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Conserved domains on  [gi|185177972]
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Chain A, Transitional endoplasmic reticulum ATPase

Protein Classification

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
RecA-like_CDC48_r2-like cd19528
second of two ATPase domains of CDC48 and similar ATPase domains; CDC48 in yeast and p97 or ...
23-183 1.07e-128

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: 362.98  E-value: 1.07e-128
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 185177972  23 VKRELQELVQYPVEHPDKFLKFGMTPSKGVLFYGPPGCGKTLLAKAIANECQANFISIKGPELLTMWFGESEANVREIFD 102
Cdd:cd19528    1 VKRELQELVQYPVEHPDKFLKFGMTPSKGVLFYGPPGCGKTLLAKAIANECQANFISVKGPELLTMWFGESEANVRDIFD 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 185177972 103 KARQAAPCVLFFDELDSIAKARGGNIGDGGGAADRVINQILTEMDGMSTKKNVFIIGATNRPDIIDPAILRPGRLDQLIY 182
Cdd:cd19528   81 KARAAAPCVLFFDELDSIAKARGGNIGDAGGAADRVINQILTEMDGMNTKKNVFIIGATNRPDIIDPAILRPGRLDQLIY 160

                 .
gi 185177972 183 I 183
Cdd:cd19528  161 I 161
AAA_lid_3 pfam17862
AAA+ lid domain; This entry represents the alpha helical AAA+ lid domain that is found to the ...
207-236 5.71e-08

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: 48.30  E-value: 5.71e-08
                          10        20        30
                  ....*....|....*....|....*....|
gi 185177972  207 DVDLEFLAKMTNGFSGADLTEICQRACKLA 236
Cdd:pfam17862   1 DVDLEELAERTEGFSGADLEALCREAALAA 30
Vps4_C super family cl07827
Vps4 C terminal oligomerization domain; This domain is found at the C terminal of ATPase ...
256-298 6.93e-05

Vps4 C terminal oligomerization domain; This domain is found at the C terminal of ATPase proteins involved in vacuolar sorting. It forms an alpha helix structure and is required for oligomerization.


The actual alignment was detected with superfamily member pfam09336:

Pssm-ID: 462762 [Multi-domain]  Cd Length: 61  Bit Score: 40.17  E-value: 6.93e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 185177972  256 SAMEVEEDD-PVPEIRRDHFEEAMRFARRSVSDNDIRKYEMFAQ 298
Cdd:pfam09336  15 TWMDIPSDKlLEPPVTMKDFLKALKSSRPTVSKEDLEKYEEFTK 58
 
Name Accession Description Interval E-value
RecA-like_CDC48_r2-like cd19528
second of two ATPase domains of CDC48 and similar ATPase domains; CDC48 in yeast and p97 or ...
23-183 1.07e-128

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: 362.98  E-value: 1.07e-128
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 185177972  23 VKRELQELVQYPVEHPDKFLKFGMTPSKGVLFYGPPGCGKTLLAKAIANECQANFISIKGPELLTMWFGESEANVREIFD 102
Cdd:cd19528    1 VKRELQELVQYPVEHPDKFLKFGMTPSKGVLFYGPPGCGKTLLAKAIANECQANFISVKGPELLTMWFGESEANVRDIFD 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 185177972 103 KARQAAPCVLFFDELDSIAKARGGNIGDGGGAADRVINQILTEMDGMSTKKNVFIIGATNRPDIIDPAILRPGRLDQLIY 182
Cdd:cd19528   81 KARAAAPCVLFFDELDSIAKARGGNIGDAGGAADRVINQILTEMDGMNTKKNVFIIGATNRPDIIDPAILRPGRLDQLIY 160

                 .
gi 185177972 183 I 183
Cdd:cd19528  161 I 161
RPT1 COG1222
ATP-dependent 26S proteasome regulatory subunit [Posttranslational modification, protein ...
8-236 3.31e-120

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


Pssm-ID: 440835 [Multi-domain]  Cd Length: 326  Bit Score: 347.76  E-value: 3.31e-120
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 185177972   8 EVPQVTWEDIGGLEDVKRELQELVQYPVEHPDKFLKFGMTPSKGVLFYGPPGCGKTLLAKAIANECQANFISIKGPELLT 87
Cdd:COG1222   71 ESPDVTFDDIGGLDEQIEEIREAVELPLKNPELFRKYGIEPPKGVLLYGPPGTGKTLLAKAVAGELGAPFIRVRGSELVS 150
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 185177972  88 MWFGESEANVREIFDKARQAAPCVLFFDELDSIAKARggNIGDGGGAADRVINQILTEMDGMSTKKNVFIIGATNRPDII 167
Cdd:COG1222  151 KYIGEGARNVREVFELAREKAPSIIFIDEIDAIAARR--TDDGTSGEVQRTVNQLLAELDGFESRGDVLIIAATNRPDLL 228
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 185177972 168 DPAILRPGRLDQLIYIPLPDEKSRVAILKANLRKSPVAKDVDLEFLAKMTNGFSGADLTEICQRACKLA 236
Cdd:COG1222  229 DPALLRPGRFDRVIEVPLPDEEAREEILKIHLRDMPLADDVDLDKLAKLTEGFSGADLKAIVTEAGMFA 297
CDC48 TIGR01243
AAA family ATPase, CDC48 subfamily; This subfamily of the AAA family ATPases includes two ...
1-301 2.26e-112

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: 341.12  E-value: 2.26e-112
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 185177972    1 ALRETVVEVPQVTWEDIGGLEDVKRELQELVQYPVEHPDKFLKFGMTPSKGVLFYGPPGCGKTLLAKAIANECQANFISI 80
Cdd:TIGR01243 439 AIREVLVEVPNVRWSDIGGLEEVKQELREAVEWPLKHPEIFEKMGIRPPKGVLLFGPPGTGKTLLAKAVATESGANFIAV 518
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 185177972   81 KGPELLTMWFGESEANVREIFDKARQAAPCVLFFDELDSIAKARggNIGDGGGAADRVINQILTEMDGMSTKKNVFIIGA 160
Cdd:TIGR01243 519 RGPEILSKWVGESEKAIREIFRKARQAAPAIIFFDEIDAIAPAR--GARFDTSVTDRIVNQLLTEMDGIQELSNVVVIAA 596
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 185177972  161 TNRPDIIDPAILRPGRLDQLIYIPLPDEKSRVAILKANLRKSPVAKDVDLEFLAKMTNGFSGADLTEICQRACKLAIRES 240
Cdd:TIGR01243 597 TNRPDILDPALLRPGRFDRLILVPPPDEEARKEIFKIHTRSMPLAEDVDLEELAEMTEGYTGADIEAVCREAAMAALRES 676
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 185177972  241 IESEIRrererqtnpSAMEVEEDDPVPE--IRRDHFEEAMRFARRSVSDNDIRKYEMFAQTLQ 301
Cdd:TIGR01243 677 IGSPAK---------EKLEVGEEEFLKDlkVEMRHFLEALKKVKPSVSKEDMLRYERLAKELK 730
PRK03992 PRK03992
proteasome-activating nucleotidase; Provisional
6-232 1.83e-94

proteasome-activating nucleotidase; Provisional


Pssm-ID: 179699 [Multi-domain]  Cd Length: 389  Bit Score: 284.42  E-value: 1.83e-94
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 185177972   6 VVEVPQVTWEDIGGLEDVKRELQELVQYPVEHPDKFLKFGMTPSKGVLFYGPPGCGKTLLAKAIANECQANFISIKGPEL 85
Cdd:PRK03992 122 VIESPNVTYEDIGGLEEQIREVREAVELPLKKPELFEEVGIEPPKGVLLYGPPGTGKTLLAKAVAHETNATFIRVVGSEL 201
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 185177972  86 LTMWFGESEANVREIFDKARQAAPCVLFFDELDSIAKARggniGDGGGAADRVIN----QILTEMDGMSTKKNVFIIGAT 161
Cdd:PRK03992 202 VQKFIGEGARLVRELFELAREKAPSIIFIDEIDAIAAKR----TDSGTSGDREVQrtlmQLLAEMDGFDPRGNVKIIAAT 277
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 185177972 162 NRPDIIDPAILRPGRLDQLIYIPLPDEKSRVAILKANLRKSPVAKDVDLEFLAKMTNGFSGADLTEICQRA 232
Cdd:PRK03992 278 NRIDILDPAILRPGRFDRIIEVPLPDEEGRLEILKIHTRKMNLADDVDLEELAELTEGASGADLKAICTEA 348
cell_div_CdvC NF041006
cell division protein CdvC;
6-294 1.05e-60

cell division protein CdvC;


Pssm-ID: 468935 [Multi-domain]  Cd Length: 371  Bit Score: 197.26  E-value: 1.05e-60
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 185177972   6 VVEVPQVTWEDIGGLEDVKRELQELVQYPVEHPDKFlkfgmtP---SKGVLFYGPPGCGKTLLAKAIANECQANFISIKG 82
Cdd:NF041006  94 VKEKPKVTFSDIVGLEDVKEALKEAIVYPSKRPDLF------PlgwPRGILLYGPPGCGKTMLAAAVANEIDSEFIHVDA 167
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 185177972  83 PELLTMWFGESEANVREIFDKARQAA-----PCVLFFDELDSIAKARGGNIGDGGgaadRVINQILTEMDGM---STKKN 154
Cdd:NF041006 168 ASIMSKWLGEAEKNVAKIFKKAREKSkeegkPAIIFIDEIDALLGVYSSEVGGEV----RVRNQFLKEMDGLqdkSENYH 243
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 185177972 155 VFIIGATNRPDIIDPAILRpgRLDQLIYIPLPDEKSRVAILKANLRKSPVAKDVDLEFLAKMTNGFSGADLTEICQRAck 234
Cdd:NF041006 244 VYVIGATNKPWRLDEPFLR--RFQKRIYIPLPDREQRLELLKYYTSKIKLENDVDLDELAEMTEGYTASDIRDIVQAA-- 319
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 185177972 235 lairesieseirrerERQTNPSAMEVEEDDPVPeIRRDHFEEAMRFARRSVSDNDIRKYE 294
Cdd:NF041006 320 ---------------HMRVVKEMFEKGLGEPRP-ITMEDFKEVLKIRKPSVNQEMLKAYE 363
AAA pfam00004
ATPase family associated with various cellular activities (AAA); AAA family proteins often ...
52-185 2.57e-57

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: 180.48  E-value: 2.57e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 185177972   52 VLFYGPPGCGKTLLAKAIANECQANFISIKGPELLTMWFGESEANVREIFDKARQAAPCVLFFDELDSIAKARggnIGDG 131
Cdd:pfam00004   1 LLLYGPPGTGKTTLAKAVAKELGAPFIEISGSELVSKYVGESEKRLRELFEAAKKLAPCVIFIDEIDALAGSR---GSGG 77
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 185177972  132 GGAADRVINQILTEMDGMSTKK-NVFIIGATNRPDIIDPAILrpGRLDQLIYIPL 185
Cdd:pfam00004  78 DSESRRVVNQLLTELDGFTSSNsKVIVIAATNRPDKLDPALL--GRFDRIIEFPL 130
AAA smart00382
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ...
48-187 6.81e-22

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: 89.35  E-value: 6.81e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 185177972    48 PSKGVLFYGPPGCGKTLLAKAIANECQAN---FISIKGPELL--------------TMWFGESEANVREIFDKARQAAPC 110
Cdd:smart00382   1 PGEVILIVGPPGSGKTTLARALARELGPPgggVIYIDGEDILeevldqllliivggKKASGSGELRLRLALALARKLKPD 80
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 185177972   111 VLFFDELDSIAKARggnigdggGAADRVINQILTEMDGMSTKKNVFIIGATNRPDIIDPAILRPgRLDQLIYIPLPD 187
Cdd:smart00382  81 VLILDEITSLLDAE--------QEALLLLLEELRLLLLLKSEKNLTVILTTNDEKDLGPALLRR-RFDRRIVLLLIL 148
AAA_lid_3 pfam17862
AAA+ lid domain; This entry represents the alpha helical AAA+ lid domain that is found to the ...
207-236 5.71e-08

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: 48.30  E-value: 5.71e-08
                          10        20        30
                  ....*....|....*....|....*....|
gi 185177972  207 DVDLEFLAKMTNGFSGADLTEICQRACKLA 236
Cdd:pfam17862   1 DVDLEELAERTEGFSGADLEALCREAALAA 30
Vps4_C pfam09336
Vps4 C terminal oligomerization domain; This domain is found at the C terminal of ATPase ...
256-298 6.93e-05

Vps4 C terminal oligomerization domain; This domain is found at the C terminal of ATPase proteins involved in vacuolar sorting. It forms an alpha helix structure and is required for oligomerization.


Pssm-ID: 462762 [Multi-domain]  Cd Length: 61  Bit Score: 40.17  E-value: 6.93e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 185177972  256 SAMEVEEDD-PVPEIRRDHFEEAMRFARRSVSDNDIRKYEMFAQ 298
Cdd:pfam09336  15 TWMDIPSDKlLEPPVTMKDFLKALKSSRPTVSKEDLEKYEEFTK 58
IS21_help_AAA NF038214
IS21-like element helper ATPase IstB; This protein family model resembles PF01695, but was ...
52-77 8.45e-04

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


Pssm-ID: 439516  Cd Length: 232  Bit Score: 40.15  E-value: 8.45e-04
                         10        20
                 ....*....|....*....|....*..
gi 185177972  52 VLFYGPPGCGKTLLAKAIANE-CQANF 77
Cdd:NF038214  93 VLLLGPPGTGKTHLAIALGYAaCRQGY 119
 
Name Accession Description Interval E-value
RecA-like_CDC48_r2-like cd19528
second of two ATPase domains of CDC48 and similar ATPase domains; CDC48 in yeast and p97 or ...
23-183 1.07e-128

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: 362.98  E-value: 1.07e-128
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 185177972  23 VKRELQELVQYPVEHPDKFLKFGMTPSKGVLFYGPPGCGKTLLAKAIANECQANFISIKGPELLTMWFGESEANVREIFD 102
Cdd:cd19528    1 VKRELQELVQYPVEHPDKFLKFGMTPSKGVLFYGPPGCGKTLLAKAIANECQANFISVKGPELLTMWFGESEANVRDIFD 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 185177972 103 KARQAAPCVLFFDELDSIAKARGGNIGDGGGAADRVINQILTEMDGMSTKKNVFIIGATNRPDIIDPAILRPGRLDQLIY 182
Cdd:cd19528   81 KARAAAPCVLFFDELDSIAKARGGNIGDAGGAADRVINQILTEMDGMNTKKNVFIIGATNRPDIIDPAILRPGRLDQLIY 160

                 .
gi 185177972 183 I 183
Cdd:cd19528  161 I 161
RPT1 COG1222
ATP-dependent 26S proteasome regulatory subunit [Posttranslational modification, protein ...
8-236 3.31e-120

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


Pssm-ID: 440835 [Multi-domain]  Cd Length: 326  Bit Score: 347.76  E-value: 3.31e-120
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 185177972   8 EVPQVTWEDIGGLEDVKRELQELVQYPVEHPDKFLKFGMTPSKGVLFYGPPGCGKTLLAKAIANECQANFISIKGPELLT 87
Cdd:COG1222   71 ESPDVTFDDIGGLDEQIEEIREAVELPLKNPELFRKYGIEPPKGVLLYGPPGTGKTLLAKAVAGELGAPFIRVRGSELVS 150
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 185177972  88 MWFGESEANVREIFDKARQAAPCVLFFDELDSIAKARggNIGDGGGAADRVINQILTEMDGMSTKKNVFIIGATNRPDII 167
Cdd:COG1222  151 KYIGEGARNVREVFELAREKAPSIIFIDEIDAIAARR--TDDGTSGEVQRTVNQLLAELDGFESRGDVLIIAATNRPDLL 228
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 185177972 168 DPAILRPGRLDQLIYIPLPDEKSRVAILKANLRKSPVAKDVDLEFLAKMTNGFSGADLTEICQRACKLA 236
Cdd:COG1222  229 DPALLRPGRFDRVIEVPLPDEEAREEILKIHLRDMPLADDVDLDKLAKLTEGFSGADLKAIVTEAGMFA 297
CDC48 TIGR01243
AAA family ATPase, CDC48 subfamily; This subfamily of the AAA family ATPases includes two ...
1-301 2.26e-112

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: 341.12  E-value: 2.26e-112
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 185177972    1 ALRETVVEVPQVTWEDIGGLEDVKRELQELVQYPVEHPDKFLKFGMTPSKGVLFYGPPGCGKTLLAKAIANECQANFISI 80
Cdd:TIGR01243 439 AIREVLVEVPNVRWSDIGGLEEVKQELREAVEWPLKHPEIFEKMGIRPPKGVLLFGPPGTGKTLLAKAVATESGANFIAV 518
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 185177972   81 KGPELLTMWFGESEANVREIFDKARQAAPCVLFFDELDSIAKARggNIGDGGGAADRVINQILTEMDGMSTKKNVFIIGA 160
Cdd:TIGR01243 519 RGPEILSKWVGESEKAIREIFRKARQAAPAIIFFDEIDAIAPAR--GARFDTSVTDRIVNQLLTEMDGIQELSNVVVIAA 596
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 185177972  161 TNRPDIIDPAILRPGRLDQLIYIPLPDEKSRVAILKANLRKSPVAKDVDLEFLAKMTNGFSGADLTEICQRACKLAIRES 240
Cdd:TIGR01243 597 TNRPDILDPALLRPGRFDRLILVPPPDEEARKEIFKIHTRSMPLAEDVDLEELAEMTEGYTGADIEAVCREAAMAALRES 676
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 185177972  241 IESEIRrererqtnpSAMEVEEDDPVPE--IRRDHFEEAMRFARRSVSDNDIRKYEMFAQTLQ 301
Cdd:TIGR01243 677 IGSPAK---------EKLEVGEEEFLKDlkVEMRHFLEALKKVKPSVSKEDMLRYERLAKELK 730
RecA-like_CDC48_r2-like cd19511
second of two ATPase domains of CDC48/p97, PEX1 and -6, VAT and NVL, and similar ATPase ...
23-183 9.93e-100

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: 289.57  E-value: 9.93e-100
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 185177972  23 VKRELQELVQYPVEHPDKFLKFGMTPSKGVLFYGPPGCGKTLLAKAIANECQANFISIKGPELLTMWFGESEANVREIFD 102
Cdd:cd19511    1 VKRELKEAVEWPLKHPDAFKRLGIRPPKGVLLYGPPGCGKTLLAKALASEAGLNFISVKGPELFSKYVGESERAVREIFQ 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 185177972 103 KARQAAPCVLFFDELDSIAKARggNIGDGGGAADRVINQILTEMDGMSTKKNVFIIGATNRPDIIDPAILRPGRLDQLIY 182
Cdd:cd19511   81 KARQAAPCIIFFDEIDSLAPRR--GQSDSSGVTDRVVSQLLTELDGIESLKGVVVIAATNRPDMIDPALLRPGRLDKLIY 158

                 .
gi 185177972 183 I 183
Cdd:cd19511  159 V 159
SpoVK COG0464
AAA+-type ATPase, SpoVK/Ycf46/Vps4 family [Cell wall/membrane/envelope biogenesis, Cell cycle ...
2-236 8.36e-96

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: 288.35  E-value: 8.36e-96
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 185177972   2 LRETVVEVPQVTWEDIGGLEDVKRELQELVQYPVEHPDKFLKFGMTPSKGVLFYGPPGCGKTLLAKAIANECQANFISIK 81
Cdd:COG0464  144 LEEELLELREAILDDLGGLEEVKEELRELVALPLKRPELREEYGLPPPRGLLLYGPPGTGKTLLARALAGELGLPLIEVD 223
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 185177972  82 GPELLTMWFGESEANVREIFDKARQAAPCVLFFDELDSIAKARggnIGDGGGAADRVINQILTEMDGMstKKNVFIIGAT 161
Cdd:COG0464  224 LSDLVSKYVGETEKNLREVFDKARGLAPCVLFIDEADALAGKR---GEVGDGVGRRVVNTLLTEMEEL--RSDVVVIAAT 298
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 185177972 162 NRPDIIDPAILRpgRLDQLIYIPLPDEKSRVAILKANLRKSPVAKDVDLEFLAKMTNGFSGADLTEICQRACKLA 236
Cdd:COG0464  299 NRPDLLDPALLR--RFDEIIFFPLPDAEERLEIFRIHLRKRPLDEDVDLEELAEATEGLSGADIRNVVRRAALQA 371
PRK03992 PRK03992
proteasome-activating nucleotidase; Provisional
6-232 1.83e-94

proteasome-activating nucleotidase; Provisional


Pssm-ID: 179699 [Multi-domain]  Cd Length: 389  Bit Score: 284.42  E-value: 1.83e-94
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 185177972   6 VVEVPQVTWEDIGGLEDVKRELQELVQYPVEHPDKFLKFGMTPSKGVLFYGPPGCGKTLLAKAIANECQANFISIKGPEL 85
Cdd:PRK03992 122 VIESPNVTYEDIGGLEEQIREVREAVELPLKKPELFEEVGIEPPKGVLLYGPPGTGKTLLAKAVAHETNATFIRVVGSEL 201
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 185177972  86 LTMWFGESEANVREIFDKARQAAPCVLFFDELDSIAKARggniGDGGGAADRVIN----QILTEMDGMSTKKNVFIIGAT 161
Cdd:PRK03992 202 VQKFIGEGARLVRELFELAREKAPSIIFIDEIDAIAAKR----TDSGTSGDREVQrtlmQLLAEMDGFDPRGNVKIIAAT 277
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 185177972 162 NRPDIIDPAILRPGRLDQLIYIPLPDEKSRVAILKANLRKSPVAKDVDLEFLAKMTNGFSGADLTEICQRA 232
Cdd:PRK03992 278 NRIDILDPAILRPGRFDRIIEVPLPDEEGRLEILKIHTRKMNLADDVDLEELAELTEGASGADLKAICTEA 348
CDC48 TIGR01243
AAA family ATPase, CDC48 subfamily; This subfamily of the AAA family ATPases includes two ...
9-236 5.68e-80

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


Pssm-ID: 273521 [Multi-domain]  Cd Length: 733  Bit Score: 256.76  E-value: 5.68e-80
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 185177972    9 VPQVTWEDIGGLEDVKRELQELVQYPVEHPDKFLKFGMTPSKGVLFYGPPGCGKTLLAKAIANECQANFISIKGPELLTM 88
Cdd:TIGR01243 172 VPKVTYEDIGGLKEAKEKIREMVELPMKHPELFEHLGIEPPKGVLLYGPPGTGKTLLAKAVANEAGAYFISINGPEIMSK 251
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 185177972   89 WFGESEANVREIFDKARQAAPCVLFFDELDSIAKARGGNIGDGGGaadRVINQILTEMDGMSTKKNVFIIGATNRPDIID 168
Cdd:TIGR01243 252 YYGESEERLREIFKEAEENAPSIIFIDEIDAIAPKREEVTGEVEK---RVVAQLLTLMDGLKGRGRVIVIGATNRPDALD 328
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 185177972  169 PAILRPGRLDQLIYIPLPDEKSRVAILKANLRKSPVAKDVDLEFLAKMTNGFSGADLTEICQRACKLA 236
Cdd:TIGR01243 329 PALRRPGRFDREIVIRVPDKRARKEILKVHTRNMPLAEDVDLDKLAEVTHGFVGADLAALAKEAAMAA 396
RecA-like_VCP_r2 cd19529
second of two ATPase domains of Valosin-containing protein-like ATPase (VAT) and similar ...
23-183 7.13e-79

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: 236.62  E-value: 7.13e-79
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 185177972  23 VKRELQELVQYPVEHPDKFLKFGMTPSKGVLFYGPPGCGKTLLAKAIANECQANFISIKGPELLTMWFGESEANVREIFD 102
Cdd:cd19529    1 VKQELKEAVEWPLLKPEVFKRLGIRPPKGILLYGPPGTGKTLLAKAVATESNANFISVKGPELLSKWVGESEKAIREIFR 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 185177972 103 KARQAAPCVLFFDELDSIAKARggNIGDGGGAADRVINQILTEMDGMSTKKNVFIIGATNRPDIIDPAILRPGRLDQLIY 182
Cdd:cd19529   81 KARQVAPCVIFFDEIDSIAPRR--GTTGDSGVTERVVNQLLTELDGLEEMNGVVVIAATNRPDIIDPALLRAGRFDRLIY 158

                 .
gi 185177972 183 I 183
Cdd:cd19529  159 I 159
FtsH_fam TIGR01241
ATP-dependent metalloprotease FtsH; HflB(FtsH) is a pleiotropic protein required for correct ...
8-236 1.44e-78

ATP-dependent metalloprotease FtsH; HflB(FtsH) is a pleiotropic protein required for correct cell division in bacteria. It has ATP-dependent zinc metalloprotease activity. It was formerly designated cell division protein FtsH. [Cellular processes, Cell division, Protein fate, Degradation of proteins, peptides, and glycopeptides]


Pssm-ID: 273520 [Multi-domain]  Cd Length: 495  Bit Score: 246.81  E-value: 1.44e-78
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 185177972    8 EVPQVTWEDIGGLEDVKRELQELVQYpVEHPDKFLKFGMTPSKGVLFYGPPGCGKTLLAKAIANECQANFISIKGPELLT 87
Cdd:TIGR01241  48 EKPKVTFKDVAGIDEAKEELMEIVDF-LKNPSKFTKLGAKIPKGVLLVGPPGTGKTLLAKAVAGEAGVPFFSISGSDFVE 126
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 185177972   88 MWFGESEANVREIFDKARQAAPCVLFFDELDSIAKARGGNIGDGGGAADRVINQILTEMDGMSTKKNVFIIGATNRPDII 167
Cdd:TIGR01241 127 MFVGVGASRVRDLFEQAKKNAPCIIFIDEIDAVGRQRGAGLGGGNDEREQTLNQLLVEMDGFGTNTGVIVIAATNRPDVL 206
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 185177972  168 DPAILRPGRLDQLIYIPLPDEKSRVAILKANLRKSPVAKDVDLEFLAKMTNGFSGADLTEICQRACKLA 236
Cdd:TIGR01241 207 DPALLRPGRFDRQVVVDLPDIKGREEILKVHAKNKKLAPDVDLKAVARRTPGFSGADLANLLNEAALLA 275
HflB COG0465
ATP-dependent Zn proteases [Posttranslational modification, protein turnover, chaperones];
10-225 6.49e-78

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


Pssm-ID: 440233 [Multi-domain]  Cd Length: 583  Bit Score: 247.64  E-value: 6.49e-78
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 185177972  10 PQVTWEDIGGLEDVKRELQELVQYpVEHPDKFLKFGMTPSKGVLFYGPPGCGKTLLAKAIANECQANFISIKGPELLTMW 89
Cdd:COG0465  137 PKVTFDDVAGVDEAKEELQEIVDF-LKDPEKFTRLGAKIPKGVLLVGPPGTGKTLLAKAVAGEAGVPFFSISGSDFVEMF 215
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 185177972  90 FGESEANVREIFDKARQAAPCVLFFDELDSIAKARggnigdgggAA---------DRVINQILTEMDGMSTKKNVFIIGA 160
Cdd:COG0465  216 VGVGASRVRDLFEQAKKNAPCIIFIDEIDAVGRQR---------GAglggghderEQTLNQLLVEMDGFEGNEGVIVIAA 286
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 185177972 161 TNRPDIIDPAILRPGRLDQLIYIPLPDEKSRVAILKANLRKSPVAKDVDLEFLAKMTNGFSGADL 225
Cdd:COG0465  287 TNRPDVLDPALLRPGRFDRQVVVDLPDVKGREAILKVHARKKPLAPDVDLEVIARRTPGFSGADL 351
RecA-like_NVL_r2-like cd19530
second of two ATPase domains of NVL (nuclear VCP-like protein) and similar ATPase domains; NVL ...
20-183 7.52e-76

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: 228.91  E-value: 7.52e-76
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 185177972  20 LEDVKRELQELVQYPVEHPDKFLKFGMTPSKGVLFYGPPGCGKTLLAKAIANECQANFISIKGPELLTMWFGESEANVRE 99
Cdd:cd19530    1 LDHVREELTMSILRPIKRPDIYKALGIDLPTGVLLYGPPGCGKTLLAKAVANESGANFISVKGPELLNKYVGESERAVRQ 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 185177972 100 IFDKARQAAPCVLFFDELDSIAKARggnIGDGGGAADRVINQILTEMDGMSTKKNVFIIGATNRPDIIDPAILRPGRLDQ 179
Cdd:cd19530   81 VFQRARASAPCVIFFDEVDALVPKR---GDGGSWASERVVNQLLTEMDGLEERSNVFVIAATNRPDIIDPAMLRPGRLDK 157

                 ....
gi 185177972 180 LIYI 183
Cdd:cd19530  158 TLYV 161
ftsH CHL00176
cell division protein; Validated
12-225 2.24e-73

cell division protein; Validated


Pssm-ID: 214386 [Multi-domain]  Cd Length: 638  Bit Score: 237.26  E-value: 2.24e-73
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 185177972  12 VTWEDIGGLEDVKRELQELVQYpVEHPDKFLKFGMTPSKGVLFYGPPGCGKTLLAKAIANECQANFISIKGPELLTMWFG 91
Cdd:CHL00176 180 ITFRDIAGIEEAKEEFEEVVSF-LKKPERFTAVGAKIPKGVLLVGPPGTGKTLLAKAIAGEAEVPFFSISGSEFVEMFVG 258
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 185177972  92 ESEANVREIFDKARQAAPCVLFFDELDSIAKARGGNIGDGGGAADRVINQILTEMDGMSTKKNVFIIGATNRPDIIDPAI 171
Cdd:CHL00176 259 VGAARVRDLFKKAKENSPCIVFIDEIDAVGRQRGAGIGGGNDEREQTLNQLLTEMDGFKGNKGVIVIAATNRVDILDAAL 338
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 185177972 172 LRPGRLDQLIYIPLPDEKSRVAILKANLRKSPVAKDVDLEFLAKMTNGFSGADL 225
Cdd:CHL00176 339 LRPGRFDRQITVSLPDREGRLDILKVHARNKKLSPDVSLELIARRTPGFSGADL 392
RecA-like_CDC48_NLV2_r1-like cd19503
first of two ATPase domains of CDC48 and NLV2, and similar ATPase domains; CDC48 in yeast and ...
16-183 2.93e-73

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


Pssm-ID: 410911 [Multi-domain]  Cd Length: 165  Bit Score: 222.55  E-value: 2.93e-73
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 185177972  16 DIGGLEDVKRELQELVQYPVEHPDKFLKFGMTPSKGVLFYGPPGCGKTLLAKAIANECQANFISIKGPELLTMWFGESEA 95
Cdd:cd19503    1 DIGGLDEQIASLKELIELPLKYPELFRALGLKPPRGVLLHGPPGTGKTLLARAVANEAGANFLSISGPSIVSKYLGESEK 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 185177972  96 NVREIFDKARQAAPCVLFFDELDSIAKARggnIGDGGGAADRVINQILTEMDGMSTKKNVFIIGATNRPDIIDPAILRPG 175
Cdd:cd19503   81 NLREIFEEARSHAPSIIFIDEIDALAPKR---EEDQREVERRVVAQLLTLMDGMSSRGKVVVIAATNRPDAIDPALRRPG 157

                 ....*...
gi 185177972 176 RLDQLIYI 183
Cdd:cd19503  158 RFDREVEI 165
RecA-like_PEX6_r2 cd19527
second of two ATPase domains of Peroxisomal biogenesis factor 6 (PEX6); PEX6(also known as ...
23-183 6.20e-71

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: 216.61  E-value: 6.20e-71
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 185177972  23 VKRELQELVQYPVEHPDKFLKfGMTPSKGVLFYGPPGCGKTLLAKAIANECQANFISIKGPELLTMWFGESEANVREIFD 102
Cdd:cd19527    1 VKKEILDTIQLPLEHPELFSS-GLRKRSGILLYGPPGTGKTLLAKAIATECSLNFLSVKGPELINMYIGESEANVREVFQ 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 185177972 103 KARQAAPCVLFFDELDSIAKARgGNIGDGGGAADRVINQILTEMDGMS-TKKNVFIIGATNRPDIIDPAILRPGRLDQLI 181
Cdd:cd19527   80 KARDAKPCVIFFDELDSLAPSR-GNSGDSGGVMDRVVSQLLAELDGMSsSGQDVFVIGATNRPDLLDPALLRPGRFDKLL 158

                 ..
gi 185177972 182 YI 183
Cdd:cd19527  159 YL 160
COG1223 COG1223
Predicted ATPase, AAA+ superfamily [General function prediction only];
14-236 8.97e-69

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


Pssm-ID: 440836 [Multi-domain]  Cd Length: 246  Bit Score: 213.98  E-value: 8.97e-69
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 185177972  14 WEDIGGLEDVKRELQELVQYpVEHPDKFLKFGMTPSKGVLFYGPPGCGKTLLAKAIANECQANFISIKGPELLTMWFGES 93
Cdd:COG1223    1 LDDVVGQEEAKKKLKLIIKE-LRRRENLRKFGLWPPRKILFYGPPGTGKTMLAEALAGELKLPLLTVRLDSLIGSYLGET 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 185177972  94 EANVREIFDKARQaAPCVLFFDELDSIAKARGGNIGDGGGAadRVINQILTEMDGMstKKNVFIIGATNRPDIIDPAILR 173
Cdd:COG1223   80 ARNLRKLFDFARR-APCVIFFDEFDAIAKDRGDQNDVGEVK--RVVNALLQELDGL--PSGSVVIAATNHPELLDSALWR 154
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 185177972 174 pgRLDQLIYIPLPDEKSRVAILKANLRKSPVAKDVDLEFLAKMTNGFSGADLTEICQRACKLA 236
Cdd:COG1223  155 --RFDEVIEFPLPDKEERKEILELNLKKFPLPFELDLKKLAKKLEGLSGADIEKVLKTALKKA 215
RecA-like_FtsH cd19501
ATP-dependent zinc metalloprotease FtsH; FtsH ATPase is a processive, ATP-dependent zinc ...
12-183 2.36e-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: 210.17  E-value: 2.36e-68
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 185177972  12 VTWEDIGGLEDVKRELQELVQYpVEHPDKFLKFGMTPSKGVLFYGPPGCGKTLLAKAIANECQANFISIKGPELLTMWFG 91
Cdd:cd19501    1 VTFKDVAGCEEAKEELKEVVEF-LKNPEKFTKLGAKIPKGVLLVGPPGTGKTLLAKAVAGEAGVPFFSISGSDFVEMFVG 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 185177972  92 ESEANVREIFDKARQAAPCVLFFDELDSIAKARGGNIGDGGGAADRVINQILTEMDGMSTKKNVFIIGATNRPDIIDPAI 171
Cdd:cd19501   80 VGASRVRDLFEQAKKNAPCIVFIDEIDAVGRKRGAGLGGGHDEREQTLNQLLVEMDGFESNTGVIVIAATNRPDVLDPAL 159
                        170
                 ....*....|..
gi 185177972 172 LRPGRLDQLIYI 183
Cdd:cd19501  160 LRPGRFDRQVYV 171
RecA-like_PAN_like cd19502
proteasome activating nucleotidase PAN and related proteasome subunits; This subfamily ...
13-181 1.51e-67

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: 208.35  E-value: 1.51e-67
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 185177972  13 TWEDIGGLEDVKRELQELVQYPVEHPDKFLKFGMTPSKGVLFYGPPGCGKTLLAKAIANECQANFISIKGPELLTMWFGE 92
Cdd:cd19502    1 TYEDIGGLDEQIREIREVVELPLKHPELFEELGIEPPKGVLLYGPPGTGKTLLAKAVANHTDATFIRVVGSELVQKYIGE 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 185177972  93 SEANVREIFDKARQAAPCVLFFDELDSIAKARGGNIGDGGGAADRVINQILTEMDGMSTKKNVFIIGATNRPDIIDPAIL 172
Cdd:cd19502   81 GARLVRELFEMAREKAPSIIFIDEIDAIGAKRFDSGTGGDREVQRTMLELLNQLDGFDPRGNIKVIMATNRPDILDPALL 160

                 ....*....
gi 185177972 173 RPGRLDQLI 181
Cdd:cd19502  161 RPGRFDRKI 169
RecA-like_PEX1_r2 cd19526
second of two ATPase domains of Peroxisomal biogenesis factor 1 (PEX1); PEX1(also known as ...
23-182 3.76e-67

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: 206.51  E-value: 3.76e-67
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 185177972  23 VKRELQELVQYPVEHPDKFLKFGMTPSKGVLFYGPPGCGKTLLAKAIANECQANFISIKGPELLTMWFGESEANVREIFD 102
Cdd:cd19526    1 VKKALEETIEWPSKYPKIFASSPLRLRSGILLYGPPGCGKTLLASAIASECGLNFISVKGPELLNKYIGASEQNVRDLFS 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 185177972 103 KARQAAPCVLFFDELDSIAKARggnIGDGGGAADRVINQILTEMDGMSTKKNVFIIGATNRPDIIDPAILRPGRLDQLIY 182
Cdd:cd19526   81 RAQSAKPCILFFDEFDSIAPKR---GHDSTGVTDRVVNQLLTQLDGVEGLDGVYVLAATSRPDLIDPALLRPGRLDKLVY 157
RecA-like_protease cd19481
proteases similar to RecA; RecA-like NTPases. This family includes the NTP binding domain of ...
23-183 3.85e-67

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: 206.75  E-value: 3.85e-67
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 185177972  23 VKRELQELVQYPVEHPdKFLKFGMTPSKGVLFYGPPGCGKTLLAKAIANECQANFISIKGPELLTMWFGESEANVREIFD 102
Cdd:cd19481    1 LKASLREAVEAPRRGS-RLRRYGLGLPKGILLYGPPGTGKTLLAKALAGELGLPLIVVKLSSLLSKYVGESEKNLRKIFE 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 185177972 103 KARQAAPCVLFFDELDSIAKARggNIGDGGGAADRVINQILTEMDGMSTKKNVFIIGATNRPDIIDPAILRPGRLDQLIY 182
Cdd:cd19481   80 RARRLAPCILFIDEIDAIGRKR--DSSGESGELRRVLNQLLTELDGVNSRSKVLVIAATNRPDLLDPALLRPGRFDEVIE 157

                 .
gi 185177972 183 I 183
Cdd:cd19481  158 F 158
PTZ00454 PTZ00454
26S protease regulatory subunit 6B-like protein; Provisional
8-236 9.11e-66

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


Pssm-ID: 240423 [Multi-domain]  Cd Length: 398  Bit Score: 211.16  E-value: 9.11e-66
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 185177972   8 EVPQVTWEDIGGLEDVKRELQELVQYPVEHPDKFLKFGMTPSKGVLFYGPPGCGKTLLAKAIANECQANFISIKGPELLT 87
Cdd:PTZ00454 138 EKPDVTYSDIGGLDIQKQEIREAVELPLTCPELYEQIGIDPPRGVLLYGPPGTGKTMLAKAVAHHTTATFIRVVGSEFVQ 217
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 185177972  88 MWFGESEANVREIFDKARQAAPCVLFFDELDSIAKARGGNIGDGGGAADRVINQILTEMDGMSTKKNVFIIGATNRPDII 167
Cdd:PTZ00454 218 KYLGEGPRMVRDVFRLARENAPSIIFIDEVDSIATKRFDAQTGADREVQRILLELLNQMDGFDQTTNVKVIMATNRADTL 297
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 185177972 168 DPAILRPGRLDQLIYIPLPDEKSRVAILKANLRKSPVAKDVDLEFLAKMTNGFSGADLTEICQRACKLA 236
Cdd:PTZ00454 298 DPALLRPGRLDRKIEFPLPDRRQKRLIFQTITSKMNLSEEVDLEDFVSRPEKISAADIAAICQEAGMQA 366
hflB PRK10733
ATP-dependent zinc metalloprotease FtsH;
11-236 4.40e-65

ATP-dependent zinc metalloprotease FtsH;


Pssm-ID: 182683 [Multi-domain]  Cd Length: 644  Bit Score: 215.67  E-value: 4.40e-65
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 185177972  11 QVTWEDIGGLEDVKRELQELVQYpVEHPDKFLKFGMTPSKGVLFYGPPGCGKTLLAKAIANECQANFISIKGPELLTMWF 90
Cdd:PRK10733 148 KTTFADVAGCDEAKEEVAELVEY-LREPSRFQKLGGKIPKGVLMVGPPGTGKTLLAKAIAGEAKVPFFTISGSDFVEMFV 226
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 185177972  91 GESEANVREIFDKARQAAPCVLFFDELDSIAKARGGNIGDGGGAADRVINQILTEMDGMSTKKNVFIIGATNRPDIIDPA 170
Cdd:PRK10733 227 GVGASRVRDMFEQAKKAAPCIIFIDEIDAVGRQRGAGLGGGHDEREQTLNQMLVEMDGFEGNEGIIVIAATNRPDVLDPA 306
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 185177972 171 ILRPGRLDQLIYIPLPDEKSRVAILKANLRKSPVAKDVDLEFLAKMTNGFSGADLTEICQRACKLA 236
Cdd:PRK10733 307 LLRPGRFDRQVVVGLPDVRGREQILKVHMRRVPLAPDIDAAIIARGTPGFSGADLANLVNEAALFA 372
pup_AAA TIGR03689
proteasome ATPase; In the Actinobacteria, as shown for Mycobacterium tuberculosis, some ...
8-207 1.74e-63

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


Pssm-ID: 200312 [Multi-domain]  Cd Length: 512  Bit Score: 208.41  E-value: 1.74e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 185177972    8 EVPQVTWEDIGGLEDVKRELQELVQYPVEHPDKFLKFGMTPSKGVLFYGPPGCGKTLLAKAIANE-CQ---------ANF 77
Cdd:TIGR03689 175 EVPDVTYADIGGLGSQIEQIRDAVELPFLHPELYREYGLKPPKGVLLYGPPGCGKTLIAKAVANSlAArigaegggkSYF 254
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 185177972   78 ISIKGPELLTMWFGESEANVREIFDKARQAA----PCVLFFDELDSIAKARGGNIGDGGGAAdrVINQILTEMDGMSTKK 153
Cdd:TIGR03689 255 LNIKGPELLNKYVGETERQIRLIFQRAREKAsegrPVIVFFDEMDSLFRTRGSGVSSDVETT--VVPQLLAEIDGVESLD 332
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 185177972  154 NVFIIGATNRPDIIDPAILRPGRLDQLIYIPLPDEKSRVAILKANLRKS-PVAKD 207
Cdd:TIGR03689 333 NVIVIGASNREDMIDPAILRPGRLDVKIRIERPDAEAAADIFAKYLTDDlPLPED 387
RecA-like_CDC48_r1-like cd19519
first of two ATPase domains of CDC48 and similar ATPase domains; CDC48 in yeast and p97 or VCP ...
16-184 5.33e-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: 196.50  E-value: 5.33e-63
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 185177972  16 DIGGLEDVKRELQELVQYPVEHPDKFLKFGMTPSKGVLFYGPPGCGKTLLAKAIANECQANFISIKGPELLTMWFGESEA 95
Cdd:cd19519    1 DIGGCRKQLAQIREMVELPLRHPELFKAIGIKPPRGILLYGPPGTGKTLIARAVANETGAFFFLINGPEIMSKLAGESES 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 185177972  96 NVREIFDKARQAAPCVLFFDELDSIAKARGGNIGDGGGaadRVINQILTEMDGMSTKKNVFIIGATNRPDIIDPAILRPG 175
Cdd:cd19519   81 NLRKAFEEAEKNAPAIIFIDEIDAIAPKREKTHGEVER---RIVSQLLTLMDGLKQRAHVIVMAATNRPNSIDPALRRFG 157

                 ....*....
gi 185177972 176 RLDQLIYIP 184
Cdd:cd19519  158 RFDREIDIG 166
cell_div_CdvC NF041006
cell division protein CdvC;
6-294 1.05e-60

cell division protein CdvC;


Pssm-ID: 468935 [Multi-domain]  Cd Length: 371  Bit Score: 197.26  E-value: 1.05e-60
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 185177972   6 VVEVPQVTWEDIGGLEDVKRELQELVQYPVEHPDKFlkfgmtP---SKGVLFYGPPGCGKTLLAKAIANECQANFISIKG 82
Cdd:NF041006  94 VKEKPKVTFSDIVGLEDVKEALKEAIVYPSKRPDLF------PlgwPRGILLYGPPGCGKTMLAAAVANEIDSEFIHVDA 167
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 185177972  83 PELLTMWFGESEANVREIFDKARQAA-----PCVLFFDELDSIAKARGGNIGDGGgaadRVINQILTEMDGM---STKKN 154
Cdd:NF041006 168 ASIMSKWLGEAEKNVAKIFKKAREKSkeegkPAIIFIDEIDALLGVYSSEVGGEV----RVRNQFLKEMDGLqdkSENYH 243
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 185177972 155 VFIIGATNRPDIIDPAILRpgRLDQLIYIPLPDEKSRVAILKANLRKSPVAKDVDLEFLAKMTNGFSGADLTEICQRAck 234
Cdd:NF041006 244 VYVIGATNKPWRLDEPFLR--RFQKRIYIPLPDREQRLELLKYYTSKIKLENDVDLDELAEMTEGYTASDIRDIVQAA-- 319
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 185177972 235 lairesieseirrerERQTNPSAMEVEEDDPVPeIRRDHFEEAMRFARRSVSDNDIRKYE 294
Cdd:NF041006 320 ---------------HMRVVKEMFEKGLGEPRP-ITMEDFKEVLKIRKPSVNQEMLKAYE 363
PTZ00361 PTZ00361
26 proteosome regulatory subunit 4-like protein; Provisional
6-236 1.36e-59

26 proteosome regulatory subunit 4-like protein; Provisional


Pssm-ID: 185575 [Multi-domain]  Cd Length: 438  Bit Score: 196.15  E-value: 1.36e-59
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 185177972   6 VVEVPQVTWEDIGGLEDVKRELQELVQYPVEHPDKFLKFGMTPSKGVLFYGPPGCGKTLLAKAIANECQANFISIKGPEL 85
Cdd:PTZ00361 174 VDKAPLESYADIGGLEQQIQEIKEAVELPLTHPELYDDIGIKPPKGVILYGPPGTGKTLLAKAVANETSATFLRVVGSEL 253
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 185177972  86 LTMWFGESEANVREIFDKARQAAPCVLFFDELDSIAKARGGNIGDGGGAADRVINQILTEMDGMSTKKNVFIIGATNRPD 165
Cdd:PTZ00361 254 IQKYLGDGPKLVRELFRVAEENAPSIVFIDEIDAIGTKRYDATSGGEKEIQRTMLELLNQLDGFDSRGDVKVIMATNRIE 333
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 185177972 166 IIDPAILRPGRLDQLIYIPLPDEKSRVAILKANLRKSPVAKDVDLEFLAKMTNGFSGADLTEICQRACKLA 236
Cdd:PTZ00361 334 SLDPALIRPGRIDRKIEFPNPDEKTKRRIFEIHTSKMTLAEDVDLEEFIMAKDELSGADIKAICTEAGLLA 404
RecA-like_NVL_r1-like cd19518
first of two ATPase domains of NVL (nuclear VCP-like protein) and similar ATPase domains; NVL ...
16-181 3.80e-58

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: 184.15  E-value: 3.80e-58
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 185177972  16 DIGGLEDVKRELQELVQYPVEHPDKFLKFGMTPSKGVLFYGPPGCGKTLLAKAIANECQANFISIKGPELLTMWFGESEA 95
Cdd:cd19518    1 DIGGMDSTLKELCELLIHPILPPEYFQHLGVEPPRGVLLHGPPGCGKTMLANAIAGELKVPFLKISATEIVSGVSGESEE 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 185177972  96 NVREIFDKARQAAPCVLFFDELDSIAKARGGNIGDGGGaadRVINQILTEMDGMSTKKN----VFIIGATNRPDIIDPAI 171
Cdd:cd19518   81 KIRELFDQAISNAPCIVFIDEIDAITPKRESAQREMER---RIVSQLLTCMDELNNEKTaggpVLVIGATNRPDSLDPAL 157
                        170
                 ....*....|
gi 185177972 172 LRPGRLDQLI 181
Cdd:cd19518  158 RRAGRFDREI 167
AAA pfam00004
ATPase family associated with various cellular activities (AAA); AAA family proteins often ...
52-185 2.57e-57

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: 180.48  E-value: 2.57e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 185177972   52 VLFYGPPGCGKTLLAKAIANECQANFISIKGPELLTMWFGESEANVREIFDKARQAAPCVLFFDELDSIAKARggnIGDG 131
Cdd:pfam00004   1 LLLYGPPGTGKTTLAKAVAKELGAPFIEISGSELVSKYVGESEKRLRELFEAAKKLAPCVIFIDEIDALAGSR---GSGG 77
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 185177972  132 GGAADRVINQILTEMDGMSTKK-NVFIIGATNRPDIIDPAILrpGRLDQLIYIPL 185
Cdd:pfam00004  78 DSESRRVVNQLLTELDGFTSSNsKVIVIAATNRPDKLDPALL--GRFDRIIEFPL 130
RecA-like_VPS4-like cd19509
ATPase domain of VPS4, ATAD1, K, KTNA1, Spastin, FIGL-1 and similar ATPase domains; This ...
17-183 8.61e-54

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: 172.92  E-value: 8.61e-54
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 185177972  17 IGGLEDVKRELQELVQYPVEHPDKFlKFGMTPSKGVLFYGPPGCGKTLLAKAIANECQANFISIKGPELLTMWFGESEAN 96
Cdd:cd19509    1 IAGLDDAKEALKEAVILPSLRPDLF-PGLRGPPRGILLYGPPGTGKTLLARAVASESGSTFFSISASSLVSKWVGESEKI 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 185177972  97 VREIFDKARQAAPCVLFFDELDSIAKARggnIGDGGGAADRVINQILTEMDGMSTKKN--VFIIGATNRPDIIDPAILRp 174
Cdd:cd19509   80 VRALFALARELQPSIIFIDEIDSLLSER---GSGEHEASRRVKTEFLVQMDGVLNKPEdrVLVLGATNRPWELDEAFLR- 155

                 ....*....
gi 185177972 175 gRLDQLIYI 183
Cdd:cd19509  156 -RFEKRIYI 163
RecA-like_Yta7-like cd19517
ATPase domain of Saccharomyces cerevisiae Yta7 and similar ATPase domains; Saccharomyces ...
16-182 4.72e-50

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


Pssm-ID: 410925 [Multi-domain]  Cd Length: 170  Bit Score: 163.45  E-value: 4.72e-50
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 185177972  16 DIGGLEDVKRELQELVQYPVEHPDKFLKFGMTPSKGVLFYGPPGCGKTLLAKAIANEC-----QANFISIKGPELLTMWF 90
Cdd:cd19517    1 DIGGLSHYINQLKEMVFFPLLYPEVFAKFKITPPRGVLFHGPPGTGKTLMARALAAECskggqKVSFFMRKGADCLSKWV 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 185177972  91 GESEANVREIFDKARQAAPCVLFFDELDSIAKARGGNIGDGGGAadrVINQILTEMDGMSTKKNVFIIGATNRPDIIDPA 170
Cdd:cd19517   81 GEAERQLRLLFEEAYRMQPSIIFFDEIDGLAPVRSSKQEQIHAS---IVSTLLALMDGLDNRGQVVVIGATNRPDALDPA 157
                        170
                 ....*....|..
gi 185177972 171 ILRPGRLDQLIY 182
Cdd:cd19517  158 LRRPGRFDREFY 169
RecA-like_ATAD1 cd19520
ATPase domain of ATPase family AAA domain-containing protein 1 and similar ATPase domains; ...
16-173 1.46e-46

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: 154.12  E-value: 1.46e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 185177972  16 DIGGLEDVKRELQELVQYPVEHPDKFLKFGMT-PSKGVLFYGPPGCGKTLLAKAIANECQANFISIKGPELLTMWFGESE 94
Cdd:cd19520    1 DIGGLDEVITELKELVILPLQRPELFDNSRLLqPPKGVLLYGPPGCGKTMLAKATAKEAGARFINLQVSSLTDKWYGESQ 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 185177972  95 ANVREIFDKARQAAPCVLFFDELDSIAKARggnIGDGGGAADRVINQILTEMDGMSTKKN--VFIIGATNRPDIIDPAIL 172
Cdd:cd19520   81 KLVAAVFSLASKLQPSIIFIDEIDSFLRQR---SSTDHEATAMMKAEFMSLWDGLSTDGNcrVIVMGATNRPQDLDEAIL 157

                 .
gi 185177972 173 R 173
Cdd:cd19520  158 R 158
RecA-like_VPS4 cd19521
ATPase domain of vacuolar protein sorting-associated protein 4; Vacuolar protein ...
10-183 7.10e-43

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


Pssm-ID: 410929 [Multi-domain]  Cd Length: 170  Bit Score: 145.00  E-value: 7.10e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 185177972  10 PQVTWEDIGGLEDVKRELQELVQYPVEHPDKFlKFGMTPSKGVLFYGPPGCGKTLLAKAIANECQANFISIKGPELLTMW 89
Cdd:cd19521    2 PNVKWEDVAGLEGAKEALKEAVILPVKFPHLF-TGNRKPWSGILLYGPPGTGKSYLAKAVATEANSTFFSVSSSDLVSKW 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 185177972  90 FGESEANVREIFDKARQAAPCVLFFDELDSIAKARggnIGDGGGAADRVINQILTEMDGMSTKKN-VFIIGATNRPDIID 168
Cdd:cd19521   81 MGESEKLVKQLFAMARENKPSIIFIDEVDSLCGTR---GEGESEASRRIKTELLVQMNGVGNDSQgVLVLGATNIPWQLD 157
                        170
                 ....*....|....*
gi 185177972 169 PAILRpgRLDQLIYI 183
Cdd:cd19521  158 SAIRR--RFEKRIYI 170
RecA-like_Figl-1 cd19525
ATPase domain of Fidgetin-Like 1 (FIGL-1); FIGL-1 may participate in DNA repair in the nucleus; ...
10-183 1.05e-41

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: 142.43  E-value: 1.05e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 185177972  10 PQVTWEDIGGLEDVKRELQELVQYPVEHPDKFLKFgMTPSKGVLFYGPPGCGKTLLAKAIANECQANFISIKGPELLTMW 89
Cdd:cd19525   17 PPINWADIAGLEFAKKTIKEIVVWPMLRPDIFTGL-RGPPKGILLFGPPGTGKTLIGKCIASQSGATFFSISASSLTSKW 95
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 185177972  90 FGESEANVREIFDKARQAAPCVLFFDELDSIAKARggnIGDGGGAADRVINQILTEMDGMST--KKNVFIIGATNRPDII 167
Cdd:cd19525   96 VGEGEKMVRALFSVARCKQPAVIFIDEIDSLLSQR---GEGEHESSRRIKTEFLVQLDGATTssEDRILVVGATNRPQEI 172
                        170
                 ....*....|....*.
gi 185177972 168 DPAILRpgRLDQLIYI 183
Cdd:cd19525  173 DEAARR--RLVKRLYI 186
RecA-like_KTNA1 cd19522
Katanin p60 ATPase-containing subunit A1; Katanin p60 ATPase-containing subunit A1 (KTNA1) is ...
16-183 3.99e-41

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


Pssm-ID: 410930 [Multi-domain]  Cd Length: 170  Bit Score: 140.50  E-value: 3.99e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 185177972  16 DIGGLEDVKRELQELVQYPVEHPDkFLKFGMTPSKGVLFYGPPGCGKTLLAKAIANECQANFISIKGPELLTMWFGESEA 95
Cdd:cd19522    1 DIADLEEAKKLLEEAVVLPMWMPE-FFKGIRRPWKGVLMVGPPGTGKTLLAKAVATECGTTFFNVSSSTLTSKYRGESEK 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 185177972  96 NVREIFDKARQAAPCVLFFDELDSIAKARggNIGDGGGAADRVINQILTEMDGMS-------TKKNVFIIGATNRPDIID 168
Cdd:cd19522   80 LVRLLFEMARFYAPTTIFIDEIDSICSRR--GTSEEHEASRRVKSELLVQMDGVGgasenddPSKMVMVLAATNFPWDID 157
                        170
                 ....*....|....*
gi 185177972 169 PAILRpgRLDQLIYI 183
Cdd:cd19522  158 EALRR--RLEKRIYI 170
RecA-like_NSF-SEC18_r1-like cd19504
first of two ATPase domains of NSF and SEC18, and similar ATPase domains; ...
43-178 1.79e-36

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: 128.76  E-value: 1.79e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 185177972  43 KFGMTPSKGVLFYGPPGCGKTLLAKAIANECQANFISI-KGPELLTMWFGESEANVREIFDKARQ--------AAPCVLF 113
Cdd:cd19504   29 QLGCKHVKGILLYGPPGTGKTLMARQIGKMLNAREPKIvNGPEILNKYVGESEANIRKLFADAEEeqrrlganSGLHIII 108
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 185177972 114 FDELDSIAKARGGNIGDGGgAADRVINQILTEMDGMSTKKNVFIIGATNRPDIIDPAILRPGRLD 178
Cdd:cd19504  109 FDEIDAICKQRGSMAGSTG-VHDTVVNQLLSKIDGVEQLNNILVIGMTNRKDLIDEALLRPGRLE 172
RecA-like_spastin cd19524
ATPase domain of spastin; Spastin is an ATP-dependent microtubule-severing protein involved in ...
16-183 2.30e-36

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: 128.04  E-value: 2.30e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 185177972  16 DIGGLEDVKRELQELVQYPVEHPDKFLKFgMTPSKGVLFYGPPGCGKTLLAKAIANECQANFISIKGPELLTMWFGESEA 95
Cdd:cd19524    1 DIAGQDLAKQALQEMVILPSLRPELFTGL-RAPARGLLLFGPPGNGKTMLAKAVAAESNATFFNISAASLTSKYVGEGEK 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 185177972  96 NVREIFDKARQAAPCVLFFDELDSIAKARggnIGDGGGAADRVINQILTEMDGMSTKKN--VFIIGATNRPDIIDPAILR 173
Cdd:cd19524   80 LVRALFAVARELQPSIIFIDEVDSLLSER---SEGEHEASRRLKTEFLIEFDGVQSNGDdrVLVMGATNRPQELDDAVLR 156
                        170
                 ....*....|
gi 185177972 174 pgRLDQLIYI 183
Cdd:cd19524  157 --RFTKRVYV 164
AAA cd00009
The AAA+ (ATPases Associated with a wide variety of cellular Activities) superfamily ...
18-185 1.95e-32

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: 117.25  E-value: 1.95e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 185177972  18 GGLEDVKRELQELVQYPvehpdkflkfgmtPSKGVLFYGPPGCGKTLLAKAIANEC---QANFISIKGPELLTMWFGESE 94
Cdd:cd00009    1 VGQEEAIEALREALELP-------------PPKNLLLYGPPGTGKTTLARAIANELfrpGAPFLYLNASDLLEGLVVAEL 67
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 185177972  95 AN---VREIFDKARQAAPCVLFFDELDSIAKArggnigdgggAADRVINQILTEMDGMSTKKNVFIIGATNRPDIIDPAI 171
Cdd:cd00009   68 FGhflVRLLFELAEKAKPGVLFIDEIDSLSRG----------AQNALLRVLETLNDLRIDRENVRVIGATNRPLLGDLDR 137
                        170
                 ....*....|....
gi 185177972 172 LRPGRLDQLIYIPL 185
Cdd:cd00009  138 ALYDRLDIRIVIPL 151
ycf46 CHL00195
Ycf46; Provisional
12-230 1.31e-27

Ycf46; Provisional


Pssm-ID: 177094 [Multi-domain]  Cd Length: 489  Bit Score: 111.65  E-value: 1.31e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 185177972  12 VTWEDIGGLEDVKRELQelvQYPVEHPDKFLKFGMTPSKGVLFYGPPGCGKTLLAKAIANECQANFISIKGPELLTMWFG 91
Cdd:CHL00195 225 EKISDIGGLDNLKDWLK---KRSTSFSKQASNYGLPTPRGLLLVGIQGTGKSLTAKAIANDWQLPLLRLDVGKLFGGIVG 301
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 185177972  92 ESEANVREIFDKARQAAPCVLFFDELDsiaKA-RGGNIGDGGGAADRVINQILTemdGMSTKKN-VFIIGATNRPDIIDP 169
Cdd:CHL00195 302 ESESRMRQMIRIAEALSPCILWIDEID---KAfSNSESKGDSGTTNRVLATFIT---WLSEKKSpVFVVATANNIDLLPL 375
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 185177972 170 AILRPGRLDQLIYIPLPDEKSRVAILKANLRKS-PVA-KDVDLEFLAKMTNGFSGAdltEICQ 230
Cdd:CHL00195 376 EILRKGRFDEIFFLDLPSLEEREKIFKIHLQKFrPKSwKKYDIKKLSKLSNKFSGA---EIEQ 435
RecA-like_Ycf46-like cd19507
ATPase domain of Ycf46 and similar ATPase domains; Ycf46 may play a role in the regulation of ...
16-183 1.95e-25

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: 99.37  E-value: 1.95e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 185177972  16 DIGGLEDVKRELQELVQypvEHPDKFLKFGMTPSKGVLFYGPPGCGKTLLAKAIANECQANFISIKGPELLTMWFGESEA 95
Cdd:cd19507    1 DVGGLDNLKDWLKKRKA---AFSKQASAYGLPTPKGLLLVGIQGTGKSLTAKAIAGVWQLPLLRLDMGRLFGGLVGESES 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 185177972  96 NVREIFDKARQAAPCVLFFDELDSiAKARGGNIGDGGGAAdRVINQILTEMDgmSTKKNVFIIGATNRPDIIDPAILRPG 175
Cdd:cd19507   78 RLRQMIQTAEAIAPCVLWIDEIEK-GFSNADSKGDSGTSS-RVLGTFLTWLQ--EKKKPVFVVATANNVQSLPPELLRKG 153

                 ....*...
gi 185177972 176 RLDQLIYI 183
Cdd:cd19507  154 RFDEIFFV 161
RecA-like_fidgetin cd19523
ATPase domain of fidgetin; Fidgetin (FIGN) is a ATP-dependent microtubule severing protein. ...
16-173 4.70e-24

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: 95.72  E-value: 4.70e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 185177972  16 DIGGLEDVKRELQELVQYPVEHPDKFLKFgMTPSKGVLFYGPPGCGKTLLAKAIANECQANFISIKGPELLTMWFGESEA 95
Cdd:cd19523    1 DIAGLGALKAAIKEEVLWPLLRPDAFSGL-LRLPRSILLFGPRGTGKTLLGRCLASQLGATFLRLRGSTLVAKWAGEGEK 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 185177972  96 NVREIFDKARQAAPCVLFFDELDSIAKARggniGDGGGAADRVINQILTEMDGM--STKKNVFIIGATNRPDIIDPAILR 173
Cdd:cd19523   80 ILQASFLAARCRQPSVLFISDLDALLSSQ----DDEASPVGRLQVELLAQLDGVlgSGEDGVLVVCTTSKPEEIDESLRR 155
AAA smart00382
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ...
48-187 6.81e-22

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: 89.35  E-value: 6.81e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 185177972    48 PSKGVLFYGPPGCGKTLLAKAIANECQAN---FISIKGPELL--------------TMWFGESEANVREIFDKARQAAPC 110
Cdd:smart00382   1 PGEVILIVGPPGSGKTTLARALARELGPPgggVIYIDGEDILeevldqllliivggKKASGSGELRLRLALALARKLKPD 80
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 185177972   111 VLFFDELDSIAKARggnigdggGAADRVINQILTEMDGMSTKKNVFIIGATNRPDIIDPAILRPgRLDQLIYIPLPD 187
Cdd:smart00382  81 VLILDEITSLLDAE--------QEALLLLLEELRLLLLLKSEKNLTVILTTNDEKDLGPALLRR-RFDRRIVLLLIL 148
RecA-like_Pch2-like cd19508
ATPase domain of Pachytene checkpoint 2 (Pch2) and similar ATPase domains; Pch2 (known as ...
52-183 9.43e-16

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


Pssm-ID: 410916 [Multi-domain]  Cd Length: 199  Bit Score: 74.02  E-value: 9.43e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 185177972  52 VLFYGPPGCGKTLLAKAIANEC---------QANFISIKGPELLTMWFGESEANVREIFDK------ARQAAPCVLfFDE 116
Cdd:cd19508   55 VLLHGPPGTGKTSLCKALAQKLsirlssryrYGQLIEINSHSLFSKWFSESGKLVTKMFQKiqelidDKDALVFVL-IDE 133
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 185177972 117 LDSIAKARGGNIGDGGGA-ADRVINQILTEMDGMSTKKNVFIIGATNRPDIIDPAILrpGRLDQLIYI 183
Cdd:cd19508  134 VESLAAARSASSSGTEPSdAIRVVNAVLTQIDRIKRYHNNVILLTSNLLEKIDVAFV--DRADIKQYI 199
RecA-like_Ycf2 cd19505
ATPase domain of plant YCF2; Ycf2 is a chloroplast ATPase which has an essential function; ...
42-183 3.11e-12

ATPase domain of plant YCF2; Ycf2 is a chloroplast ATPase which has an essential function; however, its function remains unclear. The gene encoding YCF2 is the largest known plastid gene in angiosperms and has been used to predict phylogenetic relationships. This subfamily belongs to the RecA-like NTPase family which includes the NTP binding domain of F1 and V1 H(+)ATPases, DnaB and related helicases as well as bacterial RecA and related eukaryotic and archaeal recombinases. The RecA-like NTPase family also includes bacterial conjugation proteins and related DNA transfer proteins involved in type II and type IV secretion.


Pssm-ID: 410913 [Multi-domain]  Cd Length: 161  Bit Score: 63.55  E-value: 3.11e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 185177972  42 LKFGMTPSKGVLFYGPPGCGKTLLAKAIANECQANFISIKGPELLTMWF--------------GESEANVREIFDKARQA 107
Cdd:cd19505    5 LRLGLSPSKGILLIGSIETGRSYLIKSLAANSYVPLIRISLNKLLYNKPdfgnddwidgmlilKESLHRLNLQFELAKAM 84
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 185177972 108 APCVLFFD---ELDsIAKARGGNIGDGGGAADRVINQILTEMDGMSTKKNVfIIGATNRPDIIDPAILRPGRLDQLIYI 183
Cdd:cd19505   85 SPCIIWIPnihELN-VNRSTQNLEEDPKLLLGLLLNYLSRDFEKSSTRNIL-VIASTHIPQKVDPALIAPNRLDTCINI 161
RecA-like_BCS1 cd19510
Mitochondrial chaperone BCS1; Mitochondrial chaperone BCS1 is necessary for the assembly of ...
50-183 9.20e-12

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: 61.98  E-value: 9.20e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 185177972  50 KGVLFYGPPGCGKTLLAKAIANECQANF--ISIKGPELltmwfgeSEANVREIFDKARQAApcVLFFDELDSIAKARGGN 127
Cdd:cd19510   24 RGYLLYGPPGTGKSSFIAALAGELDYDIcdLNLSEVVL-------TDDRLNHLLNTAPKQS--IILLEDIDAAFESREHN 94
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 185177972 128 IGDGGGAAD--RV-INQILTEMDGMSTKKNVFIIGATNRPDIIDPAILRPGRLDQLIYI 183
Cdd:cd19510   95 KKNPSAYGGlsRVtFSGLLNALDGVASSEERIVFMTTNHIERLDPALIRPGRVDMKIYM 153
RarA COG2256
Replication-associated recombination protein RarA (DNA-dependent ATPase) [Replication, ...
25-116 8.51e-11

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


Pssm-ID: 441857 [Multi-domain]  Cd Length: 439  Bit Score: 62.00  E-value: 8.51e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 185177972  25 RELQELV-QypvEH---PDKFL----KFGMTPSkgVLFYGPPGCGKTLLAKAIANECQANFISIKGpelltmwfgeSEAN 96
Cdd:COG2256   22 RTLDEVVgQ---EHllgPGKPLrraiEAGRLSS--MILWGPPGTGKTTLARLIANATDAEFVALSA----------VTSG 86
                         90       100
                 ....*....|....*....|....*..
gi 185177972  97 V---REIFDKARQAA----PCVLFFDE 116
Cdd:COG2256   87 VkdiREVIEEARERRaygrRTILFVDE 113
PRK13342 PRK13342
recombination factor protein RarA; Reviewed
40-116 2.11e-10

recombination factor protein RarA; Reviewed


Pssm-ID: 237355 [Multi-domain]  Cd Length: 413  Bit Score: 60.87  E-value: 2.11e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 185177972  40 KFLKFGMTPSkgVLFYGPPGCGKTLLAKAIANECQANFISIKGPElltmwfgESEANVREIFDKARQAA----PCVLFFD 115
Cdd:PRK13342  29 RMIEAGRLSS--MILWGPPGTGKTTLARIIAGATDAPFEALSAVT-------SGVKDLREVIEEARQRRsagrRTILFID 99

                 .
gi 185177972 116 E 116
Cdd:PRK13342 100 E 100
RecA-like_ATAD3-like cd19512
ATPase domains of ATPase AAA-domain protein 3A (ATAD3A), -3B, and -3C, and similar ATPase ...
48-181 1.10e-09

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


Pssm-ID: 410920 [Multi-domain]  Cd Length: 150  Bit Score: 56.00  E-value: 1.10e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 185177972  48 PSKGVLFYGPPGCGKTLLAKAIANECQANFISIKGPELLTMWfGESEANVREIFDKARQAAP-CVLFFDELDSIAKARGG 126
Cdd:cd19512   21 LYRNILFYGPPGTGKTLFAKKLALHSGMDYAIMTGGDVAPMG-REGVTAIHKVFDWANTSRRgLLLFVDEADAFLRKRST 99
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 185177972 127 NIGDGGGAAdrVINQILTEMDGMSTKknVFIIGATNRPDIIDPAIlrPGRLDQLI 181
Cdd:cd19512  100 EKISEDLRA--ALNAFLYRTGEQSNK--FMLVLASNQPEQFDWAI--NDRIDEMV 148
AAA_lid_3 pfam17862
AAA+ lid domain; This entry represents the alpha helical AAA+ lid domain that is found to the ...
207-236 5.71e-08

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: 48.30  E-value: 5.71e-08
                          10        20        30
                  ....*....|....*....|....*....|
gi 185177972  207 DVDLEFLAKMTNGFSGADLTEICQRACKLA 236
Cdd:pfam17862   1 DVDLEELAERTEGFSGADLEALCREAALAA 30
RuvB_N pfam05496
Holliday junction DNA helicase RuvB P-loop domain; The RuvB protein makes up part of the ...
52-85 2.40e-07

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: 49.42  E-value: 2.40e-07
                          10        20        30
                  ....*....|....*....|....*....|....
gi 185177972   52 VLFYGPPGCGKTLLAKAIANECQANFISIKGPEL 85
Cdd:pfam05496  36 VLLYGPPGLGKTTLANIIANEMGVNIRITSGPAI 69
ruvB PRK00080
Holliday junction branch migration DNA helicase RuvB;
52-85 3.07e-07

Holliday junction branch migration DNA helicase RuvB;


Pssm-ID: 234619 [Multi-domain]  Cd Length: 328  Bit Score: 50.90  E-value: 3.07e-07
                         10        20        30
                 ....*....|....*....|....*....|....
gi 185177972  52 VLFYGPPGCGKTLLAKAIANECQANFISIKGPEL 85
Cdd:PRK00080  54 VLLYGPPGLGKTTLANIIANEMGVNIRITSGPAL 87
T7SS_EccA TIGR03922
type VII secretion AAA-ATPase EccA; This model represents the AAA family ATPase, EccA, of the ...
19-165 3.14e-07

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: 51.38  E-value: 3.14e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 185177972   19 GLEDVKRELqELVQYPVEHPDKFLKFGMT---PSKGVLFYGPPGCGKTLLAKAIANE-C------QANFISIKGPELLTM 88
Cdd:TIGR03922 280 GLERVKRQV-AALKSSTAMALARAERGLPvaqTSNHMLFAGPPGTGKTTIARVVAKIyCglgvlrKPLVREVSRADLIGQ 358
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 185177972   89 WFGESEANVREIFDKARQAapcVLFFDELDSIAKARGGNIGDGGGAAdrvINQILTEMDGMSTKKNVFIIGATNRPD 165
Cdd:TIGR03922 359 YIGESEAKTNEIIDSALGG---VLFLDEAYTLVETGYGQKDPFGLEA---IDTLLARMENDRDRLVVIGAGYRKDLD 429
PRK04195 PRK04195
replication factor C large subunit; Provisional
13-72 1.30e-06

replication factor C large subunit; Provisional


Pssm-ID: 235250 [Multi-domain]  Cd Length: 482  Bit Score: 49.53  E-value: 1.30e-06
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 185177972  13 TWEDIGGLEDVKRELQELVqypvehpDKFLKfgMTPSKGVLFYGPPGCGKTLLAKAIANE 72
Cdd:PRK04195  12 TLSDVVGNEKAKEQLREWI-------ESWLK--GKPKKALLLYGPPGVGKTSLAHALAND 62
RuvB COG2255
Holliday junction resolvasome RuvABC, ATP-dependent DNA helicase subunit RuvB [Replication, ...
52-83 2.31e-06

Holliday junction resolvasome RuvABC, ATP-dependent DNA helicase subunit RuvB [Replication, recombination and repair];


Pssm-ID: 441856 [Multi-domain]  Cd Length: 337  Bit Score: 48.15  E-value: 2.31e-06
                         10        20        30
                 ....*....|....*....|....*....|..
gi 185177972  52 VLFYGPPGCGKTLLAKAIANECQANFISIKGP 83
Cdd:COG2255   57 VLLYGPPGLGKTTLAHIIANEMGVNIRITSGP 88
ruvB TIGR00635
Holliday junction DNA helicase, RuvB subunit; All proteins in this family for which functions ...
13-85 4.27e-06

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: 47.29  E-value: 4.27e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 185177972   13 TWEDIGGLEDVKRELQ------ELVQYPVEHpdkflkfgmtpskgVLFYGPPGCGKTLLAKAIANECQANFISIKGPEL 85
Cdd:TIGR00635   2 LLAEFIGQEKVKEQLQlfieaaKMRQEALDH--------------LLLYGPPGLGKTTLAHIIANEMGVNLKITSGPAL 66
DnaC COG1484
DNA replication protein DnaC [Replication, recombination and repair];
50-77 2.43e-05

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


Pssm-ID: 441093 [Multi-domain]  Cd Length: 242  Bit Score: 44.77  E-value: 2.43e-05
                         10        20
                 ....*....|....*....|....*....
gi 185177972  50 KGVLFYGPPGCGKTLLAKAIANE-CQANF 77
Cdd:COG1484  100 ENLILLGPPGTGKTHLAIALGHEaCRAGY 128
PRK13341 PRK13341
AAA family ATPase;
53-80 3.12e-05

AAA family ATPase;


Pssm-ID: 237354 [Multi-domain]  Cd Length: 725  Bit Score: 45.43  E-value: 3.12e-05
                         10        20
                 ....*....|....*....|....*...
gi 185177972  53 LFYGPPGCGKTLLAKAIANECQANFISI 80
Cdd:PRK13341  56 ILYGPPGVGKTTLARIIANHTRAHFSSL 83
AAA_2 pfam07724
AAA domain (Cdc48 subfamily); This Pfam entry includes some of the AAA proteins not detected ...
52-122 3.28e-05

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: 43.34  E-value: 3.28e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 185177972   52 VLFYGPPGCGKTLLAKAIANE---CQANFISIKGPELL-----TMWFGESEANVR-----EIFDKARQAAPCVLFFDELD 118
Cdd:pfam07724   6 FLFLGPTGVGKTELAKALAELlfgDERALIRIDMSEYMeehsvSRLIGAPPGYVGyeeggQLTEAVRRKPYSIVLIDEIE 85

                  ....
gi 185177972  119 SIAK 122
Cdd:pfam07724  86 KAHP 89
Vps4_C pfam09336
Vps4 C terminal oligomerization domain; This domain is found at the C terminal of ATPase ...
256-298 6.93e-05

Vps4 C terminal oligomerization domain; This domain is found at the C terminal of ATPase proteins involved in vacuolar sorting. It forms an alpha helix structure and is required for oligomerization.


Pssm-ID: 462762 [Multi-domain]  Cd Length: 61  Bit Score: 40.17  E-value: 6.93e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 185177972  256 SAMEVEEDD-PVPEIRRDHFEEAMRFARRSVSDNDIRKYEMFAQ 298
Cdd:pfam09336  15 TWMDIPSDKlLEPPVTMKDFLKALKSSRPTVSKEDLEKYEEFTK 58
TIP49 COG1224
DNA helicase TIP49, TBP-interacting protein [Transcription];
40-95 1.22e-04

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


Pssm-ID: 440837 [Multi-domain]  Cd Length: 452  Bit Score: 43.42  E-value: 1.22e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 185177972  40 KFLKFGMTPSKGVLFYGPPGCGKTLLAKAIANECQAN--FISIKGPELLTMWFGESEA 95
Cdd:COG1224   55 KMIKEGKMAGKGILIVGPPGTGKTALAVAIARELGEDtpFVAISGSEIYSAELKKTEF 112
PRK08116 PRK08116
hypothetical protein; Validated
49-72 1.81e-04

hypothetical protein; Validated


Pssm-ID: 236153 [Multi-domain]  Cd Length: 268  Bit Score: 42.32  E-value: 1.81e-04
                         10        20
                 ....*....|....*....|....
gi 185177972  49 SKGVLFYGPPGCGKTLLAKAIANE 72
Cdd:PRK08116 114 NVGLLLWGSVGTGKTYLAACIANE 137
ycf2 CHL00206
Ycf2; Provisional
42-183 3.26e-04

Ycf2; Provisional


Pssm-ID: 214396 [Multi-domain]  Cd Length: 2281  Bit Score: 42.21  E-value: 3.26e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 185177972   42 LKFGMTPSKGVLFYGPPGCGKTLLAKAIANECQANFISI----------KG-------------------------PELL 86
Cdd:CHL00206 1623 LRLALSPSRGILVIGSIGTGRSYLVKYLATNSYVPFITVflnkfldnkpKGfliddididdsddiddsddidrdldTELL 1702
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 185177972   87 TMWFG--------ESEANVREIFDKARQAAPCVLFFD---ELDsiakarggNIGDGGGAADRVINQILTEMDGMSTKKNV 155
Cdd:CHL00206 1703 TMMNAltmdmmpkIDRFYITLQFELAKAMSPCIIWIPnihDLN--------VNESNYLSLGLLVNSLSRDCERCSTRNIL 1774
                         170       180
                  ....*....|....*....|....*...
gi 185177972  156 fIIGATNRPDIIDPAILRPGRLDQLIYI 183
Cdd:CHL00206 1775 -VIASTHIPQKVDPALIAPNKLNTCIKI 1801
RNA_helicase pfam00910
RNA helicase; This family includes RNA helicases thought to be involved in duplex unwinding ...
52-72 4.40e-04

RNA helicase; This family includes RNA helicases thought to be involved in duplex unwinding during viral RNA replication. Members of this family are found in a variety of single stranded RNA viruses.


Pssm-ID: 459992  Cd Length: 102  Bit Score: 38.74  E-value: 4.40e-04
                          10        20
                  ....*....|....*....|.
gi 185177972   52 VLFYGPPGCGKTLLAKAIANE 72
Cdd:pfam00910   1 IWLYGPPGCGKSTLAKYLARA 21
PRK06835 PRK06835
DNA replication protein DnaC; Validated
47-72 5.33e-04

DNA replication protein DnaC; Validated


Pssm-ID: 235871 [Multi-domain]  Cd Length: 329  Bit Score: 41.04  E-value: 5.33e-04
                         10        20
                 ....*....|....*....|....*.
gi 185177972  47 TPSKGVLFYGPPGCGKTLLAKAIANE 72
Cdd:PRK06835 181 KNNENLLFYGNTGTGKTFLSNCIAKE 206
IS21_help_AAA NF038214
IS21-like element helper ATPase IstB; This protein family model resembles PF01695, but was ...
52-77 8.45e-04

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


Pssm-ID: 439516  Cd Length: 232  Bit Score: 40.15  E-value: 8.45e-04
                         10        20
                 ....*....|....*....|....*..
gi 185177972  52 VLFYGPPGCGKTLLAKAIANE-CQANF 77
Cdd:NF038214  93 VLLLGPPGTGKTHLAIALGYAaCRQGY 119
NACHT COG5635
Predicted NTPase, NACHT family domain [Signal transduction mechanisms];
52-173 8.48e-04

Predicted NTPase, NACHT family domain [Signal transduction mechanisms];


Pssm-ID: 444362 [Multi-domain]  Cd Length: 935  Bit Score: 40.94  E-value: 8.48e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 185177972  52 VLFYGPPGCGKTLLAKAIANECQANFISIKGP-----------------ELLTMWFGESEANVREIFDKARQAAPCVLFF 114
Cdd:COG5635  183 LLILGEPGSGKTTLLRYLALELAERYLDAEDPipilielrdlaeeasleDLLAEALEKRGGEPEDALERLLRNGRLLLLL 262
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 185177972 115 DELDSIAkarggnigdGGGAADRVINQILTEMDGMStkKNVFIIgaTNRPDIIDPAILR 173
Cdd:COG5635  263 DGLDEVP---------DEADRDEVLNQLRRFLERYP--KARVII--TSRPEGYDSSELE 308
HolB COG0470
DNA polymerase III, delta prime subunit [Replication, recombination and repair];
20-75 1.15e-03

DNA polymerase III, delta prime subunit [Replication, recombination and repair];


Pssm-ID: 440238 [Multi-domain]  Cd Length: 289  Bit Score: 39.96  E-value: 1.15e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 185177972  20 LEDVKRELQELVQYPVEHPdkflkfgmtpskGVLFYGPPGCGKTLLAKAIANE--CQA 75
Cdd:COG0470    1 QEEAWEQLLAAAESGRLPH------------ALLLHGPPGIGKTTLALALARDllCEN 46
Parvo_NS1 pfam01057
Parvovirus non-structural protein NS1; This family also contains the NS2 protein. Parvoviruses ...
52-71 1.24e-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: 39.60  E-value: 1.24e-03
                          10        20
                  ....*....|....*....|
gi 185177972   52 VLFYGPPGCGKTLLAKAIAN 71
Cdd:pfam01057 116 VWFYGPASTGKTNLAQAIAH 135
Mg_chelatase pfam01078
Magnesium chelatase, subunit ChlI; Magnesium-chelatase is a three-component enzyme that ...
52-69 1.36e-03

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


Pssm-ID: 426032 [Multi-domain]  Cd Length: 207  Bit Score: 39.06  E-value: 1.36e-03
                          10
                  ....*....|....*...
gi 185177972   52 VLFYGPPGCGKTLLAKAI 69
Cdd:pfam01078  25 LLMIGPPGSGKTMLAKRL 42
DnaX COG2812
DNA polymerase III, gamma/tau subunits [Replication, recombination and repair];
9-70 1.73e-03

DNA polymerase III, gamma/tau subunits [Replication, recombination and repair];


Pssm-ID: 442061 [Multi-domain]  Cd Length: 340  Bit Score: 39.40  E-value: 1.73e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 185177972   9 VPQvTWEDIGGLEDVKRELQELVQ-------YpvehpdkflkfgmtpskgvLFYGPPGCGKTLLAKAIA 70
Cdd:COG2812    5 VPQ-TFDDVVGQEHVVRTLKNALAsgrlahaY-------------------LFTGPRGVGKTTLARILA 53
TIP49 pfam06068
TIP49 P-loop domain; This family consists of the C-terminal region of several eukaryotic and ...
50-104 1.98e-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: 39.21  E-value: 1.98e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 185177972   50 KGVLFYGPPGCGKTLLAKAIANECQAN--FISIKGPELLTMWFGESEAnVREIFDKA 104
Cdd:pfam06068  51 RAVLIAGPPGTGKTALAIAISKELGEDtpFTSISGSEVYSLEMKKTEA-LTQAFRKA 106
YifB COG0606
Predicted Mg-chelatase, contains ChlI-like and ATPase domains, YifB family [Posttranslational ...
52-69 2.73e-03

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


Pssm-ID: 440371 [Multi-domain]  Cd Length: 502  Bit Score: 39.25  E-value: 2.73e-03
                         10
                 ....*....|....*...
gi 185177972  52 VLFYGPPGCGKTLLAKAI 69
Cdd:COG0606  214 LLMIGPPGSGKTMLARRL 231
McrB COG1401
5-methylcytosine-specific restriction endonuclease McrBC, GTP-binding regulatory subunit McrB ...
20-76 3.61e-03

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


Pssm-ID: 441011 [Multi-domain]  Cd Length: 477  Bit Score: 38.60  E-value: 3.61e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 185177972  20 LEDVKRELQELVQYPVEHPDKFLKFGMTPSKGVLFYGPPGCGKTLLAKAIANECQAN 76
Cdd:COG1401  192 LESEDDYLKDLLREKFEETLEAFLAALKTKKNVILAGPPGTGKTYLARRLAEALGGE 248
RecA-like_Lon cd19500
lon protease homolog 2 peroxisomal; Lon protease (also known as Lon peptidase) is an ...
19-71 4.94e-03

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


Pssm-ID: 410908 [Multi-domain]  Cd Length: 182  Bit Score: 37.15  E-value: 4.94e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 185177972  19 GLEDVKRELQElvqypvehpdkFLKFG-MTPS-KG--VLFYGPPGCGKTLLAKAIAN 71
Cdd:cd19500   14 GLEDVKERILE-----------YLAVRkLKGSmKGpiLCLVGPPGVGKTSLGKSIAR 59
DnaA COG0593
Chromosomal replication initiation ATPase DnaA [Replication, recombination and repair];
53-81 5.73e-03

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


Pssm-ID: 440358 [Multi-domain]  Cd Length: 303  Bit Score: 37.86  E-value: 5.73e-03
                         10        20        30
                 ....*....|....*....|....*....|
gi 185177972  53 LF-YGPPGCGKTLLAKAIANECQANFISIK 81
Cdd:COG0593   37 LFlYGGVGLGKTHLLHAIGNEALENNPGAR 66
MoxR COG0714
MoxR-like ATPase [General function prediction only]; MoxR-like ATPase is part of the Pathway ...
52-80 5.83e-03

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: 37.84  E-value: 5.83e-03
                         10        20
                 ....*....|....*....|....*....
gi 185177972  52 VLFYGPPGCGKTLLAKAIANECQANFISI 80
Cdd:COG0714   34 LLLEGVPGVGKTTLAKALARALGLPFIRI 62
rfc PRK00440
replication factor C small subunit; Reviewed
10-72 6.24e-03

replication factor C small subunit; Reviewed


Pssm-ID: 234763 [Multi-domain]  Cd Length: 319  Bit Score: 37.54  E-value: 6.24e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 185177972  10 PQvTWEDIGGLEDVKRELQelvqypvehpdKFLKFGMTPSkgVLFYGPPGCGKTLLAKAIANE 72
Cdd:PRK00440  13 PR-TLDEIVGQEEIVERLK-----------SYVKEKNMPH--LLFAGPPGTGKTTAALALARE 61
PRK12402 PRK12402
replication factor C small subunit 2; Reviewed
15-80 7.51e-03

replication factor C small subunit 2; Reviewed


Pssm-ID: 237090 [Multi-domain]  Cd Length: 337  Bit Score: 37.66  E-value: 7.51e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 185177972  15 EDIGGLEDVKRELQELVQYPvehpdkflkfgMTPSkgVLFYGPPGCGKTLLAKAIANE-----CQANFISI 80
Cdd:PRK12402  15 EDILGQDEVVERLSRAVDSP-----------NLPH--LLVQGPPGSGKTAAVRALARElygdpWENNFTEF 72
TIGR02928 TIGR02928
orc1/cdc6 family replication initiation protein; Members of this protein family are found ...
20-75 9.94e-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: 37.23  E-value: 9.94e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 185177972   20 LEDVKRELQELVQypvehpdkflkfGMTPSKgVLFYGPPGCGKTLLAKAIANECQA 75
Cdd:TIGR02928  24 IEELAKALRPILR------------GSRPSN-VFIYGKTGTGKTAVTKYVMKELEE 66
 
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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