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Conserved domains on  [gi|1246742881|ref|NP_001342870|]
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putative proteasome regulatory subunit Rpt5 [Schizosaccharomyces pombe]

Protein Classification

26S proteasome regulatory subunit family protein( domain architecture ID 1001539)

26S proteasome regulatory subunit family protein may act as a component of the 26S proteasome, a multiprotein complex facilitating the ATP-dependent degradation of ubiquitinated proteins

CATH:  3.40.50.300
Gene Ontology:  GO:0005524|GO:0016887|GO:0036402|GO:0043161|GO:0000502
PubMed:  27428775|10417703|9927482

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PRK03992 super family cl32052
proteasome-activating nucleotidase; Provisional
 36-432 3.22e-152

proteasome-activating nucleotidase; Provisional


The actual alignment was detected with superfamily member PRK03992:

Pssm-ID: 179699 [Multi-domain]  Cd Length: 389  Bit Score: 436.96  E-value: 3.22e-152
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246742881  36 IDELNSRTRLLENDIKVMKSEFQRLTHEKSTMLEKIKENQEKISNNKMLPYLVGNVVEILDmqPDEVDVQESANQNseat 115
Cdd:PRK03992    3 LEALEERNSELEEQIRQLELKLRDLEAENEKLERELERLKSELEKLKSPPLIVATVLEVLD--DGRVVVKSSGGPQ---- 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246742881 116 rvgksAVIKTSTRqtiflpliglVEPEELHPGDLIGVNKDSYLIIDKLPSEYDSRVKAMEVDEKPTERYSDIGGLSKQIE 195
Cdd:PRK03992   77 -----FLVNVSPF----------IDREKLKPGARVALNQQSLAIVEVLPSEKDPRVQAMEVIESPNVTYEDIGGLEEQIR 141

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246742881 196 ELFEAIVLPMQQADKFRKLGVKPPKGCLMFGPPGTGKTLLARACAAQSNATFLKLAAPQLVQMFIGDGAKLVRDAFALAK 275
Cdd:PRK03992  142 EVREAVELPLKKPELFEEVGIEPPKGVLLYGPPGTGKTLLAKAVAHETNATFIRVVGSELVQKFIGEGARLVRELFELAR 221

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246742881 276 EKSPAIIFIDELDAIGTKRFDSEKAGDREVQRTMLELLNQLDGFSSDDRVKVIAATNRVDTLDPALLRSGRLDRKLEFPL 355
Cdd:PRK03992  222 EKAPSIIFIDEIDAIAAKRTDSGTSGDREVQRTLMQLLAEMDGFDPRGNVKIIAATNRIDILDPAILRPGRFDRIIEVPL 301

                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1246742881 356 PNEEARVGILRIHSRKMAIDDDINWEELARSTDEYNGAMLKSVCVEAGMIALRQGDTKINHEHFMDGILEVQMRKSK 432
Cdd:PRK03992  302 PDEEGRLEILKIHTRKMNLADDVDLEELAELTEGASGADLKAICTEAGMFAIRDDRTEVTMEDFLKAIEKVMGKEEK 378
 
Name Accession Description Interval E-value
PRK03992 PRK03992
proteasome-activating nucleotidase; Provisional
 36-432 3.22e-152

proteasome-activating nucleotidase; Provisional


Pssm-ID: 179699 [Multi-domain]  Cd Length: 389  Bit Score: 436.96  E-value: 3.22e-152
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246742881  36 IDELNSRTRLLENDIKVMKSEFQRLTHEKSTMLEKIKENQEKISNNKMLPYLVGNVVEILDmqPDEVDVQESANQNseat 115
Cdd:PRK03992    3 LEALEERNSELEEQIRQLELKLRDLEAENEKLERELERLKSELEKLKSPPLIVATVLEVLD--DGRVVVKSSGGPQ---- 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246742881 116 rvgksAVIKTSTRqtiflpliglVEPEELHPGDLIGVNKDSYLIIDKLPSEYDSRVKAMEVDEKPTERYSDIGGLSKQIE 195
Cdd:PRK03992   77 -----FLVNVSPF----------IDREKLKPGARVALNQQSLAIVEVLPSEKDPRVQAMEVIESPNVTYEDIGGLEEQIR 141

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246742881 196 ELFEAIVLPMQQADKFRKLGVKPPKGCLMFGPPGTGKTLLARACAAQSNATFLKLAAPQLVQMFIGDGAKLVRDAFALAK 275
Cdd:PRK03992  142 EVREAVELPLKKPELFEEVGIEPPKGVLLYGPPGTGKTLLAKAVAHETNATFIRVVGSELVQKFIGEGARLVRELFELAR 221

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246742881 276 EKSPAIIFIDELDAIGTKRFDSEKAGDREVQRTMLELLNQLDGFSSDDRVKVIAATNRVDTLDPALLRSGRLDRKLEFPL 355
Cdd:PRK03992  222 EKAPSIIFIDEIDAIAAKRTDSGTSGDREVQRTLMQLLAEMDGFDPRGNVKIIAATNRIDILDPAILRPGRFDRIIEVPL 301

                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1246742881 356 PNEEARVGILRIHSRKMAIDDDINWEELARSTDEYNGAMLKSVCVEAGMIALRQGDTKINHEHFMDGILEVQMRKSK 432
Cdd:PRK03992  302 PDEEGRLEILKIHTRKMNLADDVDLEELAELTEGASGADLKAICTEAGMFAIRDDRTEVTMEDFLKAIEKVMGKEEK 378
26Sp45 TIGR01242
26S proteasome subunit P45 family; Many proteins may score above the trusted cutoff because an ...
 36-426 2.26e-132

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


Pssm-ID: 130309 [Multi-domain]  Cd Length: 364  Bit Score: 385.69  E-value: 2.26e-132
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246742881  36 IDELNSRTRLLENDIKVMKSEFQRLTHEkstmLEKIKENQEKIsnnKMLPYLVGNVVEILDmqPDEVDVQESAnqnseat 115
Cdd:TIGR01242   1 ISELDVRIRKLEDEKRSLEKEKIRLERE----LERLRSEIERL---RSPPLIVGTVLEVLD--DNRVVVKSST------- 64

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246742881 116 rvGKSAVIKTSTrqtiflpligLVEPEELHPGDLIGVNKDSYLIIDKLPSEYDSRVKAMEVDEKPTERYSDIGGLSKQIE 195
Cdd:TIGR01242  65 --GPNFVVNVSA----------FIDRKSLKPGARVALNQQTLTIVDVLPTSKDPLVKGMEVEERPNVSYEDIGGLEEQIR 132

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246742881 196 ELFEAIVLPMQQADKFRKLGVKPPKGCLMFGPPGTGKTLLARACAAQSNATFLKLAAPQLVQMFIGDGAKLVRDAFALAK 275
Cdd:TIGR01242 133 EIREAVELPLKHPELFEEVGIEPPKGVLLYGPPGTGKTLLAKAVAHETNATFIRVVGSELVRKYIGEGARLVREIFELAK 212

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246742881 276 EKSPAIIFIDELDAIGTKRFDSEKAGDREVQRTMLELLNQLDGFSSDDRVKVIAATNRVDTLDPALLRSGRLDRKLEFPL 355
Cdd:TIGR01242 213 EKAPSIIFIDEIDAIAAKRTDSGTSGDREVQRTLMQLLAELDGFDPRGNVKVIAATNRPDILDPALLRPGRFDRIIEVPL 292

                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1246742881 356 PNEEARVGILRIHSRKMAIDDDINWEELARSTDEYNGAMLKSVCVEAGMIALRQGDTKINHEHFMDGILEV 426
Cdd:TIGR01242 293 PDFEGRLEILKIHTRKMKLAEDVDLEAIAKMTEGASGADLKAICTEAGMFAIREERDYVTMDDFIKAVEKV 363
RPT1 COG1222
ATP-dependent 26S proteasome regulatory subunit [Posttranslational modification, protein ...
 97-432 5.90e-125

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


Pssm-ID: 440835 [Multi-domain]  Cd Length: 326  Bit Score: 365.10  E-value: 5.90e-125
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246742881  97 MQPDEVDVQESANQNSEATRVGKSAVIktstrqtiflpLIGLVEPEELHPGDLIGVNKDSYLIIDKLPSEydsrVKAMEV 176
Cdd:COG1222     5 LTIDENIKALLALIDALQERLGVELAL-----------LLQPVKALELLEEAPALLLNDANLTQKRLGTP----RGTAVP 69

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246742881 177 DEKPTERYSDIGGLSKQIEELFEAIVLPMQQADKFRKLGVKPPKGCLMFGPPGTGKTLLARACAAQSNATFLKLAAPQLV 256
Cdd:COG1222    70 AESPDVTFDDIGGLDEQIEEIREAVELPLKNPELFRKYGIEPPKGVLLYGPPGTGKTLLAKAVAGELGAPFIRVRGSELV 149

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246742881 257 QMFIGDGAKLVRDAFALAKEKSPAIIFIDELDAIGTKRFDSEKAGdrEVQRTMLELLNQLDGFSSDDRVKVIAATNRVDT 336
Cdd:COG1222   150 SKYIGEGARNVREVFELAREKAPSIIFIDEIDAIAARRTDDGTSG--EVQRTVNQLLAELDGFESRGDVLIIAATNRPDL 227

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246742881 337 LDPALLRSGRLDRKLEFPLPNEEARVGILRIHSRKMAIDDDINWEELARSTDEYNGAMLKSVCVEAGMIALRQGDTKINH 416
Cdd:COG1222   228 LDPALLRPGRFDRVIEVPLPDEEAREEILKIHLRDMPLADDVDLDKLAKLTEGFSGADLKAIVTEAGMFAIREGRDTVTM 307

                         330
                  ....*....|....*.
gi 1246742881 417 EHFMDGILEVQMRKSK 432
Cdd:COG1222   308 EDLEKAIEKVKKKTET 323
RecA-like_PAN_like cd19502
proteasome activating nucleotidase PAN and related proteasome subunits; This subfamily ...
 184-353 1.71e-95

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: 284.23  E-value: 1.71e-95
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246742881 184 YSDIGGLSKQIEELFEAIVLPMQQADKFRKLGVKPPKGCLMFGPPGTGKTLLARACAAQSNATFLKLAAPQLVQMFIGDG 263
Cdd:cd19502     2 YEDIGGLDEQIREIREVVELPLKHPELFEELGIEPPKGVLLYGPPGTGKTLLAKAVANHTDATFIRVVGSELVQKYIGEG 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246742881 264 AKLVRDAFALAKEKSPAIIFIDELDAIGTKRFDSEKAGDREVQRTMLELLNQLDGFSSDDRVKVIAATNRVDTLDPALLR 343
Cdd:cd19502    82 ARLVRELFEMAREKAPSIIFIDEIDAIGAKRFDSGTGGDREVQRTMLELLNQLDGFDPRGNIKVIMATNRPDILDPALLR 161

                         170
                  ....*....|
gi 1246742881 344 SGRLDRKLEF 353
Cdd:cd19502   162 PGRFDRKIEF 171
AAA pfam00004
ATPase family associated with various cellular activities (AAA); AAA family proteins often ...
 223-355 5.24e-50

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: 165.84  E-value: 5.24e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246742881 223 LMFGPPGTGKTLLARACAAQSNATFLKLAAPQLVQMFIGDGAKLVRDAFALAKEKSPAIIFIDELDAIGTKRFDSekaGD 302
Cdd:pfam00004   2 LLYGPPGTGKTTLAKAVAKELGAPFIEISGSELVSKYVGESEKRLRELFEAAKKLAPCVIFIDEIDALAGSRGSG---GD 78

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1246742881 303 REVQRTMLELLNQLDGFSSD-DRVKVIAATNRVDTLDPALLrsGRLDRKLEFPL 355
Cdd:pfam00004  79 SESRRVVNQLLTELDGFTSSnSKVIVIAATNRPDKLDPALL--GRFDRIIEFPL 130
AAA smart00382
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ...
 218-357 3.20e-17

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: 78.18  E-value: 3.20e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246742881  218 PPKGCLMFGPPGTGKTLLARACAAQSNAT-----------------FLKLAAPQLVQMFIGDGAKLVRDAFALAKEKSPA 280
Cdd:smart00382   1 PGEVILIVGPPGSGKTTLARALARELGPPgggviyidgedileevlDQLLLIIVGGKKASGSGELRLRLALALARKLKPD 80

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1246742881  281 IIFIDELDAIGTKRFdsekagdrEVQRTMLELLNQLDGFSSDDRVKVIAATNRVDTLDPALLRSgRLDRKLEFPLPN 357
Cdd:smart00382  81 VLILDEITSLLDAEQ--------EALLLLLEELRLLLLLKSEKNLTVILTTNDEKDLGPALLRR-RFDRRIVLLLIL 148
 
Name Accession Description Interval E-value
PRK03992 PRK03992
proteasome-activating nucleotidase; Provisional
 36-432 3.22e-152

proteasome-activating nucleotidase; Provisional


Pssm-ID: 179699 [Multi-domain]  Cd Length: 389  Bit Score: 436.96  E-value: 3.22e-152
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246742881  36 IDELNSRTRLLENDIKVMKSEFQRLTHEKSTMLEKIKENQEKISNNKMLPYLVGNVVEILDmqPDEVDVQESANQNseat 115
Cdd:PRK03992    3 LEALEERNSELEEQIRQLELKLRDLEAENEKLERELERLKSELEKLKSPPLIVATVLEVLD--DGRVVVKSSGGPQ---- 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246742881 116 rvgksAVIKTSTRqtiflpliglVEPEELHPGDLIGVNKDSYLIIDKLPSEYDSRVKAMEVDEKPTERYSDIGGLSKQIE 195
Cdd:PRK03992   77 -----FLVNVSPF----------IDREKLKPGARVALNQQSLAIVEVLPSEKDPRVQAMEVIESPNVTYEDIGGLEEQIR 141

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246742881 196 ELFEAIVLPMQQADKFRKLGVKPPKGCLMFGPPGTGKTLLARACAAQSNATFLKLAAPQLVQMFIGDGAKLVRDAFALAK 275
Cdd:PRK03992  142 EVREAVELPLKKPELFEEVGIEPPKGVLLYGPPGTGKTLLAKAVAHETNATFIRVVGSELVQKFIGEGARLVRELFELAR 221

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246742881 276 EKSPAIIFIDELDAIGTKRFDSEKAGDREVQRTMLELLNQLDGFSSDDRVKVIAATNRVDTLDPALLRSGRLDRKLEFPL 355
Cdd:PRK03992  222 EKAPSIIFIDEIDAIAAKRTDSGTSGDREVQRTLMQLLAEMDGFDPRGNVKIIAATNRIDILDPAILRPGRFDRIIEVPL 301

                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1246742881 356 PNEEARVGILRIHSRKMAIDDDINWEELARSTDEYNGAMLKSVCVEAGMIALRQGDTKINHEHFMDGILEVQMRKSK 432
Cdd:PRK03992  302 PDEEGRLEILKIHTRKMNLADDVDLEELAELTEGASGADLKAICTEAGMFAIRDDRTEVTMEDFLKAIEKVMGKEEK 378
26Sp45 TIGR01242
26S proteasome subunit P45 family; Many proteins may score above the trusted cutoff because an ...
 36-426 2.26e-132

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


Pssm-ID: 130309 [Multi-domain]  Cd Length: 364  Bit Score: 385.69  E-value: 2.26e-132
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246742881  36 IDELNSRTRLLENDIKVMKSEFQRLTHEkstmLEKIKENQEKIsnnKMLPYLVGNVVEILDmqPDEVDVQESAnqnseat 115
Cdd:TIGR01242   1 ISELDVRIRKLEDEKRSLEKEKIRLERE----LERLRSEIERL---RSPPLIVGTVLEVLD--DNRVVVKSST------- 64

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246742881 116 rvGKSAVIKTSTrqtiflpligLVEPEELHPGDLIGVNKDSYLIIDKLPSEYDSRVKAMEVDEKPTERYSDIGGLSKQIE 195
Cdd:TIGR01242  65 --GPNFVVNVSA----------FIDRKSLKPGARVALNQQTLTIVDVLPTSKDPLVKGMEVEERPNVSYEDIGGLEEQIR 132

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246742881 196 ELFEAIVLPMQQADKFRKLGVKPPKGCLMFGPPGTGKTLLARACAAQSNATFLKLAAPQLVQMFIGDGAKLVRDAFALAK 275
Cdd:TIGR01242 133 EIREAVELPLKHPELFEEVGIEPPKGVLLYGPPGTGKTLLAKAVAHETNATFIRVVGSELVRKYIGEGARLVREIFELAK 212

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246742881 276 EKSPAIIFIDELDAIGTKRFDSEKAGDREVQRTMLELLNQLDGFSSDDRVKVIAATNRVDTLDPALLRSGRLDRKLEFPL 355
Cdd:TIGR01242 213 EKAPSIIFIDEIDAIAAKRTDSGTSGDREVQRTLMQLLAELDGFDPRGNVKVIAATNRPDILDPALLRPGRFDRIIEVPL 292

                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1246742881 356 PNEEARVGILRIHSRKMAIDDDINWEELARSTDEYNGAMLKSVCVEAGMIALRQGDTKINHEHFMDGILEV 426
Cdd:TIGR01242 293 PDFEGRLEILKIHTRKMKLAEDVDLEAIAKMTEGASGADLKAICTEAGMFAIREERDYVTMDDFIKAVEKV 363
RPT1 COG1222
ATP-dependent 26S proteasome regulatory subunit [Posttranslational modification, protein ...
 97-432 5.90e-125

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


Pssm-ID: 440835 [Multi-domain]  Cd Length: 326  Bit Score: 365.10  E-value: 5.90e-125
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246742881  97 MQPDEVDVQESANQNSEATRVGKSAVIktstrqtiflpLIGLVEPEELHPGDLIGVNKDSYLIIDKLPSEydsrVKAMEV 176
Cdd:COG1222     5 LTIDENIKALLALIDALQERLGVELAL-----------LLQPVKALELLEEAPALLLNDANLTQKRLGTP----RGTAVP 69

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246742881 177 DEKPTERYSDIGGLSKQIEELFEAIVLPMQQADKFRKLGVKPPKGCLMFGPPGTGKTLLARACAAQSNATFLKLAAPQLV 256
Cdd:COG1222    70 AESPDVTFDDIGGLDEQIEEIREAVELPLKNPELFRKYGIEPPKGVLLYGPPGTGKTLLAKAVAGELGAPFIRVRGSELV 149

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246742881 257 QMFIGDGAKLVRDAFALAKEKSPAIIFIDELDAIGTKRFDSEKAGdrEVQRTMLELLNQLDGFSSDDRVKVIAATNRVDT 336
Cdd:COG1222   150 SKYIGEGARNVREVFELAREKAPSIIFIDEIDAIAARRTDDGTSG--EVQRTVNQLLAELDGFESRGDVLIIAATNRPDL 227

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246742881 337 LDPALLRSGRLDRKLEFPLPNEEARVGILRIHSRKMAIDDDINWEELARSTDEYNGAMLKSVCVEAGMIALRQGDTKINH 416
Cdd:COG1222   228 LDPALLRPGRFDRVIEVPLPDEEAREEILKIHLRDMPLADDVDLDKLAKLTEGFSGADLKAIVTEAGMFAIREGRDTVTM 307

                         330
                  ....*....|....*.
gi 1246742881 417 EHFMDGILEVQMRKSK 432
Cdd:COG1222   308 EDLEKAIEKVKKKTET 323
PTZ00361 PTZ00361
26 proteosome regulatory subunit 4-like protein; Provisional
 42-434 6.43e-115

26 proteosome regulatory subunit 4-like protein; Provisional


Pssm-ID: 185575 [Multi-domain]  Cd Length: 438  Bit Score: 343.68  E-value: 6.43e-115
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246742881  42 RTRLLEN----DIKVMKSEFQRLTHEKSTMLEKIKENQEKISNNKMLPYLVGNVVEILDMQpdevdvqesanqnseatrv 117
Cdd:PTZ00361   57 RLRLLKLerikDYLLLEEEFITNQEAQKPAQEKNEAELKKVDDLRGSPLSVGTLEEIIDEN------------------- 117

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246742881 118 gkSAVIKTSTRQTIFLPLIGLVEPEELHPGDLIGVNKDSYLIIDKLPSEYDSRVKAMEVDEKPTERYSDIGGLSKQIEEL 197
Cdd:PTZ00361  118 --HAIVSSSVGPEYYVNILSFVDKEQLEPGCSVLLHNKTHSVVGILLDEVDPLVSVMKVDKAPLESYADIGGLEQQIQEI 195

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246742881 198 FEAIVLPMQQADKFRKLGVKPPKGCLMFGPPGTGKTLLARACAAQSNATFLKLAAPQLVQMFIGDGAKLVRDAFALAKEK 277
Cdd:PTZ00361  196 KEAVELPLTHPELYDDIGIKPPKGVILYGPPGTGKTLLAKAVANETSATFLRVVGSELIQKYLGDGPKLVRELFRVAEEN 275

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246742881 278 SPAIIFIDELDAIGTKRFDSEKAGDREVQRTMLELLNQLDGFSSDDRVKVIAATNRVDTLDPALLRSGRLDRKLEFPLPN 357
Cdd:PTZ00361  276 APSIVFIDEIDAIGTKRYDATSGGEKEIQRTMLELLNQLDGFDSRGDVKVIMATNRIESLDPALIRPGRIDRKIEFPNPD 355

                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1246742881 358 EEARVGILRIHSRKMAIDDDINWEELARSTDEYNGAMLKSVCVEAGMIALRQGDTKINHEHFMDGILEVQMRKSKTL 434
Cdd:PTZ00361  356 EKTKRRIFEIHTSKMTLAEDVDLEEFIMAKDELSGADIKAICTEAGLLALRERRMKVTQADFRKAKEKVLYRKKGNI 432
PTZ00454 PTZ00454
26S protease regulatory subunit 6B-like protein; Provisional
 38-409 9.03e-105

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


Pssm-ID: 240423 [Multi-domain]  Cd Length: 398  Bit Score: 316.32  E-value: 9.03e-105
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246742881  38 ELNSRTRLLEN-DIKVM--KSEFQRLTHEKSTMLEKIKENQEkisnnkmLPYLVGNVVEILDmqpdevdvqesanqnsea 114
Cdd:PTZ00454   23 KLKELEKELEFlDIQEEyiKEEQKNLKRELIRAKEEVKRIQS-------VPLVIGQFLEMID------------------ 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246742881 115 trvGKSAVIKTSTRQTIFLPLIGLVEPEELHPGDLIGVNKDSYLIIDKLPSEYDSRVKAMEVDEKPTERYSDIGGLSKQI 194
Cdd:PTZ00454   78 ---SNYGIVSSTSGSNYYVRILSTLNRELLKPNASVALHRHSHAVVDILPPEADSSIQLLQMSEKPDVTYSDIGGLDIQK 154

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246742881 195 EELFEAIVLPMQQADKFRKLGVKPPKGCLMFGPPGTGKTLLARACAAQSNATFLKLAAPQLVQMFIGDGAKLVRDAFALA 274
Cdd:PTZ00454  155 QEIREAVELPLTCPELYEQIGIDPPRGVLLYGPPGTGKTMLAKAVAHHTTATFIRVVGSEFVQKYLGEGPRMVRDVFRLA 234

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246742881 275 KEKSPAIIFIDELDAIGTKRFDSEKAGDREVQRTMLELLNQLDGFSSDDRVKVIAATNRVDTLDPALLRSGRLDRKLEFP 354
Cdd:PTZ00454  235 RENAPSIIFIDEVDSIATKRFDAQTGADREVQRILLELLNQMDGFDQTTNVKVIMATNRADTLDPALLRPGRLDRKIEFP 314

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1246742881 355 LPNEEARVGILRIHSRKMAIDDDINWEELARSTDEYNGAMLKSVCVEAGMIALRQ 409
Cdd:PTZ00454  315 LPDRRQKRLIFQTITSKMNLSEEVDLEDFVSRPEKISAADIAAICQEAGMQAVRK 369
RecA-like_PAN_like cd19502
proteasome activating nucleotidase PAN and related proteasome subunits; This subfamily ...
 184-353 1.71e-95

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: 284.23  E-value: 1.71e-95
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246742881 184 YSDIGGLSKQIEELFEAIVLPMQQADKFRKLGVKPPKGCLMFGPPGTGKTLLARACAAQSNATFLKLAAPQLVQMFIGDG 263
Cdd:cd19502     2 YEDIGGLDEQIREIREVVELPLKHPELFEELGIEPPKGVLLYGPPGTGKTLLAKAVANHTDATFIRVVGSELVQKYIGEG 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246742881 264 AKLVRDAFALAKEKSPAIIFIDELDAIGTKRFDSEKAGDREVQRTMLELLNQLDGFSSDDRVKVIAATNRVDTLDPALLR 343
Cdd:cd19502    82 ARLVRELFEMAREKAPSIIFIDEIDAIGAKRFDSGTGGDREVQRTMLELLNQLDGFDPRGNIKVIMATNRPDILDPALLR 161

                         170
                  ....*....|
gi 1246742881 344 SGRLDRKLEF 353
Cdd:cd19502   162 PGRFDRKIEF 171
FtsH_fam TIGR01241
ATP-dependent metalloprotease FtsH; HflB(FtsH) is a pleiotropic protein required for correct ...
 169-434 1.16e-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: 252.21  E-value: 1.16e-78
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246742881 169 SRVKAMEvDEKPTERYSDIGGLSKQIEELFEaIVLPMQQADKFRKLGVKPPKGCLMFGPPGTGKTLLARACAAQSNATFL 248
Cdd:TIGR01241  40 SKAKLLN-EEKPKVTFKDVAGIDEAKEELME-IVDFLKNPSKFTKLGAKIPKGVLLVGPPGTGKTLLAKAVAGEAGVPFF 117

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246742881 249 KLAAPQLVQMFIGDGAKLVRDAFALAKEKSPAIIFIDELDAIGTKRFDSEKAGDREVQRTMLELLNQLDGFSSDDRVKVI 328
Cdd:TIGR01241 118 SISGSDFVEMFVGVGASRVRDLFEQAKKNAPCIIFIDEIDAVGRQRGAGLGGGNDEREQTLNQLLVEMDGFGTNTGVIVI 197

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246742881 329 AATNRVDTLDPALLRSGRLDRKLEFPLPNEEARVGILRIHSRKMAIDDDINWEELARSTDEYNGAMLKSVCVEAGMIALR 408
Cdd:TIGR01241 198 AATNRPDVLDPALLRPGRFDRQVVVDLPDIKGREEILKVHAKNKKLAPDVDLKAVARRTPGFSGADLANLLNEAALLAAR 277

                         250       260
                  ....*....|....*....|....*....
gi 1246742881 409 QGDTKINHEHFMDGILEVQM---RKSKTL 434
Cdd:TIGR01241 278 KNKTEITMNDIEEAIDRVIAgpeKKSRVI 306
SpoVK COG0464
AAA+-type ATPase, SpoVK/Ycf46/Vps4 family [Cell wall/membrane/envelope biogenesis, Cell cycle ...
 128-429 1.03e-77

AAA+-type ATPase, SpoVK/Ycf46/Vps4 family [Cell wall/membrane/envelope biogenesis, Cell cycle control, cell division, chromosome partitioning, Signal transduction mechanisms];


Pssm-ID: 440232 [Multi-domain]  Cd Length: 397  Bit Score: 246.75  E-value: 1.03e-77
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246742881 128 RQTIFLPLIGLVEPEELHPGDLIGVNKDSYLIIDKLPSEYDSRVKAMEVDEKPTERYSDIGGLSKQIEELFEAIVLPMQQ 207
Cdd:COG0464   100 LLLLLLLLLLLLLDLERALLELLRESAEALALAAPLVTYEDIGGLEEELLELREAILDDLGGLEEVKEELRELVALPLKR 179

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246742881 208 ADKFRKLGVKPPKGCLMFGPPGTGKTLLARACAAQSNATFLKLAAPQLVQMFIGDGAKLVRDAFALAKEKSPAIIFIDEL 287
Cdd:COG0464   180 PELREEYGLPPPRGLLLYGPPGTGKTLLARALAGELGLPLIEVDLSDLVSKYVGETEKNLREVFDKARGLAPCVLFIDEA 259

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246742881 288 DAIGTKRfdsEKAGDREVQRTMLELLNQLDGFSSDdrVKVIAATNRVDTLDPALLRsgRLDRKLEFPLPNEEARVGILRI 367
Cdd:COG0464   260 DALAGKR---GEVGDGVGRRVVNTLLTEMEELRSD--VVVIAATNRPDLLDPALLR--RFDEIIFFPLPDAEERLEIFRI 332

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1246742881 368 HSRKMAIDDDINWEELARSTDEYNGAMLKSVCVEAGMIALRQGDTKINHEHFMDGILEVQMR 429
Cdd:COG0464   333 HLRKRPLDEDVDLEELAEATEGLSGADIRNVVRRAALQALRLGREPVTTEDLLEALEREDIF 394
HflB COG0465
ATP-dependent Zn proteases [Posttranslational modification, protein turnover, chaperones];
169-434 1.91e-76

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


Pssm-ID: 440233 [Multi-domain]  Cd Length: 583  Bit Score: 248.80  E-value: 1.91e-76
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246742881 169 SRVKaMEVDEKPTERYSDIGGLSKQIEELFEaIVLPMQQADKFRKLGVKPPKGCLMFGPPGTGKTLLARACAAQSNATFL 248
Cdd:COG0465   127 SKAK-LYDEDKPKVTFDDVAGVDEAKEELQE-IVDFLKDPEKFTRLGAKIPKGVLLVGPPGTGKTLLAKAVAGEAGVPFF 204

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246742881 249 KLAAPQLVQMFIGDGAKLVRDAFALAKEKSPAIIFIDELDAIGTKRFdsekAG------DREvqRTmlelLNQL----DG 318
Cdd:COG0465   205 SISGSDFVEMFVGVGASRVRDLFEQAKKNAPCIIFIDEIDAVGRQRG----AGlggghdERE--QT----LNQLlvemDG 274

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246742881 319 FSSDDRVKVIAATNRVDTLDPALLRSGRLDRKLEFPLPNEEARVGILRIHSRKMAIDDDINWEELARSTDEYNGAMLKSV 398
Cdd:COG0465   275 FEGNEGVIVIAATNRPDVLDPALLRPGRFDRQVVVDLPDVKGREAILKVHARKKPLAPDVDLEVIARRTPGFSGADLANL 354

                         250       260       270
                  ....*....|....*....|....*....|....*....
gi 1246742881 399 CVEAGMIALRQGDTKINHEHFMDGILEVQM---RKSKTL 434
Cdd:COG0465   355 VNEAALLAARRNKKAVTMEDFEEAIDRVIAgpeRKSRVI 393
CDC48 TIGR01243
AAA family ATPase, CDC48 subfamily; This subfamily of the AAA family ATPases includes two ...
 178-432 1.39e-69

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


Pssm-ID: 273521 [Multi-domain]  Cd Length: 733  Bit Score: 234.03  E-value: 1.39e-69
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246742881 178 EKPTERYSDIGGLSKQIEELFEAIVLPMQQADKFRKLGVKPPKGCLMFGPPGTGKTLLARACAAQSNATFLKLAAPQLVQ 257
Cdd:TIGR01243 446 EVPNVRWSDIGGLEEVKQELREAVEWPLKHPEIFEKMGIRPPKGVLLFGPPGTGKTLLAKAVATESGANFIAVRGPEILS 525

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246742881 258 MFIGDGAKLVRDAFALAKEKSPAIIFIDELDAIGTKRFDSEkaGDREVQRTMLELLNQLDGFSSDDRVKVIAATNRVDTL 337
Cdd:TIGR01243 526 KWVGESEKAIREIFRKARQAAPAIIFFDEIDAIAPARGARF--DTSVTDRIVNQLLTEMDGIQELSNVVVIAATNRPDIL 603

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246742881 338 DPALLRSGRLDRKLEFPLPNEEARVGILRIHSRKMAIDDDINWEELARSTDEYNGAMLKSVCVEAGMIALRQ-------- 409
Cdd:TIGR01243 604 DPALLRPGRFDRLILVPPPDEEARKEIFKIHTRSMPLAEDVDLEELAEMTEGYTGADIEAVCREAAMAALREsigspake 683

                         250       260       270
                  ....*....|....*....|....*....|...
gi 1246742881 410 ----------GDTKINHEHFMDGILEVQMRKSK 432
Cdd:TIGR01243 684 klevgeeeflKDLKVEMRHFLEALKKVKPSVSK 716
ftsH CHL00176
cell division protein; Validated
 174-423 5.96e-65

cell division protein; Validated


Pssm-ID: 214386 [Multi-domain]  Cd Length: 638  Bit Score: 219.92  E-value: 5.96e-65
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246742881 174 MEVDEKPTerYSDIGGLSKQIEElFEAIVLPMQQADKFRKLGVKPPKGCLMFGPPGTGKTLLARACAAQSNATFLKLAAP 253
Cdd:CHL00176  174 MEADTGIT--FRDIAGIEEAKEE-FEEVVSFLKKPERFTAVGAKIPKGVLLVGPPGTGKTLLAKAIAGEAEVPFFSISGS 250

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246742881 254 QLVQMFIGDGAKLVRDAFALAKEKSPAIIFIDELDAIGTKRFDSEKAGDREVQRTMLELLNQLDGFSSDDRVKVIAATNR 333
Cdd:CHL00176  251 EFVEMFVGVGAARVRDLFKKAKENSPCIVFIDEIDAVGRQRGAGIGGGNDEREQTLNQLLTEMDGFKGNKGVIVIAATNR 330

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246742881 334 VDTLDPALLRSGRLDRKLEFPLPNEEARVGILRIHSRKMAIDDDINWEELARSTDEYNGAMLKSVCVEAGMIALRQGDTK 413
Cdd:CHL00176  331 VDILDAALLRPGRFDRQITVSLPDREGRLDILKVHARNKKLSPDVSLELIARRTPGFSGADLANLLNEAAILTARRKKAT 410

                         250
                  ....*....|
gi 1246742881 414 INHEHFMDGI 423
Cdd:CHL00176  411 ITMKEIDTAI 420
RecA-like_FtsH cd19501
ATP-dependent zinc metalloprotease FtsH; FtsH ATPase is a processive, ATP-dependent zinc ...
 183-350 6.48e-63

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: 200.92  E-value: 6.48e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246742881 183 RYSDIGGLSKQIEELFEaIVLPMQQADKFRKLGVKPPKGCLMFGPPGTGKTLLARACAAQSNATFLKLAAPQLVQMFIGD 262
Cdd:cd19501     2 TFKDVAGCEEAKEELKE-VVEFLKNPEKFTKLGAKIPKGVLLVGPPGTGKTLLAKAVAGEAGVPFFSISGSDFVEMFVGV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246742881 263 GAKLVRDAFALAKEKSPAIIFIDELDAIGTKRFDSEKAGDREVQRTMLELLNQLDGFSSDDRVKVIAATNRVDTLDPALL 342
Cdd:cd19501    81 GASRVRDLFEQAKKNAPCIVFIDEIDAVGRKRGAGLGGGHDEREQTLNQLLVEMDGFESNTGVIVIAATNRPDVLDPALL 160


                  ....*...
gi 1246742881 343 RSGRLDRK 350
Cdd:cd19501   161 RPGRFDRQ 168
CDC48 TIGR01243
AAA family ATPase, CDC48 subfamily; This subfamily of the AAA family ATPases includes two ...
 165-417 3.38e-62

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: 214.00  E-value: 3.38e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246742881 165 SEYDSRVKAMEVDEK---PTERYSDIGGLSKQIEELFEAIVLPMQQADKFRKLGVKPPKGCLMFGPPGTGKTLLARACAA 241
Cdd:TIGR01243 155 TEVEIREKPVREEIErkvPKVTYEDIGGLKEAKEKIREMVELPMKHPELFEHLGIEPPKGVLLYGPPGTGKTLLAKAVAN 234

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246742881 242 QSNATFLKLAAPQLVQMFIGDGAKLVRDAFALAKEKSPAIIFIDELDAIGTKRfdSEKAGDREvQRTMLELLNQLDGFSS 321
Cdd:TIGR01243 235 EAGAYFISINGPEIMSKYYGESEERLREIFKEAEENAPSIIFIDEIDAIAPKR--EEVTGEVE-KRVVAQLLTLMDGLKG 311

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246742881 322 DDRVKVIAATNRVDTLDPALLRSGRLDRKLEFPLPNEEARVGILRIHSRKMAIDDDINWEELARSTDEYNGAMLKSVCVE 401
Cdd:TIGR01243 312 RGRVIVIGATNRPDALDPALRRPGRFDREIVIRVPDKRARKEILKVHTRNMPLAEDVDLDKLAEVTHGFVGADLAALAKE 391

                         250
                  ....*....|....*...
gi 1246742881 402 AGMIALRQ--GDTKINHE 417
Cdd:TIGR01243 392 AAMAALRRfiREGKINFE 409
RecA-like_CDC48_NLV2_r1-like cd19503
first of two ATPase domains of CDC48 and NLV2, and similar ATPase domains; CDC48 in yeast and ...
 186-353 1.47e-61

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: 197.13  E-value: 1.47e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246742881 186 DIGGLSKQIEELFEAIVLPMQQADKFRKLGVKPPKGCLMFGPPGTGKTLLARACAAQSNATFLKLAAPQLVQMFIGDGAK 265
Cdd:cd19503     1 DIGGLDEQIASLKELIELPLKYPELFRALGLKPPRGVLLHGPPGTGKTLLARAVANEAGANFLSISGPSIVSKYLGESEK 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246742881 266 LVRDAFALAKEKSPAIIFIDELDAIGTKRfdseKAGDREVQRTML-ELLNQLDGFSSDDRVKVIAATNRVDTLDPALLRS 344
Cdd:cd19503    81 NLREIFEEARSHAPSIIFIDEIDALAPKR----EEDQREVERRVVaQLLTLMDGMSSRGKVVVIAATNRPDAIDPALRRP 156


                  ....*....
gi 1246742881 345 GRLDRKLEF 353
Cdd:cd19503   157 GRFDREVEI 165
hflB PRK10733
ATP-dependent zinc metalloprotease FtsH;
169-408 6.95e-58

ATP-dependent zinc metalloprotease FtsH;


Pssm-ID: 182683 [Multi-domain]  Cd Length: 644  Bit Score: 201.03  E-value: 6.95e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246742881 169 SRVKAMEVDEKPTErYSDIGGLSKQIEELFEaIVLPMQQADKFRKLGVKPPKGCLMFGPPGTGKTLLARACAAQSNATFL 248
Cdd:PRK10733  137 SKARMLTEDQIKTT-FADVAGCDEAKEEVAE-LVEYLREPSRFQKLGGKIPKGVLMVGPPGTGKTLLAKAIAGEAKVPFF 214

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246742881 249 KLAAPQLVQMFIGDGAKLVRDAFALAKEKSPAIIFIDELDAIGTKRFDSEKAGDREVQRTMLELLNQLDGFSSDDRVKVI 328
Cdd:PRK10733  215 TISGSDFVEMFVGVGASRVRDMFEQAKKAAPCIIFIDEIDAVGRQRGAGLGGGHDEREQTLNQMLVEMDGFEGNEGIIVI 294

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246742881 329 AATNRVDTLDPALLRSGRLDRKLEFPLPNEEARVGILRIHSRKMAIDDDINWEELARSTDEYNGAMLKSVCVEAGMIALR 408
Cdd:PRK10733  295 AATNRPDVLDPALLRPGRFDRQVVVGLPDVRGREQILKVHMRRVPLAPDIDAAIIARGTPGFSGADLANLVNEAALFAAR 374
RecA-like_CDC48_r2-like cd19511
second of two ATPase domains of CDC48/p97, PEX1 and -6, VAT and NVL, and similar ATPase ...
 195-351 9.58e-55

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: 179.02  E-value: 9.58e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246742881 195 EELFEAIVLPMQQADKFRKLGVKPPKGCLMFGPPGTGKTLLARACAAQSNATFLKLAAPQLVQMFIGDGAKLVRDAFALA 274
Cdd:cd19511     3 RELKEAVEWPLKHPDAFKRLGIRPPKGVLLYGPPGCGKTLLAKALASEAGLNFISVKGPELFSKYVGESERAVREIFQKA 82

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1246742881 275 KEKSPAIIFIDELDAIGTKRFDSEKAGDREvqRTMLELLNQLDGFSSDDRVKVIAATNRVDTLDPALLRSGRLDRKL 351
Cdd:cd19511    83 RQAAPCIIFFDEIDSLAPRRGQSDSSGVTD--RVVSQLLTELDGIESLKGVVVIAATNRPDMIDPALLRPGRLDKLI 157
COG1223 COG1223
Predicted ATPase, AAA+ superfamily [General function prediction only];
190-435 5.67e-53

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


Pssm-ID: 440836 [Multi-domain]  Cd Length: 246  Bit Score: 177.77  E-value: 5.67e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246742881 190 LSKQIEELFEAIVLPMQQADKFRKLGVKPPKGCLMFGPPGTGKTLLARACAAQSNATFLKLAAPQLVQMFIGDGAKLVRD 269
Cdd:COG1223     6 GQEEAKKKLKLIIKELRRRENLRKFGLWPPRKILFYGPPGTGKTMLAEALAGELKLPLLTVRLDSLIGSYLGETARNLRK 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246742881 270 AFALAKEKsPAIIFIDELDAIGTKRFDSEKAGdrEVQRTMLELLNQLDGFSSDdrVKVIAATNRVDTLDPALLRsgRLDR 349
Cdd:COG1223    86 LFDFARRA-PCVIFFDEFDAIAKDRGDQNDVG--EVKRVVNALLQELDGLPSG--SVVIAATNHPELLDSALWR--RFDE 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246742881 350 KLEFPLPNEEARVGILRIHSRKMAIDDDINWEELARSTDEYNGAMLKSVCVEAGMIALRQGDTKINHEHFMDGILEVQMR 429
Cdd:COG1223   159 VIEFPLPDKEERKEILELNLKKFPLPFELDLKKLAKKLEGLSGADIEKVLKTALKKAILEDREKVTKEDLEEALKQRKER 238


                  ....*.
gi 1246742881 430 KSKTLQ 435
Cdd:COG1223   239 KKEPKK 244
RecA-like_CDC48_r1-like cd19519
first of two ATPase domains of CDC48 and similar ATPase domains; CDC48 in yeast and p97 or VCP ...
 186-354 1.21e-52

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: 174.16  E-value: 1.21e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246742881 186 DIGGLSKQIEELFEAIVLPMQQADKFRKLGVKPPKGCLMFGPPGTGKTLLARACAAQSNATFLKLAAPQLVQMFIGDGAK 265
Cdd:cd19519     1 DIGGCRKQLAQIREMVELPLRHPELFKAIGIKPPRGILLYGPPGTGKTLIARAVANETGAFFFLINGPEIMSKLAGESES 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246742881 266 LVRDAFALAKEKSPAIIFIDELDAIGTKRfdsEKAGDREVQRTMLELLNQLDGFSSDDRVKVIAATNRVDTLDPALLRSG 345
Cdd:cd19519    81 NLRKAFEEAEKNAPAIIFIDEIDAIAPKR---EKTHGEVERRIVSQLLTLMDGLKQRAHVIVMAATNRPNSIDPALRRFG 157


                  ....*....
gi 1246742881 346 RLDRKLEFP 354
Cdd:cd19519   158 RFDREIDIG 166
RecA-like_protease cd19481
proteases similar to RecA; RecA-like NTPases. This family includes the NTP binding domain of ...
 193-353 2.26e-52

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: 172.85  E-value: 2.26e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246742881 193 QIEELFEAIVLPMQQaDKFRKLGVKPPKGCLMFGPPGTGKTLLARACAAQSNATFLKLAAPQLVQMFIGDGAKLVRDAFA 272
Cdd:cd19481     1 LKASLREAVEAPRRG-SRLRRYGLGLPKGILLYGPPGTGKTLLAKALAGELGLPLIVVKLSSLLSKYVGESEKNLRKIFE 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246742881 273 LAKEKSPAIIFIDELDAIGTKRFDSekAGDREVQRTMLELLNQLDGFSSDDRVKVIAATNRVDTLDPALLRSGRLDRKLE 352
Cdd:cd19481    80 RARRLAPCILFIDEIDAIGRKRDSS--GESGELRRVLNQLLTELDGVNSRSKVLVIAATNRPDLLDPALLRPGRFDEVIE 157


                  .
gi 1246742881 353 F 353
Cdd:cd19481   158 F 158
RecA-like_VCP_r2 cd19529
second of two ATPase domains of Valosin-containing protein-like ATPase (VAT) and similar ...
 195-351 4.14e-51

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: 169.60  E-value: 4.14e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246742881 195 EELFEAIVLPMQQADKFRKLGVKPPKGCLMFGPPGTGKTLLARACAAQSNATFLKLAAPQLVQMFIGDGAKLVRDAFALA 274
Cdd:cd19529     3 QELKEAVEWPLLKPEVFKRLGIRPPKGILLYGPPGTGKTLLAKAVATESNANFISVKGPELLSKWVGESEKAIREIFRKA 82

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1246742881 275 KEKSPAIIFIDELDAIGTKRFDSEKAGDREvqRTMLELLNQLDGFSSDDRVKVIAATNRVDTLDPALLRSGRLDRKL 351
Cdd:cd19529    83 RQVAPCVIFFDEIDSIAPRRGTTGDSGVTE--RVVNQLLTELDGLEEMNGVVVIAATNRPDIIDPALLRAGRFDRLI 157
AAA pfam00004
ATPase family associated with various cellular activities (AAA); AAA family proteins often ...
 223-355 5.24e-50

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: 165.84  E-value: 5.24e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246742881 223 LMFGPPGTGKTLLARACAAQSNATFLKLAAPQLVQMFIGDGAKLVRDAFALAKEKSPAIIFIDELDAIGTKRFDSekaGD 302
Cdd:pfam00004   2 LLYGPPGTGKTTLAKAVAKELGAPFIEISGSELVSKYVGESEKRLRELFEAAKKLAPCVIFIDEIDALAGSRGSG---GD 78

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1246742881 303 REVQRTMLELLNQLDGFSSD-DRVKVIAATNRVDTLDPALLrsGRLDRKLEFPL 355
Cdd:pfam00004  79 SESRRVVNQLLTELDGFTSSnSKVIVIAATNRPDKLDPALL--GRFDRIIEFPL 130
RecA-like_VPS4-like cd19509
ATPase domain of VPS4, ATAD1, K, KTNA1, Spastin, FIGL-1 and similar ATPase domains; This ...
 187-351 9.83e-47

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: 158.28  E-value: 9.83e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246742881 187 IGGLSKQIEELFEAIVLPMQQADKFRkLGVKPPKGCLMFGPPGTGKTLLARACAAQSNATFLKLAAPQLVQMFIGDGAKL 266
Cdd:cd19509     1 IAGLDDAKEALKEAVILPSLRPDLFP-GLRGPPRGILLYGPPGTGKTLLARAVASESGSTFFSISASSLVSKWVGESEKI 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246742881 267 VRDAFALAKEKSPAIIFIDELDAIGTKRFDSEKAGDREVqRTmlELLNQLDGF--SSDDRVKVIAATNRVDTLDPALLRs 344
Cdd:cd19509    80 VRALFALARELQPSIIFIDEIDSLLSERGSGEHEASRRV-KT--EFLVQMDGVlnKPEDRVLVLGATNRPWELDEAFLR- 155


                  ....*..
gi 1246742881 345 gRLDRKL 351
Cdd:cd19509   156 -RFEKRI 161
pup_AAA TIGR03689
proteasome ATPase; In the Actinobacteria, as shown for Mycobacterium tuberculosis, some ...
 142-378 1.08e-45

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: 165.27  E-value: 1.08e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246742881 142 EELHPGDLIGVNKDSYLIIDKLPSeydSRVKAMEVDEKPTERYSDIGGLSKQIEELFEAIVLPMQQADKFRKLGVKPPKG 221
Cdd:TIGR03689 142 EGLRPGDTLLVDPRAGYAFEAIPR---TEVEDLVLEEVPDVTYADIGGLGSQIEQIRDAVELPFLHPELYREYGLKPPKG 218

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246742881 222 CLMFGPPGTGKTLLARACA---AQSNAT-------FLKLAAPQLVQMFIGDGAKLVRDAFALAKEK----SPAIIFIDEL 287
Cdd:TIGR03689 219 VLLYGPPGCGKTLIAKAVAnslAARIGAegggksyFLNIKGPELLNKYVGETERQIRLIFQRAREKasegRPVIVFFDEM 298

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246742881 288 DAIgtkrFDSEKAG-DREVQRTML-ELLNQLDGFSSDDRVKVIAATNRVDTLDPALLRSGRLDRKLEFPLPNEEARVGIL 365
Cdd:TIGR03689 299 DSL----FRTRGSGvSSDVETTVVpQLLAEIDGVESLDNVIVIGASNREDMIDPAILRPGRLDVKIRIERPDAEAAADIF 374

                         250
                  ....*....|...
gi 1246742881 366 RIHsrkmaIDDDI 378
Cdd:TIGR03689 375 AKY-----LTDDL 382
RecA-like_CDC48_r2-like cd19528
second of two ATPase domains of CDC48 and similar ATPase domains; CDC48 in yeast and p97 or ...
 195-349 1.57e-45

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: 155.36  E-value: 1.57e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246742881 195 EELFEAIVLPMQQADKFRKLGVKPPKGCLMFGPPGTGKTLLARACAAQSNATFLKLAAPQLVQMFIGDGAKLVRDAFALA 274
Cdd:cd19528     3 RELQELVQYPVEHPDKFLKFGMTPSKGVLFYGPPGCGKTLLAKAIANECQANFISVKGPELLTMWFGESEANVRDIFDKA 82

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1246742881 275 KEKSPAIIFIDELDAIGTKR----FDSEKAGDREVQrtmlELLNQLDGFSSDDRVKVIAATNRVDTLDPALLRSGRLDR 349
Cdd:cd19528    83 RAAAPCVLFFDELDSIAKARggniGDAGGAADRVIN----QILTEMDGMNTKKNVFIIGATNRPDIIDPAILRPGRLDQ 157
RecA-like_NVL_r2-like cd19530
second of two ATPase domains of NVL (nuclear VCP-like protein) and similar ATPase domains; NVL ...
 195-351 4.68e-44

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: 151.49  E-value: 4.68e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246742881 195 EELFEAIVLPMQQADKFRKLGVKPPKGCLMFGPPGTGKTLLARACAAQSNATFLKLAAPQLVQMFIGDGAKLVRDAFALA 274
Cdd:cd19530     6 EELTMSILRPIKRPDIYKALGIDLPTGVLLYGPPGCGKTLLAKAVANESGANFISVKGPELLNKYVGESERAVRQVFQRA 85

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1246742881 275 KEKSPAIIFIDELDAIGTKRFDSEKAGdreVQRTMLELLNQLDGFSSDDRVKVIAATNRVDTLDPALLRSGRLDRKL 351
Cdd:cd19530    86 RASAPCVIFFDEVDALVPKRGDGGSWA---SERVVNQLLTEMDGLEERSNVFVIAATNRPDIIDPAMLRPGRLDKTL 159
RecA-like_NVL_r1-like cd19518
first of two ATPase domains of NVL (nuclear VCP-like protein) and similar ATPase domains; NVL ...
 186-351 2.13e-43

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: 149.86  E-value: 2.13e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246742881 186 DIGGLSKQIEELFEAIVLPMQQADKFRKLGVKPPKGCLMFGPPGTGKTLLARACAAQSNATFLKLAAPQLVQMFIGDGAK 265
Cdd:cd19518     1 DIGGMDSTLKELCELLIHPILPPEYFQHLGVEPPRGVLLHGPPGCGKTMLANAIAGELKVPFLKISATEIVSGVSGESEE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246742881 266 LVRDAFALAKEKSPAIIFIDELDAIGTKRFDSEKAGDRevqRTMLELLNQLDGF----SSDDRVKVIAATNRVDTLDPAL 341
Cdd:cd19518    81 KIRELFDQAISNAPCIVFIDEIDAITPKRESAQREMER---RIVSQLLTCMDELnnekTAGGPVLVIGATNRPDSLDPAL 157

                         170
                  ....*....|
gi 1246742881 342 LRSGRLDRKL 351
Cdd:cd19518   158 RRAGRFDREI 167
RecA-like_Figl-1 cd19525
ATPase domain of Fidgetin-Like 1 (FIGL-1); FIGL-1 may participate in DNA repair in the nucleus; ...
 176-351 2.30e-42

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: 147.83  E-value: 2.30e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246742881 176 VDEKPTERYSDIGGLSKQIEELFEAIVLPMQQADKFRKLGvKPPKGCLMFGPPGTGKTLLARACAAQSNATFLKLAAPQL 255
Cdd:cd19525    13 MDHGPPINWADIAGLEFAKKTIKEIVVWPMLRPDIFTGLR-GPPKGILLFGPPGTGKTLIGKCIASQSGATFFSISASSL 91

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246742881 256 VQMFIGDGAKLVRDAFALAKEKSPAIIFIDELDAIGTKRFDSEKAGDRevqRTMLELLNQLDGF--SSDDRVKVIAATNR 333
Cdd:cd19525    92 TSKWVGEGEKMVRALFSVARCKQPAVIFIDEIDSLLSQRGEGEHESSR---RIKTEFLVQLDGAttSSEDRILVVGATNR 168

                         170
                  ....*....|....*...
gi 1246742881 334 VDTLDPALLRsgRLDRKL 351
Cdd:cd19525   169 PQEIDEAARR--RLVKRL 184
RecA-like_spastin cd19524
ATPase domain of spastin; Spastin is an ATP-dependent microtubule-severing protein involved in ...
 186-343 1.24e-40

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: 142.68  E-value: 1.24e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246742881 186 DIGGLSKQIEELFEAIVLPMQQADKFRKLGvKPPKGCLMFGPPGTGKTLLARACAAQSNATFLKLAAPQLVQMFIGDGAK 265
Cdd:cd19524     1 DIAGQDLAKQALQEMVILPSLRPELFTGLR-APARGLLLFGPPGNGKTMLAKAVAAESNATFFNISAASLTSKYVGEGEK 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246742881 266 LVRDAFALAKEKSPAIIFIDELDAIGTKRFDSEKAGDRevqRTMLELLNQLDGFSS--DDRVKVIAATNRVDTLDPALLR 343
Cdd:cd19524    80 LVRALFAVARELQPSIIFIDEVDSLLSERSEGEHEASR---RLKTEFLIEFDGVQSngDDRVLVMGATNRPQELDDAVLR 156
RecA-like_PEX1_r2 cd19526
second of two ATPase domains of Peroxisomal biogenesis factor 1 (PEX1); PEX1(also known as ...
 197-352 4.17e-39

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: 138.33  E-value: 4.17e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246742881 197 LFEAIVLPMQQADKFRKLGVKPPKGCLMFGPPGTGKTLLARACAAQSNATFLKLAAPQLVQMFIGDGAKLVRDAFALAKE 276
Cdd:cd19526     5 LEETIEWPSKYPKIFASSPLRLRSGILLYGPPGCGKTLLASAIASECGLNFISVKGPELLNKYIGASEQNVRDLFSRAQS 84

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1246742881 277 KSPAIIFIDELDAIGTKR-FDSEKAGDREVQrtmlELLNQLDGFSSDDRVKVIAATNRVDTLDPALLRSGRLDRKLE 352
Cdd:cd19526    85 AKPCILFFDEFDSIAPKRgHDSTGVTDRVVN----QLLTQLDGVEGLDGVYVLAATSRPDLIDPALLRPGRLDKLVY 157
RecA-like_ATAD1 cd19520
ATPase domain of ATPase family AAA domain-containing protein 1 and similar ATPase domains; ...
 186-352 5.90e-39

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


Pssm-ID: 410928 [Multi-domain]  Cd Length: 166  Bit Score: 137.94  E-value: 5.90e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246742881 186 DIGGLSKQIEELFEAIVLPMQQADKFRKLGV-KPPKGCLMFGPPGTGKTLLARACAAQSNATFLKLAAPQLVQMFIGDGA 264
Cdd:cd19520     1 DIGGLDEVITELKELVILPLQRPELFDNSRLlQPPKGVLLYGPPGCGKTMLAKATAKEAGARFINLQVSSLTDKWYGESQ 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246742881 265 KLVRDAFALAKEKSPAIIFIDELDAIgtkrFDSEKAGDREVQRTM-LELLNQLDGFSSDD--RVKVIAATNRVDTLDPAL 341
Cdd:cd19520    81 KLVAAVFSLASKLQPSIIFIDEIDSF----LRQRSSTDHEATAMMkAEFMSLWDGLSTDGncRVIVMGATNRPQDLDEAI 156

                         170
                  ....*....|.
gi 1246742881 342 LRsgRLDRKLE 352
Cdd:cd19520   157 LR--RMPKRFH 165
RecA-like_PEX6_r2 cd19527
second of two ATPase domains of Peroxisomal biogenesis factor 6 (PEX6); PEX6(also known as ...
 196-351 1.73e-37

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: 134.18  E-value: 1.73e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246742881 196 ELFEAIVLPMQQADKFRKlGVKPPKGCLMFGPPGTGKTLLARACAAQSNATFLKLAAPQLVQMFIGDGAKLVRDAFALAK 275
Cdd:cd19527     4 EILDTIQLPLEHPELFSS-GLRKRSGILLYGPPGTGKTLLAKAIATECSLNFLSVKGPELINMYIGESEANVREVFQKAR 82

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1246742881 276 EKSPAIIFIDELDAIGTKRFDSEKAGDrEVQRTMLELLNQLDGFS-SDDRVKVIAATNRVDTLDPALLRSGRLDRKL 351
Cdd:cd19527    83 DAKPCVIFFDELDSLAPSRGNSGDSGG-VMDRVVSQLLAELDGMSsSGQDVFVIGATNRPDLLDPALLRPGRFDKLL 158
RecA-like_VPS4 cd19521
ATPase domain of vacuolar protein sorting-associated protein 4; Vacuolar protein ...
 179-351 2.50e-37

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: 133.83  E-value: 2.50e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246742881 179 KPTERYSDIGGLSKQIEELFEAIVLPMqqadKFRKL---GVKPPKGCLMFGPPGTGKTLLARACAAQSNATFLKLAAPQL 255
Cdd:cd19521     1 KPNVKWEDVAGLEGAKEALKEAVILPV----KFPHLftgNRKPWSGILLYGPPGTGKSYLAKAVATEANSTFFSVSSSDL 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246742881 256 VQMFIGDGAKLVRDAFALAKEKSPAIIFIDELDAIGTKRFDSEKAGDRevqRTMLELLNQLDGFSSD-DRVKVIAATNRV 334
Cdd:cd19521    77 VSKWMGESEKLVKQLFAMARENKPSIIFIDEVDSLCGTRGEGESEASR---RIKTELLVQMNGVGNDsQGVLVLGATNIP 153

                         170
                  ....*....|....*..
gi 1246742881 335 DTLDPALLRsgRLDRKL 351
Cdd:cd19521   154 WQLDSAIRR--RFEKRI 168
RecA-like_Yta7-like cd19517
ATPase domain of Saccharomyces cerevisiae Yta7 and similar ATPase domains; Saccharomyces ...
 186-353 7.52e-36

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: 129.94  E-value: 7.52e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246742881 186 DIGGLSKQIEELFEAIVLPMQQADKFRKLGVKPPKGCLMFGPPGTGKTLLARACAA------QSNATFLKLAAPQLVQmF 259
Cdd:cd19517     1 DIGGLSHYINQLKEMVFFPLLYPEVFAKFKITPPRGVLFHGPPGTGKTLMARALAAecskggQKVSFFMRKGADCLSK-W 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246742881 260 IGDGAKLVRDAFALAKEKSPAIIFIDELDAIGTKRFDSEKAGDREVQRTMLELlnqLDGFSSDDRVKVIAATNRVDTLDP 339
Cdd:cd19517    80 VGEAERQLRLLFEEAYRMQPSIIFFDEIDGLAPVRSSKQEQIHASIVSTLLAL---MDGLDNRGQVVVIGATNRPDALDP 156

                         170
                  ....*....|....
gi 1246742881 340 ALLRSGRLDRKLEF 353
Cdd:cd19517   157 ALRRPGRFDREFYF 170
RecA-like_KTNA1 cd19522
Katanin p60 ATPase-containing subunit A1; Katanin p60 ATPase-containing subunit A1 (KTNA1) is ...
 186-351 5.80e-34

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: 125.10  E-value: 5.80e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246742881 186 DIGGLSKQIEELFEAIVLPMQQADKFRklGVKPP-KGCLMFGPPGTGKTLLARACAAQSNATFLKLAAPQLVQMFIGDGA 264
Cdd:cd19522     1 DIADLEEAKKLLEEAVVLPMWMPEFFK--GIRRPwKGVLMVGPPGTGKTLLAKAVATECGTTFFNVSSSTLTSKYRGESE 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246742881 265 KLVRDAFALAKEKSPAIIFIDELDAIGTKR-FDSEKAGDREVQRtmlELLNQLDGFS-------SDDRVKVIAATNRVDT 336
Cdd:cd19522    79 KLVRLLFEMARFYAPTTIFIDEIDSICSRRgTSEEHEASRRVKS---ELLVQMDGVGgasenddPSKMVMVLAATNFPWD 155

                         170
                  ....*....|....*
gi 1246742881 337 LDPALLRsgRLDRKL 351
Cdd:cd19522   156 IDEALRR--RLEKRI 168
RecA-like_fidgetin cd19523
ATPase domain of fidgetin; Fidgetin (FIGN) is a ATP-dependent microtubule severing protein. ...
 186-343 1.73e-30

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


Pssm-ID: 410931 [Multi-domain]  Cd Length: 163  Bit Score: 115.37  E-value: 1.73e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246742881 186 DIGGLSKQIEELFEAIVLPMQQADKFRKLgVKPPKGCLMFGPPGTGKTLLARACAAQSNATFLKLAAPQLVQMFIGDGAK 265
Cdd:cd19523     1 DIAGLGALKAAIKEEVLWPLLRPDAFSGL-LRLPRSILLFGPRGTGKTLLGRCLASQLGATFLRLRGSTLVAKWAGEGEK 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246742881 266 LVRDAFALAKEKSPAIIFIDELDAIGTKRFDSEKAGDrevqRTMLELLNQLDGF--SSDDRVKVIAATNRVDTLDPALLR 343
Cdd:cd19523    80 ILQASFLAARCRQPSVLFISDLDALLSSQDDEASPVG----RLQVELLAQLDGVlgSGEDGVLVVCTTSKPEEIDESLRR 155
RecA-like_NSF-SEC18_r1-like cd19504
first of two ATPase domains of NSF and SEC18, and similar ATPase domains; ...
 187-352 1.62e-26

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: 104.88  E-value: 1.62e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246742881 187 IGGLSKQIEELFE----AIVLPMQQADKfrkLGVKPPKGCLMFGPPGTGKTLLARACAAQSNATFLKLA-APQLVQMFIG 261
Cdd:cd19504     2 IGGLDKEFSDIFRrafaSRVFPPEIVEQ---LGCKHVKGILLYGPPGTGKTLMARQIGKMLNAREPKIVnGPEILNKYVG 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246742881 262 DGAKLVRDAFALAKEKSPA--------IIFIDELDAIGTKRfdSEKAGDREVQRTML-ELLNQLDGFSSDDRVKVIAATN 332
Cdd:cd19504    79 ESEANIRKLFADAEEEQRRlgansglhIIIFDEIDAICKQR--GSMAGSTGVHDTVVnQLLSKIDGVEQLNNILVIGMTN 156

                         170       180
                  ....*....|....*....|
gi 1246742881 333 RVDTLDPALLRSGRLDRKLE 352
Cdd:cd19504   157 RKDLIDEALLRPGRLEVQME 176
AAA cd00009
The AAA+ (ATPases Associated with a wide variety of cellular Activities) superfamily ...
 217-355 9.20e-22

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: 91.05  E-value: 9.20e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246742881 217 KPPKGCLMFGPPGTGKTLLARACAAQS---NATFLKLAAPQLVQMFIG---DGAKLVRDAFALAKEKSPAIIFIDELDAI 290
Cdd:cd00009    17 PPPKNLLLYGPPGTGKTTLARAIANELfrpGAPFLYLNASDLLEGLVVaelFGHFLVRLLFELAEKAKPGVLFIDEIDSL 96

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1246742881 291 GtkrfdsekagdREVQRTMLELLNQL-DGFSSDDRVKVIAATNRVDTLDPALLRSGRLDRKLEFPL 355
Cdd:cd00009    97 S-----------RGAQNALLRVLETLnDLRIDRENVRVIGATNRPLLGDLDRALYDRLDIRIVIPL 151
ycf46 CHL00195
Ycf46; Provisional
 182-406 5.44e-20

Ycf46; Provisional


Pssm-ID: 177094 [Multi-domain]  Cd Length: 489  Bit Score: 92.00  E-value: 5.44e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246742881 182 ERYSDIGGLS------KQIEELFEaivlpmQQADKFrklGVKPPKGCLMFGPPGTGKTLLARACAAQSNATFLKLAAPQL 255
Cdd:CHL00195  225 EKISDIGGLDnlkdwlKKRSTSFS------KQASNY---GLPTPRGLLLVGIQGTGKSLTAKAIANDWQLPLLRLDVGKL 295

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246742881 256 VQMFIGDGAKLVRDAFALAKEKSPAIIFIDELDaigtKRF-DSEKAGD----REVQRTMLELLNQLDGFssddrVKVIAA 330
Cdd:CHL00195  296 FGGIVGESESRMRQMIRIAEALSPCILWIDEID----KAFsNSESKGDsgttNRVLATFITWLSEKKSP-----VFVVAT 366

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1246742881 331 TNRVDTLDPALLRSGRLDRKLEFPLPNEEARVGILRIHSRKMAID--DDINWEELARSTDEYNGAMLKSVCVEAGMIA 406
Cdd:CHL00195  367 ANNIDLLPLEILRKGRFDEIFFLDLPSLEEREKIFKIHLQKFRPKswKKYDIKKLSKLSNKFSGAEIEQSIIEAMYIA 444
RecA-like_Ycf46-like cd19507
ATPase domain of Ycf46 and similar ATPase domains; Ycf46 may play a role in the regulation of ...
 186-349 3.75e-19

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: 83.96  E-value: 3.75e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246742881 186 DIGGLskqiEELFEAIVLPMQQADK-FRKLGVKPPKGCLMFGPPGTGKTLLARACAAQSNATFLKLAAPQLVQMFIGDGA 264
Cdd:cd19507     1 DVGGL----DNLKDWLKKRKAAFSKqASAYGLPTPKGLLLVGIQGTGKSLTAKAIAGVWQLPLLRLDMGRLFGGLVGESE 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246742881 265 KLVRDAFALAKEKSPAIIFIDELD-AIGTKRFDSEKAGDREVQRTMLELLNQldgfsSDDRVKVIAATNRVDTLDPALLR 343
Cdd:cd19507    77 SRLRQMIQTAEAIAPCVLWIDEIEkGFSNADSKGDSGTSSRVLGTFLTWLQE-----KKKPVFVVATANNVQSLPPELLR 151


                  ....*.
gi 1246742881 344 SGRLDR 349
Cdd:cd19507   152 KGRFDE 157
AAA smart00382
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ...
 218-357 3.20e-17

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: 78.18  E-value: 3.20e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246742881  218 PPKGCLMFGPPGTGKTLLARACAAQSNAT-----------------FLKLAAPQLVQMFIGDGAKLVRDAFALAKEKSPA 280
Cdd:smart00382   1 PGEVILIVGPPGSGKTTLARALARELGPPgggviyidgedileevlDQLLLIIVGGKKASGSGELRLRLALALARKLKPD 80

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1246742881  281 IIFIDELDAIGTKRFdsekagdrEVQRTMLELLNQLDGFSSDDRVKVIAATNRVDTLDPALLRSgRLDRKLEFPLPN 357
Cdd:smart00382  81 VLILDEITSLLDAEQ--------EALLLLLEELRLLLLLKSEKNLTVILTTNDEKDLGPALLRR-RFDRRIVLLLIL 148
RecA-like_BCS1 cd19510
Mitochondrial chaperone BCS1; Mitochondrial chaperone BCS1 is necessary for the assembly of ...
 205-353 6.22e-14

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: 68.92  E-value: 6.22e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246742881 205 MQQADKFRKLGVKPPKGCLMFGPPGTGKTLLARACAAQSNATFLKLAAPQLVqmfigDGAKLVRDAFALAKEKSpaIIFI 284
Cdd:cd19510     9 IKNEDWYNDRGIPYRRGYLLYGPPGTGKSSFIAALAGELDYDICDLNLSEVV-----LTDDRLNHLLNTAPKQS--IILL 81

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1246742881 285 DELDAIGTKRFDSEK---AGDREVQRTMLELLNQLDG-FSSDDRVkVIAATNRVDTLDPALLRSGRLDRKLEF 353
Cdd:cd19510    82 EDIDAAFESREHNKKnpsAYGGLSRVTFSGLLNALDGvASSEERI-VFMTTNHIERLDPALIRPGRVDMKIYM 153
RecA-like_Ycf2 cd19505
ATPase domain of plant YCF2; Ycf2 is a chloroplast ATPase which has an essential function; ...
 213-349 2.55e-10

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: 58.93  E-value: 2.55e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246742881 213 KLGVKPPKGCLMFGPPGTGKTLLARACAAQS--------------NATFLKLAAPQLVQMFIGDGAKLVRDAFALAKEKS 278
Cdd:cd19505     6 RLGLSPSKGILLIGSIETGRSYLIKSLAANSyvplirislnkllyNKPDFGNDDWIDGMLILKESLHRLNLQFELAKAMS 85

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1246742881 279 PAIIFIDELDAIGTKRFDSEKAGDREVqrtmleLLNQLDGFSSDDRVK-------VIAATNRVDTLDPALLRSGRLDR 349
Cdd:cd19505    86 PCIIWIPNIHELNVNRSTQNLEEDPKL------LLGLLLNYLSRDFEKsstrnilVIASTHIPQKVDPALIAPNRLDT 157
AAA_lid_3 pfam17862
AAA+ lid domain; This entry represents the alpha helical AAA+ lid domain that is found to the ...
 377-421 8.15e-10

AAA+ lid domain; This entry represents the alpha helical AAA+ lid domain that is found to the C-terminus of AAA domains.


Pssm-ID: 465537 [Multi-domain]  Cd Length: 45  Bit Score: 54.08  E-value: 8.15e-10
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 1246742881 377 DINWEELARSTDEYNGAMLKSVCVEAGMIALRQGDTKINHEHFMD 421
Cdd:pfam17862   1 DVDLEELAERTEGFSGADLEALCREAALAALRRGLEAVTQEDLEE 45
RecA-like_HslU cd19498
ATP-dependent protease ATPase subunit HslU; HslU is a component of the ATP-dependent protease ...
 219-313 1.82e-09

ATP-dependent protease ATPase subunit HslU; HslU is a component of the ATP-dependent protease HslVU. In HslVU, HslU ATPase serves to unfold and translocate protein substrate, and the HslV protease degrades the unfolded proteins. This RecA-like_HslU subfamily belongs to the RecA-like NTPase family which includes the NTP binding domain of F1 and V1 H(+)ATPases, DnaB and related helicases as well as bacterial RecA and related eukaryotic and archaeal recombinases. The RecA-like NTPase family also includes bacterial conjugation proteins and related DNA transfer proteins involved in type II and type IV secretion.


Pssm-ID: 410906 [Multi-domain]  Cd Length: 183  Bit Score: 57.00  E-value: 1.82e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246742881 219 PKGCLMFGPPGTGKTLLARACAAQSNATFLKLAAPQLVQM-FIGdgaklvRDAFALAKEKSPAIIFIDELDAIGTKRFDS 297
Cdd:cd19498    46 PKNILMIGPTGVGKTEIARRLAKLAGAPFIKVEATKFTEVgYVG------RDVESIIRDLVEGIVFIDEIDKIAKRGGSS 119

                          90
                  ....*....|....*..
gi 1246742881 298 EKAGDRE-VQRTMLELL 313
Cdd:cd19498   120 GPDVSREgVQRDLLPIV 136
RarA COG2256
Replication-associated recombination protein RarA (DNA-dependent ATPase) [Replication, ...
 225-286 1.30e-08

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


Pssm-ID: 441857 [Multi-domain]  Cd Length: 439  Bit Score: 56.60  E-value: 1.30e-08
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1246742881 225 FGPPGTGKTLLARACAAQSNATFLKLAApqlvqmfIGDGAKLVRDAFALAKEKS----PAIIFIDE 286
Cdd:COG2256    55 WGPPGTGKTTLARLIANATDAEFVALSA-------VTSGVKDIREVIEEARERRaygrRTILFVDE 113
RecA-like_ATAD3-like cd19512
ATPase domains of ATPase AAA-domain protein 3A (ATAD3A), -3B, and -3C, and similar ATPase ...
 223-353 3.96e-08

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: 52.14  E-value: 3.96e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246742881 223 LMFGPPGTGKTLLARACAAQSNATFLKLAAPQLVQMFiGDGAKLVRDAFALA-KEKSPAIIFIDELDAIGTKRfDSEKAG 301
Cdd:cd19512    26 LFYGPPGTGKTLFAKKLALHSGMDYAIMTGGDVAPMG-REGVTAIHKVFDWAnTSRRGLLLFVDEADAFLRKR-STEKIS 103

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1246742881 302 drEVQRTMLELLNQLDGFSSDDRVKVIaATNRVDTLDPALlrSGRLDRKLEF 353
Cdd:cd19512   104 --EDLRAALNAFLYRTGEQSNKFMLVL-ASNQPEQFDWAI--NDRIDEMVEF 150
PRK13342 PRK13342
recombination factor protein RarA; Reviewed
 225-388 5.12e-08

recombination factor protein RarA; Reviewed


Pssm-ID: 237355 [Multi-domain]  Cd Length: 413  Bit Score: 54.71  E-value: 5.12e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246742881 225 FGPPGTGKTLLARACAAQSNATFLKLAApqlvqmfIGDGAKLVRDAFALAKEKSPA----IIFIDELdaigtKRFDseKA 300
Cdd:PRK13342   42 WGPPGTGKTTLARIIAGATDAPFEALSA-------VTSGVKDLREVIEEARQRRSAgrrtILFIDEI-----HRFN--KA 107

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246742881 301 gdrevqrtmlellnQLDGFSS---DDRVKVIAATnrvdT------LDPALL-RSgrldRKLEF-PLPNEEARVGILRIHS 369
Cdd:PRK13342  108 --------------QQDALLPhveDGTITLIGAT----TenpsfeVNPALLsRA----QVFELkPLSEEDIEQLLKRALE 165

                         170       180
                  ....*....|....*....|...
gi 1246742881 370 RK----MAIDDDInWEELARSTD 388
Cdd:PRK13342  166 DKerglVELDDEA-LDALARLAN 187
AAA_5 pfam07728
AAA domain (dynein-related subfamily); This Pfam entry includes some of the AAA proteins not ...
 223-343 1.59e-07

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


Pssm-ID: 400191 [Multi-domain]  Cd Length: 135  Bit Score: 49.98  E-value: 1.59e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246742881 223 LMFGPPGTGKTLLA-RACAAQSNATFL------KLAAPQLVQ-MFIGDGAKLVRDAFALAKEKSPAIIFIDELDAIgtkr 294
Cdd:pfam07728   3 LLVGPPGTGKTELAeRLAAALSNRPVFyvqltrDTTEEDLFGrRNIDPGGASWVDGPLVRAAREGEIAVLDEINRA---- 78

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1246742881 295 fdsekagDREVQRTMLELLN-----QLDGF----SSDDRVKVIAATNRVDT----LDPALLR 343
Cdd:pfam07728  79 -------NPDVLNSLLSLLDerrllLPDGGelvkAAPDGFRLIATMNPLDRglneLSPALRS 133
RecA-like_Pch2-like cd19508
ATPase domain of Pachytene checkpoint 2 (Pch2) and similar ATPase domains; Pch2 (known as ...
 223-341 3.52e-07

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: 50.52  E-value: 3.52e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246742881 223 LMFGPPGTGKTLLARACAAQ---------SNATFLKLAAPQLVQMFIGDGAKLVRDAF----ALAKEKSpAIIF--IDEL 287
Cdd:cd19508    56 LLHGPPGTGKTSLCKALAQKlsirlssryRYGQLIEINSHSLFSKWFSESGKLVTKMFqkiqELIDDKD-ALVFvlIDEV 134

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1246742881 288 DAIGTKRfDSEKAGD--REVQRTMLELLNQLDGFSSDDRVKVIAATNRVDTLDPAL 341
Cdd:cd19508   135 ESLAAAR-SASSSGTepSDAIRVVNAVLTQIDRIKRYHNNVILLTSNLLEKIDVAF 189
Prot_ATP_ID_OB pfam16450
Proteasomal ATPase OB C-terminal domain; This is the interdomain (ID) or oligonucleotide ...
 88-164 3.85e-07

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


Pssm-ID: 465118 [Multi-domain]  Cd Length: 56  Bit Score: 46.73  E-value: 3.85e-07
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1246742881  88 VGNVVEILDmqpdevdvqesanqnseatrvGKSAVIKTSTRQTIFLPLIGLVEPEELHPGDLIGVNKDSYLIIDKLP 164
Cdd:pfam16450   1 VATVVEVLD---------------------DGRALVKSSGGEERVVRLAGSLDEEKLRPGDRVLLDPRSGYALEVLP 56
44 PHA02544
clamp loader, small subunit; Provisional
 199-374 3.43e-05

clamp loader, small subunit; Provisional


Pssm-ID: 222866 [Multi-domain]  Cd Length: 316  Bit Score: 45.37  E-value: 3.43e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246742881 199 EAIVLPMQQADKFRKLgVKP---PKGCLMFGPPGTGKTLLARACAAQSNATFlklaapqlvqMFI-GDGAKL--VRD--- 269
Cdd:PHA02544   21 DECILPAADKETFKSI-VKKgriPNMLLHSPSPGTGKTTVAKALCNEVGAEV----------LFVnGSDCRIdfVRNrlt 89

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246742881 270 AFALAK--EKSPAIIFIDELDAIGTKrfdsekagdrEVQRTMLELLNQldgFSSDdrVKVIAATNRVDTLDPAlLRSgRL 347
Cdd:PHA02544   90 RFASTVslTGGGKVIIIDEFDRLGLA----------DAQRHLRSFMEA---YSKN--CSFIITANNKNGIIEP-LRS-RC 152

                         170       180
                  ....*....|....*....|....*....
gi 1246742881 348 dRKLEFPLPNEEARVGILR--IHsRKMAI 374
Cdd:PHA02544  153 -RVIDFGVPTKEEQIEMMKqmIV-RCKGI 179
RecA-like_ClpX cd19497
ATP-dependent Clp protease ATP-binding subunit ClpX; ClpX is a component of the ATP-dependent ...
 223-293 2.66e-04

ATP-dependent Clp protease ATP-binding subunit ClpX; ClpX is a component of the ATP-dependent protease ClpXP. In ClpXP, ClpX ATPase serves to specifically recognize, unfold, and translocate protein substrates into the chamber of ClpP protease for degradation. This RecA-like_ClpX domain subfamily belongs to the RecA-like NTPase family which includes the NTP binding domain of F1 and V1 H(+)ATPases, DnaB and related helicases as well as bacterial RecA and related eukaryotic and archaeal recombinases. The RecA-like NTPase family also includes bacterial conjugation proteins and related DNA transfer proteins involved in type II and type IV secretion.


Pssm-ID: 410905 [Multi-domain]  Cd Length: 251  Bit Score: 42.59  E-value: 2.66e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1246742881 223 LMFGPPGTGKTLLARACAAQSNATFLKLAAPQLVQM-FIGDG-----AKLVRDA-FALAK-EKspAIIFIDELDAIGTK 293
Cdd:cd19497    54 LLIGPTGSGKTLLAQTLAKILDVPFAIADATTLTEAgYVGEDvenilLKLLQAAdYDVERaQR--GIVYIDEIDKIARK 130
RecA-like_superfamily cd01120
RecA-like_NTPases; RecA-like NTPases. This superfamily includes the NTP binding domain of F1 ...
 223-338 1.14e-03

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


Pssm-ID: 410865 [Multi-domain]  Cd Length: 119  Bit Score: 38.64  E-value: 1.14e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246742881 223 LMFGPPGTGKTLLARACAAQsnatflklAAPQLVQMFIGDG-AKLVRDAFALAKEKSPAIIFIDELDAIGTkrfdsekAG 301
Cdd:cd01120     2 LITGPPGSGKTTLLLQFAEQ--------ALLSDEPVIFISFlDTILEAIEDLIEEKKLDIIIIDSLSSLAR-------AS 66

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 1246742881 302 DREVQRTMLELLNQLDGFSSDDRVKVIAATNRVDTLD 338
Cdd:cd01120    67 QGDRSSELLEDLAKLLRAARNTGITVIATIHSDKFDI 103
AAA_2 pfam07724
AAA domain (Cdc48 subfamily); This Pfam entry includes some of the AAA proteins not detected ...
 219-313 1.18e-03

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: 39.49  E-value: 1.18e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246742881 219 PKGCLMF-GPPGTGKTLLARACAAqsnatflklaapqlvQMFIGDGAKLVRDAFALAKEKS------------------- 278
Cdd:pfam07724   2 PIGSFLFlGPTGVGKTELAKALAE---------------LLFGDERALIRIDMSEYMEEHSvsrligappgyvgyeeggq 66

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 1246742881 279 ---------PAIIFIDELdaigtkrfdsEKAgDREVQRTMLELL 313
Cdd:pfam07724  67 lteavrrkpYSIVLIDEI----------EKA-HPGVQNDLLQIL 99
ruvB TIGR00635
Holliday junction DNA helicase, RuvB subunit; All proteins in this family for which functions ...
 207-291 1.38e-03

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: 40.36  E-value: 1.38e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246742881 207 QADKFRKlgvKPPKGCLMFGPPGTGKTLLARACAAQSNATFLKLAAPQLVQMfiGDGAKLVrdafALAKEKSpaIIFIDE 286
Cdd:TIGR00635  21 EAAKMRQ---EALDHLLLYGPPGLGKTTLAHIIANEMGVNLKITSGPALEKP--GDLAAIL----TNLEEGD--VLFIDE 89


                  ....*
gi 1246742881 287 LDAIG 291
Cdd:TIGR00635  90 IHRLS 94
ycf2 CHL00206
Ycf2; Provisional
 213-324 1.94e-03

Ycf2; Provisional


Pssm-ID: 214396 [Multi-domain]  Cd Length: 2281  Bit Score: 40.66  E-value: 1.94e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246742881  213 KLGVKPPKGCLMFGPPGTGKTLLARACAAQSNATFLKLAAPQLVqmfigdgaklvrdafalakEKSPAIIFIDELDAIGT 292
Cdd:CHL00206  1624 RLALSPSRGILVIGSIGTGRSYLVKYLATNSYVPFITVFLNKFL-------------------DNKPKGFLIDDIDIDDS 1684

                           90       100       110
                   ....*....|....*....|....*....|....
gi 1246742881  293 KRFDSEKAGDREVQRTMLELLNQLDG--FSSDDR 324
Cdd:CHL00206  1685 DDIDDSDDIDRDLDTELLTMMNALTMdmMPKIDR 1718
T7SS_EccA TIGR03922
type VII secretion AAA-ATPase EccA; This model represents the AAA family ATPase, EccA, of the ...
 223-387 2.28e-03

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


Pssm-ID: 188437 [Multi-domain]  Cd Length: 557  Bit Score: 40.21  E-value: 2.28e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246742881 223 LMFGPPGTGKTLLARACAAQSNATFLkLAAPQLVQM--------FIGDGAKlvrDAFALAKEKSPAIIFIDELDAIGTKR 294
Cdd:TIGR03922 316 LFAGPPGTGKTTIARVVAKIYCGLGV-LRKPLVREVsradligqYIGESEA---KTNEIIDSALGGVLFLDEAYTLVETG 391

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246742881 295 FDSEKAGDREVQRTMLELLNqldgfSSDDRVKVIAATNRVDtLDPAL-----LRSgRLDRKLEFP--LPNEearvgILRI 367
Cdd:TIGR03922 392 YGQKDPFGLEAIDTLLARME-----NDRDRLVVIGAGYRKD-LDKFLevnegLRS-RFTRVIEFPsySPDE-----LVEI 459

                         170       180
                  ....*....|....*....|
gi 1246742881 368 hSRKMAIDDDINWEELARST 387
Cdd:TIGR03922 460 -ARRMATERDSVLDDAAADA 478
YifB COG0606
Predicted Mg-chelatase, contains ChlI-like and ATPase domains, YifB family [Posttranslational ...
 223-237 3.51e-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: 39.64  E-value: 3.51e-03
                          10
                  ....*....|....*
gi 1246742881 223 LMFGPPGTGKTLLAR 237
Cdd:COG0606   215 LMIGPPGSGKTMLAR 229
PRK13341 PRK13341
AAA family ATPase;
223-286 5.05e-03

AAA family ATPase;


Pssm-ID: 237354 [Multi-domain]  Cd Length: 725  Bit Score: 39.27  E-value: 5.05e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1246742881 223 LMFGPPGTGKTLLARACAAQSNATFLKLAApqlvqmfIGDGAKLVRDAFALAKEK-----SPAIIFIDE 286
Cdd:PRK13341   56 ILYGPPGVGKTTLARIIANHTRAHFSSLNA-------VLAGVKDLRAEVDRAKERlerhgKRTILFIDE 117
RecA-like_IQCA1 cd19506
ATPase domain of IQ and AAA domain-containing protein 1 (IQCA1); IQCA1 (also known as dynein ...
 220-333 5.22e-03

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


Pssm-ID: 410914 [Multi-domain]  Cd Length: 160  Bit Score: 37.51  E-value: 5.22e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246742881 220 KGCLMFGPPGTGKTLLARACAAQSNATFLKLAAPQLVQMFIGDGA--KLVRDAFALAKEKSPAIIFIDELDAIGTKRFDS 297
Cdd:cd19506    27 KSLLLAGPSGVGKKMLVHAICTETGANLFNLSPSNIAGKYPGKNGlqMMLHLVLKVARQLQPSVIWIGDAEKTFYKKVPK 106

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 1246742881 298 EKAgDREVQRTMLELLNQLDGFSSDDRVKVIAATNR 333
Cdd:cd19506   107 TEK-QLDPKRLKKDLPKILKSLKPEDRVLIVGTTSR 141
Mg_chelatase pfam01078
Magnesium chelatase, subunit ChlI; Magnesium-chelatase is a three-component enzyme that ...
 223-238 6.63e-03

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


Pssm-ID: 426032 [Multi-domain]  Cd Length: 207  Bit Score: 37.90  E-value: 6.63e-03
                          10
                  ....*....|....*.
gi 1246742881 223 LMFGPPGTGKTLLARA 238
Cdd:pfam01078  26 LMIGPPGSGKTMLAKR 41
COG0645 COG0645
Predicted kinase, contains AAA domain [General function prediction only];
223-248 6.83e-03

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


Pssm-ID: 440410 [Multi-domain]  Cd Length: 164  Bit Score: 37.20  E-value: 6.83e-03
                          10        20
                  ....*....|....*....|....*.
gi 1246742881 223 LMFGPPGTGKTLLARACAAQSNATFL 248
Cdd:COG0645     3 LVCGLPGSGKSTLARALAERLGAVRL 28
 
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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