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Conserved domains on  [gi|213972598|ref|NP_001093979|]
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26S proteasome regulatory subunit 10B [Rattus norvegicus]

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

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
PRK03992 super family cl32052
proteasome-activating nucleotidase; Provisional
19-393 1.62e-168

proteasome-activating nucleotidase; Provisional


The actual alignment was detected with superfamily member PRK03992:

Pssm-ID: 179699 [Multi-domain]  Cd Length: 389  Bit Score: 477.02  E-value: 1.62e-168
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 213972598  19 RDKALQDYRKKLLE-HKEIDGRLKELREQLKELTKQYEKSENDLKALQSVGQIVGEVLKQLTEEKFIVKATNGPRYVVGC 97
Cdd:PRK03992   2 RLEALEERNSELEEqIRQLELKLRDLEAENEKLERELERLKSELEKLKSPPLIVATVLEVLDDGRVVVKSSGGPQFLVNV 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 213972598  98 RRQLDKSKLKPGTRVALDMTTLTIMRYLPREVDPLVYNMSHEDPGNVSYSEIGGLSEQIRELREVIELPLTNPELFQRVG 177
Cdd:PRK03992  82 SPFIDREKLKPGARVALNQQSLAIVEVLPSEKDPRVQAMEVIESPNVTYEDIGGLEEQIREVREAVELPLKKPELFEEVG 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 213972598 178 IIPPKGCLLYGPPGTGKTLLARAVASQLDCNFLKVVSSSIVDKYIGESARLIREMFNYARDHQPCIIFMDEIDAIGGRRF 257
Cdd:PRK03992 162 IEPPKGVLLYGPPGTGKTLLAKAVAHETNATFIRVVGSELVQKFIGEGARLVRELFELAREKAPSIIFIDEIDAIAAKRT 241
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 213972598 258 SEGTSADREIQRTLMELLNQMDGFDTLHRVKMIMATNRPDTLDPALLRPGRLDRKIHIDLPNEQARLDILKIHAGPITKH 337
Cdd:PRK03992 242 DSGTSGDREVQRTLMQLLAEMDGFDPRGNVKIIAATNRIDILDPAILRPGRFDRIIEVPLPDEEGRLEILKIHTRKMNLA 321
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 213972598 338 GEIDYEAIVKLSDGFNGADLRNVCTEAGMFAIRADHDFVVQEDFMKAVRKVADSKK 393
Cdd:PRK03992 322 DDVDLEELAELTEGASGADLKAICTEAGMFAIRDDRTEVTMEDFLKAIEKVMGKEE 377
 
Name Accession Description Interval E-value
PRK03992 PRK03992
proteasome-activating nucleotidase; Provisional
19-393 1.62e-168

proteasome-activating nucleotidase; Provisional


Pssm-ID: 179699 [Multi-domain]  Cd Length: 389  Bit Score: 477.02  E-value: 1.62e-168
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 213972598  19 RDKALQDYRKKLLE-HKEIDGRLKELREQLKELTKQYEKSENDLKALQSVGQIVGEVLKQLTEEKFIVKATNGPRYVVGC 97
Cdd:PRK03992   2 RLEALEERNSELEEqIRQLELKLRDLEAENEKLERELERLKSELEKLKSPPLIVATVLEVLDDGRVVVKSSGGPQFLVNV 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 213972598  98 RRQLDKSKLKPGTRVALDMTTLTIMRYLPREVDPLVYNMSHEDPGNVSYSEIGGLSEQIRELREVIELPLTNPELFQRVG 177
Cdd:PRK03992  82 SPFIDREKLKPGARVALNQQSLAIVEVLPSEKDPRVQAMEVIESPNVTYEDIGGLEEQIREVREAVELPLKKPELFEEVG 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 213972598 178 IIPPKGCLLYGPPGTGKTLLARAVASQLDCNFLKVVSSSIVDKYIGESARLIREMFNYARDHQPCIIFMDEIDAIGGRRF 257
Cdd:PRK03992 162 IEPPKGVLLYGPPGTGKTLLAKAVAHETNATFIRVVGSELVQKFIGEGARLVRELFELAREKAPSIIFIDEIDAIAAKRT 241
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 213972598 258 SEGTSADREIQRTLMELLNQMDGFDTLHRVKMIMATNRPDTLDPALLRPGRLDRKIHIDLPNEQARLDILKIHAGPITKH 337
Cdd:PRK03992 242 DSGTSGDREVQRTLMQLLAEMDGFDPRGNVKIIAATNRIDILDPAILRPGRFDRIIEVPLPDEEGRLEILKIHTRKMNLA 321
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 213972598 338 GEIDYEAIVKLSDGFNGADLRNVCTEAGMFAIRADHDFVVQEDFMKAVRKVADSKK 393
Cdd:PRK03992 322 DDVDLEELAELTEGASGADLKAICTEAGMFAIRDDRTEVTMEDFLKAIEKVMGKEE 377
26Sp45 TIGR01242
26S proteasome subunit P45 family; Many proteins may score above the trusted cutoff because an ...
33-388 5.77e-146

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: 418.82  E-value: 5.77e-146
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 213972598   33 HKEIDGRLKELREQLKELTKQYEKSENDLKALQSVGQ-------IVGEVLKQLTEEKFIVKATNGPRYVVGCRRQLDKSK 105
Cdd:TIGR01242   1 ISELDVRIRKLEDEKRSLEKEKIRLERELERLRSEIErlrspplIVGTVLEVLDDNRVVVKSSTGPNFVVNVSAFIDRKS 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 213972598  106 LKPGTRVALDMTTLTIMRYLPREVDPLVYNMSHEDPGNVSYSEIGGLSEQIRELREVIELPLTNPELFQRVGIIPPKGCL 185
Cdd:TIGR01242  81 LKPGARVALNQQTLTIVDVLPTSKDPLVKGMEVEERPNVSYEDIGGLEEQIREIREAVELPLKHPELFEEVGIEPPKGVL 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 213972598  186 LYGPPGTGKTLLARAVASQLDCNFLKVVSSSIVDKYIGESARLIREMFNYARDHQPCIIFMDEIDAIGGRRFSEGTSADR 265
Cdd:TIGR01242 161 LYGPPGTGKTLLAKAVAHETNATFIRVVGSELVRKYIGEGARLVREIFELAKEKAPSIIFIDEIDAIAAKRTDSGTSGDR 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 213972598  266 EIQRTLMELLNQMDGFDTLHRVKMIMATNRPDTLDPALLRPGRLDRKIHIDLPNEQARLDILKIHAGPITKHGEIDYEAI 345
Cdd:TIGR01242 241 EVQRTLMQLLAELDGFDPRGNVKVIAATNRPDILDPALLRPGRFDRIIEVPLPDFEGRLEILKIHTRKMKLAEDVDLEAI 320
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|...
gi 213972598  346 VKLSDGFNGADLRNVCTEAGMFAIRADHDFVVQEDFMKAVRKV 388
Cdd:TIGR01242 321 AKMTEGASGADLKAICTEAGMFAIREERDYVTMDDFIKAVEKV 363
RPT1 COG1222
ATP-dependent 26S proteasome regulatory subunit [Posttranslational modification, protein ...
137-393 2.76e-133

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


Pssm-ID: 440835 [Multi-domain]  Cd Length: 326  Bit Score: 385.13  E-value: 2.76e-133
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 213972598 137 SHEDPgNVSYSEIGGLSEQIRELREVIELPLTNPELFQRVGIIPPKGCLLYGPPGTGKTLLARAVASQLDCNFLKVVSSS 216
Cdd:COG1222   69 PAESP-DVTFDDIGGLDEQIEEIREAVELPLKNPELFRKYGIEPPKGVLLYGPPGTGKTLLAKAVAGELGAPFIRVRGSE 147
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 213972598 217 IVDKYIGESARLIREMFNYARDHQPCIIFMDEIDAIGGRRFSEGTSAdrEIQRTLMELLNQMDGFDTLHRVKMIMATNRP 296
Cdd:COG1222  148 LVSKYIGEGARNVREVFELAREKAPSIIFIDEIDAIAARRTDDGTSG--EVQRTVNQLLAELDGFESRGDVLIIAATNRP 225
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 213972598 297 DTLDPALLRPGRLDRKIHIDLPNEQARLDILKIHAGPITKHGEIDYEAIVKLSDGFNGADLRNVCTEAGMFAIRADHDFV 376
Cdd:COG1222  226 DLLDPALLRPGRFDRVIEVPLPDEEAREEILKIHLRDMPLADDVDLDKLAKLTEGFSGADLKAIVTEAGMFAIREGRDTV 305
                        250
                 ....*....|....*..
gi 213972598 377 VQEDFMKAVRKVADSKK 393
Cdd:COG1222  306 TMEDLEKAIEKVKKKTE 322
RecA-like_PAN_like cd19502
proteasome activating nucleotidase PAN and related proteasome subunits; This subfamily ...
145-315 7.44e-114

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


Pssm-ID: 410910 [Multi-domain]  Cd Length: 171  Bit Score: 329.68  E-value: 7.44e-114
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 213972598 145 SYSEIGGLSEQIRELREVIELPLTNPELFQRVGIIPPKGCLLYGPPGTGKTLLARAVASQLDCNFLKVVSSSIVDKYIGE 224
Cdd:cd19502    1 TYEDIGGLDEQIREIREVVELPLKHPELFEELGIEPPKGVLLYGPPGTGKTLLAKAVANHTDATFIRVVGSELVQKYIGE 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 213972598 225 SARLIREMFNYARDHQPCIIFMDEIDAIGGRRFSEGTSADREIQRTLMELLNQMDGFDTLHRVKMIMATNRPDTLDPALL 304
Cdd:cd19502   81 GARLVRELFEMAREKAPSIIFIDEIDAIGAKRFDSGTGGDREVQRTMLELLNQLDGFDPRGNIKVIMATNRPDILDPALL 160
                        170
                 ....*....|.
gi 213972598 305 RPGRLDRKIHI 315
Cdd:cd19502  161 RPGRFDRKIEF 171
AAA pfam00004
ATPase family associated with various cellular activities (AAA); AAA family proteins often ...
185-317 2.99e-53

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: 173.16  E-value: 2.99e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 213972598  185 LLYGPPGTGKTLLARAVASQLDCNFLKVVSSSIVDKYIGESARLIREMFNYARDHQPCIIFMDEIDAIGGRRFSEGtsaD 264
Cdd:pfam00004   2 LLYGPPGTGKTTLAKAVAKELGAPFIEISGSELVSKYVGESEKRLRELFEAAKKLAPCVIFIDEIDALAGSRGSGG---D 78
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 213972598  265 REIQRTLMELLNQMDGFDTL-HRVKMIMATNRPDTLDPALLrpGRLDRKIHIDL 317
Cdd:pfam00004  79 SESRRVVNQLLTELDGFTSSnSKVIVIAATNRPDKLDPALL--GRFDRIIEFPL 130
AAA smart00382
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ...
180-319 3.39e-18

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: 80.88  E-value: 3.39e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 213972598   180 PPKGCLLYGPPGTGKTLLARAVASQLDCNFLKVVS-----------------SSIVDKYIGESARLIREMFNYARDHQPC 242
Cdd:smart00382   1 PGEVILIVGPPGSGKTTLARALARELGPPGGGVIYidgedileevldqllliIVGGKKASGSGELRLRLALALARKLKPD 80
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 213972598   243 IIFMDEIDAIggrrfsegTSADREIQRTLMELLNQMDGFDTLHRVKMIMATNRPDTLDPALLRPgRLDRKIHIDLPN 319
Cdd:smart00382  81 VLILDEITSL--------LDAEQEALLLLLEELRLLLLLKSEKNLTVILTTNDEKDLGPALLRR-RFDRRIVLLLIL 148
 
Name Accession Description Interval E-value
PRK03992 PRK03992
proteasome-activating nucleotidase; Provisional
19-393 1.62e-168

proteasome-activating nucleotidase; Provisional


Pssm-ID: 179699 [Multi-domain]  Cd Length: 389  Bit Score: 477.02  E-value: 1.62e-168
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 213972598  19 RDKALQDYRKKLLE-HKEIDGRLKELREQLKELTKQYEKSENDLKALQSVGQIVGEVLKQLTEEKFIVKATNGPRYVVGC 97
Cdd:PRK03992   2 RLEALEERNSELEEqIRQLELKLRDLEAENEKLERELERLKSELEKLKSPPLIVATVLEVLDDGRVVVKSSGGPQFLVNV 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 213972598  98 RRQLDKSKLKPGTRVALDMTTLTIMRYLPREVDPLVYNMSHEDPGNVSYSEIGGLSEQIRELREVIELPLTNPELFQRVG 177
Cdd:PRK03992  82 SPFIDREKLKPGARVALNQQSLAIVEVLPSEKDPRVQAMEVIESPNVTYEDIGGLEEQIREVREAVELPLKKPELFEEVG 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 213972598 178 IIPPKGCLLYGPPGTGKTLLARAVASQLDCNFLKVVSSSIVDKYIGESARLIREMFNYARDHQPCIIFMDEIDAIGGRRF 257
Cdd:PRK03992 162 IEPPKGVLLYGPPGTGKTLLAKAVAHETNATFIRVVGSELVQKFIGEGARLVRELFELAREKAPSIIFIDEIDAIAAKRT 241
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 213972598 258 SEGTSADREIQRTLMELLNQMDGFDTLHRVKMIMATNRPDTLDPALLRPGRLDRKIHIDLPNEQARLDILKIHAGPITKH 337
Cdd:PRK03992 242 DSGTSGDREVQRTLMQLLAEMDGFDPRGNVKIIAATNRIDILDPAILRPGRFDRIIEVPLPDEEGRLEILKIHTRKMNLA 321
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 213972598 338 GEIDYEAIVKLSDGFNGADLRNVCTEAGMFAIRADHDFVVQEDFMKAVRKVADSKK 393
Cdd:PRK03992 322 DDVDLEELAELTEGASGADLKAICTEAGMFAIRDDRTEVTMEDFLKAIEKVMGKEE 377
26Sp45 TIGR01242
26S proteasome subunit P45 family; Many proteins may score above the trusted cutoff because an ...
33-388 5.77e-146

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: 418.82  E-value: 5.77e-146
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 213972598   33 HKEIDGRLKELREQLKELTKQYEKSENDLKALQSVGQ-------IVGEVLKQLTEEKFIVKATNGPRYVVGCRRQLDKSK 105
Cdd:TIGR01242   1 ISELDVRIRKLEDEKRSLEKEKIRLERELERLRSEIErlrspplIVGTVLEVLDDNRVVVKSSTGPNFVVNVSAFIDRKS 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 213972598  106 LKPGTRVALDMTTLTIMRYLPREVDPLVYNMSHEDPGNVSYSEIGGLSEQIRELREVIELPLTNPELFQRVGIIPPKGCL 185
Cdd:TIGR01242  81 LKPGARVALNQQTLTIVDVLPTSKDPLVKGMEVEERPNVSYEDIGGLEEQIREIREAVELPLKHPELFEEVGIEPPKGVL 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 213972598  186 LYGPPGTGKTLLARAVASQLDCNFLKVVSSSIVDKYIGESARLIREMFNYARDHQPCIIFMDEIDAIGGRRFSEGTSADR 265
Cdd:TIGR01242 161 LYGPPGTGKTLLAKAVAHETNATFIRVVGSELVRKYIGEGARLVREIFELAKEKAPSIIFIDEIDAIAAKRTDSGTSGDR 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 213972598  266 EIQRTLMELLNQMDGFDTLHRVKMIMATNRPDTLDPALLRPGRLDRKIHIDLPNEQARLDILKIHAGPITKHGEIDYEAI 345
Cdd:TIGR01242 241 EVQRTLMQLLAELDGFDPRGNVKVIAATNRPDILDPALLRPGRFDRIIEVPLPDFEGRLEILKIHTRKMKLAEDVDLEAI 320
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|...
gi 213972598  346 VKLSDGFNGADLRNVCTEAGMFAIRADHDFVVQEDFMKAVRKV 388
Cdd:TIGR01242 321 AKMTEGASGADLKAICTEAGMFAIREERDYVTMDDFIKAVEKV 363
RPT1 COG1222
ATP-dependent 26S proteasome regulatory subunit [Posttranslational modification, protein ...
137-393 2.76e-133

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


Pssm-ID: 440835 [Multi-domain]  Cd Length: 326  Bit Score: 385.13  E-value: 2.76e-133
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 213972598 137 SHEDPgNVSYSEIGGLSEQIRELREVIELPLTNPELFQRVGIIPPKGCLLYGPPGTGKTLLARAVASQLDCNFLKVVSSS 216
Cdd:COG1222   69 PAESP-DVTFDDIGGLDEQIEEIREAVELPLKNPELFRKYGIEPPKGVLLYGPPGTGKTLLAKAVAGELGAPFIRVRGSE 147
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 213972598 217 IVDKYIGESARLIREMFNYARDHQPCIIFMDEIDAIGGRRFSEGTSAdrEIQRTLMELLNQMDGFDTLHRVKMIMATNRP 296
Cdd:COG1222  148 LVSKYIGEGARNVREVFELAREKAPSIIFIDEIDAIAARRTDDGTSG--EVQRTVNQLLAELDGFESRGDVLIIAATNRP 225
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 213972598 297 DTLDPALLRPGRLDRKIHIDLPNEQARLDILKIHAGPITKHGEIDYEAIVKLSDGFNGADLRNVCTEAGMFAIRADHDFV 376
Cdd:COG1222  226 DLLDPALLRPGRFDRVIEVPLPDEEAREEILKIHLRDMPLADDVDLDKLAKLTEGFSGADLKAIVTEAGMFAIREGRDTV 305
                        250
                 ....*....|....*..
gi 213972598 377 VQEDFMKAVRKVADSKK 393
Cdd:COG1222  306 TMEDLEKAIEKVKKKTE 322
PTZ00454 PTZ00454
26S protease regulatory subunit 6B-like protein; Provisional
15-400 2.32e-116

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


Pssm-ID: 240423 [Multi-domain]  Cd Length: 398  Bit Score: 344.82  E-value: 2.32e-116
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 213972598  15 MADPRDKALQDYRKKLLEHKEIDGRLKEL-------REQLKELTKQYEKSENDLKALQSVGQIVGEVLKQLTEEKFIVKA 87
Cdd:PTZ00454   6 AAAVASSTTHTERDLYEKLKELEKELEFLdiqeeyiKEEQKNLKRELIRAKEEVKRIQSVPLVIGQFLEMIDSNYGIVSS 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 213972598  88 TNGPRYVVGCRRQLDKSKLKPGTRVALDMTTLTIMRYLPREVDPLVYNMSHEDPGNVSYSEIGGLSEQIRELREVIELPL 167
Cdd:PTZ00454  86 TSGSNYYVRILSTLNRELLKPNASVALHRHSHAVVDILPPEADSSIQLLQMSEKPDVTYSDIGGLDIQKQEIREAVELPL 165
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 213972598 168 TNPELFQRVGIIPPKGCLLYGPPGTGKTLLARAVASQLDCNFLKVVSSSIVDKYIGESARLIREMFNYARDHQPCIIFMD 247
Cdd:PTZ00454 166 TCPELYEQIGIDPPRGVLLYGPPGTGKTMLAKAVAHHTTATFIRVVGSEFVQKYLGEGPRMVRDVFRLARENAPSIIFID 245
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 213972598 248 EIDAIGGRRFSEGTSADREIQRTLMELLNQMDGFDTLHRVKMIMATNRPDTLDPALLRPGRLDRKIHIDLPNEQARLDIL 327
Cdd:PTZ00454 246 EVDSIATKRFDAQTGADREVQRILLELLNQMDGFDQTTNVKVIMATNRADTLDPALLRPGRLDRKIEFPLPDRRQKRLIF 325
                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 213972598 328 KIHAGPITKHGEIDYEAIVKLSDGFNGADLRNVCTEAGMFAIRADHDFVVQEDFMKAVRKVAdsKKLESKLDY 400
Cdd:PTZ00454 326 QTITSKMNLSEEVDLEDFVSRPEKISAADIAAICQEAGMQAVRKNRYVILPKDFEKGYKTVV--RKTDRDYDF 396
PTZ00361 PTZ00361
26 proteosome regulatory subunit 4-like protein; Provisional
45-393 6.51e-114

26 proteosome regulatory subunit 4-like protein; Provisional


Pssm-ID: 185575 [Multi-domain]  Cd Length: 438  Bit Score: 339.82  E-value: 6.51e-114
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 213972598  45 EQLKELTKQYEKSENDLKALQSVGQIVGEVLKQLTEEKFIVKATNGPRYVVGCRRQLDKSKLKPGTRVALDMTTLTIMRY 124
Cdd:PTZ00361  81 EAQKPAQEKNEAELKKVDDLRGSPLSVGTLEEIIDENHAIVSSSVGPEYYVNILSFVDKEQLEPGCSVLLHNKTHSVVGI 160
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 213972598 125 LPREVDPLVYNMSHEDPGNVSYSEIGGLSEQIRELREVIELPLTNPELFQRVGIIPPKGCLLYGPPGTGKTLLARAVASQ 204
Cdd:PTZ00361 161 LLDEVDPLVSVMKVDKAPLESYADIGGLEQQIQEIKEAVELPLTHPELYDDIGIKPPKGVILYGPPGTGKTLLAKAVANE 240
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 213972598 205 LDCNFLKVVSSSIVDKYIGESARLIREMFNYARDHQPCIIFMDEIDAIGGRRFSEGTSADREIQRTLMELLNQMDGFDTL 284
Cdd:PTZ00361 241 TSATFLRVVGSELIQKYLGDGPKLVRELFRVAEENAPSIVFIDEIDAIGTKRYDATSGGEKEIQRTMLELLNQLDGFDSR 320
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 213972598 285 HRVKMIMATNRPDTLDPALLRPGRLDRKIHIDLPNEQARLDILKIHAGPITKHGEIDYEAIVKLSDGFNGADLRNVCTEA 364
Cdd:PTZ00361 321 GDVKVIMATNRIESLDPALIRPGRIDRKIEFPNPDEKTKRRIFEIHTSKMTLAEDVDLEEFIMAKDELSGADIKAICTEA 400
                        330       340
                 ....*....|....*....|....*....
gi 213972598 365 GMFAIRADHDFVVQEDFMKAVRKVADSKK 393
Cdd:PTZ00361 401 GLLALRERRMKVTQADFRKAKEKVLYRKK 429
RecA-like_PAN_like cd19502
proteasome activating nucleotidase PAN and related proteasome subunits; This subfamily ...
145-315 7.44e-114

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


Pssm-ID: 410910 [Multi-domain]  Cd Length: 171  Bit Score: 329.68  E-value: 7.44e-114
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 213972598 145 SYSEIGGLSEQIRELREVIELPLTNPELFQRVGIIPPKGCLLYGPPGTGKTLLARAVASQLDCNFLKVVSSSIVDKYIGE 224
Cdd:cd19502    1 TYEDIGGLDEQIREIREVVELPLKHPELFEELGIEPPKGVLLYGPPGTGKTLLAKAVANHTDATFIRVVGSELVQKYIGE 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 213972598 225 SARLIREMFNYARDHQPCIIFMDEIDAIGGRRFSEGTSADREIQRTLMELLNQMDGFDTLHRVKMIMATNRPDTLDPALL 304
Cdd:cd19502   81 GARLVRELFEMAREKAPSIIFIDEIDAIGAKRFDSGTGGDREVQRTMLELLNQLDGFDPRGNIKVIMATNRPDILDPALL 160
                        170
                 ....*....|.
gi 213972598 305 RPGRLDRKIHI 315
Cdd:cd19502  161 RPGRFDRKIEF 171
SpoVK COG0464
AAA+-type ATPase, SpoVK/Ycf46/Vps4 family [Cell wall/membrane/envelope biogenesis, Cell cycle ...
146-393 3.35e-85

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: 264.85  E-value: 3.35e-85
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 213972598 146 YSEIGGLSEQIRELREVIELPLTNPELFQRVGIIPPKGCLLYGPPGTGKTLLARAVASQLDCNFLKVVSSSIVDKYIGES 225
Cdd:COG0464  156 LDDLGGLEEVKEELRELVALPLKRPELREEYGLPPPRGLLLYGPPGTGKTLLARALAGELGLPLIEVDLSDLVSKYVGET 235
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 213972598 226 ARLIREMFNYARDHQPCIIFMDEIDAIGGRRfseGTSADREIQRTLMELLNQMDGFDtlHRVKMIMATNRPDTLDPALLR 305
Cdd:COG0464  236 EKNLREVFDKARGLAPCVLFIDEADALAGKR---GEVGDGVGRRVVNTLLTEMEELR--SDVVVIAATNRPDLLDPALLR 310
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 213972598 306 pgRLDRKIHIDLPNEQARLDILKIHAGPITKHGEIDYEAIVKLSDGFNGADLRNVCTEAGMFAIRADHDFVVQEDFMKAV 385
Cdd:COG0464  311 --RFDEIIFFPLPDAEERLEIFRIHLRKRPLDEDVDLEELAEATEGLSGADIRNVVRRAALQALRLGREPVTTEDLLEAL 388

                 ....*...
gi 213972598 386 RKVADSKK 393
Cdd:COG0464  389 EREDIFLK 396
FtsH_fam TIGR01241
ATP-dependent metalloprotease FtsH; HflB(FtsH) is a pleiotropic protein required for correct ...
139-388 4.05e-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: 249.51  E-value: 4.05e-78
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 213972598  139 EDPGNVSYSEIGGLSEQIRELREVIELpLTNPELFQRVGIIPPKGCLLYGPPGTGKTLLARAVASQLDCNFLKVVSSSIV 218
Cdd:TIGR01241  47 EEKPKVTFKDVAGIDEAKEELMEIVDF-LKNPSKFTKLGAKIPKGVLLVGPPGTGKTLLAKAVAGEAGVPFFSISGSDFV 125
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 213972598  219 DKYIGESARLIREMFNYARDHQPCIIFMDEIDAIGGRRFSEGTSADREIQRTLMELLNQMDGFDTLHRVKMIMATNRPDT 298
Cdd:TIGR01241 126 EMFVGVGASRVRDLFEQAKKNAPCIIFIDEIDAVGRQRGAGLGGGNDEREQTLNQLLVEMDGFGTNTGVIVIAATNRPDV 205
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 213972598  299 LDPALLRPGRLDRKIHIDLPNEQARLDILKIHAGPITKHGEIDYEAIVKLSDGFNGADLRNVCTEAGMFAIRADHDFVVQ 378
Cdd:TIGR01241 206 LDPALLRPGRFDRQVVVDLPDIKGREEILKVHAKNKKLAPDVDLKAVARRTPGFSGADLANLLNEAALLAARKNKTEITM 285
                         250
                  ....*....|
gi 213972598  379 EDFMKAVRKV 388
Cdd:TIGR01241 286 NDIEEAIDRV 295
HflB COG0465
ATP-dependent Zn proteases [Posttranslational modification, protein turnover, chaperones];
139-388 4.42e-78

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


Pssm-ID: 440233 [Multi-domain]  Cd Length: 583  Bit Score: 251.88  E-value: 4.42e-78
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 213972598 139 EDPGNVSYSEIGGLSEQIRELREVIELpLTNPELFQRVGIIPPKGCLLYGPPGTGKTLLARAVASQLDCNFLKVVSSSIV 218
Cdd:COG0465  134 EDKPKVTFDDVAGVDEAKEELQEIVDF-LKDPEKFTRLGAKIPKGVLLVGPPGTGKTLLAKAVAGEAGVPFFSISGSDFV 212
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 213972598 219 DKYIGESARLIREMFNYARDHQPCIIFMDEIDAIGGRRFS--EGTSADREiqRTLMELLNQMDGFDTLHRVKMIMATNRP 296
Cdd:COG0465  213 EMFVGVGASRVRDLFEQAKKNAPCIIFIDEIDAVGRQRGAglGGGHDERE--QTLNQLLVEMDGFEGNEGVIVIAATNRP 290
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 213972598 297 DTLDPALLRPGRLDRKIHIDLPNEQARLDILKIHAGPITKHGEIDYEAIVKLSDGFNGADLRNVCTEAGMFAIRADHDFV 376
Cdd:COG0465  291 DVLDPALLRPGRFDRQVVVDLPDVKGREAILKVHARKKPLAPDVDLEVIARRTPGFSGADLANLVNEAALLAARRNKKAV 370
                        250
                 ....*....|..
gi 213972598 377 VQEDFMKAVRKV 388
Cdd:COG0465  371 TMEDFEEAIDRV 382
CDC48 TIGR01243
AAA family ATPase, CDC48 subfamily; This subfamily of the AAA family ATPases includes two ...
143-401 1.22e-74

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: 246.36  E-value: 1.22e-74
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 213972598  143 NVSYSEIGGLSEQIRELREVIELPLTNPELFQRVGIIPPKGCLLYGPPGTGKTLLARAVASQLDCNFLKVVSSSIVDKYI 222
Cdd:TIGR01243 449 NVRWSDIGGLEEVKQELREAVEWPLKHPEIFEKMGIRPPKGVLLFGPPGTGKTLLAKAVATESGANFIAVRGPEILSKWV 528
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 213972598  223 GESARLIREMFNYARDHQPCIIFMDEIDAIG---GRRFSEGTSadreiQRTLMELLNQMDGFDTLHRVKMIMATNRPDTL 299
Cdd:TIGR01243 529 GESEKAIREIFRKARQAAPAIIFFDEIDAIAparGARFDTSVT-----DRIVNQLLTEMDGIQELSNVVVIAATNRPDIL 603
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 213972598  300 DPALLRPGRLDRKIHIDLPNEQARLDILKIHAGPITKHGEIDYEAIVKLSDGFNGADLRNVCTEAGMFAIRADHDFVVQE 379
Cdd:TIGR01243 604 DPALLRPGRFDRLILVPPPDEEARKEIFKIHTRSMPLAEDVDLEELAEMTEGYTGADIEAVCREAAMAALRESIGSPAKE 683
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|
gi 213972598  380 ------------------DFMKAVRKVADSKKLESKLDYK 401
Cdd:TIGR01243 684 klevgeeeflkdlkvemrHFLEALKKVKPSVSKEDMLRYE 723
RecA-like_CDC48_NLV2_r1-like cd19503
first of two ATPase domains of CDC48 and NLV2, and similar ATPase domains; CDC48 in yeast and ...
148-315 5.23e-69

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: 215.23  E-value: 5.23e-69
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 213972598 148 EIGGLSEQIRELREVIELPLTNPELFQRVGIIPPKGCLLYGPPGTGKTLLARAVASQLDCNFLKVVSSSIVDKYIGESAR 227
Cdd:cd19503    1 DIGGLDEQIASLKELIELPLKYPELFRALGLKPPRGVLLHGPPGTGKTLLARAVANEAGANFLSISGPSIVSKYLGESEK 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 213972598 228 LIREMFNYARDHQPCIIFMDEIDAIGGRRfsegTSADREI-QRTLMELLNQMDGFDTLHRVKMIMATNRPDTLDPALLRP 306
Cdd:cd19503   81 NLREIFEEARSHAPSIIFIDEIDALAPKR----EEDQREVeRRVVAQLLTLMDGMSSRGKVVVIAATNRPDAIDPALRRP 156

                 ....*....
gi 213972598 307 GRLDRKIHI 315
Cdd:cd19503  157 GRFDREVEI 165
RecA-like_FtsH cd19501
ATP-dependent zinc metalloprotease FtsH; FtsH ATPase is a processive, ATP-dependent zinc ...
144-315 7.15e-68

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


Pssm-ID: 410909 [Multi-domain]  Cd Length: 171  Bit Score: 212.48  E-value: 7.15e-68
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 213972598 144 VSYSEIGGLSEQIRELREVIELpLTNPELFQRVGIIPPKGCLLYGPPGTGKTLLARAVASQLDCNFLKVVSSSIVDKYIG 223
Cdd:cd19501    1 VTFKDVAGCEEAKEELKEVVEF-LKNPEKFTKLGAKIPKGVLLVGPPGTGKTLLAKAVAGEAGVPFFSISGSDFVEMFVG 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 213972598 224 ESARLIREMFNYARDHQPCIIFMDEIDAIGGRRFSEGTSADREIQRTLMELLNQMDGFDTLHRVKMIMATNRPDTLDPAL 303
Cdd:cd19501   80 VGASRVRDLFEQAKKNAPCIVFIDEIDAVGRKRGAGLGGGHDEREQTLNQLLVEMDGFESNTGVIVIAATNRPDVLDPAL 159
                        170
                 ....*....|..
gi 213972598 304 LRPGRLDRKIHI 315
Cdd:cd19501  160 LRPGRFDRQVYV 171
CDC48 TIGR01243
AAA family ATPase, CDC48 subfamily; This subfamily of the AAA family ATPases includes two ...
144-370 5.32e-67

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: 225.94  E-value: 5.32e-67
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 213972598  144 VSYSEIGGLSEQIRELREVIELPLTNPELFQRVGIIPPKGCLLYGPPGTGKTLLARAVASQLDCNFLKVVSSSIVDKYIG 223
Cdd:TIGR01243 175 VTYEDIGGLKEAKEKIREMVELPMKHPELFEHLGIEPPKGVLLYGPPGTGKTLLAKAVANEAGAYFISINGPEIMSKYYG 254
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 213972598  224 ESARLIREMFNYARDHQPCIIFMDEIDAIGGRRfsEGTSADREiQRTLMELLNQMDGFDTLHRVKMIMATNRPDTLDPAL 303
Cdd:TIGR01243 255 ESEERLREIFKEAEENAPSIIFIDEIDAIAPKR--EEVTGEVE-KRVVAQLLTLMDGLKGRGRVIVIGATNRPDALDPAL 331
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 213972598  304 LRPGRLDRKIHIDLPNEQARLDILKIHAGPITKHGEIDYEAIVKLSDGFNGADLRNVCTEAGMFAIR 370
Cdd:TIGR01243 332 RRPGRFDREIVIRVPDKRARKEILKVHTRNMPLAEDVDLDKLAEVTHGFVGADLAALAKEAAMAALR 398
RecA-like_CDC48_r2-like cd19511
second of two ATPase domains of CDC48/p97, PEX1 and -6, VAT and NVL, and similar ATPase ...
157-315 1.70e-66

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


Pssm-ID: 410919 [Multi-domain]  Cd Length: 159  Bit Score: 208.29  E-value: 1.70e-66
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 213972598 157 RELREVIELPLTNPELFQRVGIIPPKGCLLYGPPGTGKTLLARAVASQLDCNFLKVVSSSIVDKYIGESARLIREMFNYA 236
Cdd:cd19511    3 RELKEAVEWPLKHPDAFKRLGIRPPKGVLLYGPPGCGKTLLAKALASEAGLNFISVKGPELFSKYVGESERAVREIFQKA 82
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 213972598 237 RDHQPCIIFMDEIDAIGGRRFSEGTSADREiqRTLMELLNQMDGFDTLHRVKMIMATNRPDTLDPALLRPGRLDRKIHI 315
Cdd:cd19511   83 RQAAPCIIFFDEIDSLAPRRGQSDSSGVTD--RVVSQLLTELDGIESLKGVVVIAATNRPDMIDPALLRPGRLDKLIYV 159
ftsH CHL00176
cell division protein; Validated
144-388 2.28e-62

cell division protein; Validated


Pssm-ID: 214386 [Multi-domain]  Cd Length: 638  Bit Score: 211.83  E-value: 2.28e-62
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 213972598 144 VSYSEIGGLSEQIRELREVIELpLTNPELFQRVGIIPPKGCLLYGPPGTGKTLLARAVASQLDCNFLKVVSSSIVDKYIG 223
Cdd:CHL00176 180 ITFRDIAGIEEAKEEFEEVVSF-LKKPERFTAVGAKIPKGVLLVGPPGTGKTLLAKAIAGEAEVPFFSISGSEFVEMFVG 258
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 213972598 224 ESARLIREMFNYARDHQPCIIFMDEIDAIGGRRFS--EGTSADREiqRTLMELLNQMDGFDTLHRVKMIMATNRPDTLDP 301
Cdd:CHL00176 259 VGAARVRDLFKKAKENSPCIVFIDEIDAVGRQRGAgiGGGNDERE--QTLNQLLTEMDGFKGNKGVIVIAATNRVDILDA 336
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 213972598 302 ALLRPGRLDRKIHIDLPNEQARLDILKIHAGPITKHGEIDYEAIVKLSDGFNGADLRNVCTEAGMFAIRADHDFVVQEDF 381
Cdd:CHL00176 337 ALLRPGRFDRQITVSLPDREGRLDILKVHARNKKLSPDVSLELIARRTPGFSGADLANLLNEAAILTARRKKATITMKEI 416

                 ....*..
gi 213972598 382 MKAVRKV 388
Cdd:CHL00176 417 DTAIDRV 423
hflB PRK10733
ATP-dependent zinc metalloprotease FtsH;
136-388 2.43e-62

ATP-dependent zinc metalloprotease FtsH;


Pssm-ID: 182683 [Multi-domain]  Cd Length: 644  Bit Score: 211.82  E-value: 2.43e-62
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 213972598 136 MSHEDPGNVSYSEIGGLSEQIRELREVIELpLTNPELFQRVGIIPPKGCLLYGPPGTGKTLLARAVASQLDCNFLKVVSS 215
Cdd:PRK10733 141 MLTEDQIKTTFADVAGCDEAKEEVAELVEY-LREPSRFQKLGGKIPKGVLMVGPPGTGKTLLAKAIAGEAKVPFFTISGS 219
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 213972598 216 SIVDKYIGESARLIREMFNYARDHQPCIIFMDEIDAIGGRRFSEGTSADREIQRTLMELLNQMDGFDTLHRVKMIMATNR 295
Cdd:PRK10733 220 DFVEMFVGVGASRVRDMFEQAKKAAPCIIFIDEIDAVGRQRGAGLGGGHDEREQTLNQMLVEMDGFEGNEGIIVIAATNR 299
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 213972598 296 PDTLDPALLRPGRLDRKIHIDLPNEQARLDILKIHAGPITKHGEIDYEAIVKLSDGFNGADLRNVCTEAGMFAIRADHDF 375
Cdd:PRK10733 300 PDVLDPALLRPGRFDRQVVVGLPDVRGREQILKVHMRRVPLAPDIDAAIIARGTPGFSGADLANLVNEAALFAARGNKRV 379
                        250
                 ....*....|...
gi 213972598 376 VVQEDFMKAVRKV 388
Cdd:PRK10733 380 VSMVEFEKAKDKI 392
RecA-like_VCP_r2 cd19529
second of two ATPase domains of Valosin-containing protein-like ATPase (VAT) and similar ...
157-315 6.00e-62

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


Pssm-ID: 410937 [Multi-domain]  Cd Length: 159  Bit Score: 196.95  E-value: 6.00e-62
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 213972598 157 RELREVIELPLTNPELFQRVGIIPPKGCLLYGPPGTGKTLLARAVASQLDCNFLKVVSSSIVDKYIGESARLIREMFNYA 236
Cdd:cd19529    3 QELKEAVEWPLLKPEVFKRLGIRPPKGILLYGPPGTGKTLLAKAVATESNANFISVKGPELLSKWVGESEKAIREIFRKA 82
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 213972598 237 RDHQPCIIFMDEIDAIGGRRFSEGTSADREiqRTLMELLNQMDGFDTLHRVKMIMATNRPDTLDPALLRPGRLDRKIHI 315
Cdd:cd19529   83 RQVAPCVIFFDEIDSIAPRRGTTGDSGVTE--RVVNQLLTELDGLEEMNGVVVIAATNRPDIIDPALLRAGRFDRLIYI 159
RecA-like_protease cd19481
proteases similar to RecA; RecA-like NTPases. This family includes the NTP binding domain of ...
155-315 1.26e-61

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


Pssm-ID: 410889 [Multi-domain]  Cd Length: 158  Bit Score: 195.96  E-value: 1.26e-61
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 213972598 155 QIRELREVIELPLTNPELfQRVGIIPPKGCLLYGPPGTGKTLLARAVASQLDCNFLKVVSSSIVDKYIGESARLIREMFN 234
Cdd:cd19481    1 LKASLREAVEAPRRGSRL-RRYGLGLPKGILLYGPPGTGKTLLAKALAGELGLPLIVVKLSSLLSKYVGESEKNLRKIFE 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 213972598 235 YARDHQPCIIFMDEIDAIGGRRFSEGTSADReiQRTLMELLNQMDGFDTLHRVKMIMATNRPDTLDPALLRPGRLDRKIH 314
Cdd:cd19481   80 RARRLAPCILFIDEIDAIGRKRDSSGESGEL--RRVLNQLLTELDGVNSRSKVLVIAATNRPDLLDPALLRPGRFDEVIE 157

                 .
gi 213972598 315 I 315
Cdd:cd19481  158 F 158
pup_AAA TIGR03689
proteasome ATPase; In the Actinobacteria, as shown for Mycobacterium tuberculosis, some ...
67-376 1.07e-59

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: 201.86  E-value: 1.07e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 213972598   67 VGQIVgEVLKQLTEEKFIVKATNGPRYVVGCRRQLDKSKLKPGTRVALDMTTLTIMRYLPR-EVDPLVYnmshEDPGNVS 145
Cdd:TIGR03689 106 TGEIV-TLKEVLDDGRALVTDRSGEERVVKLAGALADEGLRPGDTLLVDPRAGYAFEAIPRtEVEDLVL----EEVPDVT 180
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 213972598  146 YSEIGGLSEQIRELREVIELPLTNPELFQRVGIIPPKGCLLYGPPGTGKTLLARAVASQLdCN-----------FLKVVS 214
Cdd:TIGR03689 181 YADIGGLGSQIEQIRDAVELPFLHPELYREYGLKPPKGVLLYGPPGCGKTLIAKAVANSL-AArigaegggksyFLNIKG 259
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 213972598  215 SSIVDKYIGESARLIREMFNYAR----DHQPCIIFMDEIDAIGGRRFSeGTSADREiqRTLM-ELLNQMDGFDTLHRVKM 289
Cdd:TIGR03689 260 PELLNKYVGETERQIRLIFQRARekasEGRPVIVFFDEMDSLFRTRGS-GVSSDVE--TTVVpQLLAEIDGVESLDNVIV 336
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 213972598  290 IMATNRPDTLDPALLRPGRLDRKIHIDLPNEQARLDILKIHAGPitkhgEIDYEAIVKLSDGFNGAD---LRNVCTEAgM 366
Cdd:TIGR03689 337 IGASNREDMIDPAILRPGRLDVKIRIERPDAEAAADIFAKYLTD-----DLPLPEDLAAHDGDREATaaaLIQRVVDA-L 410
                         330
                  ....*....|
gi 213972598  367 FAIRADHDFV 376
Cdd:TIGR03689 411 YARSEANRYV 420
RecA-like_CDC48_r1-like cd19519
first of two ATPase domains of CDC48 and similar ATPase domains; CDC48 in yeast and p97 or VCP ...
148-315 3.94e-59

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: 189.95  E-value: 3.94e-59
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 213972598 148 EIGGLSEQIRELREVIELPLTNPELFQRVGIIPPKGCLLYGPPGTGKTLLARAVASQLDCNFLKVVSSSIVDKYIGESAR 227
Cdd:cd19519    1 DIGGCRKQLAQIREMVELPLRHPELFKAIGIKPPRGILLYGPPGTGKTLIARAVANETGAFFFLINGPEIMSKLAGESES 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 213972598 228 LIREMFNYARDHQPCIIFMDEIDAIGGRRfsEGTSADREiQRTLMELLNQMDGFDTLHRVKMIMATNRPDTLDPALLRPG 307
Cdd:cd19519   81 NLRKAFEEAEKNAPAIIFIDEIDAIAPKR--EKTHGEVE-RRIVSQLLTLMDGLKQRAHVIVMAATNRPNSIDPALRRFG 157

                 ....*...
gi 213972598 308 RLDRKIHI 315
Cdd:cd19519  158 RFDREIDI 165
COG1223 COG1223
Predicted ATPase, AAA+ superfamily [General function prediction only];
152-399 2.27e-58

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


Pssm-ID: 440836 [Multi-domain]  Cd Length: 246  Bit Score: 190.48  E-value: 2.27e-58
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 213972598 152 LSEQIRELREVIELPLTNPELFQRVGIIPPKGCLLYGPPGTGKTLLARAVASQLDCNFLKVVSSSIVDKYIGESARLIRE 231
Cdd:COG1223    6 GQEEAKKKLKLIIKELRRRENLRKFGLWPPRKILFYGPPGTGKTMLAEALAGELKLPLLTVRLDSLIGSYLGETARNLRK 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 213972598 232 MFNYARDHqPCIIFMDEIDAIGGRRFSegTSADREIQRTLMELLNQMDGFDTlhRVKMIMATNRPDTLDPALLRpgRLDR 311
Cdd:COG1223   86 LFDFARRA-PCVIFFDEFDAIAKDRGD--QNDVGEVKRVVNALLQELDGLPS--GSVVIAATNHPELLDSALWR--RFDE 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 213972598 312 KIHIDLPNEQARLDILKIHAGPITKHGEIDYEAIVKLSDGFNGADLRNVCTEAGMFAIRADHDFVVQEDFMKAVRKVADS 391
Cdd:COG1223  159 VIEFPLPDKEERKEILELNLKKFPLPFELDLKKLAKKLEGLSGADIEKVLKTALKKAILEDREKVTKEDLEEALKQRKER 238

                 ....*...
gi 213972598 392 KKLESKLD 399
Cdd:COG1223  239 KKEPKKEG 246
RecA-like_CDC48_r2-like cd19528
second of two ATPase domains of CDC48 and similar ATPase domains; CDC48 in yeast and p97 or ...
157-315 2.45e-53

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: 174.62  E-value: 2.45e-53
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 213972598 157 RELREVIELPLTNPELFQRVGIIPPKGCLLYGPPGTGKTLLARAVASQLDCNFLKVVSSSIVDKYIGESARLIREMFNYA 236
Cdd:cd19528    3 RELQELVQYPVEHPDKFLKFGMTPSKGVLFYGPPGCGKTLLAKAIANECQANFISVKGPELLTMWFGESEANVRDIFDKA 82
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 213972598 237 RDHQPCIIFMDEIDAIGGRRFSEGTSADREIQRTLMELLNQMDGFDTLHRVKMIMATNRPDTLDPALLRPGRLDRKIHI 315
Cdd:cd19528   83 RAAAPCVLFFDELDSIAKARGGNIGDAGGAADRVINQILTEMDGMNTKKNVFIIGATNRPDIIDPAILRPGRLDQLIYI 161
AAA pfam00004
ATPase family associated with various cellular activities (AAA); AAA family proteins often ...
185-317 2.99e-53

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: 173.16  E-value: 2.99e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 213972598  185 LLYGPPGTGKTLLARAVASQLDCNFLKVVSSSIVDKYIGESARLIREMFNYARDHQPCIIFMDEIDAIGGRRFSEGtsaD 264
Cdd:pfam00004   2 LLYGPPGTGKTTLAKAVAKELGAPFIEISGSELVSKYVGESEKRLRELFEAAKKLAPCVIFIDEIDALAGSRGSGG---D 78
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 213972598  265 REIQRTLMELLNQMDGFDTL-HRVKMIMATNRPDTLDPALLrpGRLDRKIHIDL 317
Cdd:pfam00004  79 SESRRVVNQLLTELDGFTSSnSKVIVIAATNRPDKLDPALL--GRFDRIIEFPL 130
RecA-like_NVL_r1-like cd19518
first of two ATPase domains of NVL (nuclear VCP-like protein) and similar ATPase domains; NVL ...
148-313 4.67e-52

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: 171.82  E-value: 4.67e-52
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 213972598 148 EIGGLSEQIRELREVIELPLTNPELFQRVGIIPPKGCLLYGPPGTGKTLLARAVASQLDCNFLKVVSSSIVDKYIGESAR 227
Cdd:cd19518    1 DIGGMDSTLKELCELLIHPILPPEYFQHLGVEPPRGVLLHGPPGCGKTMLANAIAGELKVPFLKISATEIVSGVSGESEE 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 213972598 228 LIREMFNYARDHQPCIIFMDEIDAIGGRRfsEGTSADREiQRTLMELLNQMDGFDTLHR----VKMIMATNRPDTLDPAL 303
Cdd:cd19518   81 KIRELFDQAISNAPCIVFIDEIDAITPKR--ESAQREME-RRIVSQLLTCMDELNNEKTaggpVLVIGATNRPDSLDPAL 157
                        170
                 ....*....|
gi 213972598 304 LRPGRLDRKI 313
Cdd:cd19518  158 RRAGRFDREI 167
RecA-like_NVL_r2-like cd19530
second of two ATPase domains of NVL (nuclear VCP-like protein) and similar ATPase domains; NVL ...
152-315 1.75e-50

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: 167.28  E-value: 1.75e-50
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 213972598 152 LSEQIRELREVIELPLTNPELFQRVGIIPPKGCLLYGPPGTGKTLLARAVASQLDCNFLKVVSSSIVDKYIGESARLIRE 231
Cdd:cd19530    1 LDHVREELTMSILRPIKRPDIYKALGIDLPTGVLLYGPPGCGKTLLAKAVANESGANFISVKGPELLNKYVGESERAVRQ 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 213972598 232 MFNYARDHQPCIIFMDEIDAIGGRRFSEGTSAdreIQRTLMELLNQMDGFDTLHRVKMIMATNRPDTLDPALLRPGRLDR 311
Cdd:cd19530   81 VFQRARASAPCVIFFDEVDALVPKRGDGGSWA---SERVVNQLLTEMDGLEERSNVFVIAATNRPDIIDPAMLRPGRLDK 157

                 ....
gi 213972598 312 KIHI 315
Cdd:cd19530  158 TLYV 161
RecA-like_VPS4-like cd19509
ATPase domain of VPS4, ATAD1, K, KTNA1, Spastin, FIGL-1 and similar ATPase domains; This ...
149-315 1.90e-50

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


Pssm-ID: 410917 [Multi-domain]  Cd Length: 163  Bit Score: 167.14  E-value: 1.90e-50
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 213972598 149 IGGLSEQIRELREVIELPLTNPELFqRVGIIPPKGCLLYGPPGTGKTLLARAVASQLDCNFLKVVSSSIVDKYIGESARL 228
Cdd:cd19509    1 IAGLDDAKEALKEAVILPSLRPDLF-PGLRGPPRGILLYGPPGTGKTLLARAVASESGSTFFSISASSLVSKWVGESEKI 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 213972598 229 IREMFNYARDHQPCIIFMDEIDAIGGRRFSEGTSADREIqRTlmELLNQMDGF--DTLHRVKMIMATNRPDTLDPALLRp 306
Cdd:cd19509   80 VRALFALARELQPSIIFIDEIDSLLSERGSGEHEASRRV-KT--EFLVQMDGVlnKPEDRVLVLGATNRPWELDEAFLR- 155

                 ....*....
gi 213972598 307 gRLDRKIHI 315
Cdd:cd19509  156 -RFEKRIYI 163
RecA-like_Yta7-like cd19517
ATPase domain of Saccharomyces cerevisiae Yta7 and similar ATPase domains; Saccharomyces ...
148-314 1.50e-48

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: 162.68  E-value: 1.50e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 213972598 148 EIGGLSEQIRELREVIELPLTNPELFQRVGIIPPKGCLLYGPPGTGKTLLARAVASQLDCNFLKVV-----SSSIVDKYI 222
Cdd:cd19517    1 DIGGLSHYINQLKEMVFFPLLYPEVFAKFKITPPRGVLFHGPPGTGKTLMARALAAECSKGGQKVSffmrkGADCLSKWV 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 213972598 223 GESARLIREMFNYARDHQPCIIFMDEIDAIGGRRFSEGTSADREIQRTLMELlnqMDGFDTLHRVKMIMATNRPDTLDPA 302
Cdd:cd19517   81 GEAERQLRLLFEEAYRMQPSIIFFDEIDGLAPVRSSKQEQIHASIVSTLLAL---MDGLDNRGQVVVIGATNRPDALDPA 157
                        170
                 ....*....|..
gi 213972598 303 LLRPGRLDRKIH 314
Cdd:cd19517  158 LRRPGRFDREFY 169
RecA-like_PEX1_r2 cd19526
second of two ATPase domains of Peroxisomal biogenesis factor 1 (PEX1); PEX1(also known as ...
159-313 5.51e-47

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: 157.98  E-value: 5.51e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 213972598 159 LREVIELPLTNPELFQRVGIIPPKGCLLYGPPGTGKTLLARAVASQLDCNFLKVVSSSIVDKYIGESARLIREMFNYARD 238
Cdd:cd19526    5 LEETIEWPSKYPKIFASSPLRLRSGILLYGPPGCGKTLLASAIASECGLNFISVKGPELLNKYIGASEQNVRDLFSRAQS 84
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 213972598 239 HQPCIIFMDEIDAIGGRRFSEGTSAdreIQRTLMELLNQMDGFDTLHRVKMIMATNRPDTLDPALLRPGRLDRKI 313
Cdd:cd19526   85 AKPCILFFDEFDSIAPKRGHDSTGV---TDRVVNQLLTQLDGVEGLDGVYVLAATSRPDLIDPALLRPGRLDKLV 156
RecA-like_ATAD1 cd19520
ATPase domain of ATPase family AAA domain-containing protein 1 and similar ATPase domains; ...
148-315 1.26e-45

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


Pssm-ID: 410928 [Multi-domain]  Cd Length: 166  Bit Score: 154.89  E-value: 1.26e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 213972598 148 EIGGLSEQIRELREVIELPLTNPELFQRVGII-PPKGCLLYGPPGTGKTLLARAVASQLDCNFLKVVSSSIVDKYIGESA 226
Cdd:cd19520    1 DIGGLDEVITELKELVILPLQRPELFDNSRLLqPPKGVLLYGPPGCGKTMLAKATAKEAGARFINLQVSSLTDKWYGESQ 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 213972598 227 RLIREMFNYARDHQPCIIFMDEIDAIGGRRFSEGTSADREIQRTLMELlnqMDGFDT--LHRVKMIMATNRPDTLDPALL 304
Cdd:cd19520   81 KLVAAVFSLASKLQPSIIFIDEIDSFLRQRSSTDHEATAMMKAEFMSL---WDGLSTdgNCRVIVMGATNRPQDLDEAIL 157
                        170
                 ....*....|.
gi 213972598 305 RpgRLDRKIHI 315
Cdd:cd19520  158 R--RMPKRFHI 166
RecA-like_PEX6_r2 cd19527
second of two ATPase domains of Peroxisomal biogenesis factor 6 (PEX6); PEX6(also known as ...
158-315 2.52e-44

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


Pssm-ID: 410935 [Multi-domain]  Cd Length: 160  Bit Score: 151.13  E-value: 2.52e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 213972598 158 ELREVIELPLTNPELFQRvGIIPPKGCLLYGPPGTGKTLLARAVASQLDCNFLKVVSSSIVDKYIGESARLIREMFNYAR 237
Cdd:cd19527    4 EILDTIQLPLEHPELFSS-GLRKRSGILLYGPPGTGKTLLAKAIATECSLNFLSVKGPELINMYIGESEANVREVFQKAR 82
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 213972598 238 DHQPCIIFMDEIDAIGGRRFSEGTSADrEIQRTLMELLNQMDGF-DTLHRVKMIMATNRPDTLDPALLRPGRLDRKIHI 315
Cdd:cd19527   83 DAKPCVIFFDELDSLAPSRGNSGDSGG-VMDRVVSQLLAELDGMsSSGQDVFVIGATNRPDLLDPALLRPGRFDKLLYL 160
RecA-like_KTNA1 cd19522
Katanin p60 ATPase-containing subunit A1; Katanin p60 ATPase-containing subunit A1 (KTNA1) is ...
148-315 1.25e-41

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


Pssm-ID: 410930 [Multi-domain]  Cd Length: 170  Bit Score: 144.74  E-value: 1.25e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 213972598 148 EIGGLSEQIRELREVIELPLTNPELFQrvGIIPP-KGCLLYGPPGTGKTLLARAVASQLDCNFLKVVSSSIVDKYIGESA 226
Cdd:cd19522    1 DIADLEEAKKLLEEAVVLPMWMPEFFK--GIRRPwKGVLMVGPPGTGKTLLAKAVATECGTTFFNVSSSTLTSKYRGESE 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 213972598 227 RLIREMFNYARDHQPCIIFMDEIDAIGGRRfseGTSADREIQRTL-MELLNQMDGF----DTLHRVKMIM---ATNRPDT 298
Cdd:cd19522   79 KLVRLLFEMARFYAPTTIFIDEIDSICSRR---GTSEEHEASRRVkSELLVQMDGVggasENDDPSKMVMvlaATNFPWD 155
                        170
                 ....*....|....*..
gi 213972598 299 LDPALLRpgRLDRKIHI 315
Cdd:cd19522  156 IDEALRR--RLEKRIYI 170
RecA-like_VPS4 cd19521
ATPase domain of vacuolar protein sorting-associated protein 4; Vacuolar protein ...
143-315 1.06e-40

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: 141.92  E-value: 1.06e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 213972598 143 NVSYSEIGGLSEQIRELREVIELPLTNPELFQRvGIIPPKGCLLYGPPGTGKTLLARAVASQLDCNFLKVVSSSIVDKYI 222
Cdd:cd19521    3 NVKWEDVAGLEGAKEALKEAVILPVKFPHLFTG-NRKPWSGILLYGPPGTGKSYLAKAVATEANSTFFSVSSSDLVSKWM 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 213972598 223 GESARLIREMFNYARDHQPCIIFMDEIDAIGGRRfSEGTS-ADREIQrtlMELLNQMDGF-DTLHRVKMIMATNRPDTLD 300
Cdd:cd19521   82 GESEKLVKQLFAMARENKPSIIFIDEVDSLCGTR-GEGESeASRRIK---TELLVQMNGVgNDSQGVLVLGATNIPWQLD 157
                        170
                 ....*....|....*
gi 213972598 301 PALLRpgRLDRKIHI 315
Cdd:cd19521  158 SAIRR--RFEKRIYI 170
RecA-like_Figl-1 cd19525
ATPase domain of Fidgetin-Like 1 (FIGL-1); FIGL-1 may participate in DNA repair in the nucleus; ...
136-315 6.87e-40

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


Pssm-ID: 410933 [Multi-domain]  Cd Length: 186  Bit Score: 140.51  E-value: 6.87e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 213972598 136 MSHEDPgnVSYSEIGGLSEQIRELREVIELPLTNPELFqrVGI-IPPKGCLLYGPPGTGKTLLARAVASQLDCNFLKVVS 214
Cdd:cd19525   13 MDHGPP--INWADIAGLEFAKKTIKEIVVWPMLRPDIF--TGLrGPPKGILLFGPPGTGKTLIGKCIASQSGATFFSISA 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 213972598 215 SSIVDKYIGESARLIREMFNYARDHQPCIIFMDEIDAIGGRRfseGTSADREIQRTLMELLNQMDGFDTL--HRVKMIMA 292
Cdd:cd19525   89 SSLTSKWVGEGEKMVRALFSVARCKQPAVIFIDEIDSLLSQR---GEGEHESSRRIKTEFLVQLDGATTSseDRILVVGA 165
                        170       180
                 ....*....|....*....|...
gi 213972598 293 TNRPDTLDPALLRpgRLDRKIHI 315
Cdd:cd19525  166 TNRPQEIDEAARR--RLVKRLYI 186
RecA-like_spastin cd19524
ATPase domain of spastin; Spastin is an ATP-dependent microtubule-severing protein involved in ...
148-315 1.92e-36

ATPase domain of spastin; Spastin is an ATP-dependent microtubule-severing protein involved in microtubule dynamics; it specifically recognizes and cuts microtubules that are polyglutamylated. This subfamily belongs to the RecA-like NTPase family which includes the NTP binding domain of F1 and V1 H(+)ATPases, DnaB and related helicases as well as bacterial RecA and related eukaryotic and archaeal recombinases. The RecA-like NTPase family also includes bacterial conjugation proteins and related DNA transfer proteins involved in type II and type IV secretion.


Pssm-ID: 410932 [Multi-domain]  Cd Length: 164  Bit Score: 130.74  E-value: 1.92e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 213972598 148 EIGGLSEQIRELREVIELPLTNPELFqrVGI-IPPKGCLLYGPPGTGKTLLARAVASQLDCNFLKVVSSSIVDKYIGESA 226
Cdd:cd19524    1 DIAGQDLAKQALQEMVILPSLRPELF--TGLrAPARGLLLFGPPGNGKTMLAKAVAAESNATFFNISAASLTSKYVGEGE 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 213972598 227 RLIREMFNYARDHQPCIIFMDEIDAIggrrFSEGTSADREIQRTL-MELLNQMDGFDT--LHRVKMIMATNRPDTLDPAL 303
Cdd:cd19524   79 KLVRALFAVARELQPSIIFIDEVDSL----LSERSEGEHEASRRLkTEFLIEFDGVQSngDDRVLVMGATNRPQELDDAV 154
                        170
                 ....*....|..
gi 213972598 304 LRpgRLDRKIHI 315
Cdd:cd19524  155 LR--RFTKRVYV 164
RecA-like_NSF-SEC18_r1-like cd19504
first of two ATPase domains of NSF and SEC18, and similar ATPase domains; ...
149-315 1.90e-32

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


Pssm-ID: 410912 [Multi-domain]  Cd Length: 177  Bit Score: 120.67  E-value: 1.90e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 213972598 149 IGGLSEQIREL-REVIELPLTNPELFQRVGIIPPKGCLLYGPPGTGKTLLARAVASQLDCNFLKVVSS-SIVDKYIGESA 226
Cdd:cd19504    2 IGGLDKEFSDIfRRAFASRVFPPEIVEQLGCKHVKGILLYGPPGTGKTLMARQIGKMLNAREPKIVNGpEILNKYVGESE 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 213972598 227 RLIREMFNYARDHQPC--------IIFMDEIDAIGGRRFSEGTSADREiQRTLMELLNQMDGFDTLHRVKMIMATNRPDT 298
Cdd:cd19504   82 ANIRKLFADAEEEQRRlgansglhIIIFDEIDAICKQRGSMAGSTGVH-DTVVNQLLSKIDGVEQLNNILVIGMTNRKDL 160
                        170
                 ....*....|....*..
gi 213972598 299 LDPALLRPGRLDRKIHI 315
Cdd:cd19504  161 IDEALLRPGRLEVQMEI 177
AAA cd00009
The AAA+ (ATPases Associated with a wide variety of cellular Activities) superfamily ...
150-317 3.97e-25

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: 99.91  E-value: 3.97e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 213972598 150 GGLSEQIRELREVIELPltnpelfqrvgiiPPKGCLLYGPPGTGKTLLARAVASQL---DCNFLKVVSSSIVDKYIGESA 226
Cdd:cd00009    1 VGQEEAIEALREALELP-------------PPKNLLLYGPPGTGKTTLARAIANELfrpGAPFLYLNASDLLEGLVVAEL 67
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 213972598 227 R---LIREMFNYARDHQPCIIFMDEIDAIGgrrfsegtsadREIQRTLMELLNQ-MDGFDTLHRVKMIMATNRPDTLDPA 302
Cdd:cd00009   68 FghfLVRLLFELAEKAKPGVLFIDEIDSLS-----------RGAQNALLRVLETlNDLRIDRENVRVIGATNRPLLGDLD 136
                        170
                 ....*....|....*
gi 213972598 303 LLRPGRLDRKIHIDL 317
Cdd:cd00009  137 RALYDRLDIRIVIPL 151
RecA-like_fidgetin cd19523
ATPase domain of fidgetin; Fidgetin (FIGN) is a ATP-dependent microtubule severing protein. ...
148-305 7.72e-25

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


Pssm-ID: 410931 [Multi-domain]  Cd Length: 163  Bit Score: 99.57  E-value: 7.72e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 213972598 148 EIGGLSEQIRELREVIELPLTNPELFQRVgIIPPKGCLLYGPPGTGKTLLARAVASQLDCNFLKVVSSSIVDKYIGESAR 227
Cdd:cd19523    1 DIAGLGALKAAIKEEVLWPLLRPDAFSGL-LRLPRSILLFGPRGTGKTLLGRCLASQLGATFLRLRGSTLVAKWAGEGEK 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 213972598 228 LIREMFNYARDHQPCIIFMDEIDAIGGRRFSEGTSADReIQrtlMELLNQMDGFDTL--HRVKMIMATNRPDTLDPALLR 305
Cdd:cd19523   80 ILQASFLAARCRQPSVLFISDLDALLSSQDDEASPVGR-LQ---VELLAQLDGVLGSgeDGVLVVCTTSKPEEIDESLRR 155
RecA-like_BCS1 cd19510
Mitochondrial chaperone BCS1; Mitochondrial chaperone BCS1 is necessary for the assembly of ...
163-315 1.54e-21

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: 90.10  E-value: 1.54e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 213972598 163 IELPLTNPELFQRVGIIPPKGCLLYGPPGTGKTLLARAVASQLDCNFLKVVSSSIVDkyigeSARLIREMFNYArdHQPC 242
Cdd:cd19510    5 LKDFIKNEDWYNDRGIPYRRGYLLYGPPGTGKSSFIAALAGELDYDICDLNLSEVVL-----TDDRLNHLLNTA--PKQS 77
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 213972598 243 IIFMDEIDA---IGGRRFSEGTSADREIQRTLMELLNQMDGFDTLHRVKMIMATNRPDTLDPALLRPGRLDRKIHI 315
Cdd:cd19510   78 IILLEDIDAafeSREHNKKNPSAYGGLSRVTFSGLLNALDGVASSEERIVFMTTNHIERLDPALIRPGRVDMKIYM 153
ycf46 CHL00195
Ycf46; Provisional
177-388 2.78e-21

Ycf46; Provisional


Pssm-ID: 177094 [Multi-domain]  Cd Length: 489  Bit Score: 95.47  E-value: 2.78e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 213972598 177 GIIPPKGCLLYGPPGTGKTLLARAVASQLDCNFLKVVSSSIVDKYIGESARLIREMFNYARDHQPCIIFMDEID-AIGGR 255
Cdd:CHL00195 255 GLPTPRGLLLVGIQGTGKSLTAKAIANDWQLPLLRLDVGKLFGGIVGESESRMRQMIRIAEALSPCILWIDEIDkAFSNS 334
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 213972598 256 RFS--EGTSAdrEIQRTLMELLNQMDGFdtlhrVKMIMATNRPDTLDPALLRPGRLDRKIHIDLPNEQARLDILKIHAGP 333
Cdd:CHL00195 335 ESKgdSGTTN--RVLATFITWLSEKKSP-----VFVVATANNIDLLPLEILRKGRFDEIFFLDLPSLEEREKIFKIHLQK 407
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 213972598 334 ITKHG--EIDYEAIVKLSDGFNGADLRNVCTEAGMFAIRADHDFVVQeDFMKAVRKV 388
Cdd:CHL00195 408 FRPKSwkKYDIKKLSKLSNKFSGAEIEQSIIEAMYIAFYEKREFTTD-DILLALKQF 463
RecA-like_Ycf46-like cd19507
ATPase domain of Ycf46 and similar ATPase domains; Ycf46 may play a role in the regulation of ...
174-311 2.03e-20

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


Pssm-ID: 410915 [Multi-domain]  Cd Length: 161  Bit Score: 87.42  E-value: 2.03e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 213972598 174 QRVGIIPPKGCLLYGPPGTGKTLLARAVASQLDCNFLKVVSSSIVDKYIGESARLIREMFNYARDHQPCIIFMDEID-AI 252
Cdd:cd19507   24 SAYGLPTPKGLLLVGIQGTGKSLTAKAIAGVWQLPLLRLDMGRLFGGLVGESESRLRQMIQTAEAIAPCVLWIDEIEkGF 103
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 213972598 253 GGRRFS--EGTSAdreiqRTLMELLNQMDgfdtlHRVK--MIMAT-NRPDTLDPALLRPGRLDR 311
Cdd:cd19507  104 SNADSKgdSGTSS-----RVLGTFLTWLQ-----EKKKpvFVVATaNNVQSLPPELLRKGRFDE 157
AAA smart00382
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ...
180-319 3.39e-18

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: 80.88  E-value: 3.39e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 213972598   180 PPKGCLLYGPPGTGKTLLARAVASQLDCNFLKVVS-----------------SSIVDKYIGESARLIREMFNYARDHQPC 242
Cdd:smart00382   1 PGEVILIVGPPGSGKTTLARALARELGPPGGGVIYidgedileevldqllliIVGGKKASGSGELRLRLALALARKLKPD 80
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 213972598   243 IIFMDEIDAIggrrfsegTSADREIQRTLMELLNQMDGFDTLHRVKMIMATNRPDTLDPALLRPgRLDRKIHIDLPN 319
Cdd:smart00382  81 VLILDEITSL--------LDAEQEALLLLLEELRLLLLLKSEKNLTVILTTNDEKDLGPALLRR-RFDRRIVLLLIL 148
RecA-like_Pch2-like cd19508
ATPase domain of Pachytene checkpoint 2 (Pch2) and similar ATPase domains; Pch2 (known as ...
185-315 3.24e-13

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: 67.86  E-value: 3.24e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 213972598 185 LLYGPPGTGKTLLARAVASQLD---------CNFLKVVSSSIVDKYIGESARLIREMFNYAR---DHQPCIIF--MDEID 250
Cdd:cd19508   56 LLHGPPGTGKTSLCKALAQKLSirlssryryGQLIEINSHSLFSKWFSESGKLVTKMFQKIQeliDDKDALVFvlIDEVE 135
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 213972598 251 AIGGRR--FSEGTSADREIqRTLMELLNQMDGFDTLHRVKMIMATNRPDTLDPALLrpGRLDRKIHI 315
Cdd:cd19508  136 SLAAARsaSSSGTEPSDAI-RVVNAVLTQIDRIKRYHNNVILLTSNLLEKIDVAFV--DRADIKQYI 199
Prot_ATP_ID_OB pfam16450
Proteasomal ATPase OB C-terminal domain; This is the interdomain (ID) or oligonucleotide ...
71-126 3.18e-12

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: 60.98  E-value: 3.18e-12
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 213972598   71 VGEVLKQLTEEKFIVKATNGPRYVVGCRRQLDKSKLKPGTRVALDMTTLTIMRYLP 126
Cdd:pfam16450   1 VATVVEVLDDGRALVKSSGGEERVVRLAGSLDEEKLRPGDRVLLDPRSGYALEVLP 56
AAA_lid_3 pfam17862
AAA+ lid domain; This entry represents the alpha helical AAA+ lid domain that is found to the ...
339-383 4.69e-12

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: 60.24  E-value: 4.69e-12
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 213972598  339 EIDYEAIVKLSDGFNGADLRNVCTEAGMFAIRADHDFVVQEDFMK 383
Cdd:pfam17862   1 DVDLEELAERTEGFSGADLEALCREAALAALRRGLEAVTQEDLEE 45
RecA-like_ATAD3-like cd19512
ATPase domains of ATPase AAA-domain protein 3A (ATAD3A), -3B, and -3C, and similar ATPase ...
185-314 5.59e-11

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


Pssm-ID: 410920 [Multi-domain]  Cd Length: 150  Bit Score: 60.23  E-value: 5.59e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 213972598 185 LLYGPPGTGKTLLARAVA--SQLDcnfLKVVSSSIVDKYIGESARLIREMFNYA-RDHQPCIIFMDEIDAIGGRRFSEGT 261
Cdd:cd19512   26 LFYGPPGTGKTLFAKKLAlhSGMD---YAIMTGGDVAPMGREGVTAIHKVFDWAnTSRRGLLLFVDEADAFLRKRSTEKI 102
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|...
gi 213972598 262 SADreIQRTLMELLNQMDgfDTLHRVKMIMATNRPDTLDPALlrPGRLDRKIH 314
Cdd:cd19512  103 SED--LRAALNAFLYRTG--EQSNKFMLVLASNQPEQFDWAI--NDRIDEMVE 149
PRK13342 PRK13342
recombination factor protein RarA; Reviewed
184-249 1.87e-10

recombination factor protein RarA; Reviewed


Pssm-ID: 237355 [Multi-domain]  Cd Length: 413  Bit Score: 62.02  E-value: 1.87e-10
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 213972598 184 CLLYGPPGTGKTLLARAVASQLDCNFLKV--VSSSIVDkyigesarlIREMFNYARDH----QPCIIFMDEI 249
Cdd:PRK13342  39 MILWGPPGTGKTTLARIIAGATDAPFEALsaVTSGVKD---------LREVIEEARQRrsagRRTILFIDEI 101
RecA-like_Ycf2 cd19505
ATPase domain of plant YCF2; Ycf2 is a chloroplast ATPase which has an essential function; ...
175-315 3.07e-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: 58.54  E-value: 3.07e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 213972598 175 RVGIIPPKGCLLYGPPGTGKTLLARAVASQLDCNFLKV--------------VSSSIVDKYIGESARLIREMFNYARDHQ 240
Cdd:cd19505    6 RLGLSPSKGILLIGSIETGRSYLIKSLAANSYVPLIRIslnkllynkpdfgnDDWIDGMLILKESLHRLNLQFELAKAMS 85
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 213972598 241 PCIIFMDEIDAIGGRRFSEGTSADREIQRTLMELLNQMDGFDTLHRVKMIMA-TNRPDTLDPALLRPGRLDRKIHI 315
Cdd:cd19505   86 PCIIWIPNIHELNVNRSTQNLEEDPKLLLGLLLNYLSRDFEKSSTRNILVIAsTHIPQKVDPALIAPNRLDTCINI 161
RarA COG2256
Replication-associated recombination protein RarA (DNA-dependent ATPase) [Replication, ...
185-258 1.58e-09

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


Pssm-ID: 441857 [Multi-domain]  Cd Length: 439  Bit Score: 59.30  E-value: 1.58e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 213972598 185 LLYGPPGTGKTLLARAVASQLDCNFLKV--VSSSIVDkyigesarlIREMFNYARDH----QPCIIFMDEIDaiggrRFS 258
Cdd:COG2256   53 ILWGPPGTGKTTLARLIANATDAEFVALsaVTSGVKD---------IREVIEEARERraygRRTILFVDEIH-----RFN 118
RecA-like_HslU cd19498
ATP-dependent protease ATPase subunit HslU; HslU is a component of the ATP-dependent protease ...
179-275 3.16e-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: 55.85  E-value: 3.16e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 213972598 179 IPPKGCLLYGPPGTGKTLLARAVASQLDCNFLKVVSSSIVD-KYIGesarliREMFNYARDHQPCIIFMDEIDAIGGRRF 257
Cdd:cd19498   44 VTPKNILMIGPTGVGKTEIARRLAKLAGAPFIKVEATKFTEvGYVG------RDVESIIRDLVEGIVFIDEIDKIAKRGG 117
                         90
                 ....*....|....*....
gi 213972598 258 SEGTSADRE-IQRTLMELL 275
Cdd:cd19498  118 SSGPDVSREgVQRDLLPIV 136
CDC6 COG1474
Cdc6-related protein, AAA superfamily ATPase [Replication, recombination and repair];
154-388 4.77e-08

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


Pssm-ID: 441083 [Multi-domain]  Cd Length: 389  Bit Score: 54.47  E-value: 4.77e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 213972598 154 EQIRELREVIElPLTNPElfqrvgiiPPKGCLLYGPPGTGKTLLARAVASQL---------DCNFLKV----------VS 214
Cdd:COG1474   33 EEIEELASALR-PALRGE--------RPSNVLIYGPTGTGKTAVAKYVLEELeeeaeergvDVRVVYVncrqastryrVL 103
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 213972598 215 SSIVDKyIGESARL------IREMFNYARDH-----QPCIIFMDEIDAIGgrrfsegtsaDREIQRTLMELLNQMDGFDT 283
Cdd:COG1474  104 SRILEE-LGSGEDIpstglsTDELFDRLYEAlderdGVLVVVLDEIDYLV----------DDEGDDLLYQLLRANEELEG 172
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 213972598 284 lHRVKMIMATNRP---DTLDPALLRpgRL-DRKIHIDLPNEQARLDILKIHA------GPITkHGEIDYeaIVKLSDGFN 353
Cdd:COG1474  173 -ARVGVIGISNDLeflENLDPRVKS--SLgEEEIVFPPYDADELRDILEDRAelafydGVLS-DEVIPL--IAALAAQEH 246
                        250       260       270
                 ....*....|....*....|....*....|....*...
gi 213972598 354 GaDLR---NVCTEAGMFAIRADHDFVVQEDFMKAVRKV 388
Cdd:COG1474  247 G-DARkaiDLLRVAGEIAEREGSDRVTEEHVREAREKI 283
RecA-like_ClpX cd19497
ATP-dependent Clp protease ATP-binding subunit ClpX; ClpX is a component of the ATP-dependent ...
185-275 1.33e-07

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: 52.22  E-value: 1.33e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 213972598 185 LLYGPPGTGKTLLARAVASQLDCNFlkvvssSIVDK-------YIGES-----ARLIRE-MFNYARdHQPCIIFMDEIDA 251
Cdd:cd19497   54 LLIGPTGSGKTLLAQTLAKILDVPF------AIADAttlteagYVGEDvenilLKLLQAaDYDVER-AQRGIVYIDEIDK 126
                         90       100
                 ....*....|....*....|....*....
gi 213972598 252 IGgrRFSEGTSADRE-----IQRTLMELL 275
Cdd:cd19497  127 IA--RKSENPSITRDvsgegVQQALLKIL 153
PRK04195 PRK04195
replication factor C large subunit; Provisional
179-255 1.01e-06

replication factor C large subunit; Provisional


Pssm-ID: 235250 [Multi-domain]  Cd Length: 482  Bit Score: 50.69  E-value: 1.01e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 213972598 179 IPPKGCLLYGPPGTGKTLLARAVASQLDcnfLKVV--------SSSIVDKYIGESARLiREMFNYARDhqpcIIFMDEID 250
Cdd:PRK04195  37 KPKKALLLYGPPGVGKTSLAHALANDYG---WEVIelnasdqrTADVIERVAGEAATS-GSLFGARRK----LILLDEVD 108

                 ....*
gi 213972598 251 AIGGR 255
Cdd:PRK04195 109 GIHGN 113
RecA-like_IQCA1 cd19506
ATPase domain of IQ and AAA domain-containing protein 1 (IQCA1); IQCA1 (also known as dynein ...
182-296 1.88e-06

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: 47.52  E-value: 1.88e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 213972598 182 KGCLLYGPPGTGKTLLARAVASQLDCNFLKVVSSSIVDKYIGESA--RLIREMFNYARDHQPCIIFMDEIDAIGGRRF-- 257
Cdd:cd19506   27 KSLLLAGPSGVGKKMLVHAICTETGANLFNLSPSNIAGKYPGKNGlqMMLHLVLKVARQLQPSVIWIGDAEKTFYKKVpk 106
                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 213972598 258 SEGTSADREIQRTLMELLNQMDGFDtlhRVKMIMATNRP 296
Cdd:cd19506  107 TEKQLDPKRLKKDLPKILKSLKPED---RVLIVGTTSRP 142
T7SS_EccA TIGR03922
type VII secretion AAA-ATPase EccA; This model represents the AAA family ATPase, EccA, of the ...
185-272 2.60e-06

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: 49.46  E-value: 2.60e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 213972598  185 LLYGPPGTGKTLLARAVASQLdC--------NFLKVVSSSIVDKYIGESARLIREMFNYARDHqpcIIFMDEIDAIGGRR 256
Cdd:TIGR03922 316 LFAGPPGTGKTTIARVVAKIY-CglgvlrkpLVREVSRADLIGQYIGESEAKTNEIIDSALGG---VLFLDEAYTLVETG 391
                          90
                  ....*....|....*.
gi 213972598  257 FSEGTSADREIQRTLM 272
Cdd:TIGR03922 392 YGQKDPFGLEAIDTLL 407
MoxR COG0714
MoxR-like ATPase [General function prediction only]; MoxR-like ATPase is part of the Pathway ...
184-348 1.49e-05

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


Pssm-ID: 440478 [Multi-domain]  Cd Length: 292  Bit Score: 46.31  E-value: 1.49e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 213972598 184 CLLYGPPGTGKTLLARAVASQLDCNFL-----------KVVSSSIVDKYIGESARLIREMFNyardhqpCIIFMDEIDai 252
Cdd:COG0714   34 LLLEGVPGVGKTTLAKALARALGLPFIriqftpdllpsDILGTYIYDQQTGEFEFRPGPLFA-------NVLLADEIN-- 104
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 213972598 253 ggRrfsegtsADREIQRTLMELLNQM----DGfdTLHRVK---MIMAT-NRPDT-----LDPALLRpgRLDRKIHIDLPN 319
Cdd:COG0714  105 --R-------APPKTQSALLEAMEERqvtiPG--GTYKLPepfLVIATqNPIEQegtypLPEAQLD--RFLLKLYIGYPD 171
                        170       180       190
                 ....*....|....*....|....*....|.
gi 213972598 320 EQARLDILKIHAGPITK--HGEIDYEAIVKL 348
Cdd:COG0714  172 AEEEREILRRHTGRHLAevEPVLSPEELLAL 202
RecA-like_Lon cd19500
lon protease homolog 2 peroxisomal; Lon protease (also known as Lon peptidase) is an ...
185-318 3.55e-05

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


Pssm-ID: 410908 [Multi-domain]  Cd Length: 182  Bit Score: 44.09  E-value: 3.55e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 213972598 185 LLYGPPGTGKTLLARAVASQLDCNFLKVVSSSIVDK---------YIGE-SARLIREMFNyARDHQPcIIFMDEIDAIGG 254
Cdd:cd19500   41 CLVGPPGVGKTSLGKSIARALGRKFVRISLGGVRDEaeirghrrtYVGAmPGRIIQALKK-AGTNNP-VFLLDEIDKIGS 118
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 213972598 255 RRFSEGTSAdreiqrtLMELLN--QMDGF-DT-------LHRVKMIMATNRPDTLDPALlrpgrLDRKIHIDLP 318
Cdd:cd19500  119 SFRGDPASA-------LLEVLDpeQNSTFsDHyldvpfdLSKVLFIATANSLDTIPGPL-----LDRMEIIELS 180
44 PHA02544
clamp loader, small subunit; Provisional
159-390 3.76e-05

clamp loader, small subunit; Provisional


Pssm-ID: 222866 [Multi-domain]  Cd Length: 316  Bit Score: 45.37  E-value: 3.76e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 213972598 159 LREVIeLPLTNPELFQrvGIIP----PKGCLLYGPPGTGKTLLARAVASQLDCNFLKVvsssivdkyIGESARL--IR-E 231
Cdd:PHA02544  20 IDECI-LPAADKETFK--SIVKkgriPNMLLHSPSPGTGKTTVAKALCNEVGAEVLFV---------NGSDCRIdfVRnR 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 213972598 232 MFNYA----RDHQPCIIFMDEIDaiggrrfSEGTSADREIQRTLMELLNQmdgfdtlhRVKMIMATNRPDTLDPALLrpG 307
Cdd:PHA02544  88 LTRFAstvsLTGGGKVIIIDEFD-------RLGLADAQRHLRSFMEAYSK--------NCSFIITANNKNGIIEPLR--S 150
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 213972598 308 RLdRKIHIDLPNEQARLDILK--IH-AGPITKHGEIDYE-----AIVKLsdgfNGADLRNVCTEAGMFA----------- 368
Cdd:PHA02544 151 RC-RVIDFGVPTKEEQIEMMKqmIVrCKGILEAEGVEVDmkvlaALVKK----NFPDFRRTINELQRYAstgkidagils 225
                        250       260
                 ....*....|....*....|....*...
gi 213972598 369 --IRADHDFVVQ----EDFmKAVRKVAD 390
Cdd:PHA02544 226 evTNSDIDDVVEalkaKDF-KAVRALAP 252
AAA_2 pfam07724
AAA domain (Cdc48 subfamily); This Pfam entry includes some of the AAA proteins not detected ...
185-275 5.81e-05

AAA domain (Cdc48 subfamily); This Pfam entry includes some of the AAA proteins not detected by the pfam00004 model.


Pssm-ID: 400187 [Multi-domain]  Cd Length: 168  Bit Score: 43.34  E-value: 5.81e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 213972598  185 LLYGPPGTGKTLLARAVASQL--DCNFLKVVSSS------IVDKYIGESARLIR-----EMFNYARDHQPCIIFMDEIDa 251
Cdd:pfam07724   7 LFLGPTGVGKTELAKALAELLfgDERALIRIDMSeymeehSVSRLIGAPPGYVGyeeggQLTEAVRRKPYSIVLIDEIE- 85
                          90       100
                  ....*....|....*....|....
gi 213972598  252 iggrrfsegtSADREIQRTLMELL 275
Cdd:pfam07724  86 ----------KAHPGVQNDLLQIL 99
clpX PRK05342
ATP-dependent Clp protease ATP-binding subunit ClpX;
185-267 9.45e-05

ATP-dependent Clp protease ATP-binding subunit ClpX;


Pssm-ID: 235422 [Multi-domain]  Cd Length: 412  Bit Score: 44.38  E-value: 9.45e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 213972598 185 LLYGPPGTGKTLLARAVASQLDCNFlkvvssSIVD-------KYIGES-----ARLIRemfnyARDH-----QPCIIFMD 247
Cdd:PRK05342 112 LLIGPTGSGKTLLAQTLARILDVPF------AIADattlteaGYVGEDvenilLKLLQ-----AADYdvekaQRGIVYID 180
                         90       100
                 ....*....|....*....|
gi 213972598 248 EIDAIGgrRFSEGTSADREI 267
Cdd:PRK05342 181 EIDKIA--RKSENPSITRDV 198
RecA-like_superfamily cd01120
RecA-like_NTPases; RecA-like NTPases. This superfamily includes the NTP binding domain of F1 ...
185-300 1.31e-04

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: 41.33  E-value: 1.31e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 213972598 185 LLYGPPGTGKTLLARAVASQLDCNFLKVVSSSIVDKYIgesaRLIREmfnYARDHQPCIIFMDEIDAIGGRRFSEGTSAD 264
Cdd:cd01120    2 LITGPPGSGKTTLLLQFAEQALLSDEPVIFISFLDTIL----EAIED---LIEEKKLDIIIIDSLSSLARASQGDRSSEL 74
                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 213972598 265 REIQRTLMELLNQmdgfdtLHrvKMIMATNRPDTLD 300
Cdd:cd01120   75 LEDLAKLLRAARN------TG--ITVIATIHSDKFD 102
ClpX COG1219
ATP-dependent protease Clp, ATPase subunit ClpX [Posttranslational modification, protein ...
185-262 1.81e-04

ATP-dependent protease Clp, ATPase subunit ClpX [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 440832 [Multi-domain]  Cd Length: 409  Bit Score: 43.50  E-value: 1.81e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 213972598 185 LLYGPPGTGKTLLARAVASQLDCNFlkvvssSIVDK-------YIGES-----ARLIRemfnyARDH-----QPCIIFMD 247
Cdd:COG1219  113 LLIGPTGSGKTLLAQTLARILDVPF------AIADAttlteagYVGEDvenilLKLLQ-----AADYdvekaERGIIYID 181
                         90
                 ....*....|....*
gi 213972598 248 EIDAIGgrRFSEGTS 262
Cdd:COG1219  182 EIDKIA--RKSENPS 194
HolB COG0470
DNA polymerase III, delta prime subunit [Replication, recombination and repair];
185-384 2.34e-04

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


Pssm-ID: 440238 [Multi-domain]  Cd Length: 289  Bit Score: 42.65  E-value: 2.34e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 213972598 185 LLYGPPGTGKTLLARAVASQLDC-----------------------NFLkVVSSSIVDKYIGESA--RLIREMFNYARDH 239
Cdd:COG0470   22 LLHGPPGIGKTTLALALARDLLCenpeggkacgqchsrlmaagnhpDLL-ELNPEEKSDQIGIDQirELGEFLSLTPLEG 100
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 213972598 240 QPCIIFMDEIDAIggrrfseGTSADREIQRTLMELLNqmdgfDTLhrvkMIMATNRPDTLDPALlrpgrLDR--KIHIDL 317
Cdd:COG0470  101 GRKVVIIDEADAM-------NEAAANALLKTLEEPPK-----NTP----FILIANDPSRLLPTI-----RSRcqVIRFRP 159
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 213972598 318 PNEQARLDILKiHAGPitkhGEIDYEAIVKLSDG--------FNGADLRNVCTEAGMFAIRADHDFVVQEDFMKA 384
Cdd:COG0470  160 PSEEEALAWLR-EEGV----DEDALEAILRLAGGdpraainlLQALAGRKELLEDLAALLSRDRALELLDALLKA 229
ruvB PRK00080
Holliday junction branch migration DNA helicase RuvB;
184-220 3.01e-04

Holliday junction branch migration DNA helicase RuvB;


Pssm-ID: 234619 [Multi-domain]  Cd Length: 328  Bit Score: 42.43  E-value: 3.01e-04
                         10        20        30
                 ....*....|....*....|....*....|....*..
gi 213972598 184 CLLYGPPGTGKTLLARAVASQLDCNfLKVVSSSIVDK 220
Cdd:PRK00080  54 VLLYGPPGLGKTTLANIIANEMGVN-IRITSGPALEK 89
RNA_helicase pfam00910
RNA helicase; This family includes RNA helicases thought to be involved in duplex unwinding ...
184-252 4.39e-04

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


Pssm-ID: 459992  Cd Length: 102  Bit Score: 39.12  E-value: 4.39e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 213972598  184 CLLYGPPGTGKTLLARAVASQLdCNFLKVVSSSIvdkYIGESArliREMFN-YarDHQPCIIfMDEIDAI 252
Cdd:pfam00910   1 IWLYGPPGCGKSTLAKYLARAL-LKKLGLPKDSV---YSRNPD---DDFWDgY--TGQPVVI-IDDFGQN 60
ExeA COG3267
Type II secretory pathway ATPase component GspA/ExeA/MshM [Intracellular trafficking, ...
152-206 5.82e-04

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


Pssm-ID: 442498 [Multi-domain]  Cd Length: 261  Bit Score: 41.31  E-value: 5.82e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 213972598 152 LSEQIRELREVIELPLTNPElfqrvGIIppkgcLLYGPPGTGKTLLARAVASQLD 206
Cdd:COG3267   24 LSPSHREALARLEYALAQGG-----GFV-----VLTGEVGTGKTTLLRRLLERLP 68
PRK13341 PRK13341
AAA family ATPase;
185-249 6.05e-04

AAA family ATPase;


Pssm-ID: 237354 [Multi-domain]  Cd Length: 725  Bit Score: 41.96  E-value: 6.05e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 213972598 185 LLYGPPGTGKTLLARAVASQLDCNF--LKVVSSSIVD-KYIGESARLIREMFNyardhQPCIIFMDEI 249
Cdd:PRK13341  56 ILYGPPGVGKTTLARIIANHTRAHFssLNAVLAGVKDlRAEVDRAKERLERHG-----KRTILFIDEV 118
ruvB TIGR00635
Holliday junction DNA helicase, RuvB subunit; All proteins in this family for which functions ...
184-220 7.37e-04

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


Pssm-ID: 129721 [Multi-domain]  Cd Length: 305  Bit Score: 41.13  E-value: 7.37e-04
                          10        20        30
                  ....*....|....*....|....*....|....*..
gi 213972598  184 CLLYGPPGTGKTLLARAVASQLDCNfLKVVSSSIVDK 220
Cdd:TIGR00635  33 LLLYGPPGLGKTTLAHIIANEMGVN-LKITSGPALEK 68
PLN00020 PLN00020
ribulose bisphosphate carboxylase/oxygenase activase -RuBisCO activase (RCA); Provisional
187-354 1.21e-03

ribulose bisphosphate carboxylase/oxygenase activase -RuBisCO activase (RCA); Provisional


Pssm-ID: 215031 [Multi-domain]  Cd Length: 413  Bit Score: 40.85  E-value: 1.21e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 213972598 187 YGPPGTGKTLLARAVASQLDCNflKVVSSS--IVDKYIGESARLIREMFNYARDH-----QPCIIFMDEIDAIGGR-RFS 258
Cdd:PLN00020 154 WGGKGQGKSFQCELVFKKMGIE--PIVMSAgeLESENAGEPGKLIRQRYREAADIikkkgKMSCLFINDLDAGAGRfGTT 231
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 213972598 259 EGTSADREIQRTLMEL--------LNQM-DGFDTLHRVKMIMATNRPDTLDPALLRPGRLDrKIHIDlPNEQARLDIlkI 329
Cdd:PLN00020 232 QYTVNNQMVNGTLMNIadnptnvsLGGDwREKEEIPRVPIIVTGNDFSTLYAPLIRDGRME-KFYWA-PTREDRIGV--V 307
                        170       180
                 ....*....|....*....|....*
gi 213972598 330 HAgpITKHGEIDYEAIVKLSDGFNG 354
Cdd:PLN00020 308 HG--IFRDDGVSREDVVKLVDTFPG 330
AAA_16 pfam13191
AAA ATPase domain; This family of domains contain a P-loop motif that is characteriztic of the ...
151-205 1.56e-03

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


Pssm-ID: 433025 [Multi-domain]  Cd Length: 167  Bit Score: 39.02  E-value: 1.56e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 213972598  151 GLSEQIRELREvielpltnpeLFQRVGIIPPKGCLLYGPPGTGKTLLARAVASQL 205
Cdd:pfam13191   4 GREEELEQLLD----------ALDRVRSGRPPSVLLTGEAGTGKTTLLRELLRAL 48
RuvB_N pfam05496
Holliday junction DNA helicase RuvB P-loop domain; The RuvB protein makes up part of the ...
185-249 1.92e-03

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


Pssm-ID: 398900 [Multi-domain]  Cd Length: 159  Bit Score: 38.64  E-value: 1.92e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 213972598  185 LLYGPPGTGKTLLARAVASQLDCNFlKVVSSSIVDKyIGESARLIREMfnYARDhqpcIIFMDEI 249
Cdd:pfam05496  37 LLYGPPGLGKTTLANIIANEMGVNI-RITSGPAIER-PGDLAAILTNL--EPGD----VLFIDEI 93
ABC_MutS-like cd03283
ATP-binding cassette domain of MutS-like homolog; The MutS protein initiates DNA mismatch ...
176-273 2.39e-03

ATP-binding cassette domain of MutS-like homolog; The MutS protein initiates DNA mismatch repair by recognizing mispaired and unpaired bases embedded in duplex DNA and activating endo- and exonucleases to remove the mismatch. Members of the MutS family possess C-terminal domain with a conserved ATPase activity that belongs to the ATP binding cassette (ABC) superfamily. MutS homologs (MSH) have been identified in most prokaryotic and all eukaryotic organisms examined. Prokaryotes have two homologs (MutS1 and MutS2), whereas seven MSH proteins (MSH1 to MSH7) have been identified in eukaryotes. The homodimer MutS1 and heterodimers MSH2-MSH3 and MSH2-MSH6 are primarily involved in mitotic mismatch repair, whereas MSH4-MSH5 is involved in resolution of Holliday junctions during meiosis. All members of the MutS family contain the highly conserved Walker A/B ATPase domain, and many share a common mechanism of action. MutS1, MSH2-MSH3, MSH2-MSH6, and MSH4-MSH5 dimerize to form sliding clamps, and recognition of specific DNA structures or lesions results in ADP/ATP exchange.


Pssm-ID: 213250 [Multi-domain]  Cd Length: 199  Bit Score: 38.82  E-value: 2.39e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 213972598 176 VGIIPPKGCLLYGPPGTGKTLLARAV--------------ASQLDCNFLKVVSSSIV--DKYIGES-----ARLIREMFN 234
Cdd:cd03283   20 IDMEKKNGILITGSNMSGKSTFLRTIgvnvilaqagapvcASSFELPPVKIFTSIRVsdDLRDGISyfyaeLRRLKEIVE 99
                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 213972598 235 YARDHQPCIIFMDEIdaIGGRRFSEGTSADREIQRTLME 273
Cdd:cd03283  100 KAKKGEPVLFLLDEI--FKGTNSRERQAASAAVLKFLKN 136
RuvB COG2255
Holliday junction resolvasome RuvABC, ATP-dependent DNA helicase subunit RuvB [Replication, ...
184-209 2.87e-03

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


Pssm-ID: 441856 [Multi-domain]  Cd Length: 337  Bit Score: 39.29  E-value: 2.87e-03
                         10        20
                 ....*....|....*....|....*.
gi 213972598 184 CLLYGPPGTGKTLLARAVASQLDCNF 209
Cdd:COG2255   57 VLLYGPPGLGKTTLAHIIANEMGVNI 82
PRK08116 PRK08116
hypothetical protein; Validated
183-217 4.44e-03

hypothetical protein; Validated


Pssm-ID: 236153 [Multi-domain]  Cd Length: 268  Bit Score: 38.46  E-value: 4.44e-03
                         10        20        30
                 ....*....|....*....|....*....|....*
gi 213972598 183 GCLLYGPPGTGKTLLARAVASQLDCNFLKVVSSSI 217
Cdd:PRK08116 116 GLLLWGSVGTGKTYLAACIANELIEKGVPVIFVNF 150
McrB COG1401
5-methylcytosine-specific restriction endonuclease McrBC, GTP-binding regulatory subunit McrB ...
185-205 5.67e-03

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


Pssm-ID: 441011 [Multi-domain]  Cd Length: 477  Bit Score: 38.60  E-value: 5.67e-03
                         10        20
                 ....*....|....*....|.
gi 213972598 185 LLYGPPGTGKTLLARAVASQL 205
Cdd:COG1401  225 ILAGPPGTGKTYLARRLAEAL 245
TIP49 COG1224
DNA helicase TIP49, TBP-interacting protein [Transcription];
182-205 7.75e-03

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


Pssm-ID: 440837 [Multi-domain]  Cd Length: 452  Bit Score: 38.41  E-value: 7.75e-03
                         10        20
                 ....*....|....*....|....
gi 213972598 182 KGCLLYGPPGTGKTLLARAVASQL 205
Cdd:COG1224   65 KGILIVGPPGTGKTALAVAIAREL 88
YifB COG0606
Predicted Mg-chelatase, contains ChlI-like and ATPase domains, YifB family [Posttranslational ...
185-203 8.50e-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: 38.10  E-value: 8.50e-03
                         10
                 ....*....|....*....
gi 213972598 185 LLYGPPGTGKTLLARAVAS 203
Cdd:COG0606  215 LMIGPPGSGKTMLARRLPG 233
Mg_chelatase pfam01078
Magnesium chelatase, subunit ChlI; Magnesium-chelatase is a three-component enzyme that ...
185-205 9.73e-03

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


Pssm-ID: 426032 [Multi-domain]  Cd Length: 207  Bit Score: 37.13  E-value: 9.73e-03
                          10        20
                  ....*....|....*....|.
gi 213972598  185 LLYGPPGTGKTLLARAVASQL 205
Cdd:pfam01078  26 LMIGPPGSGKTMLAKRLPGIL 46
 
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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