIEFPLPDEKTKKRIFQIHTSRMTLADDVTLDDLIMAKDDLSGADIKAICTEAGLMALRE- 336
Cdd:TIGR01243 321 TNRPDALDPALRRPGRFDREIVIRVPDKRARKEILKVHTRNMPLAEDVDLDKLAEVTHGFVGADLAALAKEAAMAALRRf 400
                         250       260       270
                  ....*....|....*....|....*....|....*
gi 1056850158 337 ------------------RRMKVTNEDFKKSKENV 353
Cdd:TIGR01243 401 iregkinfeaeeipaevlKELKVTMKDFMEALKMV 435
HflB COG0465
ATP-dependent Zn proteases [Posttranslational modification, protein turnover, chaperones];
101-354 1.26e-75

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


Pssm-ID: 440233 [Multi-domain]  Cd Length: 583  Bit Score: 244.18  E-value: 1.26e-75
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1056850158 101 MKVEKAPQETYADIGGLDNQIQEIKESVELpLTHPEYYEEMGIKPPKGVILYGPPGTGKTLLAKAVANQTSATFLRVVGS 180
Cdd:COG0465   131 LYDEDKPKVTFDDVAGVDEAKEELQEIVDF-LKDPEKFTRLGAKIPKGVLLVGPPGTGKTLLAKAVAGEAGVPFFSISGS 209
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1056850158 181 ELIQKYLGDGPKLVRELFRVAEEHAPSIVFIDEIDAIGTKRyDSNSGG---EREiqRTmlelLNQL----DGFDSRGDVK 253
Cdd:COG0465   210 DFVEMFVGVGASRVRDLFEQAKKNAPCIIFIDEIDAVGRQR-GAGLGGghdERE--QT----LNQLlvemDGFEGNEGVI 282
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1056850158 254 VIMATNRIETLDPALIRPGRIDRKIEFPLPDEKTKKRIFQIHTSRMTLADDVTLDDLIMAKDDLSGADIKAICTEAGLMA 333
Cdd:COG0465   283 VIAATNRPDVLDPALLRPGRFDRQVVVDLPDVKGREAILKVHARKKPLAPDVDLEVIARRTPGFSGADLANLVNEAALLA 362
                         250       260
                  ....*....|....*....|.
gi 1056850158 334 LRERRMKVTNEDFKKSKENVL 354
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 ...
113-280 1.55e-72

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: 1.55e-72
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1056850158 113 DIGGLDNQIQEIKESVELPLTHPEYYEEMGIKPPKGVILYGPPGTGKTLLAKAVANQTSATFLRVVGSELIQKYLGDGPK 192
Cdd:cd19503     1 DIGGLDEQIASLKELIELPLKYPELFRALGLKPPRGVLLHGPPGTGKTLLARAVANEAGANFLSISGPSIVSKYLGESEK 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1056850158 193 LVRELFRVAEEHAPSIVFIDEIDAIGTKRYDSNSGGEReiqRTMLELLNQLDGFDSRGDVKVIMATNRIETLDPALIRPG 272
Cdd:cd19503    81 NLREIFEEARSHAPSIIFIDEIDALAPKREEDQREVER---RVVAQLLTLMDGMSSRGKVVVIAATNRPDAIDPALRRPG 157

                  ....*...
gi 1056850158 273 RIDRKIEF 280
Cdd:cd19503   158 RFDREVEI 165
RecA-like_FtsH cd19501
ATP-dependent zinc metalloprotease FtsH; FtsH ATPase is a processive, ATP-dependent zinc ...
110-278 2.10e-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: 215.17  E-value: 2.10e-69
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1056850158 110 TYADIGGLDNQIQEIKESVELpLTHPEYYEEMGIKPPKGVILYGPPGTGKTLLAKAVANQTSATFLRVVGSELIQKYLGD 189
Cdd:cd19501     2 TFKDVAGCEEAKEELKEVVEF-LKNPEKFTKLGAKIPKGVLLVGPPGTGKTLLAKAVAGEAGVPFFSISGSDFVEMFVGV 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1056850158 190 GPKLVRELFRVAEEHAPSIVFIDEIDAIGTKRYDSNSGGEREIQRTMLELLNQLDGFDSRGDVKVIMATNRIETLDPALI 269
Cdd:cd19501    81 GASRVRDLFEQAKKNAPCIVFIDEIDAVGRKRGAGLGGGHDEREQTLNQLLVEMDGFESNTGVIVIAATNRPDVLDPALL 160

                  ....*....
gi 1056850158 270 RPGRIDRKI 278
Cdd:cd19501   161 RPGRFDRQV 169
pup_AAA TIGR03689
proteasome ATPase; In the Actinobacteria, as shown for Mycobacterium tuberculosis, some ...
38-325 1.08e-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: 221.51  E-value: 1.08e-67
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1056850158  38 TLEEIIDDNHAIVSTSVGSEHYVSILSFVDKDLLEPGCSVLLNHKV-HAVIGVLMDDTDPLVtvmkVEKAPQETYADIGG 116
Cdd:TIGR03689 111 TLKEVLDDGRALVTDRSGEERVVKLAGALADEGLRPGDTLLVDPRAgYAFEAIPRTEVEDLV----LEEVPDVTYADIGG 186
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1056850158 117 LDNQIQEIKESVELPLTHPEYYEEMGIKPPKGVILYGPPGTGKTLLAKAVAN----------QTSATFLRVVGSELIQKY 186
Cdd:TIGR03689 187 LGSQIEQIRDAVELPFLHPELYREYGLKPPKGVLLYGPPGCGKTLIAKAVANslaarigaegGGKSYFLNIKGPELLNKY 266
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1056850158 187 LGDGPKLVRELFRVAEEHA----PSIVFIDEIDAIGTKRydsNSGGEREIQRTML-ELLNQLDGFDSRGDVKVIMATNRI 261
Cdd:TIGR03689 267 VGETERQIRLIFQRAREKAsegrPVIVFFDEMDSLFRTR---GSGVSSDVETTVVpQLLAEIDGVESLDNVIVIGASNRE 343
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1056850158 262 ETLDPALIRPGRIDRKIEFPLPDEKTKKRIFQIHtsrmtLADDVTLDDLIMAKDDLSGADIKAI 325
Cdd:TIGR03689 344 DMIDPAILRPGRLDVKIRIERPDAEAAADIFAKY-----LTDDLPLPEDLAAHDGDREATAAAL 402
ftsH CHL00176
cell division protein; Validated
110-362 2.56e-67

cell division protein; Validated


Pssm-ID: 214386 [Multi-domain]  Cd Length: 638  Bit Score: 223.77  E-value: 2.56e-67
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1056850158 110 TYADIGGLDNQIQEIKESVELpLTHPEYYEEMGIKPPKGVILYGPPGTGKTLLAKAVANQTSATFLRVVGSELIQKYLGD 189
Cdd:CHL00176  181 TFRDIAGIEEAKEEFEEVVSF-LKKPERFTAVGAKIPKGVLLVGPPGTGKTLLAKAIAGEAEVPFFSISGSEFVEMFVGV 259
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1056850158 190 GPKLVRELFRVAEEHAPSIVFIDEIDAIGTKRYDSNSGGEREIQRTMLELLNQLDGFDSRGDVKVIMATNRIETLDPALI 269
Cdd:CHL00176  260 GAARVRDLFKKAKENSPCIVFIDEIDAVGRQRGAGIGGGNDEREQTLNQLLTEMDGFKGNKGVIVIAATNRVDILDAALL 339
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1056850158 270 RPGRIDRKIEFPLPDEKTKKRIFQIHTSRMTLADDVTLddLIMAKDD--LSGADIKAICTEAGLMALRERRMKVTNEDFK 347
Cdd:CHL00176  340 RPGRFDRQITVSLPDREGRLDILKVHARNKKLSPDVSL--ELIARRTpgFSGADLANLLNEAAILTARRKKATITMKEID 417
                         250
                  ....*....|....*
gi 1056850158 348 KSKENVLyKKQEGTP 362
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 ...
113-281 3.20e-66

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: 206.90  E-value: 3.20e-66
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1056850158 113 DIGGLDNQIQEIKESVELPLTHPEYYEEMGIKPPKGVILYGPPGTGKTLLAKAVANQTSATFLRVVGSELIQKYLGDGPK 192
Cdd:cd19519     1 DIGGCRKQLAQIREMVELPLRHPELFKAIGIKPPRGILLYGPPGTGKTLIARAVANETGAFFFLINGPEIMSKLAGESES 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1056850158 193 LVRELFRVAEEHAPSIVFIDEIDAIGTKRYDSNSGGEReiqRTMLELLNQLDGFDSRGDVKVIMATNRIETLDPALIRPG 272
Cdd:cd19519    81 NLRKAFEEAEKNAPAIIFIDEIDAIAPKREKTHGEVER---RIVSQLLTLMDGLKQRAHVIVMAATNRPNSIDPALRRFG 157

                  ....*....
gi 1056850158 273 RIDRKIEFP 281
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 ...
122-278 1.26e-64

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


Pssm-ID: 410919 [Multi-domain]  Cd Length: 159  Bit Score: 202.51  E-value: 1.26e-64
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1056850158 122 QEIKESVELPLTHPEYYEEMGIKPPKGVILYGPPGTGKTLLAKAVANQTSATFLRVVGSELIQKYLGDGPKLVRELFRVA 201
Cdd:cd19511     3 RELKEAVEWPLKHPDAFKRLGIRPPKGVLLYGPPGCGKTLLAKALASEAGLNFISVKGPELFSKYVGESERAVREIFQKA 82
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1056850158 202 EEHAPSIVFIDEIDAIGTKRYDSNSGGEREiqRTMLELLNQLDGFDSRGDVKVIMATNRIETLDPALIRPGRIDRKI 278
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 ...
120-280 3.93e-62

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


Pssm-ID: 410889 [Multi-domain]  Cd Length: 158  Bit Score: 195.96  E-value: 3.93e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1056850158 120 QIQEIKESVELPLTHPEYyEEMGIKPPKGVILYGPPGTGKTLLAKAVANQTSATFLRVVGSELIQKYLGDGPKLVRELFR 199
Cdd:cd19481     1 LKASLREAVEAPRRGSRL-RRYGLGLPKGILLYGPPGTGKTLLAKALAGELGLPLIVVKLSSLLSKYVGESEKNLRKIFE 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1056850158 200 VAEEHAPSIVFIDEIDAIGTKRydSNSGGEREIQRTMLELLNQLDGFDSRGDVKVIMATNRIETLDPALIRPGRIDRKIE 279
Cdd:cd19481    80 RARRLAPCILFIDEIDAIGRKR--DSSGESGELRRVLNQLLTELDGVNSRSKVLVIAATNRPDLLDPALLRPGRFDEVIE 157

                  .
gi 1056850158 280 F 280
Cdd:cd19481   158 F 158
hflB PRK10733
ATP-dependent zinc metalloprotease FtsH;
101-354 9.51e-62

ATP-dependent zinc metalloprotease FtsH;


Pssm-ID: 182683 [Multi-domain]  Cd Length: 644  Bit Score: 209.12  E-value: 9.51e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1056850158 101 MKVEKAPQETYADIGGLDNQIQEIKESVELpLTHPEYYEEMGIKPPKGVILYGPPGTGKTLLAKAVANQTSATFLRVVGS 180
Cdd:PRK10733  141 MLTEDQIKTTFADVAGCDEAKEEVAELVEY-LREPSRFQKLGGKIPKGVLMVGPPGTGKTLLAKAIAGEAKVPFFTISGS 219
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1056850158 181 ELIQKYLGDGPKLVRELFRVAEEHAPSIVFIDEIDAIGTKRYDSNSGGEREIQRTMLELLNQLDGFDSRGDVKVIMATNR 260
Cdd:PRK10733  220 DFVEMFVGVGASRVRDMFEQAKKAAPCIIFIDEIDAVGRQRGAGLGGGHDEREQTLNQMLVEMDGFEGNEGIIVIAATNR 299
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1056850158 261 IETLDPALIRPGRIDRKIEFPLPDEKTKKRIFQIHTSRMTLADDVTLDDLIMAKDDLSGADIKAICTEAGLMALRERRMK 340
Cdd:PRK10733  300 PDVLDPALLRPGRFDRQVVVGLPDVRGREQILKVHMRRVPLAPDIDAAIIARGTPGFSGADLANLVNEAALFAARGNKRV 379
                         250
                  ....*....|....
gi 1056850158 341 VTNEDFKKSKENVL 354
Cdd:PRK10733  380 VSMVEFEKAKDKIM 393
RecA-like_VCP_r2 cd19529
second of two ATPase domains of Valosin-containing protein-like ATPase (VAT) and similar ...
122-278 3.24e-61

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


Pssm-ID: 410937 [Multi-domain]  Cd Length: 159  Bit Score: 193.87  E-value: 3.24e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1056850158 122 QEIKESVELPLTHPEYYEEMGIKPPKGVILYGPPGTGKTLLAKAVANQTSATFLRVVGSELIQKYLGDGPKLVRELFRVA 201
Cdd:cd19529     3 QELKEAVEWPLLKPEVFKRLGIRPPKGILLYGPPGTGKTLLAKAVATESNANFISVKGPELLSKWVGESEKAIREIFRKA 82
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1056850158 202 EEHAPSIVFIDEIDAIGTKRYDSNSGGEREiqRTMLELLNQLDGFDSRGDVKVIMATNRIETLDPALIRPGRIDRKI 278
Cdd:cd19529    83 RQVAPCVIFFDEIDSIAPRRGTTGDSGVTE--RVVNQLLTELDGLEEMNGVVVIAATNRPDIIDPALLRAGRFDRLI 157
AAA pfam00004
ATPase family associated with various cellular activities (AAA); AAA family proteins often ...
149-282 1.93e-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: 175.47  E-value: 1.93e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1056850158 149 VILYGPPGTGKTLLAKAVANQTSATFLRVVGSELIQKYLGDGPKLVRELFRVAEEHAPSIVFIDEIDAIGTKRydsNSGG 228
Cdd:pfam00004   1 LLLYGPPGTGKTTLAKAVAKELGAPFIEISGSELVSKYVGESEKRLRELFEAAKKLAPCVIFIDEIDALAGSR---GSGG 77
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1056850158 229 EREIQRTMLELLNQLDGFDSR-GDVKVIMATNRIETLDPALIrpGRIDRKIEFPL 282
Cdd:pfam00004  78 DSESRRVVNQLLTELDGFTSSnSKVIVIAATNRPDKLDPALL--GRFDRIIEFPL 130
COG1223 COG1223
Predicted ATPase, AAA+ superfamily [General function prediction only];
123-364 8.79e-53

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


Pssm-ID: 440836 [Multi-domain]  Cd Length: 246  Bit Score: 175.07  E-value: 8.79e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1056850158 123 EIKESVEL---PLTHPEYYEEMGIKPPKGVILYGPPGTGKTLLAKAVANQTSATFLRVVGSELIQKYLGDGPKLVRELFR 199
Cdd:COG1223     9 EAKKKLKLiikELRRRENLRKFGLWPPRKILFYGPPGTGKTMLAEALAGELKLPLLTVRLDSLIGSYLGETARNLRKLFD 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1056850158 200 VAEEhAPSIVFIDEIDAIGTKRYDSNSGGerEIQRTMLELLNQLDGFDSrgDVKVIMATNRIETLDPALIRpgRIDRKIE 279
Cdd:COG1223    89 FARR-APCVIFFDEFDAIAKDRGDQNDVG--EVKRVVNALLQELDGLPS--GSVVIAATNHPELLDSALWR--RFDEVIE 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1056850158 280 FPLPDEKTKKRIFQIHTSRMTLADDVTLDDLIMAKDDLSGADIKAICTEAGLMALRERRMKVTNEDFKKSKENVLYKKQE 359
Cdd:COG1223   162 FPLPDKEERKEILELNLKKFPLPFELDLKKLAKKLEGLSGADIEKVLKTALKKAILEDREKVTKEDLEEALKQRKERKKE 241

                  ....*
gi 1056850158 360 GTPEG 364
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 ...
122-278 1.07e-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: 1.07e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1056850158 122 QEIKESVELPLTHPEYYEEMGIKPPKGVILYGPPGTGKTLLAKAVANQTSATFLRVVGSELIQKYLGDGPKLVRELFRVA 201
Cdd:cd19528     3 RELQELVQYPVEHPDKFLKFGMTPSKGVLFYGPPGCGKTLLAKAIANECQANFISVKGPELLTMWFGESEANVRDIFDKA 82
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1056850158 202 EEHAPSIVFIDEIDAIGTKRYDSNSGGEREIQRTMLELLNQLDGFDSRGDVKVIMATNRIETLDPALIRPGRIDRKI 278
Cdd:cd19528    83 RAAAPCVLFFDELDSIAKARGGNIGDAGGAADRVINQILTEMDGMNTKKNVFIIGATNRPDIIDPAILRPGRLDQLI 159
RecA-like_Yta7-like cd19517
ATPase domain of Saccharomyces cerevisiae Yta7 and similar ATPase domains; Saccharomyces ...
113-280 4.61e-50

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


Pssm-ID: 410925 [Multi-domain]  Cd Length: 170  Bit Score: 165.38  E-value: 4.61e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1056850158 113 DIGGLDNQIQEIKESVELPLTHPEYYEEMGIKPPKGVILYGPPGTGKTLLAKAVANQTSA-----TFLRVVGSELIQKYL 187
Cdd:cd19517     1 DIGGLSHYINQLKEMVFFPLLYPEVFAKFKITPPRGVLFHGPPGTGKTLMARALAAECSKggqkvSFFMRKGADCLSKWV 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1056850158 188 GDGPKLVRELFRVAEEHAPSIVFIDEIDAIGTKRYDSNSGGEREIQRTMLELlnqLDGFDSRGDVKVIMATNRIETLDPA 267
Cdd:cd19517    81 GEAERQLRLLFEEAYRMQPSIIFFDEIDGLAPVRSSKQEQIHASIVSTLLAL---MDGLDNRGQVVVIGATNRPDALDPA 157
                         170
                  ....*....|...
gi 1056850158 268 LIRPGRIDRKIEF 280
Cdd:cd19517   158 LRRPGRFDREFYF 170
RecA-like_VPS4-like cd19509
ATPase domain of VPS4, ATAD1, K, KTNA1, Spastin, FIGL-1 and similar ATPase domains; This ...
114-278 6.41e-50

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


Pssm-ID: 410917 [Multi-domain]  Cd Length: 163  Bit Score: 164.83  E-value: 6.41e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1056850158 114 IGGLDNQIQEIKESVELPLTHPEYYEeMGIKPPKGVILYGPPGTGKTLLAKAVANQTSATFLRVVGSELIQKYLGDGPKL 193
Cdd:cd19509     1 IAGLDDAKEALKEAVILPSLRPDLFP-GLRGPPRGILLYGPPGTGKTLLARAVASESGSTFFSISASSLVSKWVGESEKI 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1056850158 194 VRELFRVAEEHAPSIVFIDEIDAIGTKRYDSNSGGEREIqRTmlELLNQLDGF--DSRGDVKVIMATNRIETLDPALIRp 271
Cdd:cd19509    80 VRALFALARELQPSIIFIDEIDSLLSERGSGEHEASRRV-KT--EFLVQMDGVlnKPEDRVLVLGATNRPWELDEAFLR- 155

                  ....*..
gi 1056850158 272 gRIDRKI 278
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 ...
113-278 6.99e-50

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


Pssm-ID: 410926 [Multi-domain]  Cd Length: 169  Bit Score: 164.89  E-value: 6.99e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1056850158 113 DIGGLDNQIQEIKESVELPLTHPEYYEEMGIKPPKGVILYGPPGTGKTLLAKAVANQTSATFLRVVGSELIQKYLGDGPK 192
Cdd:cd19518     1 DIGGMDSTLKELCELLIHPILPPEYFQHLGVEPPRGVLLHGPPGCGKTMLANAIAGELKVPFLKISATEIVSGVSGESEE 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1056850158 193 LVRELFRVAEEHAPSIVFIDEIDAIGTKRydsnSGGEREIQRTML-ELLNQLDGF----DSRGDVKVIMATNRIETLDPA 267
Cdd:cd19518    81 KIRELFDQAISNAPCIVFIDEIDAITPKR----ESAQREMERRIVsQLLTCMDELnnekTAGGPVLVIGATNRPDSLDPA 156
                         170
                  ....*....|.
gi 1056850158 268 LIRPGRIDRKI 278
Cdd:cd19518   157 LRRAGRFDREI 167
RecA-like_NVL_r2-like cd19530
second of two ATPase domains of NVL (nuclear VCP-like protein) and similar ATPase domains; NVL ...
117-276 5.86e-47

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


Pssm-ID: 410938 [Multi-domain]  Cd Length: 161  Bit Score: 157.26  E-value: 5.86e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1056850158 117 LDNQIQEIKESVELPLTHPEYYEEMGIKPPKGVILYGPPGTGKTLLAKAVANQTSATFLRVVGSELIQKYLGDGPKLVRE 196
Cdd:cd19530     1 LDHVREELTMSILRPIKRPDIYKALGIDLPTGVLLYGPPGCGKTLLAKAVANESGANFISVKGPELLNKYVGESERAVRQ 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1056850158 197 LFRVAEEHAPSIVFIDEIDAIGTKRYDSNSGGereIQRTMLELLNQLDGFDSRGDVKVIMATNRIETLDPALIRPGRIDR 276
Cdd:cd19530    81 VFQRARASAPCVIFFDEVDALVPKRGDGGSWA---SERVVNQLLTEMDGLEERSNVFVIAATNRPDIIDPAMLRPGRLDK 157
RecA-like_ATAD1 cd19520
ATPase domain of ATPase family AAA domain-containing protein 1 and similar ATPase domains; ...
113-270 7.37e-45

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: 7.37e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1056850158 113 DIGGLDNQIQEIKESVELPLTHPEYYEEMGI-KPPKGVILYGPPGTGKTLLAKAVANQTSATFLRVVGSELIQKYLGDGP 191
Cdd:cd19520     1 DIGGLDEVITELKELVILPLQRPELFDNSRLlQPPKGVLLYGPPGCGKTMLAKATAKEAGARFINLQVSSLTDKWYGESQ 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1056850158 192 KLVRELFRVAEEHAPSIVFIDEIDAIGTKRydsnSGGEREIQRTM-LELLNQLDGFDSRGDVKVIM--ATNRIETLDPAL 268
Cdd:cd19520    81 KLVAAVFSLASKLQPSIIFIDEIDSFLRQR----SSTDHEATAMMkAEFMSLWDGLSTDGNCRVIVmgATNRPQDLDEAI 156

                  ..
gi 1056850158 269 IR 270
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 ...
123-276 8.77e-44

second of two ATPase domains of Peroxisomal biogenesis factor 6 (PEX6); PEX6(also known as Peroxin61)/PEX1 is a protein unfoldase; PEX6 and PEX1 form a heterohexameric Type-2 AAA-ATPase complex and are essential for peroxisome biogenesis as they are required for the import of folded proteins into the peroxisomal matrix. This subfamily represents the second ATPase domain of PEX6. This subfamily belongs to the RecA-like NTPase family which includes the NTP binding domain of F1 and V1 H(+)ATPases, DnaB and related helicases as well as bacterial RecA and related eukaryotic and archaeal recombinases. The RecA-like NTPase family also includes bacterial conjugation proteins and related DNA transfer proteins involved in type II and type IV secretion.


Pssm-ID: 410935 [Multi-domain]  Cd Length: 160  Bit Score: 148.82  E-value: 8.77e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1056850158 123 EIKESVELPLTHPEYYEEmGIKPPKGVILYGPPGTGKTLLAKAVANQTSATFLRVVGSELIQKYLGDGPKLVRELFRVAE 202
Cdd:cd19527     4 EILDTIQLPLEHPELFSS-GLRKRSGILLYGPPGTGKTLLAKAIATECSLNFLSVKGPELINMYIGESEANVREVFQKAR 82
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1056850158 203 EHAPSIVFIDEIDAIGTKRYDS-NSGGerEIQRTMLELLNQLDGF-DSRGDVKVIMATNRIETLDPALIRPGRIDR 276
Cdd:cd19527    83 DAKPCVIFFDELDSLAPSRGNSgDSGG--VMDRVVSQLLAELDGMsSSGQDVFVIGATNRPDLLDPALLRPGRFDK 156
RecA-like_PEX1_r2 cd19526
second of two ATPase domains of Peroxisomal biogenesis factor 1 (PEX1); PEX1(also known as ...
124-279 2.19e-42

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: 145.26  E-value: 2.19e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1056850158 124 IKESVELPLTHPEYYEEMGIKPPKGVILYGPPGTGKTLLAKAVANQTSATFLRVVGSELIQKYLGDGPKLVRELFRVAEE 203
Cdd:cd19526     5 LEETIEWPSKYPKIFASSPLRLRSGILLYGPPGCGKTLLASAIASECGLNFISVKGPELLNKYIGASEQNVRDLFSRAQS 84
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1056850158 204 HAPSIVFIDEIDAIGTKRYDSNSGgerEIQRTMLELLNQLDGFDSRGDVKVIMATNRIETLDPALIRPGRIDRKIE 279
Cdd:cd19526    85 AKPCILFFDEFDSIAPKRGHDSTG---VTDRVVNQLLTQLDGVEGLDGVYVLAATSRPDLIDPALLRPGRLDKLVY 157
RecA-like_VPS4 cd19521
ATPase domain of vacuolar protein sorting-associated protein 4; Vacuolar protein ...
107-278 3.17e-42

ATPase domain of vacuolar protein sorting-associated protein 4; Vacuolar protein sorting-associated protein 4 (Vps4) is believed to be involved in intracellular protein transport out of a prevacuolar endosomal compartment. This subfamily belongs to the RecA-like NTPase family which includes the NTP binding domain of F1 and V1 H(+)ATPases, DnaB and related helicases as well as bacterial RecA and related eukaryotic and archaeal recombinases. The RecA-like NTPase family also includes bacterial conjugation proteins and related DNA transfer proteins involved in type II and type IV secretion.


Pssm-ID: 410929 [Multi-domain]  Cd Length: 170  Bit Score: 145.00  E-value: 3.17e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1056850158 107 PQETYADIGGLDNQIQEIKESVELPLTHPEYYEEmGIKPPKGVILYGPPGTGKTLLAKAVANQTSATFLRVVGSELIQKY 186
Cdd:cd19521     2 PNVKWEDVAGLEGAKEALKEAVILPVKFPHLFTG-NRKPWSGILLYGPPGTGKSYLAKAVATEANSTFFSVSSSDLVSKW 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1056850158 187 LGDGPKLVRELFRVAEEHAPSIVFIDEIDAIGTKRYDSNSGGEREIQRtmlELLNQLDGF--DSRGdVKVIMATNRIETL 264
Cdd:cd19521    81 MGESEKLVKQLFAMARENKPSIIFIDEVDSLCGTRGEGESEASRRIKT---ELLVQMNGVgnDSQG-VLVLGATNIPWQL 156
                         170
                  ....*....|....
gi 1056850158 265 DPALIRpgRIDRKI 278
Cdd:cd19521   157 DSAIRR--RFEKRI 168
RecA-like_spastin cd19524
ATPase domain of spastin; Spastin is an ATP-dependent microtubule-severing protein involved in ...
113-270 1.39e-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: 1.39e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1056850158 113 DIGGLDNQIQEIKESVELPLTHPEYYeeMGIK-PPKGVILYGPPGTGKTLLAKAVANQTSATFLRVVGSELIQKYLGDGP 191
Cdd:cd19524     1 DIAGQDLAKQALQEMVILPSLRPELF--TGLRaPARGLLLFGPPGNGKTMLAKAVAAESNATFFNISAASLTSKYVGEGE 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1056850158 192 KLVRELFRVAEEHAPSIVFIDEIDAIGTKRYDSNSGGEReiqRTMLELLNQLDGFDSRGD--VKVIMATNRIETLDPALI 269
Cdd:cd19524    79 KLVRALFAVARELQPSIIFIDEVDSLLSERSEGEHEASR---RLKTEFLIEFDGVQSNGDdrVLVMGATNRPQELDDAVL 155

                  .
gi 1056850158 270 R 270
Cdd:cd19524   156 R 156
RecA-like_KTNA1 cd19522
Katanin p60 ATPase-containing subunit A1; Katanin p60 ATPase-containing subunit A1 (KTNA1) is ...
113-278 1.62e-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: 1.62e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1056850158 113 DIGGLDNQIQEIKESVELPLTHPEYYEemGIKPP-KGVILYGPPGTGKTLLAKAVANQTSATFLRVVGSELIQKYLGDGP 191
Cdd:cd19522     1 DIADLEEAKKLLEEAVVLPMWMPEFFK--GIRRPwKGVLMVGPPGTGKTLLAKAVATECGTTFFNVSSSTLTSKYRGESE 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1056850158 192 KLVRELFRVAEEHAPSIVFIDEIDAIGTKRydsNSGGEREI-QRTMLELLNQLDGF-------DSRGDVKVIMATNRIET 263
Cdd:cd19522    79 KLVRLLFEMARFYAPTTIFIDEIDSICSRR---GTSEEHEAsRRVKSELLVQMDGVggasendDPSKMVMVLAATNFPWD 155
                         170
                  ....*....|....*
gi 1056850158 264 LDPALIRpgRIDRKI 278
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; ...
107-270 2.53e-40

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


Pssm-ID: 410933 [Multi-domain]  Cd Length: 186  Bit Score: 140.89  E-value: 2.53e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1056850158 107 PQETYADIGGLDNQIQEIKESVELPLTHPEYYeeMGIK-PPKGVILYGPPGTGKTLLAKAVANQTSATFLRVVGSELIQK 185
Cdd:cd19525    17 PPINWADIAGLEFAKKTIKEIVVWPMLRPDIF--TGLRgPPKGILLFGPPGTGKTLIGKCIASQSGATFFSISASSLTSK 94
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1056850158 186 YLGDGPKLVRELFRVAEEHAPSIVFIDEIDAIGTKRYDSNSGGEREIQRtmlELLNQLDGFDSRGDVKVIM--ATNRIET 263
Cdd:cd19525    95 WVGEGEKMVRALFSVARCKQPAVIFIDEIDSLLSQRGEGEHESSRRIKT---EFLVQLDGATTSSEDRILVvgATNRPQE 171

                  ....*..
gi 1056850158 264 LDPALIR 270
Cdd:cd19525   172 IDEAARR 178
RecA-like_fidgetin cd19523
ATPase domain of fidgetin; Fidgetin (FIGN) is a ATP-dependent microtubule severing protein. ...
113-270 5.04e-31

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


Pssm-ID: 410931 [Multi-domain]  Cd Length: 163  Bit Score: 115.37  E-value: 5.04e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1056850158 113 DIGGLDNQIQEIKESVELPLTHPEYYEEMgIKPPKGVILYGPPGTGKTLLAKAVANQTSATFLRVVGSELIQKYLGDGPK 192
Cdd:cd19523     1 DIAGLGALKAAIKEEVLWPLLRPDAFSGL-LRLPRSILLFGPRGTGKTLLGRCLASQLGATFLRLRGSTLVAKWAGEGEK 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1056850158 193 LVRELFRVAEEHAPSIVFIDEIDAIGTKRYDsnsgGEREIQRTMLELLNQLDGFDSRGD--VKVIMATNRIETLDPALIR 270
Cdd:cd19523    80 ILQASFLAARCRQPSVLFISDLDALLSSQDD----EASPVGRLQVELLAQLDGVLGSGEdgVLVVCTTSKPEEIDESLRR 155
RecA-like_NSF-SEC18_r1-like cd19504
first of two ATPase domains of NSF and SEC18, and similar ATPase domains; ...
114-279 1.34e-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: 114.89  E-value: 1.34e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1056850158 114 IGGLDNQIQEI-KESVELPLTHPEYYEEMGIKPPKGVILYGPPGTGKTLLAKAVANQTSATFLRVV-GSELIQKYLGDGP 191
Cdd:cd19504     2 IGGLDKEFSDIfRRAFASRVFPPEIVEQLGCKHVKGILLYGPPGTGKTLMARQIGKMLNAREPKIVnGPEILNKYVGESE 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1056850158 192 KLVRELFRVAEEHAPS--------IVFIDEIDAIGTKRyDSNSGGEREIQRTMLELLNQLDGFDSRGDVKVIMATNRIET 263
Cdd:cd19504    82 ANIRKLFADAEEEQRRlgansglhIIIFDEIDAICKQR-GSMAGSTGVHDTVVNQLLSKIDGVEQLNNILVIGMTNRKDL 160
                         170
                  ....*....|....*.
gi 1056850158 264 LDPALIRPGRIDRKIE 279
Cdd:cd19504   161 IDEALLRPGRLEVQME 176
AAA cd00009
The AAA+ (ATPases Associated with a wide variety of cellular Activities) superfamily ...
115-282 1.34e-28

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


Pssm-ID: 99707 [Multi-domain]  Cd Length: 151  Bit Score: 108.77  E-value: 1.34e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1056850158 115 GGLDNQIQEIKESVELPlthpeyyeemgikPPKGVILYGPPGTGKTLLAKAVANQT---SATFLRVVGSELIQKYLG--- 188
Cdd:cd00009     1 VGQEEAIEALREALELP-------------PPKNLLLYGPPGTGKTTLARAIANELfrpGAPFLYLNASDLLEGLVVael 67
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1056850158 189 DGPKLVRELFRVAEEHAPSIVFIDEIDAIGtkrydsnsggeREIQRTMLELLNQL-DGFDSRGDVKVIMATNRIETLDPA 267
Cdd:cd00009    68 FGHFLVRLLFELAEKAKPGVLFIDEIDSLS-----------RGAQNALLRVLETLnDLRIDRENVRVIGATNRPLLGDLD 136
                         170
                  ....*....|....*
gi 1056850158 268 LIRPGRIDRKIEFPL 282
Cdd:cd00009   137 RALYDRLDIRIVIPL 151
RecA-like_BCS1 cd19510
Mitochondrial chaperone BCS1; Mitochondrial chaperone BCS1 is necessary for the assembly of ...
124-280 1.38e-25

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


Pssm-ID: 410918 [Multi-domain]  Cd Length: 153  Bit Score: 100.50  E-value: 1.38e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1056850158 124 IKESVELPLTHPEYYEEMGIKPPKGVILYGPPGTGKTLLAKAVANqtsatFLR--VVGSELIQKYLGDgpKLVRELFRVA 201
Cdd:cd19510     1 IIDDLKDFIKNEDWYNDRGIPYRRGYLLYGPPGTGKSSFIAALAG-----ELDydICDLNLSEVVLTD--DRLNHLLNTA 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1056850158 202 EEHapSIVFIDEIDA-----IGTKRYDSNSGGEREIqrTMLELLNQLDGFDSRGDVKVIMATNRIETLDPALIRPGRIDR 276
Cdd:cd19510    74 PKQ--SIILLEDIDAafesrEHNKKNPSAYGGLSRV--TFSGLLNALDGVASSEERIVFMTTNHIERLDPALIRPGRVDM 149

                  ....
gi 1056850158 277 KIEF 280
Cdd:cd19510   150 KIYM 153
ycf46 CHL00195
Ycf46; Provisional
106-354 9.71e-25

Ycf46; Provisional


Pssm-ID: 177094 [Multi-domain]  Cd Length: 489  Bit Score: 105.10  E-value: 9.71e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1056850158 106 APQETYADIGGLDNQIQEIKESVElplTHPEYYEEMGIKPPKGVILYGPPGTGKTLLAKAVANQTSATFLRVVGSELIQK 185
Cdd:CHL00195  222 SVNEKISDIGGLDNLKDWLKKRST---SFSKQASNYGLPTPRGLLLVGIQGTGKSLTAKAIANDWQLPLLRLDVGKLFGG 298
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1056850158 186 YLGDGPKLVRELFRVAEEHAPSIVFIDEIDAIGTKRYDSN-SGGEREIQRTMLELLNQldgfdSRGDVKVIMATNRIETL 264
Cdd:CHL00195  299 IVGESESRMRQMIRIAEALSPCILWIDEIDKAFSNSESKGdSGTTNRVLATFITWLSE-----KKSPVFVVATANNIDLL 373
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1056850158 265 DPALIRPGRIDRKIEFPLPDEKTKKRIFQIHTSRMTLADDVTLDDLIMAK--DDLSGADIKAICTEAGLMALRERRmKVT 342
Cdd:CHL00195  374 PLEILRKGRFDEIFFLDLPSLEEREKIFKIHLQKFRPKSWKKYDIKKLSKlsNKFSGAEIEQSIIEAMYIAFYEKR-EFT 452
                         250
                  ....*....|..
gi 1056850158 343 NEDFKKSKENVL 354
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 ...
113-276 5.56e-24

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


Pssm-ID: 410915 [Multi-domain]  Cd Length: 161  Bit Score: 96.67  E-value: 5.56e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1056850158 113 DIGGLDNqiqeIKESVEL--PLTHPEYyEEMGIKPPKGVILYGPPGTGKTLLAKAVANQTSATFLRVVGSELIQKYLGDG 190
Cdd:cd19507     1 DVGGLDN----LKDWLKKrkAAFSKQA-SAYGLPTPKGLLLVGIQGTGKSLTAKAIAGVWQLPLLRLDMGRLFGGLVGES 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1056850158 191 PKLVRELFRVAEEHAPSIVFIDEID-AIGTKRYDSNSGGEREIQRTMLELLNQldgfdSRGDVKVIMATNRIETLDPALI 269
Cdd:cd19507    76 ESRLRQMIQTAEAIAPCVLWIDEIEkGFSNADSKGDSGTSSRVLGTFLTWLQE-----KKKPVFVVATANNVQSLPPELL 150

                  ....*..
gi 1056850158 270 RPGRIDR 276
Cdd:cd19507   151 RKGRFDE 157
AAA smart00382
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ...
145-284 5.00e-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: 85.50  E-value: 5.00e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1056850158  145 PPKGVILYGPPGTGKTLLAKAVANQTSATFLRVV-----------------GSELIQKYLGDGPKLVRELFRVAEEHAPS 207
Cdd:smart00382   1 PGEVILIVGPPGSGKTTLARALARELGPPGGGVIyidgedileevldqlllIIVGGKKASGSGELRLRLALALARKLKPD 80
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1056850158  208 IVFIDEIDAIGTKrydsnsggEREIQRTMLELLNQLDGFDSRGDVKVIMATNRIETLDPALIRPgRIDRKIEFPLPD 284
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 ...
149-269 2.19e-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: 70.94  E-value: 2.19e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1056850158 149 VILYGPPGTGKTLLAKAVANQTS---------ATFLRVVGSELIQKYLGDGPKLVRELFR-----VAEEHAPSIVFIDEI 214
Cdd:cd19508    55 VLLHGPPGTGKTSLCKALAQKLSirlssryryGQLIEINSHSLFSKWFSESGKLVTKMFQkiqelIDDKDALVFVLIDEV 134
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1056850158 215 DAIGTKRYDSNSGGE-REIQRTMLELLNQLDGFDSRGDVKVIMATNRIETLDPALI 269
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 ...
147-280 3.05e-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: 61.00  E-value: 3.05e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1056850158 147 KGVILYGPPGTGKTLLAKAVANQTSATFLRVVGSELIQkyLG-DGPKLVRELFRVAEEHAPS-IVFIDEIDAIGTKRyds 224
Cdd:cd19512    23 RNILFYGPPGTGKTLFAKKLALHSGMDYAIMTGGDVAP--MGrEGVTAIHKVFDWANTSRRGlLLFVDEADAFLRKR--- 97
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1056850158 225 NSGGEREIQRTMLELLNQLDGFDSRgDVKVIMATNRIETLDPALirPGRIDRKIEF 280
Cdd:cd19512    98 STEKISEDLRAALNAFLYRTGEQSN-KFMLVLASNQPEQFDWAI--NDRIDEMVEF 150
RarA COG2256
Replication-associated recombination protein RarA (DNA-dependent ATPase) [Replication, ...
149-214 4.67e-10

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


Pssm-ID: 441857 [Multi-domain]  Cd Length: 439  Bit Score: 60.45  E-value: 4.67e-10
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1056850158 149 VILYGPPGTGKTLLAKAVANQTSATFLRV--VGSeliqkylgdGPKLVRELFRVAEEHA----PSIVFIDEI 214
Cdd:COG2256    52 MILWGPPGTGKTTLARLIANATDAEFVALsaVTS---------GVKDIREVIEEARERRaygrRTILFVDEI 114
AAA_lid_3 pfam17862
AAA+ lid domain; This entry represents the alpha helical AAA+ lid domain that is found to the ...
304-348 7.25e-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: 53.70  E-value: 7.25e-10
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 1056850158 304 DVTLDDLIMAKDDLSGADIKAICTEAGLMALRERRMKVTNEDFKK 348
Cdd:pfam17862   1 DVDLEELAERTEGFSGADLEALCREAALAALRRGLEAVTQEDLEE 45
RecA-like_Ycf2 cd19505
ATPase domain of plant YCF2; Ycf2 is a chloroplast ATPase which has an essential function; ...
140-280 1.71e-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: 56.23  E-value: 1.71e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1056850158 140 EMGIKPPKGVILYGPPGTGKTLLAKAVANQTSATFLRVVGSELIQKYLGDGPKLVR--------------ELFRVAEEHA 205
Cdd:cd19505     6 RLGLSPSKGILLIGSIETGRSYLIKSLAANSYVPLIRISLNKLLYNKPDFGNDDWIdgmlilkeslhrlnLQFELAKAMS 85
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1056850158 206 PSIVFIDEIDAIGTKRYDSNSGGEReiqRTMLELLNQLDGFDSRGDVK----VIMATNRIETLDPALIRPGRIDRKIEF 280
Cdd:cd19505    86 PCIIWIPNIHELNVNRSTQNLEEDP---KLLLGLLLNYLSRDFEKSSTrnilVIASTHIPQKVDPALIAPNRLDTCINI 161
Prot_ATP_ID_OB pfam16450
Proteasomal ATPase OB C-terminal domain; This is the interdomain (ID) or oligonucleotide ...
36-90 4.42e-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: 4.42e-09
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1056850158  36 VGTLEEIIDDNHAIVSTSVGSEHYVSILSFVDKDLLEPGCSVLLNHKVHAVIGVL 90
Cdd:pfam16450   1 VATVVEVLDDGRALVKSSGGEERVVRLAGSLDEEKLRPGDRVLLDPRSGYALEVL 55
PRK13342 PRK13342
recombination factor protein RarA; Reviewed
149-214 4.44e-09

recombination factor protein RarA; Reviewed


Pssm-ID: 237355 [Multi-domain]  Cd Length: 413  Bit Score: 57.40  E-value: 4.44e-09
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1056850158 149 VILYGPPGTGKTLLAKAVANQTSATFLRVVGSEliqkylgDGPKLVRELFRVAEEHAPS----IVFIDEI 214
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 ...
116-317 2.53e-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: 55.62  E-value: 2.53e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1056850158 116 GLD---NQIQEIKESVELPLTHpeyyEEMGIKPP---KGVILYGPPGTGKTLLAKAVANQTSA-TFLR------VVGSEL 182
Cdd:TIGR03922 280 GLErvkRQVAALKSSTAMALAR----AERGLPVAqtsNHMLFAGPPGTGKTTIARVVAKIYCGlGVLRkplvreVSRADL 355
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1056850158 183 IQKYLGDGPKLVRELFrvaEEHAPSIVFIDEIDAIGTKRYDSNSGGEREIQRTMLELLNqldgfDSRGDVKVIMA----- 257
Cdd:TIGR03922 356 IGQYIGESEAKTNEII---DSALGGVLFLDEAYTLVETGYGQKDPFGLEAIDTLLARME-----NDRDRLVVIGAgyrkd 427
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1056850158 258 TNRIETLDPALirPGRIDRKIEFP--LPDEktkkrIFQIhTSRMTLADDVTLDDliMAKDDL 317
Cdd:TIGR03922 428 LDKFLEVNEGL--RSRFTRVIEFPsySPDE-----LVEI-ARRMATERDSVLDD--AAADAL 479
TIGR02928 TIGR02928
orc1/cdc6 family replication initiation protein; Members of this protein family are found ...
145-353 5.82e-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: 53.79  E-value: 5.82e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1056850158 145 PPKGVILYGPPGTGKTLLAKAVANQ----TSATFLRV---------------VGSELIQKYLGDGP----------KLVR 195
Cdd:TIGR02928  39 RPSNVFIYGKTGTGKTAVTKYVMKEleeaAEDRDVRVvtvyvncqildtlyqVLVELANQLRGSGEevpttglstsEVFR 118
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1056850158 196 ELFRVAEEHAPSIVFI-DEIDAIgtkrydSNSGGEREIQRTMLELLNQLDGfdsrGDVKVIMATNRI---ETLDPAlIRP 271
Cdd:TIGR02928 119 RLYKELNERGDSLIIVlDEIDYL------VGDDDDLLYQLSRARSNGDLDN----AKVGVIGISNDLkfrENLDPR-VKS 187
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1056850158 272 GRIDRKIEFPLPDEktkKRIFQIHTSRMTLA--DDVTLDDLI------MAKDdlSGADIKAICT--EAGLMALRERRMKV 341
Cdd:TIGR02928 188 SLCEEEIIFPPYDA---EELRDILENRAEKAfyDGVLDDGVIplcaalAAQE--HGDARKAIDLlrVAGEIAEREGAERV 262
                         250
                  ....*....|..
gi 1056850158 342 TNEDFKKSKENV 353
Cdd:TIGR02928 263 TEDHVEKAQEKI 274
RecA-like_HslU cd19498
ATP-dependent protease ATPase subunit HslU; HslU is a component of the ATP-dependent protease ...
146-240 1.46e-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: 50.84  E-value: 1.46e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1056850158 146 PKGVILYGPPGTGKTLLAKAVANQTSATFLRVVGSELIQ-KYLG-DGPKLVRELfrvaeehAPSIVFIDEIDAIGTKRYD 223
Cdd:cd19498    46 PKNILMIGPTGVGKTEIARRLAKLAGAPFIKVEATKFTEvGYVGrDVESIIRDL-------VEGIVFIDEIDKIAKRGGS 118
                          90
                  ....*....|....*...
gi 1056850158 224 SNSGGERE-IQRTMLELL 240
Cdd:cd19498   119 SGPDVSREgVQRDLLPIV 136
RecA-like_ClpB_Hsp104-like cd19499
Chaperone protein ClpB/Hsp104 subfamily; Bacterial Caseinolytic peptidase B (ClpB) and ...
144-280 9.11e-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: 48.71  E-value: 9.11e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1056850158 144 KPPKGVILYGPPGTGKTLLAKAVA---NQTSATFLRVVGSELIQKY-----LGDGPKLV--RELFRVAEE---HAPSIVF 210
Cdd:cd19499    39 RPIGSFLFLGPTGVGKTELAKALAellFGDEDNLIRIDMSEYMEKHsvsrlIGAPPGYVgyTEGGQLTEAvrrKPYSVVL 118
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1056850158 211 IDEIDAigtkrydsnsgGEREIQRTMLELLNqlDGF--DSRG---DVK---VIMATNrieTLDPALIrpGRIDRKIEF 280
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 ...
146-240 1.50e-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: 47.58  E-value: 1.50e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1056850158 146 PKGVILY-GPPGTGKTLLAKAVANQ---TSATFLRVVGSELIQKYL-----GDGPKLVR-----ELFRVAEEHAPSIVFI 211
Cdd:pfam07724   2 PIGSFLFlGPTGVGKTELAKALAELlfgDERALIRIDMSEYMEEHSvsrliGAPPGYVGyeeggQLTEAVRRKPYSIVLI 81
                          90       100
                  ....*....|....*....|....*....
gi 1056850158 212 DEIDAIGtkrydsnsggeREIQRTMLELL 240
Cdd:pfam07724  82 DEIEKAH-----------PGVQNDLLQIL 99
AAA_5 pfam07728
AAA domain (dynein-related subfamily); This Pfam entry includes some of the AAA proteins not ...
148-270 1.74e-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: 1.74e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1056850158 148 GVILYGPPGTGKTLLAKAVANQTS-ATFLRVVGS------ELIQKYL--GDGPKLV-RELFRVAEEhaPSIVFIDEIDAI 217
Cdd:pfam07728   1 GVLLVGPPGTGKTELAERLAAALSnRPVFYVQLTrdtteeDLFGRRNidPGGASWVdGPLVRAARE--GEIAVLDEINRA 78
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1056850158 218 gtkrydsnsggEREIQRTMLELLN-----QLDGF----DSRGDVKVIMATNRIET----LDPALIR 270
Cdd:pfam07728  79 -----------NPDVLNSLLSLLDerrllLPDGGelvkAAPDGFRLIATMNPLDRglneLSPALRS 133
CDC6 COG1474
Cdc6-related protein, AAA superfamily ATPase [Replication, recombination and repair];
118-365 2.54e-06

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


Pssm-ID: 441083 [Multi-domain]  Cd Length: 389  Bit Score: 49.08  E-value: 2.54e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1056850158 118 DNQIQEIKESVElPLTHPEyyeemgikPPKGVILYGPPGTGKTLLAKAVANQ---------TSATFLRV----------V 178
Cdd:COG1474    32 EEEIEELASALR-PALRGE--------RPSNVLIYGPTGTGKTAVAKYVLEEleeeaeergVDVRVVYVncrqastryrV 102
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1056850158 179 GSELIQKyLGDGP----------KLVRELFRVAEEHAPSIVFI-DEIDAIGTKRYDsnsggerEIQRTMLELLNQLDGfd 247
Cdd:COG1474   103 LSRILEE-LGSGEdipstglstdELFDRLYEALDERDGVLVVVlDEIDYLVDDEGD-------DLLYQLLRANEELEG-- 172
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1056850158 248 srGDVKVIMATNRI---ETLDPALIRPGRiDRKIEFPlP---DEktkkrIFQIHTSR--MTLADDVTLDDLIMAKDDLSG 319
Cdd:COG1474   173 --ARVGVIGISNDLeflENLDPRVKSSLG-EEEIVFP-PydaDE-----LRDILEDRaeLAFYDGVLSDEVIPLIAALAA 243
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1056850158 320 ADI----KAICT--EAGLMALRERRMKVTNEDFKKSKENVLYKKQEGTPEGL 365
Cdd:COG1474   244 QEHgdarKAIDLlrVAGEIAEREGSDRVTEEHVREAREKIERDRLLEVLRGL 295
PRK04195 PRK04195
replication factor C large subunit; Provisional
144-232 6.32e-06

replication factor C large subunit; Provisional


Pssm-ID: 235250 [Multi-domain]  Cd Length: 482  Bit Score: 47.99  E-value: 6.32e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1056850158 144 KPPKGVILYGPPGTGKTLLAKAVAN-------------QTSATFL-RVVGSELIQKYLGDGPKlvrelfrvaeehapSIV 209
Cdd:PRK04195   37 KPKKALLLYGPPGVGKTSLAHALANdygwevielnasdQRTADVIeRVAGEAATSGSLFGARR--------------KLI 102
                          90       100
                  ....*....|....*....|...
gi 1056850158 210 FIDEIDAIgTKRYDsnSGGEREI 232
Cdd:PRK04195  103 LLDEVDGI-HGNED--RGGARAI 122
MoxR COG0714
MoxR-like ATPase [General function prediction only]; MoxR-like ATPase is part of the Pathway ...
149-215 9.60e-06

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


Pssm-ID: 440478 [Multi-domain]  Cd Length: 292  Bit Score: 46.70  E-value: 9.60e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1056850158 149 VILYGPPGTGKTLLAKAVANQTSATFLRV-----------VGSELIQKYLGD-----GPklvreLFRvaeehapSIVFID 212
Cdd:COG0714    34 LLLEGVPGVGKTTLAKALARALGLPFIRIqftpdllpsdiLGTYIYDQQTGEfefrpGP-----LFA-------NVLLAD 101

                  ...
gi 1056850158 213 EID 215
Cdd:COG0714   102 EIN 104
DUF815 pfam05673
Protein of unknown function (DUF815); This family consists of several bacterial proteins of ...
112-212 1.25e-05

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


Pssm-ID: 428578 [Multi-domain]  Cd Length: 250  Bit Score: 45.99  E-value: 1.25e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1056850158 112 ADIGGLDNQIQEIKESVELPLTHpeyyeemgiKPPKGVILYGPPGTGKTLLAKAVANQTSATFLRVVgsELIQKYLGDGP 191
Cdd:pfam05673  28 DDLVGIERQKEALIRNTRRFLAG---------LPANNVLLWGARGTGKSSLVKALLNEYADQGLRLI--EVDKEDLGDLP 96
                          90       100
                  ....*....|....*....|.
gi 1056850158 192 KLVRELFRVAEEHapsIVFID 212
Cdd:pfam05673  97 DLVDLLRDRPYRF---ILFCD 114
PRK13341 PRK13341
AAA family ATPase;
150-214 2.48e-05

AAA family ATPase;


Pssm-ID: 237354 [Multi-domain]  Cd Length: 725  Bit Score: 46.20  E-value: 2.48e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1056850158 150 ILYGPPGTGKTLLAKAVANQTSATFLrVVGSELiqkylgDGPKLVRELFRVAEEHAP-----SIVFIDEI 214
Cdd:PRK13341   56 ILYGPPGVGKTTLARIIANHTRAHFS-SLNAVL------AGVKDLRAEVDRAKERLErhgkrTILFIDEV 118
RecA-like_superfamily cd01120
RecA-like_NTPases; RecA-like NTPases. This superfamily includes the NTP binding domain of F1 ...
149-265 3.25e-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: 42.88  E-value: 3.25e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1056850158 149 VILYGPPGTGKTLLAKAVANQTSATFLRVVGSELIQKYLgdgpklvRELFRVAEEHAPSIVFIDEIDAIGTKRYDSNSGG 228
Cdd:cd01120     1 ILITGPPGSGKTTLLLQFAEQALLSDEPVIFISFLDTIL-------EAIEDLIEEKKLDIIIIDSLSSLARASQGDRSSE 73
                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 1056850158 229 EREIQRTMLELLNQLDgfdsrgdvKVIMATNRIETLD 265
Cdd:cd01120    74 LLEDLAKLLRAARNTG--------ITVIATIHSDKFD 102
McrB COG1401
5-methylcytosine-specific restriction endonuclease McrBC, GTP-binding regulatory subunit McrB ...
103-214 3.67e-05

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


Pssm-ID: 441011 [Multi-domain]  Cd Length: 477  Bit Score: 45.53  E-value: 3.67e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1056850158 103 VEKAPQETYADIGGLDNQIQEIKESVELPLTHPEYYEEMG-------------IKPPKGVILYGPPGTGKTLLAKAVANQ 169
Cdd:COG1401   165 LLAAPEDLSADALAAELSAAEELYSEDLESEDDYLKDLLRekfeetleaflaaLKTKKNVILAGPPGTGKTYLARRLAEA 244
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1056850158 170 TSAT----FLRVV------GSELIQKY---LGDG-----PKLVRELFRVAEEH--APSIVFIDEI 214
Cdd:COG1401   245 LGGEdngrIEFVQfhpswsYEDFLLGYrpsLDEGkyeptPGIFLRFCLKAEKNpdKPYVLIIDEI 309
AAA_22 pfam13401
AAA domain;
149-257 4.47e-05

AAA domain;


Pssm-ID: 379165 [Multi-domain]  Cd Length: 129  Bit Score: 42.71  E-value: 4.47e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1056850158 149 VILYGPPGTGKTLLAKAVANQ-----------------TSATFLRVVGSELIQKYLGDGPK--LVRELFRVAEEHAPSIV 209
Cdd:pfam13401   8 LVLTGESGTGKTTLLRRLLEQlpevrdsvvfvdlpsgtSPKDLLRALLRALGLPLSGRLSKeeLLAALQQLLLALAVAVV 87
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 1056850158 210 F-IDEIDAigtkrydsnsggereIQRTMLELLNQLDGFdSRGDVKVIMA 257
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 ...
147-218 5.15e-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: 43.32  E-value: 5.15e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1056850158 147 KGVIL--YGPPGTGKTLLAKAVANQTSATFLRV-VG-----SELI---QKYLGDGPKLVRELFRVAEEHAPSIVfIDEID 215
Cdd:cd19500    36 KGPILclVGPPGVGKTSLGKSIARALGRKFVRIsLGgvrdeAEIRghrRTYVGAMPGRIIQALKKAGTNNPVFL-LDEID 114

                  ...
gi 1056850158 216 AIG 218
Cdd:cd19500   115 KIG 117
ruvB PRK00080
Holliday junction branch migration DNA helicase RuvB;
149-214 5.65e-05

Holliday junction branch migration DNA helicase RuvB;


Pssm-ID: 234619 [Multi-domain]  Cd Length: 328  Bit Score: 44.35  E-value: 5.65e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1056850158 149 VILYGPPGTGKTLLAKAVANQTSATfLRVVGSELIQKyLGDgpkLVReLFRVAEEHapSIVFIDEI 214
Cdd:PRK00080   54 VLLYGPPGLGKTTLANIIANEMGVN-IRITSGPALEK-PGD---LAA-ILTNLEEG--DVLFIDEI 111
DnaC COG1484
DNA replication protein DnaC [Replication, recombination and repair];
143-197 7.89e-05

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


Pssm-ID: 441093 [Multi-domain]  Cd Length: 242  Bit Score: 43.62  E-value: 7.89e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1056850158 143 IKPPKGVILYGPPGTGKTLLAKAVANQ-----TSATFLRVvgseliqkylgdgPKLVREL 197
Cdd:COG1484    96 IERGENLILLGPPGTGKTHLAIALGHEacragYRVRFTTA-------------PDLVNEL 142
COG2842 COG2842
Bacteriophage DNA transposition protein, AAA+ family ATPase [Mobilome: prophages, transposons]; ...
149-348 1.30e-04

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


Pssm-ID: 442090 [Multi-domain]  Cd Length: 254  Bit Score: 43.02  E-value: 1.30e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1056850158 149 VILYGPPGTGKTLLAKAVANQ-------------TSATFLRVVGSELiqkYLGDGPKLVRELFRVAEEH---APSIVFID 212
Cdd:COG2842    53 GVVYGESGVGKTTAAREYANRnpnviyvtaspswTSKELLEELAEEL---GIPAPPGTIADLRDRILERlagTGRLLIID 129
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1056850158 213 EIDAIGTKrydsnsggereiqrtMLELLNQLdgFDsRGDVKVIMATNriETLDPALIRPGRIDRKIEFPLPDEKTKKRIF 292
Cdd:COG2842   130 EADHLKPK---------------ALEELRDI--HD-ETGVGVVLIGM--ERLPAKLKRYEQLYSRIGFWVEFKPLSLEDV 189
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1056850158 293 QIhtsrmtLAD---DVTLDDLIMAKDDLSGADIKAICT---EAGLMALRERRMKVTNEDFKK 348
Cdd:COG2842   190 RA------LAEawgELTDPDLLELLHRITRGNLRRLDRtlrLAARAAKRNGLTKITLDHVRA 245
44 PHA02544
clamp loader, small subunit; Provisional
150-294 1.58e-04

clamp loader, small subunit; Provisional


Pssm-ID: 222866 [Multi-domain]  Cd Length: 316  Bit Score: 43.05  E-value: 1.58e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1056850158 150 ILYGP-PGTGKTLLAKAVANQTSATFLRVVGSEliqkylgDGPKLVR-ELFRVAE----EHAPSIVFIDEIDAIGTKryd 223
Cdd:PHA02544   46 LLHSPsPGTGKTTVAKALCNEVGAEVLFVNGSD-------CRIDFVRnRLTRFAStvslTGGGKVIIIDEFDRLGLA--- 115
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1056850158 224 snsggerEIQRTMLELLNQLDgfdsrGDVKVIMATNRIETLDPALIrpGRIdRKIEFPLPDEKTK--------KRIFQI 294
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 ...
149-220 1.96e-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: 42.59  E-value: 1.96e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1056850158 149 VILYGPPGTGKTLLAK----------AVANQTSATFLRVVG-------SELIQKYLGDGPKlvrelfrvAEEhapSIVFI 211
Cdd:cd19497    53 ILLIGPTGSGKTLLAQtlakildvpfAIADATTLTEAGYVGedvenilLKLLQAADYDVER--------AQR---GIVYI 121

                  ....*....
gi 1056850158 212 DEIDAIGTK 220
Cdd:cd19497   122 DEIDKIARK 130
RuvB_N pfam05496
Holliday junction DNA helicase RuvB P-loop domain; The RuvB protein makes up part of the ...
149-214 2.83e-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: 2.83e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1056850158 149 VILYGPPGTGKTLLAKAVANQTSATFlRVVGSELIQKyLGDGPKLVRELfrvaEEHapSIVFIDEI 214
Cdd:pfam05496  36 VLLYGPPGLGKTTLANIIANEMGVNI-RITSGPAIER-PGDLAAILTNL----EPG--DVLFIDEI 93
IS21_help_AAA NF038214
IS21-like element helper ATPase IstB; This protein family model resembles PF01695, but was ...
149-214 2.84e-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: 41.69  E-value: 2.84e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1056850158 149 VILYGPPGTGKTLLAKAVANQ-----TSATFLRVvgSELIQKYL---GDGpKLVRELFRVAeehAPSIVFIDEI 214
Cdd:NF038214   93 VLLLGPPGTGKTHLAIALGYAacrqgYRVRFTTA--ADLVEQLAqarADG-RLGRLLRRLA---RYDLLIIDEL 160
RecA-like_IQCA1 cd19506
ATPase domain of IQ and AAA domain-containing protein 1 (IQCA1); IQCA1 (also known as dynein ...
147-213 3.20e-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: 40.97  E-value: 3.20e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1056850158 147 KGVILYGPPGTGKTLLAKAVANQTSATFLRVVGSELIQKYLGDG--PKLVRELFRVAEEHAPSIVFIDE 213
Cdd:cd19506    27 KSLLLAGPSGVGKKMLVHAICTETGANLFNLSPSNIAGKYPGKNglQMMLHLVLKVARQLQPSVIWIGD 95
PRK08116 PRK08116
hypothetical protein; Validated
138-178 5.76e-04

hypothetical protein; Validated


Pssm-ID: 236153 [Multi-domain]  Cd Length: 268  Bit Score: 41.16  E-value: 5.76e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 1056850158 138 YEEMGiKPPKGVILYGPPGTGKTLLAKAVANQTSATFLRVV 178
Cdd:PRK08116  107 FEEMK-KENVGLLLWGSVGTGKTYLAACIANELIEKGVPVI 146
RecA-like cd01393
RecA family; RecA is a bacterial enzyme which has roles in homologous recombination, DNA ...
151-271 5.87e-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: 5.87e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1056850158 151 LYGPPGTGKTLLA-KAVAN-----------QTSATF---------LRVVGSELIQKYLGDGPKLVR-----ELFRVAEEH 204
Cdd:cd01393     6 IYGPPGSGKTQLAlQLAANalllgggvvwiDTEGAFppsrlvqilEASPSSELELAEALSRLLYFRppdtlAHLLALDSL 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1056850158 205 AP--------SIVFIDEIDAIGTKRYDSNSGGEREI---QRTMLELLNQLDGFDSRGDVKVI----MATNRIETLDPALI 269
Cdd:cd01393    86 PEslfpppntSLVVVDSVSALFRKAFPRGGDGDSSSslrARLLSQLARALQKLAAQFNLAVVvtnqVTTKIRGGSGASLV 165

                  ..
gi 1056850158 270 RP 271
Cdd:cd01393   166 PP 167
ruvB TIGR00635
Holliday junction DNA helicase, RuvB subunit; All proteins in this family for which functions ...
149-218 6.97e-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: 6.97e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1056850158 149 VILYGPPGTGKTLLAKAVANQTSaTFLRVVGSELIQKylgdgPKLVRELFRVAEEHapSIVFIDEIDAIG 218
Cdd:TIGR00635  33 LLLYGPPGLGKTTLAHIIANEMG-VNLKITSGPALEK-----PGDLAAILTNLEEG--DVLFIDEIHRLS 94
ExeA COG3267
Type II secretory pathway ATPase component GspA/ExeA/MshM [Intracellular trafficking, ...
142-213 2.47e-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: 2.47e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1056850158 142 GIKPPKGVI-LYGPPGTGKTLLAKAVANQ---------------TSATFLRVVGSELIQKYLGDGPK-----LVRELFRV 200
Cdd:COG3267    38 ALAQGGGFVvLTGEVGTGKTTLLRRLLERlpddvkvayipnpqlSPAELLRAIADELGLEPKGASKAdllrqLQEFLLEL 117
                          90
                  ....*....|...
gi 1056850158 201 AEEHAPSIVFIDE 213
Cdd:COG3267   118 AAAGRRVVLIIDE 130
ycf2 CHL00206
Ycf2; Provisional
140-245 2.99e-03

Ycf2; Provisional


Pssm-ID: 214396 [Multi-domain]  Cd Length: 2281  Bit Score: 39.89  E-value: 2.99e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1056850158  140 EMGIKPPKGVILYGPPGTGKTLLAKAVANQTSATFLRVvgseLIQKYLGDGPKLvrelfrvaeehapsiVFIDEIDAIGT 219
Cdd:CHL00206  1624 RLALSPSRGILVIGSIGTGRSYLVKYLATNSYVPFITV----FLNKFLDNKPKG---------------FLIDDIDIDDS 1684
                           90       100
                   ....*....|....*....|....*.
gi 1056850158  220 KRYDSNSGGEREIQRTMLELLNQLDG 245
Cdd:CHL00206  1685 DDIDDSDDIDRDLDTELLTMMNALTM 1710
COG0645 COG0645
Predicted kinase, contains AAA domain [General function prediction only];
149-205 3.51e-03

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


Pssm-ID: 440410 [Multi-domain]  Cd Length: 164  Bit Score: 37.97  E-value: 3.51e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1056850158 149 VILYGPPGTGKTLLAKAVANQTSATFLR--VVGSEL-------IQKYLGDGPKLVRELFRVAEEHA 205
Cdd:COG0645     2 ILVCGLPGSGKSTLARALAERLGAVRLRsdVVRKRLfgaglapLERSPEATARTYARLLALARELL 67
DnaA COG0593
Chromosomal replication initiation ATPase DnaA [Replication, recombination and repair];
151-305 4.65e-03

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


Pssm-ID: 440358 [Multi-domain]  Cd Length: 303  Bit Score: 38.63  E-value: 4.65e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1056850158 151 LYGPPGTGKTLLAKAVANQTSATF--LRVV-------GSELIQKYLGDGPKLVRELFRvaeehAPSIVFIDEIDAIGTKR 221
Cdd:COG0593    39 LYGGVGLGKTHLLHAIGNEALENNpgARVVyltaeefTNDFINAIRNNTIEEFKEKYR-----SVDVLLIDDIQFLAGKE 113
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1056850158 222 YDsnsggereiQRTMLELLNQLdgFDSRGdvKVIMATNR----IETLDPAL-----------IRPgridrkiefplPDEK 286
Cdd:COG0593   114 AT---------QEEFFHTFNAL--REAGK--QIVLTSDRppkeLPGLEERLrsrlewglvvdIQP-----------PDLE 169
                         170       180
                  ....*....|....*....|.
gi 1056850158 287 TKKRIFQ--IHTSRMTLADDV 305
Cdd:COG0593   170 TRIAILRkkAADRGLELPDEV 190
RNA_helicase pfam00910
RNA helicase; This family includes RNA helicases thought to be involved in duplex unwinding ...
149-180 5.90e-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: 5.90e-03
                          10        20        30
                  ....*....|....*....|....*....|..
gi 1056850158 149 VILYGPPGTGKTLLAKAVANQTSATFLRVVGS 180
Cdd:pfam00910   1 IWLYGPPGCGKSTLAKYLARALLKKLGLPKDS 32
recomb_radB TIGR02237
DNA repair and recombination protein RadB; This family consists exclusively of archaeal RadB ...
147-271 6.96e-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: 37.40  E-value: 6.96e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1056850158 147 KGVI--LYGPPGTGKTLLAKAVANQTSATFLRVV-------GSELIQKYLGDGPKLV-------------------RELF 198
Cdd:TIGR02237  11 RGTItqIYGPPGSGKTNICMILAVNAARQGKKVVyidteglSPERFKQIAEDRPERAlsnfivfevfdfdeqgvaiQKTS 90
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1056850158 199 RVAEEHAPSIVFIDEIDAI-GTKRYDSNSGGEREIQRTMLELLnqldGFDSRGDVKVIMaTNRI-ETLDPALIRP 271
Cdd:TIGR02237  91 KFIDRDSASLVVVDSFTALyRLELSDDRISRNRELARQLTLLL----SLARKKNLAVVI-TNQVyTDVNNGTLRP 160
Mg_chelatase pfam01078
Magnesium chelatase, subunit ChlI; Magnesium-chelatase is a three-component enzyme that ...
149-165 7.75e-03

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


Pssm-ID: 426032 [Multi-domain]  Cd Length: 207  Bit Score: 37.13  E-value: 7.75e-03
                          10
                  ....*....|....*..
gi 1056850158 149 VILYGPPGTGKTLLAKA 165
Cdd:pfam01078  25 LLMIGPPGSGKTMLAKR 41
AAA_16 pfam13191
AAA ATPase domain; This family of domains contain a P-loop motif that is characteriztic of the ...
116-267 7.91e-03

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


Pssm-ID: 433025 [Multi-domain]  Cd Length: 167  Bit Score: 36.71  E-value: 7.91e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1056850158 116 GLDNQIQEIKEsvelplthpeYYEEMGIKPPKGVILYGPPGTGKTLLAKAVANQ---TSATFLRVVGSELIqKYLGDGPK 192
Cdd:pfam13191   4 GREEELEQLLD----------ALDRVRSGRPPSVLLTGEAGTGKTTLLRELLRAlerDGGYFLRGKCDENL-PYSPLLEA 72
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1056850158 193 LVRELFRVAEEHAPSIVFIDEIDAIGTKRYDSNSGGEREIQRTMLELLNQLDGFDSRGDVKVIMATNRIETLDPA 267
Cdd:pfam13191  73 LTREGLLRQLLDELESSLLEAWRAALLEALAPVPELPGDLAERLLDLLLRLLDLLARGERPLVLVLDDLQWADEA 147
YifB COG0606
Predicted Mg-chelatase, contains ChlI-like and ATPase domains, YifB family [Posttranslational ...
149-164 9.73e-03

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


Pssm-ID: 440371 [Multi-domain]  Cd Length: 502  Bit Score: 37.71  E-value: 9.73e-03
                          10
                  ....*....|....*.
gi 1056850158 149 VILYGPPGTGKTLLAK 164
Cdd:COG0606   214 LLMIGPPGSGKTMLAR 229
 
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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