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Conserved domains on  [gi|66805379|ref|XP_636422|]
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26S protease regulatory subunit 6B [Dictyostelium discoideum AX4]

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
6-403 0e+00

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


:

Pssm-ID: 240423 [Multi-domain]  Cd Length: 398  Bit Score: 773.55  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66805379    6 LATAKVTVTKEASHHREADLYQKMKSLESKLDFFNIQEEYIKYEYKNLKRELLHAQEEVKRIRSVPLLIGQLLEMVDSNT 85
Cdd:PTZ00454   1 VATTAAAAVASSTTHTERDLYEKLKELEKELEFLDIQEEYIKEEQKNLKRELIRAKEEVKRIQSVPLVIGQFLEMIDSNY 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66805379   86 GIVQSTSGSTLCVRILSTIDRELLKPSASVALQRHSNALVDTLPPESDSSIHLLGADEKPSESYSDIGGGDIQKQEMREA 165
Cdd:PTZ00454  81 GIVSSTSGSNYYVRILSTLNRELLKPNASVALHRHSHAVVDILPPEADSSIQLLQMSEKPDVTYSDIGGLDIQKQEIREA 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66805379  166 VELPLTHHNLYKQIGIDPPRGVLLYGPPGTGKTMLAKAVAHHTSAAFIRVVGSEFVQKYLGEGPRLVRDVFRLARENSPA 245
Cdd:PTZ00454 161 VELPLTCPELYEQIGIDPPRGVLLYGPPGTGKTMLAKAVAHHTTATFIRVVGSEFVQKYLGEGPRMVRDVFRLARENAPS 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66805379  246 IIFIDEIDAIATKRFDAQTGADREVQRILMELLNQMDGFDVSVNVKVIMATNRQDTLDPALLRPGRLDRKIEFPLPDRRQ 325
Cdd:PTZ00454 241 IIFIDEVDSIATKRFDAQTGADREVQRILLELLNQMDGFDQTTNVKVIMATNRADTLDPALLRPGRLDRKIEFPLPDRRQ 320
                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 66805379  326 KRLIFQVITSKMNLSDEVDLEDYVSRPDKLSGAEIQSICQEAGMHAIRKNRYVILPKDFEKGYKASIKKNTHEFNFYN 403
Cdd:PTZ00454 321 KRLIFQTITSKMNLSEEVDLEDFVSRPEKISAADIAAICQEAGMQAVRKNRYVILPKDFEKGYKTVVRKTDRDYDFYS 398
 
Name Accession Description Interval E-value
PTZ00454 PTZ00454
26S protease regulatory subunit 6B-like protein; Provisional
6-403 0e+00

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


Pssm-ID: 240423 [Multi-domain]  Cd Length: 398  Bit Score: 773.55  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66805379    6 LATAKVTVTKEASHHREADLYQKMKSLESKLDFFNIQEEYIKYEYKNLKRELLHAQEEVKRIRSVPLLIGQLLEMVDSNT 85
Cdd:PTZ00454   1 VATTAAAAVASSTTHTERDLYEKLKELEKELEFLDIQEEYIKEEQKNLKRELIRAKEEVKRIQSVPLVIGQFLEMIDSNY 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66805379   86 GIVQSTSGSTLCVRILSTIDRELLKPSASVALQRHSNALVDTLPPESDSSIHLLGADEKPSESYSDIGGGDIQKQEMREA 165
Cdd:PTZ00454  81 GIVSSTSGSNYYVRILSTLNRELLKPNASVALHRHSHAVVDILPPEADSSIQLLQMSEKPDVTYSDIGGLDIQKQEIREA 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66805379  166 VELPLTHHNLYKQIGIDPPRGVLLYGPPGTGKTMLAKAVAHHTSAAFIRVVGSEFVQKYLGEGPRLVRDVFRLARENSPA 245
Cdd:PTZ00454 161 VELPLTCPELYEQIGIDPPRGVLLYGPPGTGKTMLAKAVAHHTTATFIRVVGSEFVQKYLGEGPRMVRDVFRLARENAPS 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66805379  246 IIFIDEIDAIATKRFDAQTGADREVQRILMELLNQMDGFDVSVNVKVIMATNRQDTLDPALLRPGRLDRKIEFPLPDRRQ 325
Cdd:PTZ00454 241 IIFIDEVDSIATKRFDAQTGADREVQRILLELLNQMDGFDQTTNVKVIMATNRADTLDPALLRPGRLDRKIEFPLPDRRQ 320
                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 66805379  326 KRLIFQVITSKMNLSDEVDLEDYVSRPDKLSGAEIQSICQEAGMHAIRKNRYVILPKDFEKGYKASIKKNTHEFNFYN 403
Cdd:PTZ00454 321 KRLIFQTITSKMNLSEEVDLEDFVSRPEKISAADIAAICQEAGMQAVRKNRYVILPKDFEKGYKTVVRKTDRDYDFYS 398
26Sp45 TIGR01242
26S proteasome subunit P45 family; Many proteins may score above the trusted cutoff because an ...
32-386 7.33e-145

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: 416.12  E-value: 7.33e-145
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66805379    32 LESKLDFFNIQEEYIKYEYKNLKRELLHAQEEVKRIRSVPLLIGQLLEMVDSNTGIVQSTSGSTLCVRILSTIDRELLKP 111
Cdd:TIGR01242   4 LDVRIRKLEDEKRSLEKEKIRLERELERLRSEIERLRSPPLIVGTVLEVLDDNRVVVKSSTGPNFVVNVSAFIDRKSLKP 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66805379   112 SASVALQRHSNALVDTLPPESDSSIHLLGADEKPSESYSDIGGGDIQKQEMREAVELPLTHHNLYKQIGIDPPRGVLLYG 191
Cdd:TIGR01242  84 GARVALNQQTLTIVDVLPTSKDPLVKGMEVEERPNVSYEDIGGLEEQIREIREAVELPLKHPELFEEVGIEPPKGVLLYG 163
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66805379   192 PPGTGKTMLAKAVAHHTSAAFIRVVGSEFVQKYLGEGPRLVRDVFRLARENSPAIIFIDEIDAIATKRFDAQTGADREVQ 271
Cdd:TIGR01242 164 PPGTGKTLLAKAVAHETNATFIRVVGSELVRKYIGEGARLVREIFELAKEKAPSIIFIDEIDAIAAKRTDSGTSGDREVQ 243
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66805379   272 RILMELLNQMDGFDVSVNVKVIMATNRQDTLDPALLRPGRLDRKIEFPLPDRRQKRLIFQVITSKMNLSDEVDLEDYVSR 351
Cdd:TIGR01242 244 RTLMQLLAELDGFDPRGNVKVIAATNRPDILDPALLRPGRFDRIIEVPLPDFEGRLEILKIHTRKMKLAEDVDLEAIAKM 323
                         330       340       350
                  ....*....|....*....|....*....|....*
gi 66805379   352 PDKLSGAEIQSICQEAGMHAIRKNRYVILPKDFEK 386
Cdd:TIGR01242 324 TEGASGADLKAICTEAGMFAIREERDYVTMDDFIK 358
RPT1 COG1222
ATP-dependent 26S proteasome regulatory subunit [Posttranslational modification, protein ...
141-398 6.31e-131

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: 6.31e-131
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66805379 141 ADEKPSESYSDIGGGDIQKQEMREAVELPLTHHNLYKQIGIDPPRGVLLYGPPGTGKTMLAKAVAHHTSAAFIRVVGSEF 220
Cdd:COG1222  69 PAESPDVTFDDIGGLDEQIEEIREAVELPLKNPELFRKYGIEPPKGVLLYGPPGTGKTLLAKAVAGELGAPFIRVRGSEL 148
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66805379 221 VQKYLGEGPRLVRDVFRLARENSPAIIFIDEIDAIATKRFDAQTGAdrEVQRILMELLNQMDGFDVSVNVKVIMATNRQD 300
Cdd:COG1222 149 VSKYIGEGARNVREVFELAREKAPSIIFIDEIDAIAARRTDDGTSG--EVQRTVNQLLAELDGFESRGDVLIIAATNRPD 226
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66805379 301 TLDPALLRPGRLDRKIEFPLPDRRQKRLIFQVITSKMNLSDEVDLEDYVSRPDKLSGAEIQSICQEAGMHAIRKNRYVIL 380
Cdd:COG1222 227 LLDPALLRPGRFDRVIEVPLPDEEAREEILKIHLRDMPLADDVDLDKLAKLTEGFSGADLKAIVTEAGMFAIREGRDTVT 306
                       250
                ....*....|....*...
gi 66805379 381 PKDFEKGYKASIKKNTHE 398
Cdd:COG1222 307 MEDLEKAIEKVKKKTETA 324
RecA-like_PAN_like cd19502
proteasome activating nucleotidase PAN and related proteasome subunits; This subfamily ...
148-318 4.81e-114

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


Pssm-ID: 410910 [Multi-domain]  Cd Length: 171  Bit Score: 330.07  E-value: 4.81e-114
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66805379 148 SYSDIGGGDIQKQEMREAVELPLTHHNLYKQIGIDPPRGVLLYGPPGTGKTMLAKAVAHHTSAAFIRVVGSEFVQKYLGE 227
Cdd:cd19502   1 TYEDIGGLDEQIREIREVVELPLKHPELFEELGIEPPKGVLLYGPPGTGKTLLAKAVANHTDATFIRVVGSELVQKYIGE 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66805379 228 GPRLVRDVFRLARENSPAIIFIDEIDAIATKRFDAQTGADREVQRILMELLNQMDGFDVSVNVKVIMATNRQDTLDPALL 307
Cdd:cd19502  81 GARLVRELFEMAREKAPSIIFIDEIDAIGAKRFDSGTGGDREVQRTMLELLNQLDGFDPRGNIKVIMATNRPDILDPALL 160
                       170
                ....*....|.
gi 66805379 308 RPGRLDRKIEF 318
Cdd:cd19502 161 RPGRFDRKIEF 171
AAA pfam00004
ATPase family associated with various cellular activities (AAA); AAA family proteins often ...
187-320 2.90e-55

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: 178.56  E-value: 2.90e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66805379   187 VLLYGPPGTGKTMLAKAVAHHTSAAFIRVVGSEFVQKYLGEGPRLVRDVFRLARENSPAIIFIDEIDAIATKRFDaqtGA 266
Cdd:pfam00004   1 LLLYGPPGTGKTTLAKAVAKELGAPFIEISGSELVSKYVGESEKRLRELFEAAKKLAPCVIFIDEIDALAGSRGS---GG 77
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 66805379   267 DREVQRILMELLNQMDGFDVSV-NVKVIMATNRQDTLDPALLrpGRLDRKIEFPL 320
Cdd:pfam00004  78 DSESRRVVNQLLTELDGFTSSNsKVIVIAATNRPDKLDPALL--GRFDRIIEFPL 130
AAA smart00382
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ...
183-322 2.25e-20

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


Pssm-ID: 214640 [Multi-domain]  Cd Length: 148  Bit Score: 87.04  E-value: 2.25e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66805379    183 PPRGVLLYGPPGTGKTMLAKAVAHH---TSAAFIRVVGSEF--------------VQKYLGEGPRLVRDVFRLARENSPA 245
Cdd:smart00382   1 PGEVILIVGPPGSGKTTLARALARElgpPGGGVIYIDGEDIleevldqllliivgGKKASGSGELRLRLALALARKLKPD 80
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 66805379    246 IIFIDEIDAIATKRFdaqtgadrEVQRILMELLNQMDGFDVSVNVKVIMATNRQDTLDPALLRPgRLDRKIEFPLPD 322
Cdd:smart00382  81 VLILDEITSLLDAEQ--------EALLLLLEELRLLLLLKSEKNLTVILTTNDEKDLGPALLRR-RFDRRIVLLLIL 148
IS21_help_AAA NF038214
IS21-like element helper ATPase IstB; This protein family model resembles PF01695, but was ...
187-252 1.02e-03

IS21-like element helper ATPase IstB; This protein family model resembles PF01695, but was built to hit full-length AAA+ ATPases of IS21 family IS (insertion sequence) elements.


Pssm-ID: 439516  Cd Length: 232  Bit Score: 40.15  E-value: 1.02e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 66805379  187 VLLYGPPGTGKTMLA-----KAVAHHTSAAFIRVvgSEFVQKYL---GEGpRLVRDVFRLARensPAIIFIDEI 252
Cdd:NF038214  93 VLLLGPPGTGKTHLAialgyAACRQGYRVRFTTA--ADLVEQLAqarADG-RLGRLLRRLAR---YDLLIIDEL 160
 
Name Accession Description Interval E-value
PTZ00454 PTZ00454
26S protease regulatory subunit 6B-like protein; Provisional
6-403 0e+00

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


Pssm-ID: 240423 [Multi-domain]  Cd Length: 398  Bit Score: 773.55  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66805379    6 LATAKVTVTKEASHHREADLYQKMKSLESKLDFFNIQEEYIKYEYKNLKRELLHAQEEVKRIRSVPLLIGQLLEMVDSNT 85
Cdd:PTZ00454   1 VATTAAAAVASSTTHTERDLYEKLKELEKELEFLDIQEEYIKEEQKNLKRELIRAKEEVKRIQSVPLVIGQFLEMIDSNY 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66805379   86 GIVQSTSGSTLCVRILSTIDRELLKPSASVALQRHSNALVDTLPPESDSSIHLLGADEKPSESYSDIGGGDIQKQEMREA 165
Cdd:PTZ00454  81 GIVSSTSGSNYYVRILSTLNRELLKPNASVALHRHSHAVVDILPPEADSSIQLLQMSEKPDVTYSDIGGLDIQKQEIREA 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66805379  166 VELPLTHHNLYKQIGIDPPRGVLLYGPPGTGKTMLAKAVAHHTSAAFIRVVGSEFVQKYLGEGPRLVRDVFRLARENSPA 245
Cdd:PTZ00454 161 VELPLTCPELYEQIGIDPPRGVLLYGPPGTGKTMLAKAVAHHTTATFIRVVGSEFVQKYLGEGPRMVRDVFRLARENAPS 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66805379  246 IIFIDEIDAIATKRFDAQTGADREVQRILMELLNQMDGFDVSVNVKVIMATNRQDTLDPALLRPGRLDRKIEFPLPDRRQ 325
Cdd:PTZ00454 241 IIFIDEVDSIATKRFDAQTGADREVQRILLELLNQMDGFDQTTNVKVIMATNRADTLDPALLRPGRLDRKIEFPLPDRRQ 320
                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 66805379  326 KRLIFQVITSKMNLSDEVDLEDYVSRPDKLSGAEIQSICQEAGMHAIRKNRYVILPKDFEKGYKASIKKNTHEFNFYN 403
Cdd:PTZ00454 321 KRLIFQTITSKMNLSEEVDLEDFVSRPEKISAADIAAICQEAGMQAVRKNRYVILPKDFEKGYKTVVRKTDRDYDFYS 398
PRK03992 PRK03992
proteasome-activating nucleotidase; Provisional
15-400 1.89e-168

proteasome-activating nucleotidase; Provisional


Pssm-ID: 179699 [Multi-domain]  Cd Length: 389  Bit Score: 476.63  E-value: 1.89e-168
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66805379   15 KEASHHREADLYQKMKSLESKLDffniqeeYIKYEYKNLKRELLHAQEEVKRIRSVPLLIGQLLEMVDSNTGIVQSTSGS 94
Cdd:PRK03992   3 LEALEERNSELEEQIRQLELKLR-------DLEAENEKLERELERLKSELEKLKSPPLIVATVLEVLDDGRVVVKSSGGP 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66805379   95 TLCVRILSTIDRELLKPSASVALQRHSNALVDTLPPESDSSIHLLGADEKPSESYSDIGGGDIQKQEMREAVELPLTHHN 174
Cdd:PRK03992  76 QFLVNVSPFIDREKLKPGARVALNQQSLAIVEVLPSEKDPRVQAMEVIESPNVTYEDIGGLEEQIREVREAVELPLKKPE 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66805379  175 LYKQIGIDPPRGVLLYGPPGTGKTMLAKAVAHHTSAAFIRVVGSEFVQKYLGEGPRLVRDVFRLARENSPAIIFIDEIDA 254
Cdd:PRK03992 156 LFEEVGIEPPKGVLLYGPPGTGKTLLAKAVAHETNATFIRVVGSELVQKFIGEGARLVRELFELAREKAPSIIFIDEIDA 235
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66805379  255 IATKRFDAQTGADREVQRILMELLNQMDGFDVSVNVKVIMATNRQDTLDPALLRPGRLDRKIEFPLPDRRQKRLIFQVIT 334
Cdd:PRK03992 236 IAAKRTDSGTSGDREVQRTLMQLLAEMDGFDPRGNVKIIAATNRIDILDPAILRPGRFDRIIEVPLPDEEGRLEILKIHT 315
                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 66805379  335 SKMNLSDEVDLEDYVSRPDKLSGAEIQSICQEAGMHAIRKNRYVILPKDFEKGYKASIKKNTHEFN 400
Cdd:PRK03992 316 RKMNLADDVDLEELAELTEGASGADLKAICTEAGMFAIRDDRTEVTMEDFLKAIEKVMGKEEKDSM 381
PTZ00361 PTZ00361
26 proteosome regulatory subunit 4-like protein; Provisional
28-387 1.22e-153

26 proteosome regulatory subunit 4-like protein; Provisional


Pssm-ID: 185575 [Multi-domain]  Cd Length: 438  Bit Score: 441.13  E-value: 1.22e-153
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66805379   28 KMKSLESKLDFFNIQEEYIKyEYKNLKRELLHAQEEVKRI---RSVPLLIGQLLEMVDSNTGIVQSTSGSTLCVRILSTI 104
Cdd:PTZ00361  59 RLLKLERIKDYLLLEEEFIT-NQEAQKPAQEKNEAELKKVddlRGSPLSVGTLEEIIDENHAIVSSSVGPEYYVNILSFV 137
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66805379  105 DRELLKPSASVALQRHSNALVDTLPPESDSSIHLLGADEKPSESYSDIGGGDIQKQEMREAVELPLTHHNLYKQIGIDPP 184
Cdd:PTZ00361 138 DKEQLEPGCSVLLHNKTHSVVGILLDEVDPLVSVMKVDKAPLESYADIGGLEQQIQEIKEAVELPLTHPELYDDIGIKPP 217
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66805379  185 RGVLLYGPPGTGKTMLAKAVAHHTSAAFIRVVGSEFVQKYLGEGPRLVRDVFRLARENSPAIIFIDEIDAIATKRFDAQT 264
Cdd:PTZ00361 218 KGVILYGPPGTGKTLLAKAVANETSATFLRVVGSELIQKYLGDGPKLVRELFRVAEENAPSIVFIDEIDAIGTKRYDATS 297
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66805379  265 GADREVQRILMELLNQMDGFDVSVNVKVIMATNRQDTLDPALLRPGRLDRKIEFPLPDRRQKRLIFQVITSKMNLSDEVD 344
Cdd:PTZ00361 298 GGEKEIQRTMLELLNQLDGFDSRGDVKVIMATNRIESLDPALIRPGRIDRKIEFPNPDEKTKRRIFEIHTSKMTLAEDVD 377
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|...
gi 66805379  345 LEDYVSRPDKLSGAEIQSICQEAGMHAIRKNRYVILPKDFEKG 387
Cdd:PTZ00361 378 LEEFIMAKDELSGADIKAICTEAGLLALRERRMKVTQADFRKA 420
26Sp45 TIGR01242
26S proteasome subunit P45 family; Many proteins may score above the trusted cutoff because an ...
32-386 7.33e-145

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: 416.12  E-value: 7.33e-145
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66805379    32 LESKLDFFNIQEEYIKYEYKNLKRELLHAQEEVKRIRSVPLLIGQLLEMVDSNTGIVQSTSGSTLCVRILSTIDRELLKP 111
Cdd:TIGR01242   4 LDVRIRKLEDEKRSLEKEKIRLERELERLRSEIERLRSPPLIVGTVLEVLDDNRVVVKSSTGPNFVVNVSAFIDRKSLKP 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66805379   112 SASVALQRHSNALVDTLPPESDSSIHLLGADEKPSESYSDIGGGDIQKQEMREAVELPLTHHNLYKQIGIDPPRGVLLYG 191
Cdd:TIGR01242  84 GARVALNQQTLTIVDVLPTSKDPLVKGMEVEERPNVSYEDIGGLEEQIREIREAVELPLKHPELFEEVGIEPPKGVLLYG 163
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66805379   192 PPGTGKTMLAKAVAHHTSAAFIRVVGSEFVQKYLGEGPRLVRDVFRLARENSPAIIFIDEIDAIATKRFDAQTGADREVQ 271
Cdd:TIGR01242 164 PPGTGKTLLAKAVAHETNATFIRVVGSELVRKYIGEGARLVREIFELAKEKAPSIIFIDEIDAIAAKRTDSGTSGDREVQ 243
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66805379   272 RILMELLNQMDGFDVSVNVKVIMATNRQDTLDPALLRPGRLDRKIEFPLPDRRQKRLIFQVITSKMNLSDEVDLEDYVSR 351
Cdd:TIGR01242 244 RTLMQLLAELDGFDPRGNVKVIAATNRPDILDPALLRPGRFDRIIEVPLPDFEGRLEILKIHTRKMKLAEDVDLEAIAKM 323
                         330       340       350
                  ....*....|....*....|....*....|....*
gi 66805379   352 PDKLSGAEIQSICQEAGMHAIRKNRYVILPKDFEK 386
Cdd:TIGR01242 324 TEGASGADLKAICTEAGMFAIREERDYVTMDDFIK 358
RPT1 COG1222
ATP-dependent 26S proteasome regulatory subunit [Posttranslational modification, protein ...
141-398 6.31e-131

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: 6.31e-131
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66805379 141 ADEKPSESYSDIGGGDIQKQEMREAVELPLTHHNLYKQIGIDPPRGVLLYGPPGTGKTMLAKAVAHHTSAAFIRVVGSEF 220
Cdd:COG1222  69 PAESPDVTFDDIGGLDEQIEEIREAVELPLKNPELFRKYGIEPPKGVLLYGPPGTGKTLLAKAVAGELGAPFIRVRGSEL 148
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66805379 221 VQKYLGEGPRLVRDVFRLARENSPAIIFIDEIDAIATKRFDAQTGAdrEVQRILMELLNQMDGFDVSVNVKVIMATNRQD 300
Cdd:COG1222 149 VSKYIGEGARNVREVFELAREKAPSIIFIDEIDAIAARRTDDGTSG--EVQRTVNQLLAELDGFESRGDVLIIAATNRPD 226
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66805379 301 TLDPALLRPGRLDRKIEFPLPDRRQKRLIFQVITSKMNLSDEVDLEDYVSRPDKLSGAEIQSICQEAGMHAIRKNRYVIL 380
Cdd:COG1222 227 LLDPALLRPGRFDRVIEVPLPDEEAREEILKIHLRDMPLADDVDLDKLAKLTEGFSGADLKAIVTEAGMFAIREGRDTVT 306
                       250
                ....*....|....*...
gi 66805379 381 PKDFEKGYKASIKKNTHE 398
Cdd:COG1222 307 MEDLEKAIEKVKKKTETA 324
RecA-like_PAN_like cd19502
proteasome activating nucleotidase PAN and related proteasome subunits; This subfamily ...
148-318 4.81e-114

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


Pssm-ID: 410910 [Multi-domain]  Cd Length: 171  Bit Score: 330.07  E-value: 4.81e-114
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66805379 148 SYSDIGGGDIQKQEMREAVELPLTHHNLYKQIGIDPPRGVLLYGPPGTGKTMLAKAVAHHTSAAFIRVVGSEFVQKYLGE 227
Cdd:cd19502   1 TYEDIGGLDEQIREIREVVELPLKHPELFEELGIEPPKGVLLYGPPGTGKTLLAKAVANHTDATFIRVVGSELVQKYIGE 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66805379 228 GPRLVRDVFRLARENSPAIIFIDEIDAIATKRFDAQTGADREVQRILMELLNQMDGFDVSVNVKVIMATNRQDTLDPALL 307
Cdd:cd19502  81 GARLVRELFEMAREKAPSIIFIDEIDAIGAKRFDSGTGGDREVQRTMLELLNQLDGFDPRGNIKVIMATNRPDILDPALL 160
                       170
                ....*....|.
gi 66805379 308 RPGRLDRKIEF 318
Cdd:cd19502 161 RPGRFDRKIEF 171
CDC48 TIGR01243
AAA family ATPase, CDC48 subfamily; This subfamily of the AAA family ATPases includes two ...
143-394 5.26e-78

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


Pssm-ID: 273521 [Multi-domain]  Cd Length: 733  Bit Score: 255.22  E-value: 5.26e-78
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66805379   143 EKPSESYSDIGGGDIQKQEMREAVELPLTHHNLYKQIGIDPPRGVLLYGPPGTGKTMLAKAVAHHTSAAFIRVVGSEFVQ 222
Cdd:TIGR01243 446 EVPNVRWSDIGGLEEVKQELREAVEWPLKHPEIFEKMGIRPPKGVLLFGPPGTGKTLLAKAVATESGANFIAVRGPEILS 525
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66805379   223 KYLGEGPRLVRDVFRLARENSPAIIFIDEIDAIATKRfdaqtGADRE---VQRILMELLNQMDGFDVSVNVKVIMATNRQ 299
Cdd:TIGR01243 526 KWVGESEKAIREIFRKARQAAPAIIFFDEIDAIAPAR-----GARFDtsvTDRIVNQLLTEMDGIQELSNVVVIAATNRP 600
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66805379   300 DTLDPALLRPGRLDRKIEFPLPDRRQKRLIFQVITSKMNLSDEVDLEDYVSRPDKLSGAEIQSICQEAGMHAIRKNRYVI 379
Cdd:TIGR01243 601 DILDPALLRPGRFDRLILVPPPDEEARKEIFKIHTRSMPLAEDVDLEELAEMTEGYTGADIEAVCREAAMAALRESIGSP 680
                         250
                  ....*....|....*
gi 66805379   380 LPKDFEKGYKASIKK 394
Cdd:TIGR01243 681 AKEKLEVGEEEFLKD 695
SpoVK COG0464
AAA+-type ATPase, SpoVK/Ycf46/Vps4 family [Cell wall/membrane/envelope biogenesis, Cell cycle ...
6-386 2.02e-77

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: 244.82  E-value: 2.02e-77
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66805379   6 LATAKVTVTKEASHHREADLYQKMKSLESKLDFFNIQEEYIKYEYKNLKRELLHAQEEVKRIRSVPLLIGQLLEMVDSNT 85
Cdd:COG0464   9 VALALALLLLDDAALRLLLLLLLALAAALLLLLLLLLLLLLALLLVELLLLLLSGALAALLLLALLLLALLALLAALLSA 88
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66805379  86 GIVQSTSGSTLCVRILSTIDRELLKPSASVALQRHSNALVDTLPPESDSSIHLLGADEKPSES----YSDIGGGDIQKQE 161
Cdd:COG0464  89 LELLLLGELLLLLLLLLLLLLLLLDLERALLELLRESAEALALAAPLVTYEDIGGLEEELLELreaiLDDLGGLEEVKEE 168
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66805379 162 MREAVELPLTHHNLYKQIGIDPPRGVLLYGPPGTGKTMLAKAVAHHTSAAFIRVVGSEFVQKYLGEGPRLVRDVFRLARE 241
Cdd:COG0464 169 LRELVALPLKRPELREEYGLPPPRGLLLYGPPGTGKTLLARALAGELGLPLIEVDLSDLVSKYVGETEKNLREVFDKARG 248
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66805379 242 NSPAIIFIDEIDAIATKRfdaQTGADREVQRILMELLNQMDgfDVSVNVKVIMATNRQDTLDPALLRpgRLDRKIEFPLP 321
Cdd:COG0464 249 LAPCVLFIDEADALAGKR---GEVGDGVGRRVVNTLLTEME--ELRSDVVVIAATNRPDLLDPALLR--RFDEIIFFPLP 321
                       330       340       350       360       370       380
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 66805379 322 DRRQKRLIFQVITSKMNLSDEVDLEDYVSRPDKLSGAEIQSICQEAGMHAIRKNRYVILPKDFEK 386
Cdd:COG0464 322 DAEERLEIFRIHLRKRPLDEDVDLEELAEATEGLSGADIRNVVRRAALQALRLGREPVTTEDLLE 386
FtsH_fam TIGR01241
ATP-dependent metalloprotease FtsH; HflB(FtsH) is a pleiotropic protein required for correct ...
141-386 1.07e-74

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: 240.65  E-value: 1.07e-74
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66805379   141 ADEKPSESYSDIGGGDIQKQEMREAVELpLTHHNLYKQIGIDPPRGVLLYGPPGTGKTMLAKAVAHHTSAAFIRVVGSEF 220
Cdd:TIGR01241  46 NEEKPKVTFKDVAGIDEAKEELMEIVDF-LKNPSKFTKLGAKIPKGVLLVGPPGTGKTLLAKAVAGEAGVPFFSISGSDF 124
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66805379   221 VQKYLGEGPRLVRDVFRLARENSPAIIFIDEIDAIATKRFDAQTGADREVQRILMELLNQMDGFDVSVNVKVIMATNRQD 300
Cdd:TIGR01241 125 VEMFVGVGASRVRDLFEQAKKNAPCIIFIDEIDAVGRQRGAGLGGGNDEREQTLNQLLVEMDGFGTNTGVIVIAATNRPD 204
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66805379   301 TLDPALLRPGRLDRKIEFPLPDRRQKRLIFQVITSKMNLSDEVDLEDYVSRPDKLSGAEIQSICQEAGMHAIRKNRYVIL 380
Cdd:TIGR01241 205 VLDPALLRPGRFDRQVVVDLPDIKGREEILKVHAKNKKLAPDVDLKAVARRTPGFSGADLANLLNEAALLAARKNKTEIT 284

                  ....*.
gi 66805379   381 PKDFEK 386
Cdd:TIGR01241 285 MNDIEE 290
CDC48 TIGR01243
AAA family ATPase, CDC48 subfamily; This subfamily of the AAA family ATPases includes two ...
145-374 7.23e-69

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: 230.95  E-value: 7.23e-69
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66805379   145 PSESYSDIGGGDIQKQEMREAVELPLTHHNLYKQIGIDPPRGVLLYGPPGTGKTMLAKAVAHHTSAAFIRVVGSEFVQKY 224
Cdd:TIGR01243 173 PKVTYEDIGGLKEAKEKIREMVELPMKHPELFEHLGIEPPKGVLLYGPPGTGKTLLAKAVANEAGAYFISINGPEIMSKY 252
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66805379   225 LGEGPRLVRDVFRLARENSPAIIFIDEIDAIATKRfDAQTGadrEVQ-RILMELLNQMDGFDVSVNVKVIMATNRQDTLD 303
Cdd:TIGR01243 253 YGESEERLREIFKEAEENAPSIIFIDEIDAIAPKR-EEVTG---EVEkRVVAQLLTLMDGLKGRGRVIVIGATNRPDALD 328
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 66805379   304 PALLRPGRLDRKIEFPLPDRRQKRLIFQVITSKMNLSDEVDLEDYVSRPDKLSGAEIQSICQEAGMHAIRK 374
Cdd:TIGR01243 329 PALRRPGRFDREIVIRVPDKRARKEILKVHTRNMPLAEDVDLDKLAEVTHGFVGADLAALAKEAAMAALRR 399
RecA-like_CDC48_NLV2_r1-like cd19503
first of two ATPase domains of CDC48 and NLV2, and similar ATPase domains; CDC48 in yeast and ...
151-318 1.53e-68

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: 214.08  E-value: 1.53e-68
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66805379 151 DIGGGDIQKQEMREAVELPLTHHNLYKQIGIDPPRGVLLYGPPGTGKTMLAKAVAHHTSAAFIRVVGSEFVQKYLGEGPR 230
Cdd:cd19503   1 DIGGLDEQIASLKELIELPLKYPELFRALGLKPPRGVLLHGPPGTGKTLLARAVANEAGANFLSISGPSIVSKYLGESEK 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66805379 231 LVRDVFRLARENSPAIIFIDEIDAIATKRFDAQTGADRevqRILMELLNQMDGFDVSVNVKVIMATNRQDTLDPALLRPG 310
Cdd:cd19503  81 NLREIFEEARSHAPSIIFIDEIDALAPKREEDQREVER---RVVAQLLTLMDGMSSRGKVVVIAATNRPDAIDPALRRPG 157

                ....*...
gi 66805379 311 RLDRKIEF 318
Cdd:cd19503 158 RFDREVEI 165
RecA-like_FtsH cd19501
ATP-dependent zinc metalloprotease FtsH; FtsH ATPase is a processive, ATP-dependent zinc ...
148-316 5.34e-68

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: 212.86  E-value: 5.34e-68
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66805379 148 SYSDIGGGDIQKQEMREAVELpLTHHNLYKQIGIDPPRGVLLYGPPGTGKTMLAKAVAHHTSAAFIRVVGSEFVQKYLGE 227
Cdd:cd19501   2 TFKDVAGCEEAKEELKEVVEF-LKNPEKFTKLGAKIPKGVLLVGPPGTGKTLLAKAVAGEAGVPFFSISGSDFVEMFVGV 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66805379 228 GPRLVRDVFRLARENSPAIIFIDEIDAIATKRFDAQTGADREVQRILMELLNQMDGFDVSVNVKVIMATNRQDTLDPALL 307
Cdd:cd19501  81 GASRVRDLFEQAKKNAPCIVFIDEIDAVGRKRGAGLGGGHDEREQTLNQLLVEMDGFESNTGVIVIAATNRPDVLDPALL 160

                ....*....
gi 66805379 308 RPGRLDRKI 316
Cdd:cd19501 161 RPGRFDRQV 169
RecA-like_CDC48_r2-like cd19511
second of two ATPase domains of CDC48/p97, PEX1 and -6, VAT and NVL, and similar ATPase ...
159-316 3.21e-66

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: 207.91  E-value: 3.21e-66
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66805379 159 KQEMREAVELPLTHHNLYKQIGIDPPRGVLLYGPPGTGKTMLAKAVAHHTSAAFIRVVGSEFVQKYLGEGPRLVRDVFRL 238
Cdd:cd19511   2 KRELKEAVEWPLKHPDAFKRLGIRPPKGVLLYGPPGCGKTLLAKALASEAGLNFISVKGPELFSKYVGESERAVREIFQK 81
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 66805379 239 ARENSPAIIFIDEIDAIATKRfdAQTGADREVQRILMELLNQMDGFDVSVNVKVIMATNRQDTLDPALLRPGRLDRKI 316
Cdd:cd19511  82 ARQAAPCIIFFDEIDSLAPRR--GQSDSSGVTDRVVSQLLTELDGIESLKGVVVIAATNRPDMIDPALLRPGRLDKLI 157
HflB COG0465
ATP-dependent Zn proteases [Posttranslational modification, protein turnover, chaperones];
142-386 3.24e-66

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


Pssm-ID: 440233 [Multi-domain]  Cd Length: 583  Bit Score: 220.68  E-value: 3.24e-66
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66805379 142 DEKPSESYSDIGGGDIQKQEMREAVELpLTHHNLYKQIGIDPPRGVLLYGPPGTGKTMLAKAVAHHTSAAFIRVVGSEFV 221
Cdd:COG0465 134 EDKPKVTFDDVAGVDEAKEELQEIVDF-LKDPEKFTRLGAKIPKGVLLVGPPGTGKTLLAKAVAGEAGVPFFSISGSDFV 212
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66805379 222 QKYLGEGPRLVRDVFRLARENSPAIIFIDEIDAIATKRFDAQTGADREVQRILMELLNQMDGFDVSVNVKVIMATNRQDT 301
Cdd:COG0465 213 EMFVGVGASRVRDLFEQAKKNAPCIIFIDEIDAVGRQRGAGLGGGHDEREQTLNQLLVEMDGFEGNEGVIVIAATNRPDV 292
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66805379 302 LDPALLRPGRLDRKIEFPLPDRRQKRLIFQVITSKMNLSDEVDLEDYVSRPDKLSGAEIQSICQEAGMHAIRKNRYVILP 381
Cdd:COG0465 293 LDPALLRPGRFDRQVVVDLPDVKGREAILKVHARKKPLAPDVDLEVIARRTPGFSGADLANLVNEAALLAARRNKKAVTM 372

                ....*
gi 66805379 382 KDFEK 386
Cdd:COG0465 373 EDFEE 377
RecA-like_CDC48_r1-like cd19519
first of two ATPase domains of CDC48 and similar ATPase domains; CDC48 in yeast and p97 or VCP ...
151-319 1.85e-63

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: 201.13  E-value: 1.85e-63
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66805379 151 DIGGGDIQKQEMREAVELPLTHHNLYKQIGIDPPRGVLLYGPPGTGKTMLAKAVAHHTSAAFIRVVGSEFVQKYLGEGPR 230
Cdd:cd19519   1 DIGGCRKQLAQIREMVELPLRHPELFKAIGIKPPRGILLYGPPGTGKTLIARAVANETGAFFFLINGPEIMSKLAGESES 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66805379 231 LVRDVFRLARENSPAIIFIDEIDAIATKRFDAQTGADRevqRILMELLNQMDGFDVSVNVKVIMATNRQDTLDPALLRPG 310
Cdd:cd19519  81 NLRKAFEEAEKNAPAIIFIDEIDAIAPKREKTHGEVER---RIVSQLLTLMDGLKQRAHVIVMAATNRPNSIDPALRRFG 157

                ....*....
gi 66805379 311 RLDRKIEFP 319
Cdd:cd19519 158 RFDREIDIG 166
ftsH CHL00176
cell division protein; Validated
148-386 2.38e-62

cell division protein; Validated


Pssm-ID: 214386 [Multi-domain]  Cd Length: 638  Bit Score: 211.83  E-value: 2.38e-62
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66805379  148 SYSDIGGGDIQKQEMREAVELpLTHHNLYKQIGIDPPRGVLLYGPPGTGKTMLAKAVAHHTSAAFIRVVGSEFVQKYLGE 227
Cdd:CHL00176 181 TFRDIAGIEEAKEEFEEVVSF-LKKPERFTAVGAKIPKGVLLVGPPGTGKTLLAKAIAGEAEVPFFSISGSEFVEMFVGV 259
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66805379  228 GPRLVRDVFRLARENSPAIIFIDEIDAIATKRFDAQTGADREVQRILMELLNQMDGFDVSVNVKVIMATNRQDTLDPALL 307
Cdd:CHL00176 260 GAARVRDLFKKAKENSPCIVFIDEIDAVGRQRGAGIGGGNDEREQTLNQLLTEMDGFKGNKGVIVIAATNRVDILDAALL 339
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 66805379  308 RPGRLDRKIEFPLPDRRQKRLIFQVITSKMNLSDEVDLEDYVSRPDKLSGAEIQSICQEAGMHAIRKNRYVILPKDFEK 386
Cdd:CHL00176 340 RPGRFDRQITVSLPDREGRLDILKVHARNKKLSPDVSLELIARRTPGFSGADLANLLNEAAILTARRKKATITMKEIDT 418
RecA-like_VCP_r2 cd19529
second of two ATPase domains of Valosin-containing protein-like ATPase (VAT) and similar ...
159-316 8.74e-62

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


Pssm-ID: 410937 [Multi-domain]  Cd Length: 159  Bit Score: 196.56  E-value: 8.74e-62
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66805379 159 KQEMREAVELPLTHHNLYKQIGIDPPRGVLLYGPPGTGKTMLAKAVAHHTSAAFIRVVGSEFVQKYLGEGPRLVRDVFRL 238
Cdd:cd19529   2 KQELKEAVEWPLLKPEVFKRLGIRPPKGILLYGPPGTGKTLLAKAVATESNANFISVKGPELLSKWVGESEKAIREIFRK 81
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 66805379 239 ARENSPAIIFIDEIDAIATKRfdAQTGADREVQRILMELLNQMDGFDVSVNVKVIMATNRQDTLDPALLRPGRLDRKI 316
Cdd:cd19529  82 ARQVAPCVIFFDEIDSIAPRR--GTTGDSGVTERVVNQLLTELDGLEEMNGVVVIAATNRPDIIDPALLRAGRFDRLI 157
RecA-like_protease cd19481
proteases similar to RecA; RecA-like NTPases. This family includes the NTP binding domain of ...
158-318 1.37e-60

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


Pssm-ID: 410889 [Multi-domain]  Cd Length: 158  Bit Score: 193.27  E-value: 1.37e-60
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66805379 158 QKQEMREAVELPLTHHNLYKQiGIDPPRGVLLYGPPGTGKTMLAKAVAHHTSAAFIRVVGSEFVQKYLGEGPRLVRDVFR 237
Cdd:cd19481   1 LKASLREAVEAPRRGSRLRRY-GLGLPKGILLYGPPGTGKTLLAKALAGELGLPLIVVKLSSLLSKYVGESEKNLRKIFE 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66805379 238 LARENSPAIIFIDEIDAIATKRFDaqTGADREVQRILMELLNQMDGFDVSVNVKVIMATNRQDTLDPALLRPGRLDRKIE 317
Cdd:cd19481  80 RARRLAPCILFIDEIDAIGRKRDS--SGESGELRRVLNQLLTELDGVNSRSKVLVIAATNRPDLLDPALLRPGRFDEVIE 157

                .
gi 66805379 318 F 318
Cdd:cd19481 158 F 158
hflB PRK10733
ATP-dependent zinc metalloprotease FtsH;
148-387 3.36e-56

ATP-dependent zinc metalloprotease FtsH;


Pssm-ID: 182683 [Multi-domain]  Cd Length: 644  Bit Score: 195.25  E-value: 3.36e-56
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66805379  148 SYSDIGGGDIQKQEMREAVELpLTHHNLYKQIGIDPPRGVLLYGPPGTGKTMLAKAVAHHTSAAFIRVVGSEFVQKYLGE 227
Cdd:PRK10733 150 TFADVAGCDEAKEEVAELVEY-LREPSRFQKLGGKIPKGVLMVGPPGTGKTLLAKAIAGEAKVPFFTISGSDFVEMFVGV 228
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66805379  228 GPRLVRDVFRLARENSPAIIFIDEIDAIATKRFDAQTGADREVQRILMELLNQMDGFDVSVNVKVIMATNRQDTLDPALL 307
Cdd:PRK10733 229 GASRVRDMFEQAKKAAPCIIFIDEIDAVGRQRGAGLGGGHDEREQTLNQMLVEMDGFEGNEGIIVIAATNRPDVLDPALL 308
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66805379  308 RPGRLDRKIEFPLPDRRQKRLIFQVITSKMNLSDEVDLEDYVSRPDKLSGAEIQSICQEAGMHAIRKNRYVILPKDFEKG 387
Cdd:PRK10733 309 RPGRFDRQVVVGLPDVRGREQILKVHMRRVPLAPDIDAAIIARGTPGFSGADLANLVNEAALFAARGNKRVVSMVEFEKA 388
RecA-like_CDC48_r2-like cd19528
second of two ATPase domains of CDC48 and similar ATPase domains; CDC48 in yeast and p97 or ...
159-316 2.10e-55

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: 180.01  E-value: 2.10e-55
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66805379 159 KQEMREAVELPLTHHNLYKQIGIDPPRGVLLYGPPGTGKTMLAKAVAHHTSAAFIRVVGSEFVQKYLGEGPRLVRDVFRL 238
Cdd:cd19528   2 KRELQELVQYPVEHPDKFLKFGMTPSKGVLFYGPPGCGKTLLAKAIANECQANFISVKGPELLTMWFGESEANVRDIFDK 81
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 66805379 239 ARENSPAIIFIDEIDAIATKRFDAQTGADREVQRILMELLNQMDGFDVSVNVKVIMATNRQDTLDPALLRPGRLDRKI 316
Cdd:cd19528  82 ARAAAPCVLFFDELDSIAKARGGNIGDAGGAADRVINQILTEMDGMNTKKNVFIIGATNRPDIIDPAILRPGRLDQLI 159
AAA pfam00004
ATPase family associated with various cellular activities (AAA); AAA family proteins often ...
187-320 2.90e-55

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: 178.56  E-value: 2.90e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66805379   187 VLLYGPPGTGKTMLAKAVAHHTSAAFIRVVGSEFVQKYLGEGPRLVRDVFRLARENSPAIIFIDEIDAIATKRFDaqtGA 266
Cdd:pfam00004   1 LLLYGPPGTGKTTLAKAVAKELGAPFIEISGSELVSKYVGESEKRLRELFEAAKKLAPCVIFIDEIDALAGSRGS---GG 77
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 66805379   267 DREVQRILMELLNQMDGFDVSV-NVKVIMATNRQDTLDPALLrpGRLDRKIEFPL 320
Cdd:pfam00004  78 DSESRRVVNQLLTELDGFTSSNsKVIVIAATNRPDKLDPALL--GRFDRIIEFPL 130
COG1223 COG1223
Predicted ATPase, AAA+ superfamily [General function prediction only];
150-386 3.19e-54

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


Pssm-ID: 440836 [Multi-domain]  Cd Length: 246  Bit Score: 179.69  E-value: 3.19e-54
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66805379 150 SDIGGGDIQKQEMREAVElPLTHHNLYKQIGIDPPRGVLLYGPPGTGKTMLAKAVAHHTSAAFIRVVGSEFVQKYLGEGP 229
Cdd:COG1223   2 DDVVGQEEAKKKLKLIIK-ELRRRENLRKFGLWPPRKILFYGPPGTGKTMLAEALAGELKLPLLTVRLDSLIGSYLGETA 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66805379 230 RLVRDVFRLARENsPAIIFIDEIDAIATKRFDAQtgaDR-EVQRILMELLNQMDGFdvSVNVKVIMATNRQDTLDPALLR 308
Cdd:COG1223  81 RNLRKLFDFARRA-PCVIFFDEFDAIAKDRGDQN---DVgEVKRVVNALLQELDGL--PSGSVVIAATNHPELLDSALWR 154
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 66805379 309 pgRLDRKIEFPLPDRRQKRLIFQVITSKMNLSDEVDLEDYVSRPDKLSGAEIQSICQEAGMHAIRKNRYVILPKDFEK 386
Cdd:COG1223 155 --RFDEVIEFPLPDKEERKEILELNLKKFPLPFELDLKKLAKKLEGLSGADIEKVLKTALKKAILEDREKVTKEDLEE 230
RecA-like_NVL_r2-like cd19530
second of two ATPase domains of NVL (nuclear VCP-like protein) and similar ATPase domains; NVL ...
159-314 1.15e-51

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: 170.36  E-value: 1.15e-51
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66805379 159 KQEMREAVELPLTHHNLYKQIGIDPPRGVLLYGPPGTGKTMLAKAVAHHTSAAFIRVVGSEFVQKYLGEGPRLVRDVFRL 238
Cdd:cd19530   5 REELTMSILRPIKRPDIYKALGIDLPTGVLLYGPPGCGKTLLAKAVANESGANFISVKGPELLNKYVGESERAVRQVFQR 84
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 66805379 239 ARENSPAIIFIDEIDAIATKRFDAQTGAdreVQRILMELLNQMDGFDVSVNVKVIMATNRQDTLDPALLRPGRLDR 314
Cdd:cd19530  85 ARASAPCVIFFDEVDALVPKRGDGGSWA---SERVVNQLLTEMDGLEERSNVFVIAATNRPDIIDPAMLRPGRLDK 157
RecA-like_NVL_r1-like cd19518
first of two ATPase domains of NVL (nuclear VCP-like protein) and similar ATPase domains; NVL ...
151-316 3.90e-49

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


Pssm-ID: 410926 [Multi-domain]  Cd Length: 169  Bit Score: 164.11  E-value: 3.90e-49
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66805379 151 DIGGGDIQKQEMREAVELPLTHHNLYKQIGIDPPRGVLLYGPPGTGKTMLAKAVAHHTSAAFIRVVGSEFVQKYLGEGPR 230
Cdd:cd19518   1 DIGGMDSTLKELCELLIHPILPPEYFQHLGVEPPRGVLLHGPPGCGKTMLANAIAGELKVPFLKISATEIVSGVSGESEE 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66805379 231 LVRDVFRLARENSPAIIFIDEIDAIATKRFDAQTGADRevqRILMELLNQMDGF----DVSVNVKVIMATNRQDTLDPAL 306
Cdd:cd19518  81 KIRELFDQAISNAPCIVFIDEIDAITPKRESAQREMER---RIVSQLLTCMDELnnekTAGGPVLVIGATNRPDSLDPAL 157
                       170
                ....*....|
gi 66805379 307 LRPGRLDRKI 316
Cdd:cd19518 158 RRAGRFDREI 167
RecA-like_VPS4-like cd19509
ATPase domain of VPS4, ATAD1, K, KTNA1, Spastin, FIGL-1 and similar ATPase domains; This ...
152-316 8.20e-45

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: 152.51  E-value: 8.20e-45
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66805379 152 IGGGDIQKQEMREAVELPLTHHNLYKQIgIDPPRGVLLYGPPGTGKTMLAKAVAHHTSAAFIRVVGSEFVQKYLGEGPRL 231
Cdd:cd19509   1 IAGLDDAKEALKEAVILPSLRPDLFPGL-RGPPRGILLYGPPGTGKTLLARAVASESGSTFFSISASSLVSKWVGESEKI 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66805379 232 VRDVFRLARENSPAIIFIDEIDAIATKRFDAQTGADRevqRILMELLNQMDGFDVSVN--VKVIMATNRQDTLDPALLRp 309
Cdd:cd19509  80 VRALFALARELQPSIIFIDEIDSLLSERGSGEHEASR---RVKTEFLVQMDGVLNKPEdrVLVLGATNRPWELDEAFLR- 155

                ....*..
gi 66805379 310 gRLDRKI 316
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 ...
158-317 4.37e-44

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: 150.66  E-value: 4.37e-44
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66805379 158 QKQEMREAVELPLTHHNLYKQIGIDPPRGVLLYGPPGTGKTMLAKAVAHHTSAAFIRVVGSEFVQKYLGEGPRLVRDVFR 237
Cdd:cd19526   1 VKKALEETIEWPSKYPKIFASSPLRLRSGILLYGPPGCGKTLLASAIASECGLNFISVKGPELLNKYIGASEQNVRDLFS 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66805379 238 LARENSPAIIFIDEIDAIATKRFDAQTGAdreVQRILMELLNQMDGFDVSVNVKVIMATNRQDTLDPALLRPGRLDRKIE 317
Cdd:cd19526  81 RAQSAKPCILFFDEFDSIAPKRGHDSTGV---TDRVVNQLLTQLDGVEGLDGVYVLAATSRPDLIDPALLRPGRLDKLVY 157
RecA-like_VPS4 cd19521
ATPase domain of vacuolar protein sorting-associated protein 4; Vacuolar protein ...
144-316 4.99e-42

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


Pssm-ID: 410929 [Multi-domain]  Cd Length: 170  Bit Score: 145.39  E-value: 4.99e-42
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66805379 144 KPSESYSDIGGGDIQKQEMREAVELPLTHHNLYKQiGIDPPRGVLLYGPPGTGKTMLAKAVAHHTSAAFIRVVGSEFVQK 223
Cdd:cd19521   1 KPNVKWEDVAGLEGAKEALKEAVILPVKFPHLFTG-NRKPWSGILLYGPPGTGKSYLAKAVATEANSTFFSVSSSDLVSK 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66805379 224 YLGEGPRLVRDVFRLARENSPAIIFIDEIDAIATKRFDAQTGADRevqRILMELLNQMDGFDV-SVNVKVIMATNRQDTL 302
Cdd:cd19521  80 WMGESEKLVKQLFAMARENKPSIIFIDEVDSLCGTRGEGESEASR---RIKTELLVQMNGVGNdSQGVLVLGATNIPWQL 156
                       170
                ....*....|....
gi 66805379 303 DPALLRpgRLDRKI 316
Cdd:cd19521 157 DSAIRR--RFEKRI 168
RecA-like_Yta7-like cd19517
ATPase domain of Saccharomyces cerevisiae Yta7 and similar ATPase domains; Saccharomyces ...
151-318 9.11e-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: 144.96  E-value: 9.11e-42
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66805379 151 DIGGGDIQKQEMREAVELPLTHHNLYKQIGIDPPRGVLLYGPPGTGKTMLAKAVAHHTSA-----AFIRVVGSEFVQKYL 225
Cdd:cd19517   1 DIGGLSHYINQLKEMVFFPLLYPEVFAKFKITPPRGVLFHGPPGTGKTLMARALAAECSKggqkvSFFMRKGADCLSKWV 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66805379 226 GEGPRLVRDVFRLARENSPAIIFIDEIDAIATKRFDAQtgaDREVQRILMELLNQMDGFDVSVNVKVIMATNRQDTLDPA 305
Cdd:cd19517  81 GEAERQLRLLFEEAYRMQPSIIFFDEIDGLAPVRSSKQ---EQIHASIVSTLLALMDGLDNRGQVVVIGATNRPDALDPA 157
                       170
                ....*....|...
gi 66805379 306 LLRPGRLDRKIEF 318
Cdd:cd19517 158 LRRPGRFDREFYF 170
RecA-like_PEX6_r2 cd19527
second of two ATPase domains of Peroxisomal biogenesis factor 6 (PEX6); PEX6(also known as ...
159-314 4.66e-41

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: 142.65  E-value: 4.66e-41
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66805379 159 KQEMREAVELPLTHHNLYKQiGIDPPRGVLLYGPPGTGKTMLAKAVAHHTSAAFIRVVGSEFVQKYLGEGPRLVRDVFRL 238
Cdd:cd19527   2 KKEILDTIQLPLEHPELFSS-GLRKRSGILLYGPPGTGKTLLAKAIATECSLNFLSVKGPELINMYIGESEANVREVFQK 80
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 66805379 239 ARENSPAIIFIDEIDAIATKRfDAQTGADREVQRILMELLNQMDGF-DVSVNVKVIMATNRQDTLDPALLRPGRLDR 314
Cdd:cd19527  81 ARDAKPCVIFFDELDSLAPSR-GNSGDSGGVMDRVVSQLLAELDGMsSSGQDVFVIGATNRPDLLDPALLRPGRFDK 156
RecA-like_ATAD1 cd19520
ATPase domain of ATPase family AAA domain-containing protein 1 and similar ATPase domains; ...
151-308 9.57e-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: 136.79  E-value: 9.57e-39
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66805379 151 DIGGGDIQKQEMREAVELPLTHHNLYKQIGI-DPPRGVLLYGPPGTGKTMLAKAVAHHTSAAFIRVVGSEFVQKYLGEGP 229
Cdd:cd19520   1 DIGGLDEVITELKELVILPLQRPELFDNSRLlQPPKGVLLYGPPGCGKTMLAKATAKEAGARFINLQVSSLTDKWYGESQ 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66805379 230 RLVRDVFRLARENSPAIIFIDEIDAIATKRfdaqTGADREVQRIL-MELLNQMDGFDVSVNVKVIM--ATNRQDTLDPAL 306
Cdd:cd19520  81 KLVAAVFSLASKLQPSIIFIDEIDSFLRQR----SSTDHEATAMMkAEFMSLWDGLSTDGNCRVIVmgATNRPQDLDEAI 156

                ..
gi 66805379 307 LR 308
Cdd:cd19520 157 LR 158
RecA-like_spastin cd19524
ATPase domain of spastin; Spastin is an ATP-dependent microtubule-severing protein involved in ...
151-316 3.16e-38

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: 135.36  E-value: 3.16e-38
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66805379 151 DIGGGDIQKQEMREAVELPLTHHNLYKQIGIdPPRGVLLYGPPGTGKTMLAKAVAHHTSAAFIRVVGSEFVQKYLGEGPR 230
Cdd:cd19524   1 DIAGQDLAKQALQEMVILPSLRPELFTGLRA-PARGLLLFGPPGNGKTMLAKAVAAESNATFFNISAASLTSKYVGEGEK 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66805379 231 LVRDVFRLARENSPAIIFIDEIDAIATKRFDAQTGADRevqRILMELLNQMDGFDVSVN--VKVIMATNRQDTLDPALLR 308
Cdd:cd19524  80 LVRALFAVARELQPSIIFIDEVDSLLSERSEGEHEASR---RLKTEFLIEFDGVQSNGDdrVLVMGATNRPQELDDAVLR 156

                ....*...
gi 66805379 309 pgRLDRKI 316
Cdd:cd19524 157 --RFTKRV 162
RecA-like_Figl-1 cd19525
ATPase domain of Fidgetin-Like 1 (FIGL-1); FIGL-1 may participate in DNA repair in the nucleus; ...
142-316 3.54e-37

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: 133.19  E-value: 3.54e-37
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66805379 142 DEKPSESYSDIGGGDIQKQEMREAVELPLTHHNLYKQIGiDPPRGVLLYGPPGTGKTMLAKAVAHHTSAAFIRVVGSEFV 221
Cdd:cd19525  14 DHGPPINWADIAGLEFAKKTIKEIVVWPMLRPDIFTGLR-GPPKGILLFGPPGTGKTLIGKCIASQSGATFFSISASSLT 92
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66805379 222 QKYLGEGPRLVRDVFRLARENSPAIIFIDEIDAIATKRFDAQTGADRevqRILMELLNQMDGFDVSVNVKVIM--ATNRQ 299
Cdd:cd19525  93 SKWVGEGEKMVRALFSVARCKQPAVIFIDEIDSLLSQRGEGEHESSR---RIKTEFLVQLDGATTSSEDRILVvgATNRP 169
                       170
                ....*....|....*..
gi 66805379 300 DTLDPALLRpgRLDRKI 316
Cdd:cd19525 170 QEIDEAARR--RLVKRL 184
RecA-like_KTNA1 cd19522
Katanin p60 ATPase-containing subunit A1; Katanin p60 ATPase-containing subunit A1 (KTNA1) is ...
151-316 1.06e-35

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: 128.95  E-value: 1.06e-35
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66805379 151 DIGGGDIQKQEMREAVELPLTHHNLYKqiGIDPP-RGVLLYGPPGTGKTMLAKAVAHHTSAAFIRVVGSEFVQKYLGEGP 229
Cdd:cd19522   1 DIADLEEAKKLLEEAVVLPMWMPEFFK--GIRRPwKGVLMVGPPGTGKTLLAKAVATECGTTFFNVSSSTLTSKYRGESE 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66805379 230 RLVRDVFRLARENSPAIIFIDEIDAIATKRfdaQTGADREV-QRILMELLNQMDGF-------DVSVNVKVIMATNRQDT 301
Cdd:cd19522  79 KLVRLLFEMARFYAPTTIFIDEIDSICSRR---GTSEEHEAsRRVKSELLVQMDGVggasendDPSKMVMVLAATNFPWD 155
                       170
                ....*....|....*
gi 66805379 302 LDPALLRpgRLDRKI 316
Cdd:cd19522 156 IDEALRR--RLEKRI 168
RecA-like_NSF-SEC18_r1-like cd19504
first of two ATPase domains of NSF and SEC18, and similar ATPase domains; ...
152-317 6.45e-29

first of two ATPase domains of NSF and SEC18, and similar ATPase domains; N-ethylmaleimide-sensitive factor (NSF) and Saccharomyces cerevisiae Vesicular-fusion protein Sec18, key factors for eukaryotic trafficking, are ATPases and SNARE disassembly chaperones. NSF/Sec18 activate or prime SNAREs, the terminal catalysts of membrane fusion. Sec18/NSF associates with SNARE complexes through binding Sec17/alpha-SNAP. Sec18 has an N-terminal cap domain and two nucleotide-binding domains (D1 and D2) which form the two rings of the hexameric complex. The hydrolysis of ATP by D1 generates most of the energy necessary to disassemble inactive SNARE bundles, while the D2 ring binds ATP to stabilize the homohexamer. This subfamily includes the first (D1) ATPase domain of NSF/Sec18, and belongs to the RecA-like NTPase family which includes the NTP binding domain of F1 and V1 H(+)ATPases, DnaB and related helicases as well as bacterial RecA and related eukaryotic and archaeal recombinases. The RecA-like NTPase family also includes bacterial conjugation proteins and related DNA transfer proteins involved in type II and type IV secretion.


Pssm-ID: 410912 [Multi-domain]  Cd Length: 177  Bit Score: 111.04  E-value: 6.45e-29
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66805379 152 IGGGDIQKQEM-REAVELPLTHHNLYKQIGIDPPRGVLLYGPPGTGKTMLAKAVAHHTSAAFIRVV-GSEFVQKYLGEGP 229
Cdd:cd19504   2 IGGLDKEFSDIfRRAFASRVFPPEIVEQLGCKHVKGILLYGPPGTGKTLMARQIGKMLNAREPKIVnGPEILNKYVGESE 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66805379 230 RLVRDVFRLARENSPA--------IIFIDEIDAIATKRfdAQTGADREV-QRILMELLNQMDGFDVSVNVKVIMATNRQD 300
Cdd:cd19504  82 ANIRKLFADAEEEQRRlgansglhIIIFDEIDAICKQR--GSMAGSTGVhDTVVNQLLSKIDGVEQLNNILVIGMTNRKD 159
                       170
                ....*....|....*..
gi 66805379 301 TLDPALLRPGRLDRKIE 317
Cdd:cd19504 160 LIDEALLRPGRLEVQME 176
RecA-like_fidgetin cd19523
ATPase domain of fidgetin; Fidgetin (FIGN) is a ATP-dependent microtubule severing protein. ...
151-308 4.89e-27

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: 105.35  E-value: 4.89e-27
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66805379 151 DIGGGDIQKQEMREAVELPLTHHNLYKQIgIDPPRGVLLYGPPGTGKTMLAKAVAHHTSAAFIRVVGSEFVQKYLGEGPR 230
Cdd:cd19523   1 DIAGLGALKAAIKEEVLWPLLRPDAFSGL-LRLPRSILLFGPRGTGKTLLGRCLASQLGATFLRLRGSTLVAKWAGEGEK 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66805379 231 LVRDVFRLARENSPAIIFIDEIDAIATKRFDAQTgadrEVQRILMELLNQMDGFDVSV--NVKVIMATNRQDTLDPALLR 308
Cdd:cd19523  80 ILQASFLAARCRQPSVLFISDLDALLSSQDDEAS----PVGRLQVELLAQLDGVLGSGedGVLVVCTTSKPEEIDESLRR 155
AAA cd00009
The AAA+ (ATPases Associated with a wide variety of cellular Activities) superfamily ...
153-320 1.45e-26

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: 103.77  E-value: 1.45e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66805379 153 GGGDIQKQEMREAVELPlthhnlykqigidPPRGVLLYGPPGTGKTMLAKAVAHHT---SAAFIRVVGSEFVQKYLGE-- 227
Cdd:cd00009   1 VGQEEAIEALREALELP-------------PPKNLLLYGPPGTGKTTLARAIANELfrpGAPFLYLNASDLLEGLVVAel 67
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66805379 228 -GPRLVRDVFRLARENSPAIIFIDEIDAIAtkrfdaqtgadREVQRILMELLNQ-MDGFDVSVNVKVIMATNRQDTLDPA 305
Cdd:cd00009  68 fGHFLVRLLFELAEKAKPGVLFIDEIDSLS-----------RGAQNALLRVLETlNDLRIDRENVRVIGATNRPLLGDLD 136
                       170
                ....*....|....*
gi 66805379 306 LLRPGRLDRKIEFPL 320
Cdd:cd00009 137 RALYDRLDIRIVIPL 151
AAA smart00382
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ...
183-322 2.25e-20

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


Pssm-ID: 214640 [Multi-domain]  Cd Length: 148  Bit Score: 87.04  E-value: 2.25e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66805379    183 PPRGVLLYGPPGTGKTMLAKAVAHH---TSAAFIRVVGSEF--------------VQKYLGEGPRLVRDVFRLARENSPA 245
Cdd:smart00382   1 PGEVILIVGPPGSGKTTLARALARElgpPGGGVIYIDGEDIleevldqllliivgGKKASGSGELRLRLALALARKLKPD 80
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 66805379    246 IIFIDEIDAIATKRFdaqtgadrEVQRILMELLNQMDGFDVSVNVKVIMATNRQDTLDPALLRPgRLDRKIEFPLPD 322
Cdd:smart00382  81 VLILDEITSLLDAEQ--------EALLLLLEELRLLLLLKSEKNLTVILTTNDEKDLGPALLRR-RFDRRIVLLLIL 148
RecA-like_Ycf46-like cd19507
ATPase domain of Ycf46 and similar ATPase domains; Ycf46 may play a role in the regulation of ...
180-314 3.45e-20

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: 86.65  E-value: 3.45e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66805379 180 GIDPPRGVLLYGPPGTGKTMLAKAVAHHTSAAFIRVVGSEFVQKYLGEGPRLVRDVFRLARENSPAIIFIDEID-AIATK 258
Cdd:cd19507  27 GLPTPKGLLLVGIQGTGKSLTAKAIAGVWQLPLLRLDMGRLFGGLVGESESRLRQMIQTAEAIAPCVLWIDEIEkGFSNA 106
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 66805379 259 RFDAQTGADRevqRILMELLNQMDgfDVSVNVKVIMATNRQDTLDPALLRPGRLDR 314
Cdd:cd19507 107 DSKGDSGTSS---RVLGTFLTWLQ--EKKKPVFVVATANNVQSLPPELLRKGRFDE 157
ycf46 CHL00195
Ycf46; Provisional
145-376 1.75e-17

Ycf46; Provisional


Pssm-ID: 177094 [Multi-domain]  Cd Length: 489  Bit Score: 83.92  E-value: 1.75e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66805379  145 PSESYSDIGGGDIQKQEMREAVElplthhNLYKQ---IGIDPPRGVLLYGPPGTGKTMLAKAVAHHTSAAFIRV-VGSEF 220
Cdd:CHL00195 223 VNEKISDIGGLDNLKDWLKKRST------SFSKQasnYGLPTPRGLLLVGIQGTGKSLTAKAIANDWQLPLLRLdVGKLF 296
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66805379  221 vQKYLGEGPRLVRDVFRLARENSPAIIFIDEID-AIATKRFDAQTGADREVQRILMELLNQMdgfdvSVNVKVIMATNRQ 299
Cdd:CHL00195 297 -GGIVGESESRMRQMIRIAEALSPCILWIDEIDkAFSNSESKGDSGTTNRVLATFITWLSEK-----KSPVFVVATANNI 370
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66805379  300 DTLDPALLRPGRLDRKIEFPLPDRRQKRLIFQVITSKM--NLSDEVDLEDYVSRPDKLSGAEI-QSICqEAGMHAIRKNR 376
Cdd:CHL00195 371 DLLPLEILRKGRFDEIFFLDLPSLEEREKIFKIHLQKFrpKSWKKYDIKKLSKLSNKFSGAEIeQSII-EAMYIAFYEKR 449
RecA-like_BCS1 cd19510
Mitochondrial chaperone BCS1; Mitochondrial chaperone BCS1 is necessary for the assembly of ...
176-318 5.90e-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: 77.39  E-value: 5.90e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66805379 176 YKQIGIDPPRGVLLYGPPGTGKTMLAKAVAHHTSAAFIRVVGSEFVqkylgegprLVRDVFRLARENSP--AIIFIDEID 253
Cdd:cd19510  15 YNDRGIPYRRGYLLYGPPGTGKSSFIAALAGELDYDICDLNLSEVV---------LTDDRLNHLLNTAPkqSIILLEDID 85
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 66805379 254 -AIATKRFDAQTGADRE-VQRI-LMELLNQMDGFDVSVNVKVIMATNRQDTLDPALLRPGRLDRKIEF 318
Cdd:cd19510  86 aAFESREHNKKNPSAYGgLSRVtFSGLLNALDGVASSEERIVFMTTNHIERLDPALIRPGRVDMKIYM 153
RecA-like_Pch2-like cd19508
ATPase domain of Pachytene checkpoint 2 (Pch2) and similar ATPase domains; Pch2 (known as ...
185-306 1.11e-12

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: 66.32  E-value: 1.11e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66805379 185 RGVLLYGPPGTGKTMLAKAVAHHTS---------AAFIRVVGSEFVQKYLGEGPRLVRDVFRLARE---NSPAIIF--ID 250
Cdd:cd19508  53 RLVLLHGPPGTGKTSLCKALAQKLSirlssryryGQLIEINSHSLFSKWFSESGKLVTKMFQKIQElidDKDALVFvlID 132
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 66805379 251 EIDAIATKRFDAQTGAD-REVQRILMELLNQMDGFDVSVNVKVIMATNRQDTLDPAL 306
Cdd:cd19508 133 EVESLAAARSASSSGTEpSDAIRVVNAVLTQIDRIKRYHNNVILLTSNLLEKIDVAF 189
RecA-like_ATAD3-like cd19512
ATPase domains of ATPase AAA-domain protein 3A (ATAD3A), -3B, and -3C, and similar ATPase ...
185-318 2.68e-12

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: 64.08  E-value: 2.68e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66805379 185 RGVLLYGPPGTGKTMLAKAVAHHTSAAFIRVVGSEfVQKYLGEGPRLVRDVFRLA-RENSPAIIFIDEIDAIATKRfdAQ 263
Cdd:cd19512  23 RNILFYGPPGTGKTLFAKKLALHSGMDYAIMTGGD-VAPMGREGVTAIHKVFDWAnTSRRGLLLFVDEADAFLRKR--ST 99
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*
gi 66805379 264 TGADREVQRILMELLNQMDgfDVSVNVKVIMATNRQDTLDPALlrPGRLDRKIEF 318
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; ...
178-318 3.29e-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: 64.32  E-value: 3.29e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66805379 178 QIGIDPPRGVLLYGPPGTGKTMLAKAVAHHTSAAFIRVVGSEFVQK--------------YLGEGPRLVRDVFRLARENS 243
Cdd:cd19505   6 RLGLSPSKGILLIGSIETGRSYLIKSLAANSYVPLIRISLNKLLYNkpdfgnddwidgmlILKESLHRLNLQFELAKAMS 85
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 66805379 244 PAIIFIDEIDAIATKRFDAQTGADREVqrILMELLN--QMDGFDVSV-NVKVIMATNRQDTLDPALLRPGRLDRKIEF 318
Cdd:cd19505  86 PCIIWIPNIHELNVNRSTQNLEEDPKL--LLGLLLNylSRDFEKSSTrNILVIASTHIPQKVDPALIAPNRLDTCINI 161
AAA_5 pfam07728
AAA domain (dynein-related subfamily); This Pfam entry includes some of the AAA proteins not ...
186-308 4.23e-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: 60.38  E-value: 4.23e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66805379   186 GVLLYGPPGTGKTMLAKAVAHHTSAAFIRVV-------GSEFVQKYL--GEGPRLVRDVF-RLAREnsPAIIFIDEIDAi 255
Cdd:pfam07728   1 GVLLVGPPGTGKTELAERLAAALSNRPVFYVqltrdttEEDLFGRRNidPGGASWVDGPLvRAARE--GEIAVLDEINR- 77
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 66805379   256 atkrfdaqtgADREVQRILMELLN-----QMDGFDVSV----NVKVIMATNRQDT----LDPALLR 308
Cdd:pfam07728  78 ----------ANPDVLNSLLSLLDerrllLPDGGELVKaapdGFRLIATMNPLDRglneLSPALRS 133
RecA-like_HslU cd19498
ATP-dependent protease ATPase subunit HslU; HslU is a component of the ATP-dependent protease ...
184-278 6.58e-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: 60.86  E-value: 6.58e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66805379 184 PRGVLLYGPPGTGKTMLAKAVAHHTSAAFIRVVGSEFVQ-KYLGegprlvRDVFRLARENSPAIIFIDEIDAIATKRFDA 262
Cdd:cd19498  46 PKNILMIGPTGVGKTEIARRLAKLAGAPFIKVEATKFTEvGYVG------RDVESIIRDLVEGIVFIDEIDKIAKRGGSS 119
                        90
                ....*....|....*..
gi 66805379 263 QTGADRE-VQRILMELL 278
Cdd:cd19498 120 GPDVSREgVQRDLLPIV 136
RecA-like_ClpB_Hsp104-like cd19499
Chaperone protein ClpB/Hsp104 subfamily; Bacterial Caseinolytic peptidase B (ClpB) and ...
184-318 1.12e-10

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: 60.27  E-value: 1.12e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66805379 184 PRGVLLY-GPPGTGKTMLAKAVA---HHTSAAFIRVVGSEFVQK------------YLG--EGPRLVRDVfrlaRENSPA 245
Cdd:cd19499  40 PIGSFLFlGPTGVGKTELAKALAellFGDEDNLIRIDMSEYMEKhsvsrligappgYVGytEGGQLTEAV----RRKPYS 115
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 66805379 246 IIFIDEIDAiatkrfdaqtgADREVQRILMEL-----LNQMDGFDVSV-NVKVIMATNrqdTLDPALLrpGRLDRKIEF 318
Cdd:cd19499 116 VVLLDEIEK-----------AHPDVQNLLLQVlddgrLTDSHGRTVDFkNTIIIMTSN---HFRPEFL--NRIDEIVVF 178
RarA COG2256
Replication-associated recombination protein RarA (DNA-dependent ATPase) [Replication, ...
175-252 3.53e-09

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


Pssm-ID: 441857 [Multi-domain]  Cd Length: 439  Bit Score: 58.14  E-value: 3.53e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66805379 175 LYKQIGIDPPRGVLLYGPPGTGKTMLAKAVAHHTSAAFIRV--VGSefvqkylgeGPRLVRDVFRLARENS----PAIIF 248
Cdd:COG2256  40 LRRAIEAGRLSSMILWGPPGTGKTTLARLIANATDAEFVALsaVTS---------GVKDIREVIEEARERRaygrRTILF 110

                ....
gi 66805379 249 IDEI 252
Cdd:COG2256 111 VDEI 114
AAA_lid_3 pfam17862
AAA+ lid domain; This entry represents the alpha helical AAA+ lid domain that is found to the ...
342-386 4.23e-09

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: 51.77  E-value: 4.23e-09
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 66805379   342 EVDLEDYVSRPDKLSGAEIQSICQEAGMHAIRKNRYVILPKDFEK 386
Cdd:pfam17862   1 DVDLEELAERTEGFSGADLEALCREAALAALRRGLEAVTQEDLEE 45
Prot_ATP_ID_OB pfam16450
Proteasomal ATPase OB C-terminal domain; This is the interdomain (ID) or oligonucleotide ...
74-129 4.88e-09

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


Pssm-ID: 465118 [Multi-domain]  Cd Length: 56  Bit Score: 52.12  E-value: 4.88e-09
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 66805379    74 IGQLLEMVDSNTGIVQSTSGSTLCVRILSTIDRELLKPSASVALQRHSNALVDTLP 129
Cdd:pfam16450   1 VATVVEVLDDGRALVKSSGGEERVVRLAGSLDEEKLRPGDRVLLDPRSGYALEVLP 56
AAA_2 pfam07724
AAA domain (Cdc48 subfamily); This Pfam entry includes some of the AAA proteins not detected ...
187-329 8.25e-09

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: 54.51  E-value: 8.25e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66805379   187 VLLYGPPGTGKTMLAKAVA---HHTSAAFIRVVGSEFVQKYL--------------GEGPRLVRDVfrlaRENSPAIIFI 249
Cdd:pfam07724   6 FLFLGPTGVGKTELAKALAellFGDERALIRIDMSEYMEEHSvsrligappgyvgyEEGGQLTEAV----RRKPYSIVLI 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66805379   250 DEIDAIAtkrfdaqtgadREVQRILMELLNQ---MDGFDVSVNVK---VIMATNR--QDTLDPALLRPGRLDRKIEFPLP 321
Cdd:pfam07724  82 DEIEKAH-----------PGVQNDLLQILEGgtlTDKQGRTVDFKntlFIMTGNFgsEKISDASRLGDSPDYELLKEEVM 150

                  ....*...
gi 66805379   322 DRRQKRLI 329
Cdd:pfam07724 151 DLLKKGFI 158
PRK13342 PRK13342
recombination factor protein RarA; Reviewed
175-252 1.16e-08

recombination factor protein RarA; Reviewed


Pssm-ID: 237355 [Multi-domain]  Cd Length: 413  Bit Score: 56.63  E-value: 1.16e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66805379  175 LYKQIGIDPPRGVLLYGPPGTGKTMLAKAVAHHTSAAFIRVVGSEF-VQKylgegprlVRDVFRLARENSPA----IIFI 249
Cdd:PRK13342  27 LRRMIEAGRLSSMILWGPPGTGKTTLARIIAGATDAPFEALSAVTSgVKD--------LREVIEEARQRRSAgrrtILFI 98

                 ...
gi 66805379  250 DEI 252
Cdd:PRK13342  99 DEI 101
MoxR COG0714
MoxR-like ATPase [General function prediction only]; MoxR-like ATPase is part of the Pathway ...
187-253 4.04e-08

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: 54.40  E-value: 4.04e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66805379 187 VLLYGPPGTGKTMLAKAVAHHTSAAFIRV-----------VGSE-FVQK----YLGEGPrlvrdVFRlarenspAIIFID 250
Cdd:COG0714  34 LLLEGVPGVGKTTLAKALARALGLPFIRIqftpdllpsdiLGTYiYDQQtgefEFRPGP-----LFA-------NVLLAD 101

                ...
gi 66805379 251 EID 253
Cdd:COG0714 102 EIN 104
CDC6 COG1474
Cdc6-related protein, AAA superfamily ATPase [Replication, recombination and repair];
182-319 4.81e-07

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


Pssm-ID: 441083 [Multi-domain]  Cd Length: 389  Bit Score: 51.39  E-value: 4.81e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66805379 182 DPPRGVLLYGPPGTGKTMLAKAVAHH---------TSAAFIRV----------VGSEFVQKyLGEGPRLVR------DVF 236
Cdd:COG1474  49 ERPSNVLIYGPTGTGKTAVAKYVLEEleeeaeergVDVRVVYVncrqastryrVLSRILEE-LGSGEDIPStglstdELF 127
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66805379 237 -----RLARENSPAIIFIDEIDAIatkrfdaqtgADREVQRILMELLNQMDGFDvSVNVKVIMATNRQ---DTLDPALLR 308
Cdd:COG1474 128 drlyeALDERDGVLVVVLDEIDYL----------VDDEGDDLLYQLLRANEELE-GARVGVIGISNDLeflENLDPRVKS 196
                       170
                ....*....|..
gi 66805379 309 pgRL-DRKIEFP 319
Cdd:COG1474 197 --SLgEEEIVFP 206
44 PHA02544
clamp loader, small subunit; Provisional
188-326 3.22e-06

clamp loader, small subunit; Provisional


Pssm-ID: 222866 [Multi-domain]  Cd Length: 316  Bit Score: 48.45  E-value: 3.22e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66805379  188 LLYGP-PGTGKTMLAKAVAHHTSAAFIRVVGS----EFVQkylGEGPRLVRDVfrlARENSPAIIFIDEIDAIATKrfda 262
Cdd:PHA02544  46 LLHSPsPGTGKTTVAKALCNEVGAEVLFVNGSdcriDFVR---NRLTRFASTV---SLTGGGKVIIIDEFDRLGLA---- 115
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 66805379  263 qtgadrEVQRILMELLNQmdgfdVSVNVKVIMATNRQDTLDPALLrpGRLdRKIEFPLPDRRQK 326
Cdd:PHA02544 116 ------DAQRHLRSFMEA-----YSKNCSFIITANNKNGIIEPLR--SRC-RVIDFGVPTKEEQ 165
ycf2 CHL00206
Ycf2; Provisional
178-283 7.84e-06

Ycf2; Provisional


Pssm-ID: 214396 [Multi-domain]  Cd Length: 2281  Bit Score: 48.37  E-value: 7.84e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66805379   178 QIGIDPPRGVLLYGPPGTGKTMLAKAVAHHTSAAFIRVvgseFVQKYLgegprlvrdvfrlarENSPAIIFIDEIDAIAT 257
Cdd:CHL00206 1624 RLALSPSRGILVIGSIGTGRSYLVKYLATNSYVPFITV----FLNKFL---------------DNKPKGFLIDDIDIDDS 1684
                          90       100
                  ....*....|....*....|....*.
gi 66805379   258 KRFDAQTGADREVQRILMELLNQMDG 283
Cdd:CHL00206 1685 DDIDDSDDIDRDLDTELLTMMNALTM 1710
DnaC COG1484
DNA replication protein DnaC [Replication, recombination and repair];
181-280 2.29e-05

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


Pssm-ID: 441093 [Multi-domain]  Cd Length: 242  Bit Score: 45.54  E-value: 2.29e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66805379 181 IDPPRGVLLYGPPGTGKTMLAKAVAHH-----TSAAFIRVvgSEFVQKY---LGEGpRLVRDVFRLARensPAIIFIDEi 252
Cdd:COG1484  96 IERGENLILLGPPGTGKTHLAIALGHEacragYRVRFTTA--PDLVNELkeaRADG-RLERLLKRLAK---VDLLILDE- 168
                        90       100
                ....*....|....*....|....*...
gi 66805379 253 daIATKRFDAQTGADrevqriLMELLNQ 280
Cdd:COG1484 169 --LGYLPLDAEGAEL------LFELISD 188
RecA-like_superfamily cd01120
RecA-like_NTPases; RecA-like NTPases. This superfamily includes the NTP binding domain of F1 ...
187-278 3.05e-05

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


Pssm-ID: 410865 [Multi-domain]  Cd Length: 119  Bit Score: 43.26  E-value: 3.05e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66805379 187 VLLYGPPGTGKTMLAKAVAHHTSAAFIRVVGSEFVQKYLgegprlvRDVFRLARENSPAIIFIDEIDAIATKRfdaQTGA 266
Cdd:cd01120   1 ILITGPPGSGKTTLLLQFAEQALLSDEPVIFISFLDTIL-------EAIEDLIEEKKLDIIIIDSLSSLARAS---QGDR 70
                        90
                ....*....|..
gi 66805379 267 DREVQRILMELL 278
Cdd:cd01120  71 SSELLEDLAKLL 82
RecA-like_IQCA1 cd19506
ATPase domain of IQ and AAA domain-containing protein 1 (IQCA1); IQCA1 (also known as dynein ...
185-251 3.10e-05

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


Pssm-ID: 410914 [Multi-domain]  Cd Length: 160  Bit Score: 44.06  E-value: 3.10e-05
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 66805379 185 RGVLLYGPPGTGKTMLAKAVAHHTSAAFIRVVGSEFVQKYLGEG--PRLVRDVFRLARENSPAIIFIDE 251
Cdd:cd19506  27 KSLLLAGPSGVGKKMLVHAICTETGANLFNLSPSNIAGKYPGKNglQMMLHLVLKVARQLQPSVIWIGD 95
McrB COG1401
5-methylcytosine-specific restriction endonuclease McrBC, GTP-binding regulatory subunit McrB ...
187-252 3.23e-05

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


Pssm-ID: 441011 [Multi-domain]  Cd Length: 477  Bit Score: 45.92  E-value: 3.23e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66805379 187 VLLYGPPGTGKTMLAKAVAHHTSAA---FIRVV-------GSEFVQKY---LGEG-----PRLVRDVFRLARENS--PAI 246
Cdd:COG1401 224 VILAGPPGTGKTYLARRLAEALGGEdngRIEFVqfhpswsYEDFLLGYrpsLDEGkyeptPGIFLRFCLKAEKNPdkPYV 303

                ....*.
gi 66805379 247 IFIDEI 252
Cdd:COG1401 304 LIIDEI 309
DUF815 pfam05673
Protein of unknown function (DUF815); This family consists of several bacterial proteins of ...
187-250 4.75e-05

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


Pssm-ID: 428578 [Multi-domain]  Cd Length: 250  Bit Score: 44.45  E-value: 4.75e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 66805379   187 VLLYGPPGTGKTMLAKAVAHHTSAAFIRVVgsEFVQKYLGEGPRLVRdvfRLARENSPAIIFID 250
Cdd:pfam05673  56 VLLWGARGTGKSSLVKALLNEYADQGLRLI--EVDKEDLGDLPDLVD---LLRDRPYRFILFCD 114
PRK04195 PRK04195
replication factor C large subunit; Provisional
183-274 5.08e-05

replication factor C large subunit; Provisional


Pssm-ID: 235250 [Multi-domain]  Cd Length: 482  Bit Score: 45.30  E-value: 5.08e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66805379  183 PPRGVLLYGPPGTGKTMLAKAVAH--------------HTSAAFIRVVGSEFVQKYLGEGPRlvrdvfrlarenspAIIF 248
Cdd:PRK04195  38 PKKALLLYGPPGVGKTSLAHALANdygwevielnasdqRTADVIERVAGEAATSGSLFGARR--------------KLIL 103
                         90       100
                 ....*....|....*....|....*.
gi 66805379  249 IDEIDAIATKrfdAQTGADREVQRIL 274
Cdd:PRK04195 104 LDEVDGIHGN---EDRGGARAILELI 126
COG2842 COG2842
Bacteriophage DNA transposition protein, AAA+ family ATPase [Mobilome: prophages, transposons]; ...
187-253 6.98e-05

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


Pssm-ID: 442090 [Multi-domain]  Cd Length: 254  Bit Score: 44.17  E-value: 6.98e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66805379 187 VLLYGPPGTGKTMLAKAVA-HHTSAAFIRVVGS----EFVQK---YLG--EGPRLVRDVFRLARE---NSPAIIFIDEID 253
Cdd:COG2842  53 GVVYGESGVGKTTAAREYAnRNPNVIYVTASPSwtskELLEElaeELGipAPPGTIADLRDRILErlaGTGRLLIIDEAD 132
PRK13341 PRK13341
AAA family ATPase;
188-252 7.15e-05

AAA family ATPase;


Pssm-ID: 237354 [Multi-domain]  Cd Length: 725  Bit Score: 45.05  E-value: 7.15e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 66805379  188 LLYGPPGTGKTMLAKAVAHHTSAAFIR----VVGSEFVQKYLGEGPRlvrdvfRLARENSPAIIFIDEI 252
Cdd:PRK13341  56 ILYGPPGVGKTTLARIIANHTRAHFSSlnavLAGVKDLRAEVDRAKE------RLERHGKRTILFIDEV 118
ruvB TIGR00635
Holliday junction DNA helicase, RuvB subunit; All proteins in this family for which functions ...
187-362 8.37e-05

Holliday junction DNA helicase, RuvB subunit; All proteins in this family for which functions are known are 5'-3' DNA helicases that, as part of a complex with RuvA homologs serve as a 5'-3' Holliday junction helicase. RuvA specifically binds Holliday junctions as a sandwich of two tetramers and maintains the configuration of the junction. It forms a complex with two hexameric rings of RuvB, the subunit that contains helicase activity. The complex drives ATP-dependent branch migration of the Holliday junction recombination intermediate. The endonuclease RuvC resolves junctions. [DNA metabolism, DNA replication, recombination, and repair]


Pssm-ID: 129721 [Multi-domain]  Cd Length: 305  Bit Score: 44.21  E-value: 8.37e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66805379   187 VLLYGPPGTGKTMLAKAVAHHTSAAfIRVVGSEFVQKylgegPRLVRDVFRLARENSpaIIFIDEIDAIAtkrfdaqtga 266
Cdd:TIGR00635  33 LLLYGPPGLGKTTLAHIIANEMGVN-LKITSGPALEK-----PGDLAAILTNLEEGD--VLFIDEIHRLS---------- 94
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66805379   267 drevqRILMELL-NQMDGFDVSV------NVKVIMATNRQDTLDPALLRPGrldrKIEFPLPDRrqkrliFQvITSKMNL 339
Cdd:TIGR00635  95 -----PAVEELLyPAMEDFRLDIvigkgpSARSVRLDLPPFTLVGATTRAG----MLTSPLRDR------FG-IILRLEF 158
                         170       180
                  ....*....|....*....|...
gi 66805379   340 SDEVDLEDYVSRPDKLSGAEIQS 362
Cdd:TIGR00635 159 YTVEELAEIVSRSAGLLNVEIEP 181
AAA_16 pfam13191
AAA ATPase domain; This family of domains contain a P-loop motif that is characteriztic of the ...
173-281 1.18e-04

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: 42.49  E-value: 1.18e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66805379   173 HNLYKQIGIDPPRGVLLYGPPGTGKTMLAKAVAHHTSAAFIRVVGSEFVQ--KYLGEGPRLVRDVFRLARENSPAIIFID 250
Cdd:pfam13191  13 LDALDRVRSGRPPSVLLTGEAGTGKTTLLRELLRALERDGGYFLRGKCDEnlPYSPLLEALTREGLLRQLLDELESSLLE 92
                          90       100       110
                  ....*....|....*....|....*....|.
gi 66805379   251 EIDAIATKRFDAQTGADREVQRILMELLNQM 281
Cdd:pfam13191  93 AWRAALLEALAPVPELPGDLAERLLDLLLRL 123
ruvB PRK00080
Holliday junction branch migration DNA helicase RuvB;
187-252 2.25e-04

Holliday junction branch migration DNA helicase RuvB;


Pssm-ID: 234619 [Multi-domain]  Cd Length: 328  Bit Score: 42.81  E-value: 2.25e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 66805379  187 VLLYGPPGTGKTMLAKAVAHHTSAAfIRVVgsefvqkylgEGPRLVR--DvfrLA------RENSpaIIFIDEI 252
Cdd:PRK00080  54 VLLYGPPGLGKTTLANIIANEMGVN-IRIT----------SGPALEKpgD---LAailtnlEEGD--VLFIDEI 111
RecA-like_Lon cd19500
lon protease homolog 2 peroxisomal; Lon protease (also known as Lon peptidase) is an ...
188-307 2.69e-04

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


Pssm-ID: 410908 [Multi-domain]  Cd Length: 182  Bit Score: 41.39  E-value: 2.69e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66805379 188 LLYGPPGTGKTMLAKAVAHHTSAAFIRV-VG-----SEFV---QKYLGEGPRLVRDVFRLARENSPaIIFIDEIDAIATK 258
Cdd:cd19500  41 CLVGPPGVGKTSLGKSIARALGRKFVRIsLGgvrdeAEIRghrRTYVGAMPGRIIQALKKAGTNNP-VFLLDEIDKIGSS 119
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 66805379 259 RFDAQTGAdrevqriLMELLN--QMDGF---------DVSvNVKVIMATNRQDTLDPALL 307
Cdd:cd19500 120 FRGDPASA-------LLEVLDpeQNSTFsdhyldvpfDLS-KVLFIATANSLDTIPGPLL 171
YifB COG0606
Predicted Mg-chelatase, contains ChlI-like and ATPase domains, YifB family [Posttranslational ...
172-202 3.17e-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: 42.72  E-value: 3.17e-04
                        10        20        30
                ....*....|....*....|....*....|.
gi 66805379 172 HHNLykqigidpprgvLLYGPPGTGKTMLAK 202
Cdd:COG0606 211 GHNL------------LMIGPPGSGKTMLAR 229
Mg_chelatase pfam01078
Magnesium chelatase, subunit ChlI; Magnesium-chelatase is a three-component enzyme that ...
187-203 5.44e-04

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: 40.98  E-value: 5.44e-04
                          10
                  ....*....|....*..
gi 66805379   187 VLLYGPPGTGKTMLAKA 203
Cdd:pfam01078  25 LLMIGPPGSGKTMLAKR 41
TIP49 COG1224
DNA helicase TIP49, TBP-interacting protein [Transcription];
134-220 6.14e-04

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


Pssm-ID: 440837 [Multi-domain]  Cd Length: 452  Bit Score: 41.88  E-value: 6.14e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66805379 134 SSIHLLGADEKPSESysDIGGGDIQKQEMREAVELPLthhNLYKQiGIDPPRGVLLYGPPGTGKTMLAKAVAHHTSA--A 211
Cdd:COG1224  20 SHIRGLGLDENGKAK--FVADGLVGQVEAREAAGIVV---KMIKE-GKMAGKGILIVGPPGTGKTALAVAIARELGEdtP 93

                ....*....
gi 66805379 212 FIRVVGSEF 220
Cdd:COG1224  94 FVAISGSEI 102
PRK08116 PRK08116
hypothetical protein; Validated
185-216 7.32e-04

hypothetical protein; Validated


Pssm-ID: 236153 [Multi-domain]  Cd Length: 268  Bit Score: 41.16  E-value: 7.32e-04
                         10        20        30
                 ....*....|....*....|....*....|..
gi 66805379  185 RGVLLYGPPGTGKTMLAKAVAHHTSAAFIRVV 216
Cdd:PRK08116 115 VGLLLWGSVGTGKTYLAACIANELIEKGVPVI 146
IS21_help_AAA NF038214
IS21-like element helper ATPase IstB; This protein family model resembles PF01695, but was ...
187-252 1.02e-03

IS21-like element helper ATPase IstB; This protein family model resembles PF01695, but was built to hit full-length AAA+ ATPases of IS21 family IS (insertion sequence) elements.


Pssm-ID: 439516  Cd Length: 232  Bit Score: 40.15  E-value: 1.02e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 66805379  187 VLLYGPPGTGKTMLA-----KAVAHHTSAAFIRVvgSEFVQKYL---GEGpRLVRDVFRLARensPAIIFIDEI 252
Cdd:NF038214  93 VLLLGPPGTGKTHLAialgyAACRQGYRVRFTTA--ADLVEQLAqarADG-RLGRLLRRLAR---YDLLIIDEL 160
Parvo_NS1 pfam01057
Parvovirus non-structural protein NS1; This family also contains the NS2 protein. Parvoviruses ...
177-206 1.21e-03

Parvovirus non-structural protein NS1; This family also contains the NS2 protein. Parvoviruses encode two non-structural proteins, NS1 and NS2. The mRNA for NS2 contains the coding sequence for the first 87 amino acids of NS1, then by an alternative splicing mechanism mRNA from a different reading frame, encoding the last 78 amino acids, makes up the full length of the NS2 mRNA. NS1, is the major non-structural protein. It is essential for DNA replication. It is an 83-kDa nuclear phosphoprotein. It has DNA helicase and ATPase activity.


Pssm-ID: 426020  Cd Length: 271  Bit Score: 40.37  E-value: 1.21e-03
                          10        20        30
                  ....*....|....*....|....*....|.
gi 66805379   177 KQIGidpPRG-VLLYGPPGTGKTMLAKAVAH 206
Cdd:pfam01057 108 KQFG---KRNtVWFYGPASTGKTNLAQAIAH 135
TIP49 pfam06068
TIP49 P-loop domain; This family consists of the C-terminal region of several eukaryotic and ...
134-220 1.26e-03

TIP49 P-loop domain; This family consists of the C-terminal region of several eukaryotic and archaeal RuvB-like 1 (Pontin or TIP49a) and RuvB-like 2 (Reptin or TIP49b) proteins. The N-terminal domain contains the pfam00004 domain. In zebrafish, the liebeskummer (lik) mutation, causes development of hyperplastic embryonic hearts. lik encodes Reptin, a component of a DNA-stimulated ATPase complex. Beta-catenin and Pontin, a DNA-stimulated ATPase that is often part of complexes with Reptin, are in the same genetic pathways. The Reptin/Pontin ratio serves to regulate heart growth during development, at least in part via the beta-catenin pathway. TBP-interacting protein 49 (TIP49) was originally identified as a TBP-binding protein, and two related proteins are encoded by individual genes, tip49a and b. Although the function of this gene family has not been elucidated, they are supposed to play a critical role in nuclear events because they interact with various kinds of nuclear factors and have DNA helicase activities.TIP49a has been suggested to act as an autoantigen in some patients with autoimmune diseases.


Pssm-ID: 399217 [Multi-domain]  Cd Length: 347  Bit Score: 40.76  E-value: 1.26e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66805379   134 SSIHLLGADEkpSESYSDIGGGDIQKQEMREAVELPLthhNLYKQiGIDPPRGVLLYGPPGTGKTMLAKAVAHH--TSAA 211
Cdd:pfam06068   6 SHIRGLGLDE--DGEARYVSGGLVGQEKAREAAGVIV---EMIKE-GKIAGRAVLIAGPPGTGKTALAIAISKElgEDTP 79

                  ....*....
gi 66805379   212 FIRVVGSEF 220
Cdd:pfam06068  80 FTSISGSEV 88
COG0645 COG0645
Predicted kinase, contains AAA domain [General function prediction only];
187-215 2.11e-03

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


Pssm-ID: 440410 [Multi-domain]  Cd Length: 164  Bit Score: 38.74  E-value: 2.11e-03
                        10        20
                ....*....|....*....|....*....
gi 66805379 187 VLLYGPPGTGKTMLAKAVAHHTSAAFIRV 215
Cdd:COG0645   2 ILVCGLPGSGKSTLARALAERLGAVRLRS 30
AAA_22 pfam13401
AAA domain;
187-302 2.19e-03

AAA domain;


Pssm-ID: 379165 [Multi-domain]  Cd Length: 129  Bit Score: 38.09  E-value: 2.19e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66805379   187 VLLYGPPGTGKTMLAKAVAHH-----------------TSAAFIRVVGSEFVQKYLGEGP--RLVRDVFRLARE-NSPAI 246
Cdd:pfam13401   8 LVLTGESGTGKTTLLRRLLEQlpevrdsvvfvdlpsgtSPKDLLRALLRALGLPLSGRLSkeELLAALQQLLLAlAVAVV 87
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 66805379   247 IFIDEIDAIATKrfdaqtgadrevqrILMELLNQMDGFDVSVNVKVIMATNRQDTL 302
Cdd:pfam13401  88 LIIDEAQHLSLE--------------ALEELRDLLNLSSKLLQLILVGTPELRELL 129
T7SS_EccA TIGR03922
type VII secretion AAA-ATPase EccA; This model represents the AAA family ATPase, EccA, of the ...
185-319 2.19e-03

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


Pssm-ID: 188437 [Multi-domain]  Cd Length: 557  Bit Score: 40.21  E-value: 2.19e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66805379   185 RGVLLYGPPGTGKTMLAKAVAHHTSA-------AFIRVVGSEFVQKYLGEGPRLVRDVFRLAREnspAIIFIDEIDAIAT 257
Cdd:TIGR03922 313 NHMLFAGPPGTGKTTIARVVAKIYCGlgvlrkpLVREVSRADLIGQYIGESEAKTNEIIDSALG---GVLFLDEAYTLVE 389
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 66805379   258 KRFDAQTGADRE-VQRILMELLNQMDGFdvsvnvKVIMATNRQDtLDPAL-----LRpGRLDRKIEFP 319
Cdd:TIGR03922 390 TGYGQKDPFGLEaIDTLLARMENDRDRL------VVIGAGYRKD-LDKFLevnegLR-SRFTRVIEFP 449
hslU PRK05201
ATP-dependent protease ATPase subunit HslU;
246-272 2.47e-03

ATP-dependent protease ATPase subunit HslU;


Pssm-ID: 235364 [Multi-domain]  Cd Length: 443  Bit Score: 39.68  E-value: 2.47e-03
                         10        20        30
                 ....*....|....*....|....*....|
gi 66805379  246 IIFIDEIDAIATKrfDAQTGAD--RE-VQR 272
Cdd:PRK05201 252 IVFIDEIDKIAAR--GGSSGPDvsREgVQR 279
TIGR02928 TIGR02928
orc1/cdc6 family replication initiation protein; Members of this protein family are found ...
183-288 3.95e-03

orc1/cdc6 family replication initiation protein; Members of this protein family are found exclusively in the archaea. This set of DNA binding proteins shows homology to the origin recognition complex subunit 1/cell division control protein 6 family in eukaryotes. Several members may be found in genome and interact with each other. [DNA metabolism, DNA replication, recombination, and repair]


Pssm-ID: 274354 [Multi-domain]  Cd Length: 365  Bit Score: 39.15  E-value: 3.95e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66805379   183 PPRGVLLYGPPGTGKTMLAKAV-------AHHTSAAFIRV------------VGSEFVQKYLGEGP----------RLVR 233
Cdd:TIGR02928  39 RPSNVFIYGKTGTGKTAVTKYVmkeleeaAEDRDVRVVTVyvncqildtlyqVLVELANQLRGSGEevpttglstsEVFR 118
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 66805379   234 DVFRLARENSPAIIFI-DEIDAIAtkrfdaqtgadREVQRILMELL-----NQMDGFDVSV 288
Cdd:TIGR02928 119 RLYKELNERGDSLIIVlDEIDYLV-----------GDDDDLLYQLSrarsnGDLDNAKVGV 168
ExeA COG3267
Type II secretory pathway ATPase component GspA/ExeA/MshM [Intracellular trafficking, ...
187-251 4.21e-03

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


Pssm-ID: 442498 [Multi-domain]  Cd Length: 261  Bit Score: 38.62  E-value: 4.21e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66805379 187 VLLYGPPGTGKTMLAKAVAHH---------------TSAAFIRVVGSEFVQKYLGEGP-----RLVRDVFRLARENSPAI 246
Cdd:COG3267  46 VVLTGEVGTGKTTLLRRLLERlpddvkvayipnpqlSPAELLRAIADELGLEPKGASKadllrQLQEFLLELAAAGRRVV 125

                ....*
gi 66805379 247 IFIDE 251
Cdd:COG3267 126 LIIDE 130
RuvB_N pfam05496
Holliday junction DNA helicase RuvB P-loop domain; The RuvB protein makes up part of the ...
187-206 4.45e-03

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


Pssm-ID: 398900 [Multi-domain]  Cd Length: 159  Bit Score: 37.48  E-value: 4.45e-03
                          10        20
                  ....*....|....*....|
gi 66805379   187 VLLYGPPGTGKTMLAKAVAH 206
Cdd:pfam05496  36 VLLYGPPGLGKTTLANIIAN 55
HslU COG1220
ATP-dependent protease HslVU (ClpYQ), ATPase subunit HslU [Posttranslational modification, ...
246-272 6.05e-03

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


Pssm-ID: 440833 [Multi-domain]  Cd Length: 454  Bit Score: 38.49  E-value: 6.05e-03
                        10        20        30
                ....*....|....*....|....*....|
gi 66805379 246 IIFIDEIDAIATKrfDAQTGAD--RE-VQR 272
Cdd:COG1220 263 IIFIDEIDKIASR--GGGSGPDvsREgVQR 290
COG3903 COG3903
Predicted ATPase [General function prediction only];
187-212 9.92e-03

Predicted ATPase [General function prediction only];


Pssm-ID: 443109 [Multi-domain]  Cd Length: 933  Bit Score: 38.07  E-value: 9.92e-03
                        10        20
                ....*....|....*....|....*.
gi 66805379 187 VLLYGPPGTGKTMLAKAVAHHTSAAF 212
Cdd:COG3903 179 VTLTGPGGVGKTRLALEVAHRLADRF 204
 
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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