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Conserved domains on  [gi|18860063|ref|NP_572686|]
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regulatory particle triple-A ATPase 3, isoform A [Drosophila melanogaster]

Protein Classification

26S proteasome regulatory subunit 6B( domain architecture ID 11488542)

26S proteasome regulatory subunit 6B 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
PTZ00454 PTZ00454
26S protease regulatory subunit 6B-like protein; Provisional
22-413 0e+00

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


:

Pssm-ID: 240423 [Multi-domain]  Cd Length: 398  Bit Score: 771.63  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18860063   22 DAHSSLDELDMEDLYVRYKKLQKTLEFIEVQEEYIKDEQRNLKKEYLHAQEEVKRIQSVPLVIGQFLEAVDQNTGIVGST 101
Cdd:PTZ00454   7 AAVASSTTHTERDLYEKLKELEKELEFLDIQEEYIKEEQKNLKRELIRAKEEVKRIQSVPLVIGQFLEMIDSNYGIVSST 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18860063  102 TGSNYYVRILSTIDRELLKPSASVALHKHSNALVDVLPPEADSSISMLQPDEKPDVSYADIGGMDMQKQEIREAVELPLT 181
Cdd:PTZ00454  87 SGSNYYVRILSTLNRELLKPNASVALHRHSHAVVDILPPEADSSIQLLQMSEKPDVTYSDIGGLDIQKQEIREAVELPLT 166
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18860063  182 HFELYKQIGIDPPRGVLMYGPPGCGKTMLAKAVAHHTTASFIRVVGSEFVQKYLGEGPRMVRDVFRLAKENAPAIIFIDE 261
Cdd:PTZ00454 167 CPELYEQIGIDPPRGVLLYGPPGTGKTMLAKAVAHHTTATFIRVVGSEFVQKYLGEGPRMVRDVFRLARENAPSIIFIDE 246
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18860063  262 IDAIATKRFDAQTGADREVQRILLELLNQMDGFDQTTNVKVIMATNRADTLDPALLRPGRLDRKIEFPLPDRRQKRLVFS 341
Cdd:PTZ00454 247 VDSIATKRFDAQTGADREVQRILLELLNQMDGFDQTTNVKVIMATNRADTLDPALLRPGRLDRKIEFPLPDRRQKRLIFQ 326
                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 18860063  342 TITSKMNLSEDVDLEEFVARPDKISGADINAICQEAGMHAVRENRYIVLAKDFEKGYKNNIKKDEQEHEFYK 413
Cdd:PTZ00454 327 TITSKMNLSEEVDLEDFVSRPEKISAADIAAICQEAGMQAVRKNRYVILPKDFEKGYKTVVRKTDRDYDFYS 398
 
Name Accession Description Interval E-value
PTZ00454 PTZ00454
26S protease regulatory subunit 6B-like protein; Provisional
22-413 0e+00

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


Pssm-ID: 240423 [Multi-domain]  Cd Length: 398  Bit Score: 771.63  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18860063   22 DAHSSLDELDMEDLYVRYKKLQKTLEFIEVQEEYIKDEQRNLKKEYLHAQEEVKRIQSVPLVIGQFLEAVDQNTGIVGST 101
Cdd:PTZ00454   7 AAVASSTTHTERDLYEKLKELEKELEFLDIQEEYIKEEQKNLKRELIRAKEEVKRIQSVPLVIGQFLEMIDSNYGIVSST 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18860063  102 TGSNYYVRILSTIDRELLKPSASVALHKHSNALVDVLPPEADSSISMLQPDEKPDVSYADIGGMDMQKQEIREAVELPLT 181
Cdd:PTZ00454  87 SGSNYYVRILSTLNRELLKPNASVALHRHSHAVVDILPPEADSSIQLLQMSEKPDVTYSDIGGLDIQKQEIREAVELPLT 166
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18860063  182 HFELYKQIGIDPPRGVLMYGPPGCGKTMLAKAVAHHTTASFIRVVGSEFVQKYLGEGPRMVRDVFRLAKENAPAIIFIDE 261
Cdd:PTZ00454 167 CPELYEQIGIDPPRGVLLYGPPGTGKTMLAKAVAHHTTATFIRVVGSEFVQKYLGEGPRMVRDVFRLARENAPSIIFIDE 246
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18860063  262 IDAIATKRFDAQTGADREVQRILLELLNQMDGFDQTTNVKVIMATNRADTLDPALLRPGRLDRKIEFPLPDRRQKRLVFS 341
Cdd:PTZ00454 247 VDSIATKRFDAQTGADREVQRILLELLNQMDGFDQTTNVKVIMATNRADTLDPALLRPGRLDRKIEFPLPDRRQKRLIFQ 326
                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 18860063  342 TITSKMNLSEDVDLEEFVARPDKISGADINAICQEAGMHAVRENRYIVLAKDFEKGYKNNIKKDEQEHEFYK 413
Cdd:PTZ00454 327 TITSKMNLSEEVDLEDFVSRPEKISAADIAAICQEAGMQAVRKNRYVILPKDFEKGYKTVVRKTDRDYDFYS 398
26Sp45 TIGR01242
26S proteasome subunit P45 family; Many proteins may score above the trusted cutoff because an ...
34-396 8.86e-149

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


Pssm-ID: 130309 [Multi-domain]  Cd Length: 364  Bit Score: 426.14  E-value: 8.86e-149
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18860063    34 DLYVRYKKLQKTLEFIEVQEEYIKDEQRNLKKEylhaqeeVKRIQSVPLVIGQFLEAVDQNTGIVGSTTGSNYYVRILST 113
Cdd:TIGR01242   3 ELDVRIRKLEDEKRSLEKEKIRLERELERLRSE-------IERLRSPPLIVGTVLEVLDDNRVVVKSSTGPNFVVNVSAF 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18860063   114 IDRELLKPSASVALHKHSNALVDVLPPEADSSISMLQPDEKPDVSYADIGGMDMQKQEIREAVELPLTHFELYKQIGIDP 193
Cdd:TIGR01242  76 IDRKSLKPGARVALNQQTLTIVDVLPTSKDPLVKGMEVEERPNVSYEDIGGLEEQIREIREAVELPLKHPELFEEVGIEP 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18860063   194 PRGVLMYGPPGCGKTMLAKAVAHHTTASFIRVVGSEFVQKYLGEGPRMVRDVFRLAKENAPAIIFIDEIDAIATKRFDAQ 273
Cdd:TIGR01242 156 PKGVLLYGPPGTGKTLLAKAVAHETNATFIRVVGSELVRKYIGEGARLVREIFELAKEKAPSIIFIDEIDAIAAKRTDSG 235
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18860063   274 TGADREVQRILLELLNQMDGFDQTTNVKVIMATNRADTLDPALLRPGRLDRKIEFPLPDRRQKRLVFSTITSKMNLSEDV 353
Cdd:TIGR01242 236 TSGDREVQRTLMQLLAELDGFDPRGNVKVIAATNRPDILDPALLRPGRFDRIIEVPLPDFEGRLEILKIHTRKMKLAEDV 315
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|...
gi 18860063   354 DLEEFVARPDKISGADINAICQEAGMHAVRENRYIVLAKDFEK 396
Cdd:TIGR01242 316 DLEAIAKMTEGASGADLKAICTEAGMFAIREERDYVTMDDFIK 358
RPT1 COG1222
ATP-dependent 26S proteasome regulatory subunit [Posttranslational modification, protein ...
151-408 1.08e-130

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


Pssm-ID: 440835 [Multi-domain]  Cd Length: 326  Bit Score: 378.97  E-value: 1.08e-130
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18860063 151 PDEKPDVSYADIGGMDMQKQEIREAVELPLTHFELYKQIGIDPPRGVLMYGPPGCGKTMLAKAVAHHTTASFIRVVGSEF 230
Cdd:COG1222  69 PAESPDVTFDDIGGLDEQIEEIREAVELPLKNPELFRKYGIEPPKGVLLYGPPGTGKTLLAKAVAGELGAPFIRVRGSEL 148
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18860063 231 VQKYLGEGPRMVRDVFRLAKENAPAIIFIDEIDAIATKRFDAQTGAdrEVQRILLELLNQMDGFDQTTNVKVIMATNRAD 310
Cdd:COG1222 149 VSKYIGEGARNVREVFELAREKAPSIIFIDEIDAIAARRTDDGTSG--EVQRTVNQLLAELDGFESRGDVLIIAATNRPD 226
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18860063 311 TLDPALLRPGRLDRKIEFPLPDRRQKRLVFSTITSKMNLSEDVDLEEFVARPDKISGADINAICQEAGMHAVRENRYIVL 390
Cdd:COG1222 227 LLDPALLRPGRFDRVIEVPLPDEEAREEILKIHLRDMPLADDVDLDKLAKLTEGFSGADLKAIVTEAGMFAIREGRDTVT 306
                       250
                ....*....|....*...
gi 18860063 391 AKDFEKGYKNNIKKDEQE 408
Cdd:COG1222 307 MEDLEKAIEKVKKKTETA 324
RecA-like_PAN_like cd19502
proteasome activating nucleotidase PAN and related proteasome subunits; This subfamily ...
158-328 5.70e-117

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: 338.16  E-value: 5.70e-117
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18860063 158 SYADIGGMDMQKQEIREAVELPLTHFELYKQIGIDPPRGVLMYGPPGCGKTMLAKAVAHHTTASFIRVVGSEFVQKYLGE 237
Cdd:cd19502   1 TYEDIGGLDEQIREIREVVELPLKHPELFEELGIEPPKGVLLYGPPGTGKTLLAKAVANHTDATFIRVVGSELVQKYIGE 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18860063 238 GPRMVRDVFRLAKENAPAIIFIDEIDAIATKRFDAQTGADREVQRILLELLNQMDGFDQTTNVKVIMATNRADTLDPALL 317
Cdd:cd19502  81 GARLVRELFEMAREKAPSIIFIDEIDAIGAKRFDSGTGGDREVQRTMLELLNQLDGFDPRGNIKVIMATNRPDILDPALL 160
                       170
                ....*....|.
gi 18860063 318 RPGRLDRKIEF 328
Cdd:cd19502 161 RPGRFDRKIEF 171
AAA pfam00004
ATPase family associated with various cellular activities (AAA); AAA family proteins often ...
197-330 2.22e-54

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


Pssm-ID: 459627 [Multi-domain]  Cd Length: 130  Bit Score: 176.63  E-value: 2.22e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18860063   197 VLMYGPPGCGKTMLAKAVAHHTTASFIRVVGSEFVQKYLGEGPRMVRDVFRLAKENAPAIIFIDEIDAIATKRFDaqtGA 276
Cdd:pfam00004   1 LLLYGPPGTGKTTLAKAVAKELGAPFIEISGSELVSKYVGESEKRLRELFEAAKKLAPCVIFIDEIDALAGSRGS---GG 77
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 18860063   277 DREVQRILLELLNQMDGFDQTT-NVKVIMATNRADTLDPALLrpGRLDRKIEFPL 330
Cdd:pfam00004  78 DSESRRVVNQLLTELDGFTSSNsKVIVIAATNRPDKLDPALL--GRFDRIIEFPL 130
cell_div_CdvC NF041006
cell division protein CdvC;
153-384 1.79e-51

cell division protein CdvC;


Pssm-ID: 468935 [Multi-domain]  Cd Length: 371  Bit Score: 176.85  E-value: 1.79e-51
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18860063  153 EKPDVSYADIGGMDMQKQEIREAVELPLTHFELYKqigIDPPRGVLMYGPPGCGKTMLAKAVAHHTTASFIRVVGSEFVQ 232
Cdd:NF041006  96 EKPKVTFSDIVGLEDVKEALKEAIVYPSKRPDLFP---LGWPRGILLYGPPGCGKTMLAAAVANEIDSEFIHVDAASIMS 172
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18860063  233 KYLGEGPRMVRDVFRLA-----KENAPAIIFIDEIDAIATKrFDAQTGADREVQRillELLNQMDGF---DQTTNVKVIM 304
Cdd:NF041006 173 KWLGEAEKNVAKIFKKArekskEEGKPAIIFIDEIDALLGV-YSSEVGGEVRVRN---QFLKEMDGLqdkSENYHVYVIG 248
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18860063  305 ATNRADTLDPALLRpgRLDRKIEFPLPDRRQKRLVFSTITSKMNLSEDVDLEEFVARPDKISGADINAICQEAGMHAVRE 384
Cdd:NF041006 249 ATNKPWRLDEPFLR--RFQKRIYIPLPDREQRLELLKYYTSKIKLENDVDLDELAEMTEGYTASDIRDIVQAAHMRVVKE 326
AAA smart00382
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ...
193-332 6.25e-21

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: 88.58  E-value: 6.25e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18860063    193 PPRGVLMYGPPGCGKTMLAKAVAHH---TTASFIRVVGSEF--------------VQKYLGEGPRMVRDVFRLAKENAPA 255
Cdd:smart00382   1 PGEVILIVGPPGSGKTTLARALARElgpPGGGVIYIDGEDIleevldqllliivgGKKASGSGELRLRLALALARKLKPD 80
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 18860063    256 IIFIDEIDAIATKRFdaqtgadrEVQRILLELLNQMDGFDQTTNVKVIMATNRADTLDPALLRPgRLDRKIEFPLPD 332
Cdd:smart00382  81 VLILDEITSLLDAEQ--------EALLLLLEELRLLLLLKSEKNLTVILTTNDEKDLGPALLRR-RFDRRIVLLLIL 148
 
Name Accession Description Interval E-value
PTZ00454 PTZ00454
26S protease regulatory subunit 6B-like protein; Provisional
22-413 0e+00

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


Pssm-ID: 240423 [Multi-domain]  Cd Length: 398  Bit Score: 771.63  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18860063   22 DAHSSLDELDMEDLYVRYKKLQKTLEFIEVQEEYIKDEQRNLKKEYLHAQEEVKRIQSVPLVIGQFLEAVDQNTGIVGST 101
Cdd:PTZ00454   7 AAVASSTTHTERDLYEKLKELEKELEFLDIQEEYIKEEQKNLKRELIRAKEEVKRIQSVPLVIGQFLEMIDSNYGIVSST 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18860063  102 TGSNYYVRILSTIDRELLKPSASVALHKHSNALVDVLPPEADSSISMLQPDEKPDVSYADIGGMDMQKQEIREAVELPLT 181
Cdd:PTZ00454  87 SGSNYYVRILSTLNRELLKPNASVALHRHSHAVVDILPPEADSSIQLLQMSEKPDVTYSDIGGLDIQKQEIREAVELPLT 166
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18860063  182 HFELYKQIGIDPPRGVLMYGPPGCGKTMLAKAVAHHTTASFIRVVGSEFVQKYLGEGPRMVRDVFRLAKENAPAIIFIDE 261
Cdd:PTZ00454 167 CPELYEQIGIDPPRGVLLYGPPGTGKTMLAKAVAHHTTATFIRVVGSEFVQKYLGEGPRMVRDVFRLARENAPSIIFIDE 246
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18860063  262 IDAIATKRFDAQTGADREVQRILLELLNQMDGFDQTTNVKVIMATNRADTLDPALLRPGRLDRKIEFPLPDRRQKRLVFS 341
Cdd:PTZ00454 247 VDSIATKRFDAQTGADREVQRILLELLNQMDGFDQTTNVKVIMATNRADTLDPALLRPGRLDRKIEFPLPDRRQKRLIFQ 326
                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 18860063  342 TITSKMNLSEDVDLEEFVARPDKISGADINAICQEAGMHAVRENRYIVLAKDFEKGYKNNIKKDEQEHEFYK 413
Cdd:PTZ00454 327 TITSKMNLSEEVDLEDFVSRPEKISAADIAAICQEAGMQAVRKNRYVILPKDFEKGYKTVVRKTDRDYDFYS 398
PRK03992 PRK03992
proteasome-activating nucleotidase; Provisional
31-408 4.07e-171

proteasome-activating nucleotidase; Provisional


Pssm-ID: 179699 [Multi-domain]  Cd Length: 389  Bit Score: 483.95  E-value: 4.07e-171
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18860063   31 DMEDLYVRYKKLQKTLEFIEVQEEYIKDEQRNLKKEYLHAQEEVKRIQSVPLVIGQFLEAVDQNTGIVGSTTGSNYYVRI 110
Cdd:PRK03992   2 RLEALEERNSELEEQIRQLELKLRDLEAENEKLERELERLKSELEKLKSPPLIVATVLEVLDDGRVVVKSSGGPQFLVNV 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18860063  111 LSTIDRELLKPSASVALHKHSNALVDVLPPEADSSISMLQPDEKPDVSYADIGGMDMQKQEIREAVELPLTHFELYKQIG 190
Cdd:PRK03992  82 SPFIDREKLKPGARVALNQQSLAIVEVLPSEKDPRVQAMEVIESPNVTYEDIGGLEEQIREVREAVELPLKKPELFEEVG 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18860063  191 IDPPRGVLMYGPPGCGKTMLAKAVAHHTTASFIRVVGSEFVQKYLGEGPRMVRDVFRLAKENAPAIIFIDEIDAIATKRF 270
Cdd:PRK03992 162 IEPPKGVLLYGPPGTGKTLLAKAVAHETNATFIRVVGSELVQKFIGEGARLVRELFELAREKAPSIIFIDEIDAIAAKRT 241
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18860063  271 DAQTGADREVQRILLELLNQMDGFDQTTNVKVIMATNRADTLDPALLRPGRLDRKIEFPLPDRRQKRLVFSTITSKMNLS 350
Cdd:PRK03992 242 DSGTSGDREVQRTLMQLLAEMDGFDPRGNVKIIAATNRIDILDPAILRPGRFDRIIEVPLPDEEGRLEILKIHTRKMNLA 321
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 18860063  351 EDVDLEEFVARPDKISGADINAICQEAGMHAVRENRYIVLAKDFEKGYKNNIKKDEQE 408
Cdd:PRK03992 322 DDVDLEELAELTEGASGADLKAICTEAGMFAIRDDRTEVTMEDFLKAIEKVMGKEEKD 379
PTZ00361 PTZ00361
26 proteosome regulatory subunit 4-like protein; Provisional
37-400 6.18e-160

26 proteosome regulatory subunit 4-like protein; Provisional


Pssm-ID: 185575 [Multi-domain]  Cd Length: 438  Bit Score: 457.31  E-value: 6.18e-160
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18860063   37 VRYKKLQKTLEFIEVQEEYIKDEQRnLKKEYLHAQEEVKRIQSV---PLVIGQFLEAVDQNTGIVGSTTGSNYYVRILST 113
Cdd:PTZ00361  58 LRLLKLERIKDYLLLEEEFITNQEA-QKPAQEKNEAELKKVDDLrgsPLSVGTLEEIIDENHAIVSSSVGPEYYVNILSF 136
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18860063  114 IDRELLKPSASVALHKHSNALVDVLPPEADSSISMLQPDEKPDVSYADIGGMDMQKQEIREAVELPLTHFELYKQIGIDP 193
Cdd:PTZ00361 137 VDKEQLEPGCSVLLHNKTHSVVGILLDEVDPLVSVMKVDKAPLESYADIGGLEQQIQEIKEAVELPLTHPELYDDIGIKP 216
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18860063  194 PRGVLMYGPPGCGKTMLAKAVAHHTTASFIRVVGSEFVQKYLGEGPRMVRDVFRLAKENAPAIIFIDEIDAIATKRFDAQ 273
Cdd:PTZ00361 217 PKGVILYGPPGTGKTLLAKAVANETSATFLRVVGSELIQKYLGDGPKLVRELFRVAEENAPSIVFIDEIDAIGTKRYDAT 296
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18860063  274 TGADREVQRILLELLNQMDGFDQTTNVKVIMATNRADTLDPALLRPGRLDRKIEFPLPDRRQKRLVFSTITSKMNLSEDV 353
Cdd:PTZ00361 297 SGGEKEIQRTMLELLNQLDGFDSRGDVKVIMATNRIESLDPALIRPGRIDRKIEFPNPDEKTKRRIFEIHTSKMTLAEDV 376
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....*..
gi 18860063  354 DLEEFVARPDKISGADINAICQEAGMHAVRENRYIVLAKDFEKGYKN 400
Cdd:PTZ00361 377 DLEEFIMAKDELSGADIKAICTEAGLLALRERRMKVTQADFRKAKEK 423
26Sp45 TIGR01242
26S proteasome subunit P45 family; Many proteins may score above the trusted cutoff because an ...
34-396 8.86e-149

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


Pssm-ID: 130309 [Multi-domain]  Cd Length: 364  Bit Score: 426.14  E-value: 8.86e-149
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18860063    34 DLYVRYKKLQKTLEFIEVQEEYIKDEQRNLKKEylhaqeeVKRIQSVPLVIGQFLEAVDQNTGIVGSTTGSNYYVRILST 113
Cdd:TIGR01242   3 ELDVRIRKLEDEKRSLEKEKIRLERELERLRSE-------IERLRSPPLIVGTVLEVLDDNRVVVKSSTGPNFVVNVSAF 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18860063   114 IDRELLKPSASVALHKHSNALVDVLPPEADSSISMLQPDEKPDVSYADIGGMDMQKQEIREAVELPLTHFELYKQIGIDP 193
Cdd:TIGR01242  76 IDRKSLKPGARVALNQQTLTIVDVLPTSKDPLVKGMEVEERPNVSYEDIGGLEEQIREIREAVELPLKHPELFEEVGIEP 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18860063   194 PRGVLMYGPPGCGKTMLAKAVAHHTTASFIRVVGSEFVQKYLGEGPRMVRDVFRLAKENAPAIIFIDEIDAIATKRFDAQ 273
Cdd:TIGR01242 156 PKGVLLYGPPGTGKTLLAKAVAHETNATFIRVVGSELVRKYIGEGARLVREIFELAKEKAPSIIFIDEIDAIAAKRTDSG 235
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18860063   274 TGADREVQRILLELLNQMDGFDQTTNVKVIMATNRADTLDPALLRPGRLDRKIEFPLPDRRQKRLVFSTITSKMNLSEDV 353
Cdd:TIGR01242 236 TSGDREVQRTLMQLLAELDGFDPRGNVKVIAATNRPDILDPALLRPGRFDRIIEVPLPDFEGRLEILKIHTRKMKLAEDV 315
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|...
gi 18860063   354 DLEEFVARPDKISGADINAICQEAGMHAVRENRYIVLAKDFEK 396
Cdd:TIGR01242 316 DLEAIAKMTEGASGADLKAICTEAGMFAIREERDYVTMDDFIK 358
RPT1 COG1222
ATP-dependent 26S proteasome regulatory subunit [Posttranslational modification, protein ...
151-408 1.08e-130

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


Pssm-ID: 440835 [Multi-domain]  Cd Length: 326  Bit Score: 378.97  E-value: 1.08e-130
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18860063 151 PDEKPDVSYADIGGMDMQKQEIREAVELPLTHFELYKQIGIDPPRGVLMYGPPGCGKTMLAKAVAHHTTASFIRVVGSEF 230
Cdd:COG1222  69 PAESPDVTFDDIGGLDEQIEEIREAVELPLKNPELFRKYGIEPPKGVLLYGPPGTGKTLLAKAVAGELGAPFIRVRGSEL 148
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18860063 231 VQKYLGEGPRMVRDVFRLAKENAPAIIFIDEIDAIATKRFDAQTGAdrEVQRILLELLNQMDGFDQTTNVKVIMATNRAD 310
Cdd:COG1222 149 VSKYIGEGARNVREVFELAREKAPSIIFIDEIDAIAARRTDDGTSG--EVQRTVNQLLAELDGFESRGDVLIIAATNRPD 226
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18860063 311 TLDPALLRPGRLDRKIEFPLPDRRQKRLVFSTITSKMNLSEDVDLEEFVARPDKISGADINAICQEAGMHAVRENRYIVL 390
Cdd:COG1222 227 LLDPALLRPGRFDRVIEVPLPDEEAREEILKIHLRDMPLADDVDLDKLAKLTEGFSGADLKAIVTEAGMFAIREGRDTVT 306
                       250
                ....*....|....*...
gi 18860063 391 AKDFEKGYKNNIKKDEQE 408
Cdd:COG1222 307 MEDLEKAIEKVKKKTETA 324
RecA-like_PAN_like cd19502
proteasome activating nucleotidase PAN and related proteasome subunits; This subfamily ...
158-328 5.70e-117

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: 338.16  E-value: 5.70e-117
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18860063 158 SYADIGGMDMQKQEIREAVELPLTHFELYKQIGIDPPRGVLMYGPPGCGKTMLAKAVAHHTTASFIRVVGSEFVQKYLGE 237
Cdd:cd19502   1 TYEDIGGLDEQIREIREVVELPLKHPELFEELGIEPPKGVLLYGPPGTGKTLLAKAVANHTDATFIRVVGSELVQKYIGE 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18860063 238 GPRMVRDVFRLAKENAPAIIFIDEIDAIATKRFDAQTGADREVQRILLELLNQMDGFDQTTNVKVIMATNRADTLDPALL 317
Cdd:cd19502  81 GARLVRELFEMAREKAPSIIFIDEIDAIGAKRFDSGTGGDREVQRTMLELLNQLDGFDPRGNIKVIMATNRPDILDPALL 160
                       170
                ....*....|.
gi 18860063 318 RPGRLDRKIEF 328
Cdd:cd19502 161 RPGRFDRKIEF 171
CDC48 TIGR01243
AAA family ATPase, CDC48 subfamily; This subfamily of the AAA family ATPases includes two ...
153-412 3.04e-80

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: 261.77  E-value: 3.04e-80
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18860063   153 EKPDVSYADIGGMDMQKQEIREAVELPLTHFELYKQIGIDPPRGVLMYGPPGCGKTMLAKAVAHHTTASFIRVVGSEFVQ 232
Cdd:TIGR01243 446 EVPNVRWSDIGGLEEVKQELREAVEWPLKHPEIFEKMGIRPPKGVLLFGPPGTGKTLLAKAVATESGANFIAVRGPEILS 525
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18860063   233 KYLGEGPRMVRDVFRLAKENAPAIIFIDEIDAIATKRfdaqtGADRE---VQRILLELLNQMDGFDQTTNVKVIMATNRA 309
Cdd:TIGR01243 526 KWVGESEKAIREIFRKARQAAPAIIFFDEIDAIAPAR-----GARFDtsvTDRIVNQLLTEMDGIQELSNVVVIAATNRP 600
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18860063   310 DTLDPALLRPGRLDRKIEFPLPDRRQKRLVFSTITSKMNLSEDVDLEEFVARPDKISGADINAICQEAGMHAVRENRYIV 389
Cdd:TIGR01243 601 DILDPALLRPGRFDRLILVPPPDEEARKEIFKIHTRSMPLAEDVDLEELAEMTEGYTGADIEAVCREAAMAALRESIGSP 680
                         250       260
                  ....*....|....*....|...
gi 18860063   390 LAKDFEKGYKNNIKKDEQEHEFY 412
Cdd:TIGR01243 681 AKEKLEVGEEEFLKDLKVEMRHF 703
SpoVK COG0464
AAA+-type ATPase, SpoVK/Ycf46/Vps4 family [Cell wall/membrane/envelope biogenesis, Cell cycle ...
149-396 1.74e-79

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: 250.60  E-value: 1.74e-79
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18860063 149 LQPDEKPDVSYADIGGMDMQKQEIREAVELPLTHFELYKQIGIDPPRGVLMYGPPGCGKTMLAKAVAHHTTASFIRVVGS 228
Cdd:COG0464 146 EELLELREAILDDLGGLEEVKEELRELVALPLKRPELREEYGLPPPRGLLLYGPPGTGKTLLARALAGELGLPLIEVDLS 225
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18860063 229 EFVQKYLGEGPRMVRDVFRLAKENAPAIIFIDEIDAIATKRfdaQTGADREVQRILLELLNQMDGFdqTTNVKVIMATNR 308
Cdd:COG0464 226 DLVSKYVGETEKNLREVFDKARGLAPCVLFIDEADALAGKR---GEVGDGVGRRVVNTLLTEMEEL--RSDVVVIAATNR 300
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18860063 309 ADTLDPALLRpgRLDRKIEFPLPDRRQKRLVFSTITSKMNLSEDVDLEEFVARPDKISGADINAICQEAGMHAVRENRYI 388
Cdd:COG0464 301 PDLLDPALLR--RFDEIIFFPLPDAEERLEIFRIHLRKRPLDEDVDLEELAEATEGLSGADIRNVVRRAALQALRLGREP 378

                ....*...
gi 18860063 389 VLAKDFEK 396
Cdd:COG0464 379 VTTEDLLE 386
FtsH_fam TIGR01241
ATP-dependent metalloprotease FtsH; HflB(FtsH) is a pleiotropic protein required for correct ...
149-396 6.69e-76

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: 244.12  E-value: 6.69e-76
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18860063   149 LQPDEKPDVSYADIGGMDMQKQEIREAVELpLTHFELYKQIGIDPPRGVLMYGPPGCGKTMLAKAVAHHTTASFIRVVGS 228
Cdd:TIGR01241  44 LLNEEKPKVTFKDVAGIDEAKEELMEIVDF-LKNPSKFTKLGAKIPKGVLLVGPPGTGKTLLAKAVAGEAGVPFFSISGS 122
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18860063   229 EFVQKYLGEGPRMVRDVFRLAKENAPAIIFIDEIDAIATKRFDAQTGADREVQRILLELLNQMDGFDQTTNVKVIMATNR 308
Cdd:TIGR01241 123 DFVEMFVGVGASRVRDLFEQAKKNAPCIIFIDEIDAVGRQRGAGLGGGNDEREQTLNQLLVEMDGFGTNTGVIVIAATNR 202
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18860063   309 ADTLDPALLRPGRLDRKIEFPLPDRRQKRLVFSTITSKMNLSEDVDLEEFVARPDKISGADINAICQEAGMHAVRENRYI 388
Cdd:TIGR01241 203 PDVLDPALLRPGRFDRQVVVDLPDIKGREEILKVHAKNKKLAPDVDLKAVARRTPGFSGADLANLLNEAALLAARKNKTE 282

                  ....*...
gi 18860063   389 VLAKDFEK 396
Cdd:TIGR01241 283 ITMNDIEE 290
CDC48 TIGR01243
AAA family ATPase, CDC48 subfamily; This subfamily of the AAA family ATPases includes two ...
155-383 3.62e-72

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: 240.19  E-value: 3.62e-72
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18860063   155 PDVSYADIGGMDMQKQEIREAVELPLTHFELYKQIGIDPPRGVLMYGPPGCGKTMLAKAVAHHTTASFIRVVGSEFVQKY 234
Cdd:TIGR01243 173 PKVTYEDIGGLKEAKEKIREMVELPMKHPELFEHLGIEPPKGVLLYGPPGTGKTLLAKAVANEAGAYFISINGPEIMSKY 252
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18860063   235 LGEGPRMVRDVFRLAKENAPAIIFIDEIDAIATKRfDAQTGadrEVQ-RILLELLNQMDGFDQTTNVKVIMATNRADTLD 313
Cdd:TIGR01243 253 YGESEERLREIFKEAEENAPSIIFIDEIDAIAPKR-EEVTG---EVEkRVVAQLLTLMDGLKGRGRVIVIGATNRPDALD 328
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18860063   314 PALLRPGRLDRKIEFPLPDRRQKRLVFSTITSKMNLSEDVDLEEFVARPDKISGADINAICQEAGMHAVR 383
Cdd:TIGR01243 329 PALRRPGRFDREIVIRVPDKRARKEILKVHTRNMPLAEDVDLDKLAEVTHGFVGADLAALAKEAAMAALR 398
RecA-like_CDC48_NLV2_r1-like cd19503
first of two ATPase domains of CDC48 and NLV2, and similar ATPase domains; CDC48 in yeast and ...
161-328 1.15e-71

first of two ATPase domains of CDC48 and NLV2, and similar ATPase domains; CDC48 in yeast and p97 or VCP metazoans is an ATP-dependent molecular chaperone which plays an essential role in many cellular processes, by segregating polyubiquitinated proteins from complexes or membranes. Cdc48/p97 consists of an N-terminal domain and two ATPase domains; this subfamily represents the first of the two ATPase domains. This subfamily also includes the first of the two ATPase domains of NVL (nuclear VCP-like protein) 2, an isoform of NVL mainly present in the nucleolus, which is involved in ribosome biogenesis, in telomerase assembly and the regulation of telomerase activity, and in pre-rRNA processing. This subfamily belongs to the RecA-like NTPase family which includes the NTP binding domain of F1 and V1 H(+)ATPases, DnaB and related helicases as well as bacterial RecA and related eukaryotic and archaeal recombinases. The RecA-like NTPase family also includes bacterial conjugation proteins and related DNA transfer proteins involved in type II and type IV secretion.


Pssm-ID: 410911 [Multi-domain]  Cd Length: 165  Bit Score: 222.17  E-value: 1.15e-71
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18860063 161 DIGGMDMQKQEIREAVELPLTHFELYKQIGIDPPRGVLMYGPPGCGKTMLAKAVAHHTTASFIRVVGSEFVQKYLGEGPR 240
Cdd:cd19503   1 DIGGLDEQIASLKELIELPLKYPELFRALGLKPPRGVLLHGPPGTGKTLLARAVANEAGANFLSISGPSIVSKYLGESEK 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18860063 241 MVRDVFRLAKENAPAIIFIDEIDAIATKRFDAQTGADRevqRILLELLNQMDGFDQTTNVKVIMATNRADTLDPALLRPG 320
Cdd:cd19503  81 NLREIFEEARSHAPSIIFIDEIDALAPKREEDQREVER---RVVAQLLTLMDGMSSRGKVVVIAATNRPDAIDPALRRPG 157

                ....*...
gi 18860063 321 RLDRKIEF 328
Cdd:cd19503 158 RFDREVEI 165
RecA-like_FtsH cd19501
ATP-dependent zinc metalloprotease FtsH; FtsH ATPase is a processive, ATP-dependent zinc ...
157-326 8.24e-71

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


Pssm-ID: 410909 [Multi-domain]  Cd Length: 171  Bit Score: 220.18  E-value: 8.24e-71
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18860063 157 VSYADIGGMDMQKQEIREAVELpLTHFELYKQIGIDPPRGVLMYGPPGCGKTMLAKAVAHHTTASFIRVVGSEFVQKYLG 236
Cdd:cd19501   1 VTFKDVAGCEEAKEELKEVVEF-LKNPEKFTKLGAKIPKGVLLVGPPGTGKTLLAKAVAGEAGVPFFSISGSDFVEMFVG 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18860063 237 EGPRMVRDVFRLAKENAPAIIFIDEIDAIATKRFDAQTGADREVQRILLELLNQMDGFDQTTNVKVIMATNRADTLDPAL 316
Cdd:cd19501  80 VGASRVRDLFEQAKKNAPCIVFIDEIDAVGRKRGAGLGGGHDEREQTLNQLLVEMDGFESNTGVIVIAATNRPDVLDPAL 159
                       170
                ....*....|
gi 18860063 317 LRPGRLDRKI 326
Cdd:cd19501 160 LRPGRFDRQV 169
HflB COG0465
ATP-dependent Zn proteases [Posttranslational modification, protein turnover, chaperones];
149-396 6.32e-69

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


Pssm-ID: 440233 [Multi-domain]  Cd Length: 583  Bit Score: 228.00  E-value: 6.32e-69
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18860063 149 LQPDEKPDVSYADIGGMDMQKQEIREAVELpLTHFELYKQIGIDPPRGVLMYGPPGCGKTMLAKAVAHHTTASFIRVVGS 228
Cdd:COG0465 131 LYDEDKPKVTFDDVAGVDEAKEELQEIVDF-LKDPEKFTRLGAKIPKGVLLVGPPGTGKTLLAKAVAGEAGVPFFSISGS 209
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18860063 229 EFVQKYLGEGPRMVRDVFRLAKENAPAIIFIDEIDAIATKRFDAQTGADREVQRILLELLNQMDGFDQTTNVKVIMATNR 308
Cdd:COG0465 210 DFVEMFVGVGASRVRDLFEQAKKNAPCIIFIDEIDAVGRQRGAGLGGGHDEREQTLNQLLVEMDGFEGNEGVIVIAATNR 289
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18860063 309 ADTLDPALLRPGRLDRKIEFPLPDRRQKRLVFSTITSKMNLSEDVDLEEfVAR--PDkISGADINAICQEAGMHAVRENR 386
Cdd:COG0465 290 PDVLDPALLRPGRFDRQVVVDLPDVKGREAILKVHARKKPLAPDVDLEV-IARrtPG-FSGADLANLVNEAALLAARRNK 367
                       250
                ....*....|
gi 18860063 387 YIVLAKDFEK 396
Cdd:COG0465 368 KAVTMEDFEE 377
pup_AAA TIGR03689
proteasome ATPase; In the Actinobacteria, as shown for Mycobacterium tuberculosis, some ...
84-390 1.33e-68

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


Pssm-ID: 200312 [Multi-domain]  Cd Length: 512  Bit Score: 225.74  E-value: 1.33e-68
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18860063    84 IGQFLEAVDQNTGIVGSTTGSNYYVRILSTIDRELLKPSASVALHKHSNALVDVLPpeaDSSISMLQPDEKPDVSYADIG 163
Cdd:TIGR03689 109 IVTLKEVLDDGRALVTDRSGEERVVKLAGALADEGLRPGDTLLVDPRAGYAFEAIP---RTEVEDLVLEEVPDVTYADIG 185
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18860063   164 GMDMQKQEIREAVELPLTHFELYKQIGIDPPRGVLMYGPPGCGKTMLAKAVAH----------HTTASFIRVVGSEFVQK 233
Cdd:TIGR03689 186 GLGSQIEQIRDAVELPFLHPELYREYGLKPPKGVLLYGPPGCGKTLIAKAVANslaarigaegGGKSYFLNIKGPELLNK 265
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18860063   234 YLGEGPRMVRDVFRLAKENA----PAIIFIDEIDAIATKRfdaQTGADREVQR-ILLELLNQMDGFDQTTNVKVIMATNR 308
Cdd:TIGR03689 266 YVGETERQIRLIFQRAREKAsegrPVIVFFDEMDSLFRTR---GSGVSSDVETtVVPQLLAEIDGVESLDNVIVIGASNR 342
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18860063   309 ADTLDPALLRPGRLDRKIEFPLPDRRQKRLVFSTitskmNLSEDVDLEEFVARPDKISGADINAICQEA--GMHAVRE-N 385
Cdd:TIGR03689 343 EDMIDPAILRPGRLDVKIRIERPDAEAAADIFAK-----YLTDDLPLPEDLAAHDGDREATAAALIQRVvdALYARSEaN 417

                  ....*
gi 18860063   386 RYIVL 390
Cdd:TIGR03689 418 RYVEV 422
RecA-like_CDC48_r2-like cd19511
second of two ATPase domains of CDC48/p97, PEX1 and -6, VAT and NVL, and similar ATPase ...
169-326 1.80e-67

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


Pssm-ID: 410919 [Multi-domain]  Cd Length: 159  Bit Score: 211.37  E-value: 1.80e-67
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18860063 169 KQEIREAVELPLTHFELYKQIGIDPPRGVLMYGPPGCGKTMLAKAVAHHTTASFIRVVGSEFVQKYLGEGPRMVRDVFRL 248
Cdd:cd19511   2 KRELKEAVEWPLKHPDAFKRLGIRPPKGVLLYGPPGCGKTLLAKALASEAGLNFISVKGPELFSKYVGESERAVREIFQK 81
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 18860063 249 AKENAPAIIFIDEIDAIATKRfdAQTGADREVQRILLELLNQMDGFDQTTNVKVIMATNRADTLDPALLRPGRLDRKI 326
Cdd:cd19511  82 ARQAAPCIIFFDEIDSLAPRR--GQSDSSGVTDRVVSQLLTELDGIESLKGVVVIAATNRPDMIDPALLRPGRLDKLI 157
RecA-like_CDC48_r1-like cd19519
first of two ATPase domains of CDC48 and similar ATPase domains; CDC48 in yeast and p97 or VCP ...
161-329 2.15e-65

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


Pssm-ID: 410927 [Multi-domain]  Cd Length: 166  Bit Score: 206.13  E-value: 2.15e-65
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18860063 161 DIGGMDMQKQEIREAVELPLTHFELYKQIGIDPPRGVLMYGPPGCGKTMLAKAVAHHTTASFIRVVGSEFVQKYLGEGPR 240
Cdd:cd19519   1 DIGGCRKQLAQIREMVELPLRHPELFKAIGIKPPRGILLYGPPGTGKTLIARAVANETGAFFFLINGPEIMSKLAGESES 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18860063 241 MVRDVFRLAKENAPAIIFIDEIDAIATKRFDAQTGADRevqRILLELLNQMDGFDQTTNVKVIMATNRADTLDPALLRPG 320
Cdd:cd19519  81 NLRKAFEEAEKNAPAIIFIDEIDAIAPKREKTHGEVER---RIVSQLLTLMDGLKQRAHVIVMAATNRPNSIDPALRRFG 157

                ....*....
gi 18860063 321 RLDRKIEFP 329
Cdd:cd19519 158 RFDREIDIG 166
RecA-like_protease cd19481
proteases similar to RecA; RecA-like NTPases. This family includes the NTP binding domain of ...
168-328 1.27e-62

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


Pssm-ID: 410889 [Multi-domain]  Cd Length: 158  Bit Score: 198.66  E-value: 1.27e-62
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18860063 168 QKQEIREAVELPLTHFELYKQiGIDPPRGVLMYGPPGCGKTMLAKAVAHHTTASFIRVVGSEFVQKYLGEGPRMVRDVFR 247
Cdd:cd19481   1 LKASLREAVEAPRRGSRLRRY-GLGLPKGILLYGPPGTGKTLLAKALAGELGLPLIVVKLSSLLSKYVGESEKNLRKIFE 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18860063 248 LAKENAPAIIFIDEIDAIATKRFDaqTGADREVQRILLELLNQMDGFDQTTNVKVIMATNRADTLDPALLRPGRLDRKIE 327
Cdd:cd19481  80 RARRLAPCILFIDEIDAIGRKRDS--SGESGELRRVLNQLLTELDGVNSRSKVLVIAATNRPDLLDPALLRPGRFDEVIE 157

                .
gi 18860063 328 F 328
Cdd:cd19481 158 F 158
ftsH CHL00176
cell division protein; Validated
147-396 1.64e-61

cell division protein; Validated


Pssm-ID: 214386 [Multi-domain]  Cd Length: 638  Bit Score: 209.91  E-value: 1.64e-61
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18860063  147 SMLQPDEKPDVSYADIGGMDMQKQEIREAVELpLTHFELYKQIGIDPPRGVLMYGPPGCGKTMLAKAVAHHTTASFIRVV 226
Cdd:CHL00176 170 ARFQMEADTGITFRDIAGIEEAKEEFEEVVSF-LKKPERFTAVGAKIPKGVLLVGPPGTGKTLLAKAIAGEAEVPFFSIS 248
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18860063  227 GSEFVQKYLGEGPRMVRDVFRLAKENAPAIIFIDEIDAIATKRFDAQTGADREVQRILLELLNQMDGFDQTTNVKVIMAT 306
Cdd:CHL00176 249 GSEFVEMFVGVGAARVRDLFKKAKENSPCIVFIDEIDAVGRQRGAGIGGGNDEREQTLNQLLTEMDGFKGNKGVIVIAAT 328
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18860063  307 NRADTLDPALLRPGRLDRKIEFPLPDRRQKRLVFSTITSKMNLSEDVDLEEFVARPDKISGADINAICQEAGMHAVRENR 386
Cdd:CHL00176 329 NRVDILDAALLRPGRFDRQITVSLPDREGRLDILKVHARNKKLSPDVSLELIARRTPGFSGADLANLLNEAAILTARRKK 408
                        250
                 ....*....|
gi 18860063  387 YIVLAKDFEK 396
Cdd:CHL00176 409 ATITMKEIDT 418
RecA-like_VCP_r2 cd19529
second of two ATPase domains of Valosin-containing protein-like ATPase (VAT) and similar ...
169-326 1.76e-61

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


Pssm-ID: 410937 [Multi-domain]  Cd Length: 159  Bit Score: 195.79  E-value: 1.76e-61
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18860063 169 KQEIREAVELPLTHFELYKQIGIDPPRGVLMYGPPGCGKTMLAKAVAHHTTASFIRVVGSEFVQKYLGEGPRMVRDVFRL 248
Cdd:cd19529   2 KQELKEAVEWPLLKPEVFKRLGIRPPKGILLYGPPGTGKTLLAKAVATESNANFISVKGPELLSKWVGESEKAIREIFRK 81
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 18860063 249 AKENAPAIIFIDEIDAIATKRfdAQTGADREVQRILLELLNQMDGFDQTTNVKVIMATNRADTLDPALLRPGRLDRKI 326
Cdd:cd19529  82 ARQVAPCVIFFDEIDSIAPRR--GTTGDSGVTERVVNQLLTELDGLEEMNGVVVIAATNRPDIIDPALLRAGRFDRLI 157
hflB PRK10733
ATP-dependent zinc metalloprotease FtsH;
144-397 6.41e-58

ATP-dependent zinc metalloprotease FtsH;


Pssm-ID: 182683 [Multi-domain]  Cd Length: 644  Bit Score: 200.26  E-value: 6.41e-58
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18860063  144 SSISMLQPDEKpDVSYADIGGMDMQKQEIREAVELpLTHFELYKQIGIDPPRGVLMYGPPGCGKTMLAKAVAHHTTASFI 223
Cdd:PRK10733 137 SKARMLTEDQI-KTTFADVAGCDEAKEEVAELVEY-LREPSRFQKLGGKIPKGVLMVGPPGTGKTLLAKAIAGEAKVPFF 214
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18860063  224 RVVGSEFVQKYLGEGPRMVRDVFRLAKENAPAIIFIDEIDAIATKRFDAQTGADREVQRILLELLNQMDGFDQTTNVKVI 303
Cdd:PRK10733 215 TISGSDFVEMFVGVGASRVRDMFEQAKKAAPCIIFIDEIDAVGRQRGAGLGGGHDEREQTLNQMLVEMDGFEGNEGIIVI 294
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18860063  304 MATNRADTLDPALLRPGRLDRKIEFPLPDRRQKRLVFSTITSKMNLSEDVDLEEFVARPDKISGADINAICQEAGMHAVR 383
Cdd:PRK10733 295 AATNRPDVLDPALLRPGRFDRQVVVGLPDVRGREQILKVHMRRVPLAPDIDAAIIARGTPGFSGADLANLVNEAALFAAR 374
                        250
                 ....*....|....
gi 18860063  384 ENRYIVLAKDFEKG 397
Cdd:PRK10733 375 GNKRVVSMVEFEKA 388
RecA-like_CDC48_r2-like cd19528
second of two ATPase domains of CDC48 and similar ATPase domains; CDC48 in yeast and p97 or ...
169-326 1.60e-56

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: 183.10  E-value: 1.60e-56
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18860063 169 KQEIREAVELPLTHFELYKQIGIDPPRGVLMYGPPGCGKTMLAKAVAHHTTASFIRVVGSEFVQKYLGEGPRMVRDVFRL 248
Cdd:cd19528   2 KRELQELVQYPVEHPDKFLKFGMTPSKGVLFYGPPGCGKTLLAKAIANECQANFISVKGPELLTMWFGESEANVRDIFDK 81
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 18860063 249 AKENAPAIIFIDEIDAIATKRFDAQTGADREVQRILLELLNQMDGFDQTTNVKVIMATNRADTLDPALLRPGRLDRKI 326
Cdd:cd19528  82 ARAAAPCVLFFDELDSIAKARGGNIGDAGGAADRVINQILTEMDGMNTKKNVFIIGATNRPDIIDPAILRPGRLDQLI 159
COG1223 COG1223
Predicted ATPase, AAA+ superfamily [General function prediction only];
161-410 1.05e-55

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


Pssm-ID: 440836 [Multi-domain]  Cd Length: 246  Bit Score: 183.93  E-value: 1.05e-55
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18860063 161 DIGGMDMQKQEIREAVElPLTHFELYKQIGIDPPRGVLMYGPPGCGKTMLAKAVAHHTTASFIRVVGSEFVQKYLGEGPR 240
Cdd:COG1223   3 DVVGQEEAKKKLKLIIK-ELRRRENLRKFGLWPPRKILFYGPPGTGKTMLAEALAGELKLPLLTVRLDSLIGSYLGETAR 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18860063 241 MVRDVFRLAKEnAPAIIFIDEIDAIATKRFDAQtgaDR-EVQRILLELLNQMDGFDQttNVKVIMATNRADTLDPALLRp 319
Cdd:COG1223  82 NLRKLFDFARR-APCVIFFDEFDAIAKDRGDQN---DVgEVKRVVNALLQELDGLPS--GSVVIAATNHPELLDSALWR- 154
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18860063 320 gRLDRKIEFPLPDRRQKRLVFSTITSKMNLSEDVDLEEFVARPDKISGADINAICQEAGMHAVRENRYIVLAKDFEKGYK 399
Cdd:COG1223 155 -RFDEVIEFPLPDKEERKEILELNLKKFPLPFELDLKKLAKKLEGLSGADIEKVLKTALKKAILEDREKVTKEDLEEALK 233
                       250
                ....*....|.
gi 18860063 400 NNIKKDEQEHE 410
Cdd:COG1223 234 QRKERKKEPKK 244
AAA pfam00004
ATPase family associated with various cellular activities (AAA); AAA family proteins often ...
197-330 2.22e-54

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


Pssm-ID: 459627 [Multi-domain]  Cd Length: 130  Bit Score: 176.63  E-value: 2.22e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18860063   197 VLMYGPPGCGKTMLAKAVAHHTTASFIRVVGSEFVQKYLGEGPRMVRDVFRLAKENAPAIIFIDEIDAIATKRFDaqtGA 276
Cdd:pfam00004   1 LLLYGPPGTGKTTLAKAVAKELGAPFIEISGSELVSKYVGESEKRLRELFEAAKKLAPCVIFIDEIDALAGSRGS---GG 77
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 18860063   277 DREVQRILLELLNQMDGFDQTT-NVKVIMATNRADTLDPALLrpGRLDRKIEFPL 330
Cdd:pfam00004  78 DSESRRVVNQLLTELDGFTSSNsKVIVIAATNRPDKLDPALL--GRFDRIIEFPL 130
RecA-like_NVL_r1-like cd19518
first of two ATPase domains of NVL (nuclear VCP-like protein) and similar ATPase domains; NVL ...
161-326 1.16e-53

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: 176.06  E-value: 1.16e-53
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18860063 161 DIGGMDMQKQEIREAVELPLTHFELYKQIGIDPPRGVLMYGPPGCGKTMLAKAVAHHTTASFIRVVGSEFVQKYLGEGPR 240
Cdd:cd19518   1 DIGGMDSTLKELCELLIHPILPPEYFQHLGVEPPRGVLLHGPPGCGKTMLANAIAGELKVPFLKISATEIVSGVSGESEE 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18860063 241 MVRDVFRLAKENAPAIIFIDEIDAIATKRFDAQTGADRevqRILLELLNQMDGF----DQTTNVKVIMATNRADTLDPAL 316
Cdd:cd19518  81 KIRELFDQAISNAPCIVFIDEIDAITPKRESAQREMER---RIVSQLLTCMDELnnekTAGGPVLVIGATNRPDSLDPAL 157
                       170
                ....*....|
gi 18860063 317 LRPGRLDRKI 326
Cdd:cd19518 158 RRAGRFDREI 167
RecA-like_NVL_r2-like cd19530
second of two ATPase domains of NVL (nuclear VCP-like protein) and similar ATPase domains; NVL ...
169-324 1.36e-53

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: 175.75  E-value: 1.36e-53
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18860063 169 KQEIREAVELPLTHFELYKQIGIDPPRGVLMYGPPGCGKTMLAKAVAHHTTASFIRVVGSEFVQKYLGEGPRMVRDVFRL 248
Cdd:cd19530   5 REELTMSILRPIKRPDIYKALGIDLPTGVLLYGPPGCGKTLLAKAVANESGANFISVKGPELLNKYVGESERAVRQVFQR 84
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 18860063 249 AKENAPAIIFIDEIDAIATKRFDAQTGAdreVQRILLELLNQMDGFDQTTNVKVIMATNRADTLDPALLRPGRLDR 324
Cdd:cd19530  85 ARASAPCVIFFDEVDALVPKRGDGGSWA---SERVVNQLLTEMDGLEERSNVFVIAATNRPDIIDPAMLRPGRLDK 157
cell_div_CdvC NF041006
cell division protein CdvC;
153-384 1.79e-51

cell division protein CdvC;


Pssm-ID: 468935 [Multi-domain]  Cd Length: 371  Bit Score: 176.85  E-value: 1.79e-51
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18860063  153 EKPDVSYADIGGMDMQKQEIREAVELPLTHFELYKqigIDPPRGVLMYGPPGCGKTMLAKAVAHHTTASFIRVVGSEFVQ 232
Cdd:NF041006  96 EKPKVTFSDIVGLEDVKEALKEAIVYPSKRPDLFP---LGWPRGILLYGPPGCGKTMLAAAVANEIDSEFIHVDAASIMS 172
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18860063  233 KYLGEGPRMVRDVFRLA-----KENAPAIIFIDEIDAIATKrFDAQTGADREVQRillELLNQMDGF---DQTTNVKVIM 304
Cdd:NF041006 173 KWLGEAEKNVAKIFKKArekskEEGKPAIIFIDEIDALLGV-YSSEVGGEVRVRN---QFLKEMDGLqdkSENYHVYVIG 248
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18860063  305 ATNRADTLDPALLRpgRLDRKIEFPLPDRRQKRLVFSTITSKMNLSEDVDLEEFVARPDKISGADINAICQEAGMHAVRE 384
Cdd:NF041006 249 ATNKPWRLDEPFLR--RFQKRIYIPLPDREQRLELLKYYTSKIKLENDVDLDELAEMTEGYTASDIRDIVQAAHMRVVKE 326
RecA-like_VPS4-like cd19509
ATPase domain of VPS4, ATAD1, K, KTNA1, Spastin, FIGL-1 and similar ATPase domains; This ...
162-326 1.30e-46

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: 157.51  E-value: 1.30e-46
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18860063 162 IGGMDMQKQEIREAVELPLTHFELYKQIgIDPPRGVLMYGPPGCGKTMLAKAVAHHTTASFIRVVGSEFVQKYLGEGPRM 241
Cdd:cd19509   1 IAGLDDAKEALKEAVILPSLRPDLFPGL-RGPPRGILLYGPPGTGKTLLARAVASESGSTFFSISASSLVSKWVGESEKI 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18860063 242 VRDVFRLAKENAPAIIFIDEIDAIATKRFDAQTGADRevqRILLELLNQMDGFDQTTN--VKVIMATNRADTLDPALLRp 319
Cdd:cd19509  80 VRALFALARELQPSIIFIDEIDSLLSERGSGEHEASR---RVKTEFLVQMDGVLNKPEdrVLVLGATNRPWELDEAFLR- 155

                ....*..
gi 18860063 320 gRLDRKI 326
Cdd:cd19509 156 -RFEKRI 161
RecA-like_PEX1_r2 cd19526
second of two ATPase domains of Peroxisomal biogenesis factor 1 (PEX1); PEX1(also known as ...
168-327 1.34e-45

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: 154.89  E-value: 1.34e-45
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18860063 168 QKQEIREAVELPLTHFELYKQIGIDPPRGVLMYGPPGCGKTMLAKAVAHHTTASFIRVVGSEFVQKYLGEGPRMVRDVFR 247
Cdd:cd19526   1 VKKALEETIEWPSKYPKIFASSPLRLRSGILLYGPPGCGKTLLASAIASECGLNFISVKGPELLNKYIGASEQNVRDLFS 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18860063 248 LAKENAPAIIFIDEIDAIATKRFDAQTGAdreVQRILLELLNQMDGFDQTTNVKVIMATNRADTLDPALLRPGRLDRKIE 327
Cdd:cd19526  81 RAQSAKPCILFFDEFDSIAPKRGHDSTGV---TDRVVNQLLTQLDGVEGLDGVYVLAATSRPDLIDPALLRPGRLDKLVY 157
RecA-like_Yta7-like cd19517
ATPase domain of Saccharomyces cerevisiae Yta7 and similar ATPase domains; Saccharomyces ...
161-328 4.29e-42

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: 146.12  E-value: 4.29e-42
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18860063 161 DIGGMDMQKQEIREAVELPLTHFELYKQIGIDPPRGVLMYGPPGCGKTMLAKAVAHHTTA-----SFIRVVGSEFVQKYL 235
Cdd:cd19517   1 DIGGLSHYINQLKEMVFFPLLYPEVFAKFKITPPRGVLFHGPPGTGKTLMARALAAECSKggqkvSFFMRKGADCLSKWV 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18860063 236 GEGPRMVRDVFRLAKENAPAIIFIDEIDAIATKRFDAQtgaDREVQRILLELLNQMDGFDQTTNVKVIMATNRADTLDPA 315
Cdd:cd19517  81 GEAERQLRLLFEEAYRMQPSIIFFDEIDGLAPVRSSKQ---EQIHASIVSTLLALMDGLDNRGQVVVIGATNRPDALDPA 157
                       170
                ....*....|...
gi 18860063 316 LLRPGRLDRKIEF 328
Cdd:cd19517 158 LRRPGRFDREFYF 170
RecA-like_VPS4 cd19521
ATPase domain of vacuolar protein sorting-associated protein 4; Vacuolar protein ...
154-326 2.11e-41

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


Pssm-ID: 410929 [Multi-domain]  Cd Length: 170  Bit Score: 144.23  E-value: 2.11e-41
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18860063 154 KPDVSYADIGGMDMQKQEIREAVELPLTHFELYKQiGIDPPRGVLMYGPPGCGKTMLAKAVAHHTTASFIRVVGSEFVQK 233
Cdd:cd19521   1 KPNVKWEDVAGLEGAKEALKEAVILPVKFPHLFTG-NRKPWSGILLYGPPGTGKSYLAKAVATEANSTFFSVSSSDLVSK 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18860063 234 YLGEGPRMVRDVFRLAKENAPAIIFIDEIDAIATKRFDAQTGADRevqRILLELLNQMDGF-DQTTNVKVIMATNRADTL 312
Cdd:cd19521  80 WMGESEKLVKQLFAMARENKPSIIFIDEVDSLCGTRGEGESEASR---RIKTELLVQMNGVgNDSQGVLVLGATNIPWQL 156
                       170
                ....*....|....
gi 18860063 313 DPALLRpgRLDRKI 326
Cdd:cd19521 157 DSAIRR--RFEKRI 168
RecA-like_PEX6_r2 cd19527
second of two ATPase domains of Peroxisomal biogenesis factor 6 (PEX6); PEX6(also known as ...
169-324 3.65e-40

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: 140.73  E-value: 3.65e-40
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18860063 169 KQEIREAVELPLTHFELYKQiGIDPPRGVLMYGPPGCGKTMLAKAVAHHTTASFIRVVGSEFVQKYLGEGPRMVRDVFRL 248
Cdd:cd19527   2 KKEILDTIQLPLEHPELFSS-GLRKRSGILLYGPPGTGKTLLAKAIATECSLNFLSVKGPELINMYIGESEANVREVFQK 80
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 18860063 249 AKENAPAIIFIDEIDAIATKRfDAQTGADREVQRILLELLNQMDGFDQTT-NVKVIMATNRADTLDPALLRPGRLDR 324
Cdd:cd19527  81 ARDAKPCVIFFDELDSLAPSR-GNSGDSGGVMDRVVSQLLAELDGMSSSGqDVFVIGATNRPDLLDPALLRPGRFDK 156
RecA-like_ATAD1 cd19520
ATPase domain of ATPase family AAA domain-containing protein 1 and similar ATPase domains; ...
161-318 1.01e-39

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: 139.48  E-value: 1.01e-39
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18860063 161 DIGGMDMQKQEIREAVELPLTHFELYKQIGI-DPPRGVLMYGPPGCGKTMLAKAVAHHTTASFIRVVGSEFVQKYLGEGP 239
Cdd:cd19520   1 DIGGLDEVITELKELVILPLQRPELFDNSRLlQPPKGVLLYGPPGCGKTMLAKATAKEAGARFINLQVSSLTDKWYGESQ 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18860063 240 RMVRDVFRLAKENAPAIIFIDEIDAIATKRfdaqTGADREVQRIL-LELLNQMDGFDQTTNVKVIM--ATNRADTLDPAL 316
Cdd:cd19520  81 KLVAAVFSLASKLQPSIIFIDEIDSFLRQR----SSTDHEATAMMkAEFMSLWDGLSTDGNCRVIVmgATNRPQDLDEAI 156

                ..
gi 18860063 317 LR 318
Cdd:cd19520 157 LR 158
RecA-like_Figl-1 cd19525
ATPase domain of Fidgetin-Like 1 (FIGL-1); FIGL-1 may participate in DNA repair in the nucleus; ...
152-326 4.89e-38

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


Pssm-ID: 410933 [Multi-domain]  Cd Length: 186  Bit Score: 135.89  E-value: 4.89e-38
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18860063 152 DEKPDVSYADIGGMDMQKQEIREAVELPLTHFELYKQIGiDPPRGVLMYGPPGCGKTMLAKAVAHHTTASFIRVVGSEFV 231
Cdd:cd19525  14 DHGPPINWADIAGLEFAKKTIKEIVVWPMLRPDIFTGLR-GPPKGILLFGPPGTGKTLIGKCIASQSGATFFSISASSLT 92
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18860063 232 QKYLGEGPRMVRDVFRLAKENAPAIIFIDEIDAIATKRFDAQTGADRevqRILLELLNQMDGFDQTTNVKVIM--ATNRA 309
Cdd:cd19525  93 SKWVGEGEKMVRALFSVARCKQPAVIFIDEIDSLLSQRGEGEHESSR---RIKTEFLVQLDGATTSSEDRILVvgATNRP 169
                       170
                ....*....|....*..
gi 18860063 310 DTLDPALLRpgRLDRKI 326
Cdd:cd19525 170 QEIDEAARR--RLVKRL 184
RecA-like_KTNA1 cd19522
Katanin p60 ATPase-containing subunit A1; Katanin p60 ATPase-containing subunit A1 (KTNA1) is ...
161-326 2.56e-37

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


Pssm-ID: 410930 [Multi-domain]  Cd Length: 170  Bit Score: 133.57  E-value: 2.56e-37
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18860063 161 DIGGMDMQKQEIREAVELPLTHFELYKqiGIDPP-RGVLMYGPPGCGKTMLAKAVAHHTTASFIRVVGSEFVQKYLGEGP 239
Cdd:cd19522   1 DIADLEEAKKLLEEAVVLPMWMPEFFK--GIRRPwKGVLMVGPPGTGKTLLAKAVATECGTTFFNVSSSTLTSKYRGESE 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18860063 240 RMVRDVFRLAKENAPAIIFIDEIDAIATKRfdaQTGADREV-QRILLELLNQMDGF-------DQTTNVKVIMATNRADT 311
Cdd:cd19522  79 KLVRLLFEMARFYAPTTIFIDEIDSICSRR---GTSEEHEAsRRVKSELLVQMDGVggasendDPSKMVMVLAATNFPWD 155
                       170
                ....*....|....*
gi 18860063 312 LDPALLRpgRLDRKI 326
Cdd:cd19522 156 IDEALRR--RLEKRI 168
RecA-like_spastin cd19524
ATPase domain of spastin; Spastin is an ATP-dependent microtubule-severing protein involved in ...
161-326 4.06e-37

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: 132.67  E-value: 4.06e-37
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18860063 161 DIGGMDMQKQEIREAVELPLTHFELYKQIGIdPPRGVLMYGPPGCGKTMLAKAVAHHTTASFIRVVGSEFVQKYLGEGPR 240
Cdd:cd19524   1 DIAGQDLAKQALQEMVILPSLRPELFTGLRA-PARGLLLFGPPGNGKTMLAKAVAAESNATFFNISAASLTSKYVGEGEK 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18860063 241 MVRDVFRLAKENAPAIIFIDEIDAIATKRFDAQTGADRevqRILLELLNQMDGFDQTTN--VKVIMATNRADTLDPALLR 318
Cdd:cd19524  80 LVRALFAVARELQPSIIFIDEVDSLLSERSEGEHEASR---RLKTEFLIEFDGVQSNGDdrVLVMGATNRPQELDDAVLR 156

                ....*...
gi 18860063 319 pgRLDRKI 326
Cdd:cd19524 157 --RFTKRV 162
RecA-like_NSF-SEC18_r1-like cd19504
first of two ATPase domains of NSF and SEC18, and similar ATPase domains; ...
162-327 7.92e-32

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: 119.13  E-value: 7.92e-32
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18860063 162 IGGMDMQKQEI-REAVELPLTHFELYKQIGIDPPRGVLMYGPPGCGKTMLAKAVAHHTTASFIRVV-GSEFVQKYLGEGP 239
Cdd:cd19504   2 IGGLDKEFSDIfRRAFASRVFPPEIVEQLGCKHVKGILLYGPPGTGKTLMARQIGKMLNAREPKIVnGPEILNKYVGESE 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18860063 240 RMVRDVFRLAKENAPA--------IIFIDEIDAIATKRfdAQTGADREV-QRILLELLNQMDGFDQTTNVKVIMATNRAD 310
Cdd:cd19504  82 ANIRKLFADAEEEQRRlgansglhIIIFDEIDAICKQR--GSMAGSTGVhDTVVNQLLSKIDGVEQLNNILVIGMTNRKD 159
                       170
                ....*....|....*..
gi 18860063 311 TLDPALLRPGRLDRKIE 327
Cdd:cd19504 160 LIDEALLRPGRLEVQME 176
AAA cd00009
The AAA+ (ATPases Associated with a wide variety of cellular Activities) superfamily ...
163-330 2.55e-27

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


Pssm-ID: 99707 [Multi-domain]  Cd Length: 151  Bit Score: 106.08  E-value: 2.55e-27
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18860063 163 GGMDMQKQEIREAVELPlthfelykqigidPPRGVLMYGPPGCGKTMLAKAVAHHTT---ASFIRVVGSEFVQKYLGE-- 237
Cdd:cd00009   1 VGQEEAIEALREALELP-------------PPKNLLLYGPPGTGKTTLARAIANELFrpgAPFLYLNASDLLEGLVVAel 67
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18860063 238 -GPRMVRDVFRLAKENAPAIIFIDEIDAIAtkrfdaqtgadREVQRILLELLNQ-MDGFDQTTNVKVIMATNRADTLDPA 315
Cdd:cd00009  68 fGHFLVRLLFELAEKAKPGVLFIDEIDSLS-----------RGAQNALLRVLETlNDLRIDRENVRVIGATNRPLLGDLD 136
                       170
                ....*....|....*
gi 18860063 316 LLRPGRLDRKIEFPL 330
Cdd:cd00009 137 RALYDRLDIRIVIPL 151
RecA-like_fidgetin cd19523
ATPase domain of fidgetin; Fidgetin (FIGN) is a ATP-dependent microtubule severing protein. ...
161-318 1.07e-25

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: 101.88  E-value: 1.07e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18860063 161 DIGGMDMQKQEIREAVELPLTHFELYKQIgIDPPRGVLMYGPPGCGKTMLAKAVAHHTTASFIRVVGSEFVQKYLGEGPR 240
Cdd:cd19523   1 DIAGLGALKAAIKEEVLWPLLRPDAFSGL-LRLPRSILLFGPRGTGKTLLGRCLASQLGATFLRLRGSTLVAKWAGEGEK 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18860063 241 MVRDVFRLAKENAPAIIFIDEIDAIATKRFDAQTgadrEVQRILLELLNQMDGF--DQTTNVKVIMATNRADTLDPALLR 318
Cdd:cd19523  80 ILQASFLAARCRQPSVLFISDLDALLSSQDDEAS----PVGRLQVELLAQLDGVlgSGEDGVLVVCTTSKPEEIDESLRR 155
RecA-like_Ycf46-like cd19507
ATPase domain of Ycf46 and similar ATPase domains; Ycf46 may play a role in the regulation of ...
161-324 1.64e-23

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


Pssm-ID: 410915 [Multi-domain]  Cd Length: 161  Bit Score: 95.90  E-value: 1.64e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18860063 161 DIGGMDMQKQ--EIREAVELPLThfelyKQIGIDPPRGVLMYGPPGCGKTMLAKAVAHHTTASFIRVVGSEFVQKYLGEG 238
Cdd:cd19507   1 DVGGLDNLKDwlKKRKAAFSKQA-----SAYGLPTPKGLLLVGIQGTGKSLTAKAIAGVWQLPLLRLDMGRLFGGLVGES 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18860063 239 PRMVRDVFRLAKENAPAIIFIDEID-AIATKRFDAQTGADRevqRILLELLNQMDgfDQTTNVKVIMATNRADTLDPALL 317
Cdd:cd19507  76 ESRLRQMIQTAEAIAPCVLWIDEIEkGFSNADSKGDSGTSS---RVLGTFLTWLQ--EKKKPVFVVATANNVQSLPPELL 150

                ....*..
gi 18860063 318 RPGRLDR 324
Cdd:cd19507 151 RKGRFDE 157
AAA smart00382
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ...
193-332 6.25e-21

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: 88.58  E-value: 6.25e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18860063    193 PPRGVLMYGPPGCGKTMLAKAVAHH---TTASFIRVVGSEF--------------VQKYLGEGPRMVRDVFRLAKENAPA 255
Cdd:smart00382   1 PGEVILIVGPPGSGKTTLARALARElgpPGGGVIYIDGEDIleevldqllliivgGKKASGSGELRLRLALALARKLKPD 80
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 18860063    256 IIFIDEIDAIATKRFdaqtgadrEVQRILLELLNQMDGFDQTTNVKVIMATNRADTLDPALLRPgRLDRKIEFPLPD 332
Cdd:smart00382  81 VLILDEITSLLDAEQ--------EALLLLLEELRLLLLLKSEKNLTVILTTNDEKDLGPALLRR-RFDRRIVLLLIL 148
RecA-like_BCS1 cd19510
Mitochondrial chaperone BCS1; Mitochondrial chaperone BCS1 is necessary for the assembly of ...
186-328 1.72e-17

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: 78.93  E-value: 1.72e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18860063 186 YKQIGIDPPRGVLMYGPPGCGKTMLAKAVAHHTTASFirvvgsefvqkYLGEGPRMVRDVFRLAK--ENAP--AIIFIDE 261
Cdd:cd19510  15 YNDRGIPYRRGYLLYGPPGTGKSSFIAALAGELDYDI-----------CDLNLSEVVLTDDRLNHllNTAPkqSIILLED 83
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18860063 262 ID-AIATKRFDAQTGADRE-VQRILLE-LLNQMDGFDQTTNVKVIMATNRADTLDPALLRPGRLDRKIEF 328
Cdd:cd19510  84 IDaAFESREHNKKNPSAYGgLSRVTFSgLLNALDGVASSEERIVFMTTNHIERLDPALIRPGRVDMKIYM 153
ycf46 CHL00195
Ycf46; Provisional
155-386 2.40e-16

Ycf46; Provisional


Pssm-ID: 177094 [Multi-domain]  Cd Length: 489  Bit Score: 80.83  E-value: 2.40e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18860063  155 PDVSYADIGGMDMQKQEIREAVElplTHFELYKQIGIDPPRGVLMYGPPGCGKTMLAKAVAHHTTASFIRV-VGSEFvQK 233
Cdd:CHL00195 223 VNEKISDIGGLDNLKDWLKKRST---SFSKQASNYGLPTPRGLLLVGIQGTGKSLTAKAIANDWQLPLLRLdVGKLF-GG 298
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18860063  234 YLGEGPRMVRDVFRLAKENAPAIIFIDEID-AIATKRFDAQTGADREVQRILLELLNQmdgfdQTTNVKVIMATNRADTL 312
Cdd:CHL00195 299 IVGESESRMRQMIRIAEALSPCILWIDEIDkAFSNSESKGDSGTTNRVLATFITWLSE-----KKSPVFVVATANNIDLL 373
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 18860063  313 DPALLRPGRLDRKIEFPLPDRRQKRLVFSTITSKM--NLSEDVDLEEFVARPDKISGADINAICQEAGMHAVRENR 386
Cdd:CHL00195 374 PLEILRKGRFDEIFFLDLPSLEEREKIFKIHLQKFrpKSWKKYDIKKLSKLSNKFSGAEIEQSIIEAMYIAFYEKR 449
RecA-like_ATAD3-like cd19512
ATPase domains of ATPase AAA-domain protein 3A (ATAD3A), -3B, and -3C, and similar ATPase ...
195-328 5.97e-13

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: 66.01  E-value: 5.97e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18860063 195 RGVLMYGPPGCGKTMLAKAVAHHTTASFIRVVGSEfVQKYLGEGPRMVRDVFRLA-KENAPAIIFIDEIDAIATKRfdAQ 273
Cdd:cd19512  23 RNILFYGPPGTGKTLFAKKLALHSGMDYAIMTGGD-VAPMGREGVTAIHKVFDWAnTSRRGLLLFVDEADAFLRKR--ST 99
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*
gi 18860063 274 TGADREVQRILLELLNQMDgfDQTTNVKVIMATNRADTLDPALlrPGRLDRKIEF 328
Cdd:cd19512 100 EKISEDLRAALNAFLYRTG--EQSNKFMLVLASNQPEQFDWAI--NDRIDEMVEF 150
RecA-like_Ycf2 cd19505
ATPase domain of plant YCF2; Ycf2 is a chloroplast ATPase which has an essential function; ...
188-328 4.60e-12

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: 63.93  E-value: 4.60e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18860063 188 QIGIDPPRGVLMYGPPGCGKTMLAKAVAHHTTASFIRVVGSEFVQK--------------YLGEGPRMVRDVFRLAKENA 253
Cdd:cd19505   6 RLGLSPSKGILLIGSIETGRSYLIKSLAANSYVPLIRISLNKLLYNkpdfgnddwidgmlILKESLHRLNLQFELAKAMS 85
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 18860063 254 PAIIFIDEIDAIATKRFDAQTGADREVQR-ILLELLNQMDGFDQTTNVKVIMATNRADTLDPALLRPGRLDRKIEF 328
Cdd:cd19505  86 PCIIWIPNIHELNVNRSTQNLEEDPKLLLgLLLNYLSRDFEKSSTRNILVIASTHIPQKVDPALIAPNRLDTCINI 161
RecA-like_Pch2-like cd19508
ATPase domain of Pachytene checkpoint 2 (Pch2) and similar ATPase domains; Pch2 (known as ...
195-316 1.15e-11

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: 63.62  E-value: 1.15e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18860063 195 RGVLMYGPPGCGKTMLAKAVAHHTT---------ASFIRVVGSEFVQKYLGEGPRMVRDVFR-----LAKENAPAIIFID 260
Cdd:cd19508  53 RLVLLHGPPGTGKTSLCKALAQKLSirlssryryGQLIEINSHSLFSKWFSESGKLVTKMFQkiqelIDDKDALVFVLID 132
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 18860063 261 EIDAIATKRFDAQTGAD-REVQRILLELLNQMDGFDQTTNVKVIMATNRADTLDPAL 316
Cdd:cd19508 133 EVESLAAARSASSSGTEpSDAIRVVNAVLTQIDRIKRYHNNVILLTSNLLEKIDVAF 189
RecA-like_HslU cd19498
ATP-dependent protease ATPase subunit HslU; HslU is a component of the ATP-dependent protease ...
194-288 1.37e-11

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: 62.78  E-value: 1.37e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18860063 194 PRGVLMYGPPGCGKTMLAKAVAHHTTASFIRVVGSEFVQ-KYLGegprmvRDVFRLAKENAPAIIFIDEIDAIATKRFDA 272
Cdd:cd19498  46 PKNILMIGPTGVGKTEIARRLAKLAGAPFIKVEATKFTEvGYVG------RDVESIIRDLVEGIVFIDEIDKIAKRGGSS 119
                        90
                ....*....|....*..
gi 18860063 273 QTGADRE-VQRILLELL 288
Cdd:cd19498 120 GPDVSREgVQRDLLPIV 136
AAA_5 pfam07728
AAA domain (dynein-related subfamily); This Pfam entry includes some of the AAA proteins not ...
196-318 6.25e-11

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: 59.61  E-value: 6.25e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18860063   196 GVLMYGPPGCGKTMLAKAVAHHTT-ASFIRVVGS------EFVQKYL--GEGPRMVRDVF-RLAKEnaPAIIFIDEIDAi 265
Cdd:pfam07728   1 GVLLVGPPGTGKTELAERLAAALSnRPVFYVQLTrdtteeDLFGRRNidPGGASWVDGPLvRAARE--GEIAVLDEINR- 77
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 18860063   266 atkrfdaqtgADREVQRILLELLN-----QMDGF----DQTTNVKVIMATNRADT----LDPALLR 318
Cdd:pfam07728  78 ----------ANPDVLNSLLSLLDerrllLPDGGelvkAAPDGFRLIATMNPLDRglneLSPALRS 133
Prot_ATP_ID_OB pfam16450
Proteasomal ATPase OB C-terminal domain; This is the interdomain (ID) or oligonucleotide ...
84-139 1.09e-10

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


Pssm-ID: 465118 [Multi-domain]  Cd Length: 56  Bit Score: 56.75  E-value: 1.09e-10
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 18860063    84 IGQFLEAVDQNTGIVGSTTGSNYYVRILSTIDRELLKPSASVALHKHSNALVDVLP 139
Cdd:pfam16450   1 VATVVEVLDDGRALVKSSGGEERVVRLAGSLDEEKLRPGDRVLLDPRSGYALEVLP 56
AAA_lid_3 pfam17862
AAA+ lid domain; This entry represents the alpha helical AAA+ lid domain that is found to the ...
352-396 3.18e-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: 55.24  E-value: 3.18e-10
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 18860063   352 DVDLEEFVARPDKISGADINAICQEAGMHAVRENRYIVLAKDFEK 396
Cdd:pfam17862   1 DVDLEELAERTEGFSGADLEALCREAALAALRRGLEAVTQEDLEE 45
RecA-like_ClpB_Hsp104-like cd19499
Chaperone protein ClpB/Hsp104 subfamily; Bacterial Caseinolytic peptidase B (ClpB) and ...
194-328 4.11e-09

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: 55.65  E-value: 4.11e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18860063 194 PRGVLMY-GPPGCGKTMLAKAVA---HHTTASFIRVVGSEFVQK------------YLG--EGPRMVRDVfrlaKENAPA 255
Cdd:cd19499  40 PIGSFLFlGPTGVGKTELAKALAellFGDEDNLIRIDMSEYMEKhsvsrligappgYVGytEGGQLTEAV----RRKPYS 115
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 18860063 256 IIFIDEIDAiatkrfdaqtgADREVQRILLELLNQ---MDGFDQTTNVK---VIMATNradTLDPALLrpGRLDRKIEF 328
Cdd:cd19499 116 VVLLDEIEK-----------AHPDVQNLLLQVLDDgrlTDSHGRTVDFKntiIIMTSN---HFRPEFL--NRIDEIVVF 178
AAA_2 pfam07724
AAA domain (Cdc48 subfamily); This Pfam entry includes some of the AAA proteins not detected ...
197-307 1.90e-08

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: 53.35  E-value: 1.90e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18860063   197 VLMYGPPGCGKTMLAKAVA---HHTTASFIRVVGSEFVQKYL--------------GEGPRMVRDVFRlakeNAPAIIFI 259
Cdd:pfam07724   6 FLFLGPTGVGKTELAKALAellFGDERALIRIDMSEYMEEHSvsrligappgyvgyEEGGQLTEAVRR----KPYSIVLI 81
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 18860063   260 DEIDAIAtkrfdaqtgadREVQRILLELL----------NQMDgfdqTTNVKVIMATN 307
Cdd:pfam07724  82 DEIEKAH-----------PGVQNDLLQILeggtltdkqgRTVD----FKNTLFIMTGN 124
RarA COG2256
Replication-associated recombination protein RarA (DNA-dependent ATPase) [Replication, ...
185-262 1.11e-07

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


Pssm-ID: 441857 [Multi-domain]  Cd Length: 439  Bit Score: 53.52  E-value: 1.11e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18860063 185 LYKQIGIDPPRGVLMYGPPGCGKTMLAKAVAHHTTASFIRV--VGSefvqkylgeGPRMVRDVFRLAKENA----PAIIF 258
Cdd:COG2256  40 LRRAIEAGRLSSMILWGPPGTGKTTLARLIANATDAEFVALsaVTS---------GVKDIREVIEEARERRaygrRTILF 110

                ....
gi 18860063 259 IDEI 262
Cdd:COG2256 111 VDEI 114
MoxR COG0714
MoxR-like ATPase [General function prediction only]; MoxR-like ATPase is part of the Pathway ...
197-288 1.20e-07

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: 52.86  E-value: 1.20e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18860063 197 VLMYGPPGCGKTMLAKAVAHHTTASFIRV-----------VGSE-FVQK----YLGEGPrmvrdVFRlakenapAIIFID 260
Cdd:COG0714  34 LLLEGVPGVGKTTLAKALARALGLPFIRIqftpdllpsdiLGTYiYDQQtgefEFRPGP-----LFA-------NVLLAD 101
                        90       100
                ....*....|....*....|....*...
gi 18860063 261 EIDaiatkRfdaqtgADREVQRILLELL 288
Cdd:COG0714 102 EIN-----R------APPKTQSALLEAM 118
PRK13342 PRK13342
recombination factor protein RarA; Reviewed
185-262 8.74e-07

recombination factor protein RarA; Reviewed


Pssm-ID: 237355 [Multi-domain]  Cd Length: 413  Bit Score: 50.85  E-value: 8.74e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18860063  185 LYKQIGIDPPRGVLMYGPPGCGKTMLAKAVAHHTTASFIRVVGSEF-VQKylgegprmVRDVFRLAKENAPA----IIFI 259
Cdd:PRK13342  27 LRRMIEAGRLSSMILWGPPGTGKTTLARIIAGATDAPFEALSAVTSgVKD--------LREVIEEARQRRSAgrrtILFI 98

                 ...
gi 18860063  260 DEI 262
Cdd:PRK13342  99 DEI 101
RecA-like_superfamily cd01120
RecA-like_NTPases; RecA-like NTPases. This superfamily includes the NTP binding domain of F1 ...
197-308 5.45e-06

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: 45.19  E-value: 5.45e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18860063 197 VLMYGPPGCGKTMLAKAVAHHTTASFIRVVGSEFVQKYLgegpRMVRDvfrLAKENAPAIIFIDEIDAIATKRfdaQTGA 276
Cdd:cd01120   1 ILITGPPGSGKTTLLLQFAEQALLSDEPVIFISFLDTIL----EAIED---LIEEKKLDIIIIDSLSSLARAS---QGDR 70
                        90       100       110
                ....*....|....*....|....*....|..
gi 18860063 277 DREVQRILLELLnqmdGFDQTTNVKVIMATNR 308
Cdd:cd01120  71 SSELLEDLAKLL----RAARNTGITVIATIHS 98
ycf2 CHL00206
Ycf2; Provisional
188-343 5.97e-05

Ycf2; Provisional


Pssm-ID: 214396 [Multi-domain]  Cd Length: 2281  Bit Score: 45.67  E-value: 5.97e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18860063   188 QIGIDPPRGVLMYGPPGCGKTMLAKAVAHHTTASFIRVvgseFVQKYLgegprmvrdvfrlakENAPAIIFIDEIDAIAT 267
Cdd:CHL00206 1624 RLALSPSRGILVIGSIGTGRSYLVKYLATNSYVPFITV----FLNKFL---------------DNKPKGFLIDDIDIDDS 1684
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18860063   268 KRFDAQTGADREVQRILLELLN--------QMDGFD-------------------------------------------- 295
Cdd:CHL00206 1685 DDIDDSDDIDRDLDTELLTMMNaltmdmmpKIDRFYitlqfelakamspciiwipnihdlnvnesnylslgllvnslsrd 1764
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 18860063   296 ----QTTNVKVIMATNRADTLDPALLRPGRLDRKIEFP---LPDRRQKRLVFSTI 343
Cdd:CHL00206 1765 cercSTRNILVIASTHIPQKVDPALIAPNKLNTCIKIRrllIPQQRKHFFTLSYT 1819
Mg_chelatase pfam01078
Magnesium chelatase, subunit ChlI; Magnesium-chelatase is a three-component enzyme that ...
197-213 9.46e-05

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: 43.29  E-value: 9.46e-05
                          10
                  ....*....|....*..
gi 18860063   197 VLMYGPPGCGKTMLAKA 213
Cdd:pfam01078  25 LLMIGPPGSGKTMLAKR 41
RecA-like_IQCA1 cd19506
ATPase domain of IQ and AAA domain-containing protein 1 (IQCA1); IQCA1 (also known as dynein ...
195-308 1.02e-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: 42.51  E-value: 1.02e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18860063 195 RGVLMYGPPGCGKTMLAKAVAHHTTASFIRVVGSEFVQKYLGEG--PRMVRDVFRLAKENAPAIIFIDEIDAIATKRF-- 270
Cdd:cd19506  27 KSLLLAGPSGVGKKMLVHAICTETGANLFNLSPSNIAGKYPGKNglQMMLHLVLKVARQLQPSVIWIGDAEKTFYKKVpk 106
                        90       100       110
                ....*....|....*....|....*....|....*....
gi 18860063 271 -DAQTGADReVQRILLELLNQMDGFDQttnVKVIMATNR 308
Cdd:cd19506 107 tEKQLDPKR-LKKDLPKILKSLKPEDR---VLIVGTTSR 141
PRK04195 PRK04195
replication factor C large subunit; Provisional
193-328 1.04e-04

replication factor C large subunit; Provisional


Pssm-ID: 235250 [Multi-domain]  Cd Length: 482  Bit Score: 44.14  E-value: 1.04e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18860063  193 PPRGVLMYGPPGCGKTMLAKAVAH-------------HTTASFI-RVVGSEFVQKYLGEGPRMvrdvfrlakenapaIIF 258
Cdd:PRK04195  38 PKKALLLYGPPGVGKTSLAHALANdygwevielnasdQRTADVIeRVAGEAATSGSLFGARRK--------------LIL 103
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 18860063  259 IDEIDAIatkrfdaQTGADREVQRILLELLNQmdgfdqtTNVKVIMATNraDTLDPAL--LRPgrLDRKIEF 328
Cdd:PRK04195 104 LDEVDGI-------HGNEDRGGARAILELIKK-------AKQPIILTAN--DPYDPSLreLRN--ACLMIEF 157
YifB COG0606
Predicted Mg-chelatase, contains ChlI-like and ATPase domains, YifB family [Posttranslational ...
197-212 1.13e-04

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: 44.26  E-value: 1.13e-04
                        10
                ....*....|....*.
gi 18860063 197 VLMYGPPGCGKTMLAK 212
Cdd:COG0606 214 LLMIGPPGSGKTMLAR 229
DnaC COG1484
DNA replication protein DnaC [Replication, recombination and repair];
191-290 1.28e-04

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


Pssm-ID: 441093 [Multi-domain]  Cd Length: 242  Bit Score: 43.23  E-value: 1.28e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18860063 191 IDPPRGVLMYGPPGCGKTMLAKAVAHH-----TTASFIRVvgSEFVQKY---LGEG--PRMVRdvfRLAKenAPAIIfID 260
Cdd:COG1484  96 IERGENLILLGPPGTGKTHLAIALGHEacragYRVRFTTA--PDLVNELkeaRADGrlERLLK---RLAK--VDLLI-LD 167
                        90       100       110
                ....*....|....*....|....*....|
gi 18860063 261 EidaIATKRFDAQTGADrevqriLLELLNQ 290
Cdd:COG1484 168 E---LGYLPLDAEGAEL------LFELISD 188
ruvB TIGR00635
Holliday junction DNA helicase, RuvB subunit; All proteins in this family for which functions ...
197-372 3.59e-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: 42.29  E-value: 3.59e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18860063   197 VLMYGPPGCGKTMLAKAVAHHTTASfIRVVGSEFVQKylgegPRMVRDVFRLAKENapAIIFIDEIDAIAtkrfdaqtga 276
Cdd:TIGR00635  33 LLLYGPPGLGKTTLAHIIANEMGVN-LKITSGPALEK-----PGDLAAILTNLEEG--DVLFIDEIHRLS---------- 94
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18860063   277 drevqRILLELL-NQMDGF------DQTTNVKVImatnRAD----TLDPALLRPGrldrKIEFPLPDRrqkrlvFStITS 345
Cdd:TIGR00635  95 -----PAVEELLyPAMEDFrldiviGKGPSARSV----RLDlppfTLVGATTRAG----MLTSPLRDR------FG-IIL 154
                         170       180
                  ....*....|....*....|....*..
gi 18860063   346 KMNLSEDVDLEEFVARPDKISGADINA 372
Cdd:TIGR00635 155 RLEFYTVEELAEIVSRSAGLLNVEIEP 181
44 PHA02544
clamp loader, small subunit; Provisional
194-336 5.21e-04

clamp loader, small subunit; Provisional


Pssm-ID: 222866 [Multi-domain]  Cd Length: 316  Bit Score: 41.90  E-value: 5.21e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18860063  194 PRGVLMYGPPGCGKTMLAKAVAHHTTASFIRVVGS----EFVQkylGEGPRMVRDVFRLAKenaPAIIFIDEIDAIATKr 269
Cdd:PHA02544  43 PNMLLHSPSPGTGKTTVAKALCNEVGAEVLFVNGSdcriDFVR---NRLTRFASTVSLTGG---GKVIIIDEFDRLGLA- 115
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 18860063  270 fdaqtgadrEVQRILLELLNQMDGfdqttNVKVIMATNRADTLDPALLrpGRLdRKIEFPLPDRRQK 336
Cdd:PHA02544 116 ---------DAQRHLRSFMEAYSK-----NCSFIITANNKNGIIEPLR--SRC-RVIDFGVPTKEEQ 165
hslU PRK05201
ATP-dependent protease ATPase subunit HslU;
256-285 7.66e-04

ATP-dependent protease ATPase subunit HslU;


Pssm-ID: 235364 [Multi-domain]  Cd Length: 443  Bit Score: 41.60  E-value: 7.66e-04
                         10        20        30
                 ....*....|....*....|....*....|...
gi 18860063  256 IIFIDEIDAIATKrfDAQTGAD--RE-VQRILL 285
Cdd:PRK05201 252 IVFIDEIDKIAAR--GGSSGPDvsREgVQRDLL 282
McrB COG1401
5-methylcytosine-specific restriction endonuclease McrBC, GTP-binding regulatory subunit McrB ...
197-262 1.73e-03

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


Pssm-ID: 441011 [Multi-domain]  Cd Length: 477  Bit Score: 40.52  E-value: 1.73e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18860063 197 VLMYGPPGCGKTMLAKAVAHHTTA---SFIRVV-------GSEFVQKY---LGEG-----PRMVRDVFRLAKEN--APAI 256
Cdd:COG1401 224 VILAGPPGTGKTYLARRLAEALGGednGRIEFVqfhpswsYEDFLLGYrpsLDEGkyeptPGIFLRFCLKAEKNpdKPYV 303

                ....*.
gi 18860063 257 IFIDEI 262
Cdd:COG1401 304 LIIDEI 309
HslU COG1220
ATP-dependent protease HslVU (ClpYQ), ATPase subunit HslU [Posttranslational modification, ...
256-285 2.34e-03

ATP-dependent protease HslVU (ClpYQ), ATPase subunit HslU [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 440833 [Multi-domain]  Cd Length: 454  Bit Score: 40.03  E-value: 2.34e-03
                        10        20        30
                ....*....|....*....|....*....|...
gi 18860063 256 IIFIDEIDAIATKrfDAQTGAD--RE-VQRILL 285
Cdd:COG1220 263 IIFIDEIDKIASR--GGGSGPDvsREgVQRDLL 293
PRK13341 PRK13341
AAA family ATPase;
198-223 2.56e-03

AAA family ATPase;


Pssm-ID: 237354 [Multi-domain]  Cd Length: 725  Bit Score: 40.04  E-value: 2.56e-03
                         10        20
                 ....*....|....*....|....*.
gi 18860063  198 LMYGPPGCGKTMLAKAVAHHTTASFI 223
Cdd:PRK13341  56 ILYGPPGVGKTTLARIIANHTRAHFS 81
AAA_16 pfam13191
AAA ATPase domain; This family of domains contain a P-loop motif that is characteriztic of the ...
184-232 3.41e-03

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


Pssm-ID: 433025 [Multi-domain]  Cd Length: 167  Bit Score: 38.25  E-value: 3.41e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 18860063   184 ELYKQIGIDPPRGVLMYGPPGCGKTMLAKAVAHHTTASFIRVVGSEFVQ 232
Cdd:pfam13191  14 DALDRVRSGRPPSVLLTGEAGTGKTTLLRELLRALERDGGYFLRGKCDE 62
RNA_helicase pfam00910
RNA helicase; This family includes RNA helicases thought to be involved in duplex unwinding ...
197-217 8.36e-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: 35.66  E-value: 8.36e-03
                          10        20
                  ....*....|....*....|.
gi 18860063   197 VLMYGPPGCGKTMLAKAVAHH 217
Cdd:pfam00910   1 IWLYGPPGCGKSTLAKYLARA 21
RecA-like_Lon cd19500
lon protease homolog 2 peroxisomal; Lon protease (also known as Lon peptidase) is an ...
198-317 8.57e-03

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: 37.15  E-value: 8.57e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18860063 198 LMYGPPGCGKTMLAKAVAHHTTASFIRV-VG-----SEFV---QKYLGEGP-RMVRDVfRLAKENAPaIIFIDEIDAIAT 267
Cdd:cd19500  41 CLVGPPGVGKTSLGKSIARALGRKFVRIsLGgvrdeAEIRghrRTYVGAMPgRIIQAL-KKAGTNNP-VFLLDEIDKIGS 118
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 18860063 268 KRFDAQTGAdrevqriLLELLN--QMDGF-DQTTNV-----KVI-MAT-NRADTLDPALL 317
Cdd:cd19500 119 SFRGDPASA-------LLEVLDpeQNSTFsDHYLDVpfdlsKVLfIATaNSLDTIPGPLL 171
 
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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