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Conserved domains on  [gi|228008337|ref|NP_032974|]
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26S proteasome regulatory subunit 6A [Mus musculus]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PRK03992 super family cl32052
proteasome-activating nucleotidase; Provisional
 42-435 3.40e-166

proteasome-activating nucleotidase; Provisional


The actual alignment was detected with superfamily member PRK03992:

Pssm-ID: 179699 [Multi-domain]  Cd Length: 389  Bit Score: 472.78  E-value: 3.40e-166
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008337  42 EEIVQRTRLLDSEIKIMKSEVLRVTHELQAMKdkiKENsEKIKvnkTLPYLVSNVIELLDvdpndqeeDGAnidldsqrk 121
Cdd:PRK03992  11 SELEEQIRQLELKLRDLEAENEKLERELERLK---SEL-EKLK---SPPLIVATVLEVLD--------DGR--------- 66

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008337 122 gkcAVIKTSTRQTYFLPVIGLVDAEKLKPGDLVGVNKDSYLILETLPTEYDSRVKAMEVDERPTEQYSDIGGLDKQIQEL 201
Cdd:PRK03992  67 ---VVVKSSGGPQFLVNVSPFIDREKLKPGARVALNQQSLAIVEVLPSEKDPRVQAMEVIESPNVTYEDIGGLEEQIREV 143

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008337 202 VEAIVLPMNHKEKFENLGIQPPKGVLMYGPPGTGKTLLARACAAQTKATFLKLAGPQLVQMFIGDGAKLVRDAFALAKEK 281
Cdd:PRK03992 144 REAVELPLKKPELFEEVGIEPPKGVLLYGPPGTGKTLLAKAVAHETNATFIRVVGSELVQKFIGEGARLVRELFELAREK 223

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008337 282 APSIIFIDELDAIGTKRFDSEKAGDREVQRTMLELLNQLDGFQPNTQVKVIAATNRVDILDPALLRSGRLDRKIEFPMPN 361
Cdd:PRK03992 224 APSIIFIDEIDAIAAKRTDSGTSGDREVQRTLMQLLAEMDGFDPRGNVKIIAATNRIDILDPAILRPGRFDRIIEVPLPD 303

                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 228008337 362 EEARARIMQIHSRKMNVSPDVNYEELARCTDDFNGAQCKAVCVEAGMIALRRGATELTHEDYMEGILEVQAKKK 435
Cdd:PRK03992 304 EEGRLEILKIHTRKMNLADDVDLEELAELTEGASGADLKAICTEAGMFAIRDDRTEVTMEDFLKAIEKVMGKEE 377
 
Name Accession Description Interval E-value
PRK03992 PRK03992
proteasome-activating nucleotidase; Provisional
 42-435 3.40e-166

proteasome-activating nucleotidase; Provisional


Pssm-ID: 179699 [Multi-domain]  Cd Length: 389  Bit Score: 472.78  E-value: 3.40e-166
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008337  42 EEIVQRTRLLDSEIKIMKSEVLRVTHELQAMKdkiKENsEKIKvnkTLPYLVSNVIELLDvdpndqeeDGAnidldsqrk 121
Cdd:PRK03992  11 SELEEQIRQLELKLRDLEAENEKLERELERLK---SEL-EKLK---SPPLIVATVLEVLD--------DGR--------- 66

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008337 122 gkcAVIKTSTRQTYFLPVIGLVDAEKLKPGDLVGVNKDSYLILETLPTEYDSRVKAMEVDERPTEQYSDIGGLDKQIQEL 201
Cdd:PRK03992  67 ---VVVKSSGGPQFLVNVSPFIDREKLKPGARVALNQQSLAIVEVLPSEKDPRVQAMEVIESPNVTYEDIGGLEEQIREV 143

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008337 202 VEAIVLPMNHKEKFENLGIQPPKGVLMYGPPGTGKTLLARACAAQTKATFLKLAGPQLVQMFIGDGAKLVRDAFALAKEK 281
Cdd:PRK03992 144 REAVELPLKKPELFEEVGIEPPKGVLLYGPPGTGKTLLAKAVAHETNATFIRVVGSELVQKFIGEGARLVRELFELAREK 223

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008337 282 APSIIFIDELDAIGTKRFDSEKAGDREVQRTMLELLNQLDGFQPNTQVKVIAATNRVDILDPALLRSGRLDRKIEFPMPN 361
Cdd:PRK03992 224 APSIIFIDEIDAIAAKRTDSGTSGDREVQRTLMQLLAEMDGFDPRGNVKIIAATNRIDILDPAILRPGRFDRIIEVPLPD 303

                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 228008337 362 EEARARIMQIHSRKMNVSPDVNYEELARCTDDFNGAQCKAVCVEAGMIALRRGATELTHEDYMEGILEVQAKKK 435
Cdd:PRK03992 304 EEGRLEILKIHTRKMNLADDVDLEELAELTEGASGADLKAICTEAGMFAIRDDRTEVTMEDFLKAIEKVMGKEE 377
26Sp45 TIGR01242
26S proteasome subunit P45 family; Many proteins may score above the trusted cutoff because an ...
 43-430 1.13e-141

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: 409.57  E-value: 1.13e-141
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008337   43 EIVQRTRLLDSEIKIMKSEVLRVTHELQAMKDKIkensEKIKvnkTLPYLVSNVIELLDVDPndqeedganidldsqrkg 122
Cdd:TIGR01242   3 ELDVRIRKLEDEKRSLEKEKIRLERELERLRSEI----ERLR---SPPLIVGTVLEVLDDNR------------------ 57

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008337  123 kcAVIKTSTRQTYFLPVIGLVDAEKLKPGDLVGVNKDSYLILETLPTEYDSRVKAMEVDERPTEQYSDIGGLDKQIQELV 202
Cdd:TIGR01242  58 --VVVKSSTGPNFVVNVSAFIDRKSLKPGARVALNQQTLTIVDVLPTSKDPLVKGMEVEERPNVSYEDIGGLEEQIREIR 135

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008337  203 EAIVLPMNHKEKFENLGIQPPKGVLMYGPPGTGKTLLARACAAQTKATFLKLAGPQLVQMFIGDGAKLVRDAFALAKEKA 282
Cdd:TIGR01242 136 EAVELPLKHPELFEEVGIEPPKGVLLYGPPGTGKTLLAKAVAHETNATFIRVVGSELVRKYIGEGARLVREIFELAKEKA 215

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008337  283 PSIIFIDELDAIGTKRFDSEKAGDREVQRTMLELLNQLDGFQPNTQVKVIAATNRVDILDPALLRSGRLDRKIEFPMPNE 362
Cdd:TIGR01242 216 PSIIFIDEIDAIAAKRTDSGTSGDREVQRTLMQLLAELDGFDPRGNVKVIAATNRPDILDPALLRPGRFDRIIEVPLPDF 295

                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 228008337  363 EARARIMQIHSRKMNVSPDVNYEELARCTDDFNGAQCKAVCVEAGMIALRRGATELTHEDYMEGILEV 430
Cdd:TIGR01242 296 EGRLEILKIHTRKMKLAEDVDLEAIAKMTEGASGADLKAICTEAGMFAIREERDYVTMDDFIKAVEKV 363
RPT1 COG1222
ATP-dependent 26S proteasome regulatory subunit [Posttranslational modification, protein ...
 172-435 1.67e-126

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


Pssm-ID: 440835 [Multi-domain]  Cd Length: 326  Bit Score: 369.34  E-value: 1.67e-126
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008337 172 DSRVKAMEVDERPTEQYSDIGGLDKQIQELVEAIVLPMNHKEKFENLGIQPPKGVLMYGPPGTGKTLLARACAAQTKATF 251
Cdd:COG1222   61 GTPRGTAVPAESPDVTFDDIGGLDEQIEEIREAVELPLKNPELFRKYGIEPPKGVLLYGPPGTGKTLLAKAVAGELGAPF 140

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008337 252 LKLAGPQLVQMFIGDGAKLVRDAFALAKEKAPSIIFIDELDAIGTKRFDSEKAGdrEVQRTMLELLNQLDGFQPNTQVKV 331
Cdd:COG1222  141 IRVRGSELVSKYIGEGARNVREVFELAREKAPSIIFIDEIDAIAARRTDDGTSG--EVQRTVNQLLAELDGFESRGDVLI 218

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008337 332 IAATNRVDILDPALLRSGRLDRKIEFPMPNEEARARIMQIHSRKMNVSPDVNYEELARCTDDFNGAQCKAVCVEAGMIAL 411
Cdd:COG1222  219 IAATNRPDLLDPALLRPGRFDRVIEVPLPDEEAREEILKIHLRDMPLADDVDLDKLAKLTEGFSGADLKAIVTEAGMFAI 298

                        250       260
                 ....*....|....*....|....
gi 228008337 412 RRGATELTHEDYMEGILEVQAKKK 435
Cdd:COG1222  299 REGRDTVTMEDLEKAIEKVKKKTE 322
RecA-like_PAN_like cd19502
proteasome activating nucleotidase PAN and related proteasome subunits; This subfamily ...
 188-357 3.64e-102

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: 301.56  E-value: 3.64e-102
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008337 188 YSDIGGLDKQIQELVEAIVLPMNHKEKFENLGIQPPKGVLMYGPPGTGKTLLARACAAQTKATFLKLAGPQLVQMFIGDG 267
Cdd:cd19502    2 YEDIGGLDEQIREIREVVELPLKHPELFEELGIEPPKGVLLYGPPGTGKTLLAKAVANHTDATFIRVVGSELVQKYIGEG 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008337 268 AKLVRDAFALAKEKAPSIIFIDELDAIGTKRFDSEKAGDREVQRTMLELLNQLDGFQPNTQVKVIAATNRVDILDPALLR 347
Cdd:cd19502   82 ARLVRELFEMAREKAPSIIFIDEIDAIGAKRFDSGTGGDREVQRTMLELLNQLDGFDPRGNIKVIMATNRPDILDPALLR 161

                        170
                 ....*....|
gi 228008337 348 SGRLDRKIEF 357
Cdd:cd19502  162 PGRFDRKIEF 171
AAA pfam00004
ATPase family associated with various cellular activities (AAA); AAA family proteins often ...
 226-358 3.89e-52

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: 171.62  E-value: 3.89e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008337  226 VLMYGPPGTGKTLLARACAAQTKATFLKLAGPQLVQMFIGDGAKLVRDAFALAKEKAPSIIFIDELDAIGTKRFDSekaG 305
Cdd:pfam00004   1 LLLYGPPGTGKTTLAKAVAKELGAPFIEISGSELVSKYVGESEKRLRELFEAAKKLAPCVIFIDEIDALAGSRGSG---G 77

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 228008337  306 DREVQRTMLELLNQLDGFQPNTQ-VKVIAATNRVDILDPALLrsGRLDRKIEFP 358
Cdd:pfam00004  78 DSESRRVVNQLLTELDGFTSSNSkVIVIAATNRPDKLDPALL--GRFDRIIEFP 129
AAA smart00382
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ...
 222-358 2.70e-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: 81.27  E-value: 2.70e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008337   222 PPKGVLMYGPPGTGKTLLARACAAQTKAT-----------------FLKLAGPQLVQMFIGDGAKLVRDAFALAKEKAPS 284
Cdd:smart00382   1 PGEVILIVGPPGSGKTTLARALARELGPPgggviyidgedileevlDQLLLIIVGGKKASGSGELRLRLALALARKLKPD 80

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 228008337   285 IIFIDELDAIGTKRFdsekagdrEVQRTMLELLNQLDGFQPNTQVKVIAATNRVDILDPALLRSgRLDRKIEFP 358
Cdd:smart00382  81 VLILDEITSLLDAEQ--------EALLLLLEELRLLLLLKSEKNLTVILTTNDEKDLGPALLRR-RFDRRIVLL 145
 
Name Accession Description Interval E-value
PRK03992 PRK03992
proteasome-activating nucleotidase; Provisional
 42-435 3.40e-166

proteasome-activating nucleotidase; Provisional


Pssm-ID: 179699 [Multi-domain]  Cd Length: 389  Bit Score: 472.78  E-value: 3.40e-166
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008337  42 EEIVQRTRLLDSEIKIMKSEVLRVTHELQAMKdkiKENsEKIKvnkTLPYLVSNVIELLDvdpndqeeDGAnidldsqrk 121
Cdd:PRK03992  11 SELEEQIRQLELKLRDLEAENEKLERELERLK---SEL-EKLK---SPPLIVATVLEVLD--------DGR--------- 66

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008337 122 gkcAVIKTSTRQTYFLPVIGLVDAEKLKPGDLVGVNKDSYLILETLPTEYDSRVKAMEVDERPTEQYSDIGGLDKQIQEL 201
Cdd:PRK03992  67 ---VVVKSSGGPQFLVNVSPFIDREKLKPGARVALNQQSLAIVEVLPSEKDPRVQAMEVIESPNVTYEDIGGLEEQIREV 143

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008337 202 VEAIVLPMNHKEKFENLGIQPPKGVLMYGPPGTGKTLLARACAAQTKATFLKLAGPQLVQMFIGDGAKLVRDAFALAKEK 281
Cdd:PRK03992 144 REAVELPLKKPELFEEVGIEPPKGVLLYGPPGTGKTLLAKAVAHETNATFIRVVGSELVQKFIGEGARLVRELFELAREK 223

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008337 282 APSIIFIDELDAIGTKRFDSEKAGDREVQRTMLELLNQLDGFQPNTQVKVIAATNRVDILDPALLRSGRLDRKIEFPMPN 361
Cdd:PRK03992 224 APSIIFIDEIDAIAAKRTDSGTSGDREVQRTLMQLLAEMDGFDPRGNVKIIAATNRIDILDPAILRPGRFDRIIEVPLPD 303

                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 228008337 362 EEARARIMQIHSRKMNVSPDVNYEELARCTDDFNGAQCKAVCVEAGMIALRRGATELTHEDYMEGILEVQAKKK 435
Cdd:PRK03992 304 EEGRLEILKIHTRKMNLADDVDLEELAELTEGASGADLKAICTEAGMFAIRDDRTEVTMEDFLKAIEKVMGKEE 377
26Sp45 TIGR01242
26S proteasome subunit P45 family; Many proteins may score above the trusted cutoff because an ...
 43-430 1.13e-141

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: 409.57  E-value: 1.13e-141
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008337   43 EIVQRTRLLDSEIKIMKSEVLRVTHELQAMKDKIkensEKIKvnkTLPYLVSNVIELLDVDPndqeedganidldsqrkg 122
Cdd:TIGR01242   3 ELDVRIRKLEDEKRSLEKEKIRLERELERLRSEI----ERLR---SPPLIVGTVLEVLDDNR------------------ 57

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008337  123 kcAVIKTSTRQTYFLPVIGLVDAEKLKPGDLVGVNKDSYLILETLPTEYDSRVKAMEVDERPTEQYSDIGGLDKQIQELV 202
Cdd:TIGR01242  58 --VVVKSSTGPNFVVNVSAFIDRKSLKPGARVALNQQTLTIVDVLPTSKDPLVKGMEVEERPNVSYEDIGGLEEQIREIR 135

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008337  203 EAIVLPMNHKEKFENLGIQPPKGVLMYGPPGTGKTLLARACAAQTKATFLKLAGPQLVQMFIGDGAKLVRDAFALAKEKA 282
Cdd:TIGR01242 136 EAVELPLKHPELFEEVGIEPPKGVLLYGPPGTGKTLLAKAVAHETNATFIRVVGSELVRKYIGEGARLVREIFELAKEKA 215

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008337  283 PSIIFIDELDAIGTKRFDSEKAGDREVQRTMLELLNQLDGFQPNTQVKVIAATNRVDILDPALLRSGRLDRKIEFPMPNE 362
Cdd:TIGR01242 216 PSIIFIDEIDAIAAKRTDSGTSGDREVQRTLMQLLAELDGFDPRGNVKVIAATNRPDILDPALLRPGRFDRIIEVPLPDF 295

                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 228008337  363 EARARIMQIHSRKMNVSPDVNYEELARCTDDFNGAQCKAVCVEAGMIALRRGATELTHEDYMEGILEV 430
Cdd:TIGR01242 296 EGRLEILKIHTRKMKLAEDVDLEAIAKMTEGASGADLKAICTEAGMFAIREERDYVTMDDFIKAVEKV 363
PTZ00361 PTZ00361
26 proteosome regulatory subunit 4-like protein; Provisional
 47-438 5.79e-128

26 proteosome regulatory subunit 4-like protein; Provisional


Pssm-ID: 185575 [Multi-domain]  Cd Length: 438  Bit Score: 377.19  E-value: 5.79e-128
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008337  47 RTRLLDSE-IK---IMKSEVLRVTHELQAMKDKIKENSEKIKVNKTLPYLVSNVIELLDvdpndqeedganidlDSQrkg 122
Cdd:PTZ00361  57 RLRLLKLErIKdylLLEEEFITNQEAQKPAQEKNEAELKKVDDLRGSPLSVGTLEEIID---------------ENH--- 118

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008337 123 kcAVIKTSTRQTYFLPVIGLVDAEKLKPGDLVGVNKDSYLILETLPTEYDSRVKAMEVDERPTEQYSDIGGLDKQIQELV 202
Cdd:PTZ00361 119 --AIVSSSVGPEYYVNILSFVDKEQLEPGCSVLLHNKTHSVVGILLDEVDPLVSVMKVDKAPLESYADIGGLEQQIQEIK 196

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008337 203 EAIVLPMNHKEKFENLGIQPPKGVLMYGPPGTGKTLLARACAAQTKATFLKLAGPQLVQMFIGDGAKLVRDAFALAKEKA 282
Cdd:PTZ00361 197 EAVELPLTHPELYDDIGIKPPKGVILYGPPGTGKTLLAKAVANETSATFLRVVGSELIQKYLGDGPKLVRELFRVAEENA 276

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008337 283 PSIIFIDELDAIGTKRFDSEKAGDREVQRTMLELLNQLDGFQPNTQVKVIAATNRVDILDPALLRSGRLDRKIEFPMPNE 362
Cdd:PTZ00361 277 PSIVFIDEIDAIGTKRYDATSGGEKEIQRTMLELLNQLDGFDSRGDVKVIMATNRIESLDPALIRPGRIDRKIEFPNPDE 356

                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 228008337 363 EARARIMQIHSRKMNVSPDVNYEELARCTDDFNGAQCKAVCVEAGMIALRRGATELTHEDYMEGILEVQAKKKANL 438
Cdd:PTZ00361 357 KTKRRIFEIHTSKMTLAEDVDLEEFIMAKDELSGADIKAICTEAGLLALRERRMKVTQADFRKAKEKVLYRKKGNI 432
RPT1 COG1222
ATP-dependent 26S proteasome regulatory subunit [Posttranslational modification, protein ...
 172-435 1.67e-126

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


Pssm-ID: 440835 [Multi-domain]  Cd Length: 326  Bit Score: 369.34  E-value: 1.67e-126
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008337 172 DSRVKAMEVDERPTEQYSDIGGLDKQIQELVEAIVLPMNHKEKFENLGIQPPKGVLMYGPPGTGKTLLARACAAQTKATF 251
Cdd:COG1222   61 GTPRGTAVPAESPDVTFDDIGGLDEQIEEIREAVELPLKNPELFRKYGIEPPKGVLLYGPPGTGKTLLAKAVAGELGAPF 140

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008337 252 LKLAGPQLVQMFIGDGAKLVRDAFALAKEKAPSIIFIDELDAIGTKRFDSEKAGdrEVQRTMLELLNQLDGFQPNTQVKV 331
Cdd:COG1222  141 IRVRGSELVSKYIGEGARNVREVFELAREKAPSIIFIDEIDAIAARRTDDGTSG--EVQRTVNQLLAELDGFESRGDVLI 218

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008337 332 IAATNRVDILDPALLRSGRLDRKIEFPMPNEEARARIMQIHSRKMNVSPDVNYEELARCTDDFNGAQCKAVCVEAGMIAL 411
Cdd:COG1222  219 IAATNRPDLLDPALLRPGRFDRVIEVPLPDEEAREEILKIHLRDMPLADDVDLDKLAKLTEGFSGADLKAIVTEAGMFAI 298

                        250       260
                 ....*....|....*....|....
gi 228008337 412 RRGATELTHEDYMEGILEVQAKKK 435
Cdd:COG1222  299 REGRDTVTMEDLEKAIEKVKKKTE 322
PTZ00454 PTZ00454
26S protease regulatory subunit 6B-like protein; Provisional
 18-442 2.58e-121

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


Pssm-ID: 240423 [Multi-domain]  Cd Length: 398  Bit Score: 358.69  E-value: 2.58e-121
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008337  18 EKMATVWDEAEQDGIGEEVLKMSTEEIVQRTRLLDSEIKIMKSEVLRVTHELQAMKdkikensEKIKVNKTLPYLVSNVI 97
Cdd:PTZ00454   1 VATTAAAAVASSTTHTERDLYEKLKELEKELEFLDIQEEYIKEEQKNLKRELIRAK-------EEVKRIQSVPLVIGQFL 73

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008337  98 ELLDVDPndqeedganidldsqrkgkcAVIKTSTRQTYFLPVIGLVDAEKLKPGDLVGVNKDSYLILETLPTEYDSRVKA 177
Cdd:PTZ00454  74 EMIDSNY--------------------GIVSSTSGSNYYVRILSTLNRELLKPNASVALHRHSHAVVDILPPEADSSIQL 133

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008337 178 MEVDERPTEQYSDIGGLDKQIQELVEAIVLPMNHKEKFENLGIQPPKGVLMYGPPGTGKTLLARACAAQTKATFLKLAGP 257
Cdd:PTZ00454 134 LQMSEKPDVTYSDIGGLDIQKQEIREAVELPLTCPELYEQIGIDPPRGVLLYGPPGTGKTMLAKAVAHHTTATFIRVVGS 213

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008337 258 QLVQMFIGDGAKLVRDAFALAKEKAPSIIFIDELDAIGTKRFDSEKAGDREVQRTMLELLNQLDGFQPNTQVKVIAATNR 337
Cdd:PTZ00454 214 EFVQKYLGEGPRMVRDVFRLARENAPSIIFIDEVDSIATKRFDAQTGADREVQRILLELLNQMDGFDQTTNVKVIMATNR 293

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008337 338 VDILDPALLRSGRLDRKIEFPMPNEEARARIMQIHSRKMNVSPDVNYEELARCTDDFNGAQCKAVCVEAGMIALRRGATE 417
Cdd:PTZ00454 294 ADTLDPALLRPGRLDRKIEFPLPDRRQKRLIFQTITSKMNLSEEVDLEDFVSRPEKISAADIAAICQEAGMQAVRKNRYV 373

                        410       420
                 ....*....|....*....|....*
gi 228008337 418 LTHEDYMEGILEVQAKKKANLQYYA 442
Cdd:PTZ00454 374 ILPKDFEKGYKTVVRKTDRDYDFYS 398
RecA-like_PAN_like cd19502
proteasome activating nucleotidase PAN and related proteasome subunits; This subfamily ...
 188-357 3.64e-102

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: 301.56  E-value: 3.64e-102
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008337 188 YSDIGGLDKQIQELVEAIVLPMNHKEKFENLGIQPPKGVLMYGPPGTGKTLLARACAAQTKATFLKLAGPQLVQMFIGDG 267
Cdd:cd19502    2 YEDIGGLDEQIREIREVVELPLKHPELFEELGIEPPKGVLLYGPPGTGKTLLAKAVANHTDATFIRVVGSELVQKYIGEG 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008337 268 AKLVRDAFALAKEKAPSIIFIDELDAIGTKRFDSEKAGDREVQRTMLELLNQLDGFQPNTQVKVIAATNRVDILDPALLR 347
Cdd:cd19502   82 ARLVRELFEMAREKAPSIIFIDEIDAIGAKRFDSGTGGDREVQRTMLELLNQLDGFDPRGNIKVIMATNRPDILDPALLR 161

                        170
                 ....*....|
gi 228008337 348 SGRLDRKIEF 357
Cdd:cd19502  162 PGRFDRKIEF 171
FtsH_fam TIGR01241
ATP-dependent metalloprotease FtsH; HflB(FtsH) is a pleiotropic protein required for correct ...
 173-427 4.31e-80

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: 256.06  E-value: 4.31e-80
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008337  173 SRVKAMEvDERPTEQYSDIGGLDKQIQELVEaIVLPMNHKEKFENLGIQPPKGVLMYGPPGTGKTLLARACAAQTKATFL 252
Cdd:TIGR01241  40 SKAKLLN-EEKPKVTFKDVAGIDEAKEELME-IVDFLKNPSKFTKLGAKIPKGVLLVGPPGTGKTLLAKAVAGEAGVPFF 117

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008337  253 KLAGPQLVQMFIGDGAKLVRDAFALAKEKAPSIIFIDELDAIGTKRFDSEKAGDREVQRTMLELLNQLDGFQPNTQVKVI 332
Cdd:TIGR01241 118 SISGSDFVEMFVGVGASRVRDLFEQAKKNAPCIIFIDEIDAVGRQRGAGLGGGNDEREQTLNQLLVEMDGFGTNTGVIVI 197

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008337  333 AATNRVDILDPALLRSGRLDRKIEFPMPNEEARARIMQIHSRKMNVSPDVNYEELARCTDDFNGAQCKAVCVEAGMIALR 412
Cdd:TIGR01241 198 AATNRPDVLDPALLRPGRFDRQVVVDLPDIKGREEILKVHAKNKKLAPDVDLKAVARRTPGFSGADLANLLNEAALLAAR 277

                         250
                  ....*....|....*
gi 228008337  413 RGATELTHEDYMEGI 427
Cdd:TIGR01241 278 KNKTEITMNDIEEAI 292
SpoVK COG0464
AAA+-type ATPase, SpoVK/Ycf46/Vps4 family [Cell wall/membrane/envelope biogenesis, Cell cycle ...
 132-436 8.66e-79

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


Pssm-ID: 440232 [Multi-domain]  Cd Length: 397  Bit Score: 249.83  E-value: 8.66e-79
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008337 132 RQTYFLPVIGLVDAEKLKPGDLVGVNKDSYLILETLPTEYDSRVKAMEVDERPTEQYSDIGGLDKQIQELVEAIVLPMNH 211
Cdd:COG0464  100 LLLLLLLLLLLLLDLERALLELLRESAEALALAAPLVTYEDIGGLEEELLELREAILDDLGGLEEVKEELRELVALPLKR 179

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008337 212 KEKFENLGIQPPKGVLMYGPPGTGKTLLARACAAQTKATFLKLAGPQLVQMFIGDGAKLVRDAFALAKEKAPSIIFIDEL 291
Cdd:COG0464  180 PELREEYGLPPPRGLLLYGPPGTGKTLLARALAGELGLPLIEVDLSDLVSKYVGETEKNLREVFDKARGLAPCVLFIDEA 259

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008337 292 DAIGTKRfdsEKAGDREVQRTMLELLNQLDGFQPNtqVKVIAATNRVDILDPALLRsgRLDRKIEFPMPNEEARARIMQI 371
Cdd:COG0464  260 DALAGKR---GEVGDGVGRRVVNTLLTEMEELRSD--VVVIAATNRPDLLDPALLR--RFDEIIFFPLPDAEERLEIFRI 332

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 228008337 372 HSRKMNVSPDVNYEELARCTDDFNGAQCKAVCVEAGMIALRRGATELTHEDYMEGILEVQAKKKA 436
Cdd:COG0464  333 HLRKRPLDEDVDLEELAEATEGLSGADIRNVVRRAALQALRLGREPVTTEDLLEALEREDIFLKR 397
CDC48 TIGR01243
AAA family ATPase, CDC48 subfamily; This subfamily of the AAA family ATPases includes two ...
 182-441 3.54e-76

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: 251.75  E-value: 3.54e-76
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008337  182 ERPTEQYSDIGGLDKQIQELVEAIVLPMNHKEKFENLGIQPPKGVLMYGPPGTGKTLLARACAAQTKATFLKLAGPQLVQ 261
Cdd:TIGR01243 446 EVPNVRWSDIGGLEEVKQELREAVEWPLKHPEIFEKMGIRPPKGVLLFGPPGTGKTLLAKAVATESGANFIAVRGPEILS 525

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008337  262 MFIGDGAKLVRDAFALAKEKAPSIIFIDELDAIGTKRFDSEkaGDREVQRTMLELLNQLDGFQPNTQVKVIAATNRVDIL 341
Cdd:TIGR01243 526 KWVGESEKAIREIFRKARQAAPAIIFFDEIDAIAPARGARF--DTSVTDRIVNQLLTEMDGIQELSNVVVIAATNRPDIL 603

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008337  342 DPALLRSGRLDRKIEFPMPNEEARARIMQIHSRKMNVSPDVNYEELARCTDDFNGAQCKAVCVEAGMIALRRGATELTHE 421
Cdd:TIGR01243 604 DPALLRPGRFDRLILVPPPDEEARKEIFKIHTRSMPLAEDVDLEELAEMTEGYTGADIEAVCREAAMAALRESIGSPAKE 683

                         250       260
                  ....*....|....*....|
gi 228008337  422 DYMEGILEVQAKKKANLQYY 441
Cdd:TIGR01243 684 KLEVGEEEFLKDLKVEMRHF 703
HflB COG0465
ATP-dependent Zn proteases [Posttranslational modification, protein turnover, chaperones];
173-432 1.74e-74

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


Pssm-ID: 440233 [Multi-domain]  Cd Length: 583  Bit Score: 243.79  E-value: 1.74e-74
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008337 173 SRVKaMEVDERPTEQYSDIGGLDKQIQELVEaIVLPMNHKEKFENLGIQPPKGVLMYGPPGTGKTLLARACAAQTKATFL 252
Cdd:COG0465  127 SKAK-LYDEDKPKVTFDDVAGVDEAKEELQE-IVDFLKDPEKFTRLGAKIPKGVLLVGPPGTGKTLLAKAVAGEAGVPFF 204

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008337 253 KLAGPQLVQMFIGDGAKLVRDAFALAKEKAPSIIFIDELDAIGTKRFdsekAG------DREvqRTmlelLNQL----DG 322
Cdd:COG0465  205 SISGSDFVEMFVGVGASRVRDLFEQAKKNAPCIIFIDEIDAVGRQRG----AGlggghdERE--QT----LNQLlvemDG 274

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008337 323 FQPNTQVKVIAATNRVDILDPALLRSGRLDRKIEFPMPNEEARARIMQIHSRKMNVSPDVNYEELARCTDDFNGAQCKAV 402
Cdd:COG0465  275 FEGNEGVIVIAATNRPDVLDPALLRPGRFDRQVVVDLPDVKGREAILKVHARKKPLAPDVDLEVIARRTPGFSGADLANL 354

                        250       260       270
                 ....*....|....*....|....*....|
gi 228008337 403 CVEAGMIALRRGATELTHEDYMEGILEVQA 432
Cdd:COG0465  355 VNEAALLAARRNKKAVTMEDFEEAIDRVIA 384
CDC48 TIGR01243
AAA family ATPase, CDC48 subfamily; This subfamily of the AAA family ATPases includes two ...
 166-413 4.45e-68

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


Pssm-ID: 273521 [Multi-domain]  Cd Length: 733  Bit Score: 230.18  E-value: 4.45e-68
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008337  166 TLPTEYDSRVKAMEVDER---PTEQYSDIGGLDKQIQELVEAIVLPMNHKEKFENLGIQPPKGVLMYGPPGTGKTLLARA 242
Cdd:TIGR01243 152 TEATEVEIREKPVREEIErkvPKVTYEDIGGLKEAKEKIREMVELPMKHPELFEHLGIEPPKGVLLYGPPGTGKTLLAKA 231

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008337  243 CAAQTKATFLKLAGPQLVQMFIGDGAKLVRDAFALAKEKAPSIIFIDELDAIGTKRfdSEKAGDREvQRTMLELLNQLDG 322
Cdd:TIGR01243 232 VANEAGAYFISINGPEIMSKYYGESEERLREIFKEAEENAPSIIFIDEIDAIAPKR--EEVTGEVE-KRVVAQLLTLMDG 308

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008337  323 FQPNTQVKVIAATNRVDILDPALLRSGRLDRKIEFPMPNEEARARIMQIHSRKMNVSPDVNYEELARCTDDFNGAQCKAV 402
Cdd:TIGR01243 309 LKGRGRVIVIGATNRPDALDPALRRPGRFDREIVIRVPDKRARKEILKVHTRNMPLAEDVDLDKLAEVTHGFVGADLAAL 388

                         250
                  ....*....|.
gi 228008337  403 CVEAGMIALRR 413
Cdd:TIGR01243 389 AKEAAMAALRR 399
ftsH CHL00176
cell division protein; Validated
 188-419 7.54e-68

cell division protein; Validated


Pssm-ID: 214386 [Multi-domain]  Cd Length: 638  Bit Score: 227.63  E-value: 7.54e-68
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008337 188 YSDIGGLDKQIQELvEAIVLPMNHKEKFENLGIQPPKGVLMYGPPGTGKTLLARACAAQTKATFLKLAGPQLVQMFIGDG 267
Cdd:CHL00176 182 FRDIAGIEEAKEEF-EEVVSFLKKPERFTAVGAKIPKGVLLVGPPGTGKTLLAKAIAGEAEVPFFSISGSEFVEMFVGVG 260

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008337 268 AKLVRDAFALAKEKAPSIIFIDELDAIGTKRFDSEKAGDREVQRTMLELLNQLDGFQPNTQVKVIAATNRVDILDPALLR 347
Cdd:CHL00176 261 AARVRDLFKKAKENSPCIVFIDEIDAVGRQRGAGIGGGNDEREQTLNQLLTEMDGFKGNKGVIVIAATNRVDILDAALLR 340

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 228008337 348 SGRLDRKIEFPMPNEEARARIMQIHSRKMNVSPDVNYEELARCTDDFNGAQCKAVCVEAGMIALRRGATELT 419
Cdd:CHL00176 341 PGRFDRQITVSLPDREGRLDILKVHARNKKLSPDVSLELIARRTPGFSGADLANLLNEAAILTARRKKATIT 412
RecA-like_FtsH cd19501
ATP-dependent zinc metalloprotease FtsH; FtsH ATPase is a processive, ATP-dependent zinc ...
 188-355 6.97e-67

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


Pssm-ID: 410909 [Multi-domain]  Cd Length: 171  Bit Score: 210.94  E-value: 6.97e-67
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008337 188 YSDIGGLDKQIQELVEaIVLPMNHKEKFENLGIQPPKGVLMYGPPGTGKTLLARACAAQTKATFLKLAGPQLVQMFIGDG 267
Cdd:cd19501    3 FKDVAGCEEAKEELKE-VVEFLKNPEKFTKLGAKIPKGVLLVGPPGTGKTLLAKAVAGEAGVPFFSISGSDFVEMFVGVG 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008337 268 AKLVRDAFALAKEKAPSIIFIDELDAIGTKRFDSEKAGDREVQRTMLELLNQLDGFQPNTQVKVIAATNRVDILDPALLR 347
Cdd:cd19501   82 ASRVRDLFEQAKKNAPCIVFIDEIDAVGRKRGAGLGGGHDEREQTLNQLLVEMDGFESNTGVIVIAATNRPDVLDPALLR 161


                 ....*...
gi 228008337 348 SGRLDRKI 355
Cdd:cd19501  162 PGRFDRQV 169
RecA-like_CDC48_NLV2_r1-like cd19503
first of two ATPase domains of CDC48 and NLV2, and similar ATPase domains; CDC48 in yeast and ...
 190-357 1.77e-64

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: 204.83  E-value: 1.77e-64
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008337 190 DIGGLDKQIQELVEAIVLPMNHKEKFENLGIQPPKGVLMYGPPGTGKTLLARACAAQTKATFLKLAGPQLVQMFIGDGAK 269
Cdd:cd19503    1 DIGGLDEQIASLKELIELPLKYPELFRALGLKPPRGVLLHGPPGTGKTLLARAVANEAGANFLSISGPSIVSKYLGESEK 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008337 270 LVRDAFALAKEKAPSIIFIDELDAIGTKRfdseKAGDREVQRTML-ELLNQLDGFQPNTQVKVIAATNRVDILDPALLRS 348
Cdd:cd19503   81 NLREIFEEARSHAPSIIFIDEIDALAPKR----EEDQREVERRVVaQLLTLMDGMSSRGKVVVIAATNRPDAIDPALRRP 156


                 ....*....
gi 228008337 349 GRLDRKIEF 357
Cdd:cd19503  157 GRFDREVEI 165
hflB PRK10733
ATP-dependent zinc metalloprotease FtsH;
173-412 8.93e-60

ATP-dependent zinc metalloprotease FtsH;


Pssm-ID: 182683 [Multi-domain]  Cd Length: 644  Bit Score: 206.04  E-value: 8.93e-60
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008337 173 SRVKAMEVDERPTeQYSDIGGLDKQIQELVEaIVLPMNHKEKFENLGIQPPKGVLMYGPPGTGKTLLARACAAQTKATFL 252
Cdd:PRK10733 137 SKARMLTEDQIKT-TFADVAGCDEAKEEVAE-LVEYLREPSRFQKLGGKIPKGVLMVGPPGTGKTLLAKAIAGEAKVPFF 214

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008337 253 KLAGPQLVQMFIGDGAKLVRDAFALAKEKAPSIIFIDELDAIGTKRFDSEKAGDREVQRTMLELLNQLDGFQPNTQVKVI 332
Cdd:PRK10733 215 TISGSDFVEMFVGVGASRVRDMFEQAKKAAPCIIFIDEIDAVGRQRGAGLGGGHDEREQTLNQMLVEMDGFEGNEGIIVI 294

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008337 333 AATNRVDILDPALLRSGRLDRKIEFPMPNEEARARIMQIHSRKMNVSPDVNYEELARCTDDFNGAQCKAVCVEAGMIALR 412
Cdd:PRK10733 295 AATNRPDVLDPALLRPGRFDRQVVVGLPDVRGREQILKVHMRRVPLAPDIDAAIIARGTPGFSGADLANLVNEAALFAAR 374
RecA-like_CDC48_r2-like cd19511
second of two ATPase domains of CDC48/p97, PEX1 and -6, VAT and NVL, and similar ATPase ...
 199-355 1.01e-58

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: 189.42  E-value: 1.01e-58
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008337 199 QELVEAIVLPMNHKEKFENLGIQPPKGVLMYGPPGTGKTLLARACAAQTKATFLKLAGPQLVQMFIGDGAKLVRDAFALA 278
Cdd:cd19511    3 RELKEAVEWPLKHPDAFKRLGIRPPKGVLLYGPPGCGKTLLAKALASEAGLNFISVKGPELFSKYVGESERAVREIFQKA 82

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 228008337 279 KEKAPSIIFIDELDAIGTKRFDSEKAGDREvqRTMLELLNQLDGFQPNTQVKVIAATNRVDILDPALLRSGRLDRKI 355
Cdd:cd19511   83 RQAAPCIIFFDEIDSLAPRRGQSDSSGVTD--RVVSQLLTELDGIESLKGVVVIAATNRPDMIDPALLRPGRLDKLI 157
RecA-like_CDC48_r1-like cd19519
first of two ATPase domains of CDC48 and similar ATPase domains; CDC48 in yeast and p97 or VCP ...
 190-358 2.08e-57

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: 186.49  E-value: 2.08e-57
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008337 190 DIGGLDKQIQELVEAIVLPMNHKEKFENLGIQPPKGVLMYGPPGTGKTLLARACAAQTKATFLKLAGPQLVQMFIGDGAK 269
Cdd:cd19519    1 DIGGCRKQLAQIREMVELPLRHPELFKAIGIKPPRGILLYGPPGTGKTLIARAVANETGAFFFLINGPEIMSKLAGESES 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008337 270 LVRDAFALAKEKAPSIIFIDELDAIGTKRfdsEKAGDREVQRTMLELLNQLDGFQPNTQVKVIAATNRVDILDPALLRSG 349
Cdd:cd19519   81 NLRKAFEEAEKNAPAIIFIDEIDAIAPKR---EKTHGEVERRIVSQLLTLMDGLKQRAHVIVMAATNRPNSIDPALRRFG 157


                 ....*....
gi 228008337 350 RLDRKIEFP 358
Cdd:cd19519  158 RFDREIDIG 166
RecA-like_protease cd19481
proteases similar to RecA; RecA-like NTPases. This family includes the NTP binding domain of ...
 197-357 6.22e-56

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: 182.48  E-value: 6.22e-56
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008337 197 QIQELVEAIVLPMNHKEKFEnLGIQPPKGVLMYGPPGTGKTLLARACAAQTKATFLKLAGPQLVQMFIGDGAKLVRDAFA 276
Cdd:cd19481    1 LKASLREAVEAPRRGSRLRR-YGLGLPKGILLYGPPGTGKTLLAKALAGELGLPLIVVKLSSLLSKYVGESEKNLRKIFE 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008337 277 LAKEKAPSIIFIDELDAIGTKRFDSekAGDREVQRTMLELLNQLDGFQPNTQVKVIAATNRVDILDPALLRSGRLDRKIE 356
Cdd:cd19481   80 RARRLAPCILFIDEIDAIGRKRDSS--GESGELRRVLNQLLTELDGVNSRSKVLVIAATNRPDLLDPALLRPGRFDEVIE 157


                 .
gi 228008337 357 F 357
Cdd:cd19481  158 F 158
RecA-like_VCP_r2 cd19529
second of two ATPase domains of Valosin-containing protein-like ATPase (VAT) and similar ...
 199-355 2.62e-54

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: 178.07  E-value: 2.62e-54
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008337 199 QELVEAIVLPMNHKEKFENLGIQPPKGVLMYGPPGTGKTLLARACAAQTKATFLKLAGPQLVQMFIGDGAKLVRDAFALA 278
Cdd:cd19529    3 QELKEAVEWPLLKPEVFKRLGIRPPKGILLYGPPGTGKTLLAKAVATESNANFISVKGPELLSKWVGESEKAIREIFRKA 82

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 228008337 279 KEKAPSIIFIDELDAIGTKRFDSEKAGDREvqRTMLELLNQLDGFQPNTQVKVIAATNRVDILDPALLRSGRLDRKI 355
Cdd:cd19529   83 RQVAPCVIFFDEIDSIAPRRGTTGDSGVTE--RVVNQLLTELDGLEEMNGVVVIAATNRPDIIDPALLRAGRFDRLI 157
AAA pfam00004
ATPase family associated with various cellular activities (AAA); AAA family proteins often ...
 226-358 3.89e-52

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: 171.62  E-value: 3.89e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008337  226 VLMYGPPGTGKTLLARACAAQTKATFLKLAGPQLVQMFIGDGAKLVRDAFALAKEKAPSIIFIDELDAIGTKRFDSekaG 305
Cdd:pfam00004   1 LLLYGPPGTGKTTLAKAVAKELGAPFIEISGSELVSKYVGESEKRLRELFEAAKKLAPCVIFIDEIDALAGSRGSG---G 77

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 228008337  306 DREVQRTMLELLNQLDGFQPNTQ-VKVIAATNRVDILDPALLrsGRLDRKIEFP 358
Cdd:pfam00004  78 DSESRRVVNQLLTELDGFTSSNSkVIVIAATNRPDKLDPALL--GRFDRIIEFP 129
RecA-like_CDC48_r2-like cd19528
second of two ATPase domains of CDC48 and similar ATPase domains; CDC48 in yeast and p97 or ...
 199-355 1.09e-50

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: 168.84  E-value: 1.09e-50
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008337 199 QELVEAIVLPMNHKEKFENLGIQPPKGVLMYGPPGTGKTLLARACAAQTKATFLKLAGPQLVQMFIGDGAKLVRDAFALA 278
Cdd:cd19528    3 RELQELVQYPVEHPDKFLKFGMTPSKGVLFYGPPGCGKTLLAKAIANECQANFISVKGPELLTMWFGESEANVRDIFDKA 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008337 279 KEKAPSIIFIDELDAIGTKR----FDSEKAGDREVQrtmlELLNQLDGFQPNTQVKVIAATNRVDILDPALLRSGRLDRK 354
Cdd:cd19528   83 RAAAPCVLFFDELDSIAKARggniGDAGGAADRVIN----QILTEMDGMNTKKNVFIIGATNRPDIIDPAILRPGRLDQL 158


                 .
gi 228008337 355 I 355
Cdd:cd19528  159 I 159
pup_AAA TIGR03689
proteasome ATPase; In the Actinobacteria, as shown for Mycobacterium tuberculosis, some ...
 139-372 1.50e-50

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: 178.75  E-value: 1.50e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008337  139 VIGLVDA---EKLKPGDLVGVNKDSYLILETLPTeydSRVKAMEVDERPTEQYSDIGGLDKQIQELVEAIVLPMNHKEKF 215
Cdd:TIGR03689 132 VVKLAGAladEGLRPGDTLLVDPRAGYAFEAIPR---TEVEDLVLEEVPDVTYADIGGLGSQIEQIRDAVELPFLHPELY 208

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008337  216 ENLGIQPPKGVLMYGPPGTGKTLLARACAA----------QTKATFLKLAGPQLVQMFIGDGAKLVRDAFALAKEKA--- 282
Cdd:TIGR03689 209 REYGLKPPKGVLLYGPPGCGKTLIAKAVANslaarigaegGGKSYFLNIKGPELLNKYVGETERQIRLIFQRAREKAseg 288

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008337  283 -PSIIFIDELDAIgtkrFDSEKAG-DREVQRTML-ELLNQLDGFQPNTQVKVIAATNRVDILDPALLRSGRLDRKIEFPM 359
Cdd:TIGR03689 289 rPVIVFFDEMDSL----FRTRGSGvSSDVETTVVpQLLAEIDGVESLDNVIVIGASNREDMIDPAILRPGRLDVKIRIER 364

                         250
                  ....*....|...
gi 228008337  360 PNEEARARIMQIH 372
Cdd:TIGR03689 365 PDAEAAADIFAKY 377
COG1223 COG1223
Predicted ATPase, AAA+ superfamily [General function prediction only];
194-439 3.00e-50

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


Pssm-ID: 440836 [Multi-domain]  Cd Length: 246  Bit Score: 170.45  E-value: 3.00e-50
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008337 194 LDKQIQELVEAIVLPMNHKEKFENLGIQPPKGVLMYGPPGTGKTLLARACAAQTKATFLKLAGPQLVQMFIGDGAKLVRD 273
Cdd:COG1223    6 GQEEAKKKLKLIIKELRRRENLRKFGLWPPRKILFYGPPGTGKTMLAEALAGELKLPLLTVRLDSLIGSYLGETARNLRK 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008337 274 AFALAKEkAPSIIFIDELDAIGTKRFDSEKAGdrEVQRTMLELLNQLDGFqpNTQVKVIAATNRVDILDPALLRsgRLDR 353
Cdd:COG1223   86 LFDFARR-APCVIFFDEFDAIAKDRGDQNDVG--EVKRVVNALLQELDGL--PSGSVVIAATNHPELLDSALWR--RFDE 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008337 354 KIEFPMPNEEARARIMQIHSRKMNVSPDVNYEELARCTDDFNGAQCKAVCVEAGMIALRRGATELTHEDYMEGILEVQAK 433
Cdd:COG1223  159 VIEFPLPDKEERKEILELNLKKFPLPFELDLKKLAKKLEGLSGADIEKVLKTALKKAILEDREKVTKEDLEEALKQRKER 238


                 ....*.
gi 228008337 434 KKANLQ 439
Cdd:COG1223  239 KKEPKK 244
RecA-like_NVL_r1-like cd19518
first of two ATPase domains of NVL (nuclear VCP-like protein) and similar ATPase domains; NVL ...
 190-355 4.42e-48

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: 162.19  E-value: 4.42e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008337 190 DIGGLDKQIQELVEAIVLPMNHKEKFENLGIQPPKGVLMYGPPGTGKTLLARACAAQTKATFLKLAGPQLVQMFIGDGAK 269
Cdd:cd19518    1 DIGGMDSTLKELCELLIHPILPPEYFQHLGVEPPRGVLLHGPPGCGKTMLANAIAGELKVPFLKISATEIVSGVSGESEE 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008337 270 LVRDAFALAKEKAPSIIFIDELDAIGTKRFDSEKAGDREVQRTMLELLNQLDGFQPNTQ-VKVIAATNRVDILDPALLRS 348
Cdd:cd19518   81 KIRELFDQAISNAPCIVFIDEIDAITPKRESAQREMERRIVSQLLTCMDELNNEKTAGGpVLVIGATNRPDSLDPALRRA 160


                 ....*..
gi 228008337 349 GRLDRKI 355
Cdd:cd19518  161 GRFDREI 167
RecA-like_VPS4-like cd19509
ATPase domain of VPS4, ATAD1, K, KTNA1, Spastin, FIGL-1 and similar ATPase domains; This ...
 191-355 7.65e-48

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: 161.37  E-value: 7.65e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008337 191 IGGLDKQIQELVEAIVLPMNHKEKFENLgIQPPKGVLMYGPPGTGKTLLARACAAQTKATFLKLAGPQLVQMFIGDGAKL 270
Cdd:cd19509    1 IAGLDDAKEALKEAVILPSLRPDLFPGL-RGPPRGILLYGPPGTGKTLLARAVASESGSTFFSISASSLVSKWVGESEKI 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008337 271 VRDAFALAKEKAPSIIFIDELDAIGTKRFDSEKAGDREVqRTmlELLNQLDGFQ--PNTQVKVIAATNRVDILDPALLRs 348
Cdd:cd19509   80 VRALFALARELQPSIIFIDEIDSLLSERGSGEHEASRRV-KT--EFLVQMDGVLnkPEDRVLVLGATNRPWELDEAFLR- 155


                 ....*..
gi 228008337 349 gRLDRKI 355
Cdd:cd19509  156 -RFEKRI 161
RecA-like_NVL_r2-like cd19530
second of two ATPase domains of NVL (nuclear VCP-like protein) and similar ATPase domains; NVL ...
 194-353 5.50e-47

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: 159.19  E-value: 5.50e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008337 194 LDKQIQELVEAIVLPMNHKEKFENLGIQPPKGVLMYGPPGTGKTLLARACAAQTKATFLKLAGPQLVQMFIGDGAKLVRD 273
Cdd:cd19530    1 LDHVREELTMSILRPIKRPDIYKALGIDLPTGVLLYGPPGCGKTLLAKAVANESGANFISVKGPELLNKYVGESERAVRQ 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008337 274 AFALAKEKAPSIIFIDELDAIGTKRFDSEKAGdreVQRTMLELLNQLDGFQPNTQVKVIAATNRVDILDPALLRSGRLDR 353
Cdd:cd19530   81 VFQRARASAPCVIFFDEVDALVPKRGDGGSWA---SERVVNQLLTEMDGLEERSNVFVIAATNRPDIIDPAMLRPGRLDK 157
RecA-like_Yta7-like cd19517
ATPase domain of Saccharomyces cerevisiae Yta7 and similar ATPase domains; Saccharomyces ...
 190-357 1.42e-41

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: 145.34  E-value: 1.42e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008337 190 DIGGLDKQIQELVEAIVLPMNHKEKFENLGIQPPKGVLMYGPPGTGKTLLARACAAQ-----TKATFLKLAGPQLVQMFI 264
Cdd:cd19517    1 DIGGLSHYINQLKEMVFFPLLYPEVFAKFKITPPRGVLFHGPPGTGKTLMARALAAEcskggQKVSFFMRKGADCLSKWV 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008337 265 GDGAKLVRDAFALAKEKAPSIIFIDELDAIGTKRFDSEKAGDREVQRTMLELLNQLDGfqpNTQVKVIAATNRVDILDPA 344
Cdd:cd19517   81 GEAERQLRLLFEEAYRMQPSIIFFDEIDGLAPVRSSKQEQIHASIVSTLLALMDGLDN---RGQVVVIGATNRPDALDPA 157

                        170
                 ....*....|...
gi 228008337 345 LLRSGRLDRKIEF 357
Cdd:cd19517  158 LRRPGRFDREFYF 170
RecA-like_PEX1_r2 cd19526
second of two ATPase domains of Peroxisomal biogenesis factor 1 (PEX1); PEX1(also known as ...
 201-356 1.54e-41

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: 144.88  E-value: 1.54e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008337 201 LVEAIVLPMNHKEKFENLGIQPPKGVLMYGPPGTGKTLLARACAAQTKATFLKLAGPQLVQMFIGDGAKLVRDAFALAKE 280
Cdd:cd19526    5 LEETIEWPSKYPKIFASSPLRLRSGILLYGPPGCGKTLLASAIASECGLNFISVKGPELLNKYIGASEQNVRDLFSRAQS 84

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 228008337 281 KAPSIIFIDELDAIGTKR-FDSEKAGDREVQrtmlELLNQLDGFQPNTQVKVIAATNRVDILDPALLRSGRLDRKIE 356
Cdd:cd19526   85 AKPCILFFDEFDSIAPKRgHDSTGVTDRVVN----QLLTQLDGVEGLDGVYVLAATSRPDLIDPALLRPGRLDKLVY 157
RecA-like_ATAD1 cd19520
ATPase domain of ATPase family AAA domain-containing protein 1 and similar ATPase domains; ...
 190-347 2.14e-41

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: 144.49  E-value: 2.14e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008337 190 DIGGLDKQIQELVEAIVLPMNHKEKFENLGI-QPPKGVLMYGPPGTGKTLLARACAAQTKATFLKLAGPQLVQMFIGDGA 268
Cdd:cd19520    1 DIGGLDEVITELKELVILPLQRPELFDNSRLlQPPKGVLLYGPPGCGKTMLAKATAKEAGARFINLQVSSLTDKWYGESQ 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008337 269 KLVRDAFALAKEKAPSIIFIDELDAIgtkrFDSEKAGDREVQRTM-LELLNQLDGF--QPNTQVKVIAATNRVDILDPAL 345
Cdd:cd19520   81 KLVAAVFSLASKLQPSIIFIDEIDSF----LRQRSSTDHEATAMMkAEFMSLWDGLstDGNCRVIVMGATNRPQDLDEAI 156


                 ..
gi 228008337 346 LR 347
Cdd:cd19520  157 LR 158
RecA-like_PEX6_r2 cd19527
second of two ATPase domains of Peroxisomal biogenesis factor 6 (PEX6); PEX6(also known as ...
 200-353 3.26e-41

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


Pssm-ID: 410935 [Multi-domain]  Cd Length: 160  Bit Score: 143.81  E-value: 3.26e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008337 200 ELVEAIVLPMNHKEKFeNLGIQPPKGVLMYGPPGTGKTLLARACAAQTKATFLKLAGPQLVQMFIGDGAKLVRDAFALAK 279
Cdd:cd19527    4 EILDTIQLPLEHPELF-SSGLRKRSGILLYGPPGTGKTLLAKAIATECSLNFLSVKGPELINMYIGESEANVREVFQKAR 82

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 228008337 280 EKAPSIIFIDELDAIGTKRFDSEKAGDrEVQRTMLELLNQLDGFQPNTQ-VKVIAATNRVDILDPALLRSGRLDR 353
Cdd:cd19527   83 DAKPCVIFFDELDSLAPSRGNSGDSGG-VMDRVVSQLLAELDGMSSSGQdVFVIGATNRPDLLDPALLRPGRFDK 156
RecA-like_spastin cd19524
ATPase domain of spastin; Spastin is an ATP-dependent microtubule-severing protein involved in ...
 190-355 1.43e-39

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: 139.60  E-value: 1.43e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008337 190 DIGGLDKQIQELVEAIVLPMNHKEKFENLGiQPPKGVLMYGPPGTGKTLLARACAAQTKATFLKLAGPQLVQMFIGDGAK 269
Cdd:cd19524    1 DIAGQDLAKQALQEMVILPSLRPELFTGLR-APARGLLLFGPPGNGKTMLAKAVAAESNATFFNISAASLTSKYVGEGEK 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008337 270 LVRDAFALAKEKAPSIIFIDELDAIGTKRFDSEKAGDRevqRTMLELLNQLDGFQ--PNTQVKVIAATNRVDILDPALLR 347
Cdd:cd19524   80 LVRALFAVARELQPSIIFIDEVDSLLSERSEGEHEASR---RLKTEFLIEFDGVQsnGDDRVLVMGATNRPQELDDAVLR 156


                 ....*...
gi 228008337 348 sgRLDRKI 355
Cdd:cd19524  157 --RFTKRV 162
RecA-like_Figl-1 cd19525
ATPase domain of Fidgetin-Like 1 (FIGL-1); FIGL-1 may participate in DNA repair in the nucleus; ...
 180-355 2.24e-38

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


Pssm-ID: 410933 [Multi-domain]  Cd Length: 186  Bit Score: 137.43  E-value: 2.24e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008337 180 VDERPTEQYSDIGGLDKQIQELVEAIVLPMNHKEKFENLGiQPPKGVLMYGPPGTGKTLLARACAAQTKATFLKLAGPQL 259
Cdd:cd19525   13 MDHGPPINWADIAGLEFAKKTIKEIVVWPMLRPDIFTGLR-GPPKGILLFGPPGTGKTLIGKCIASQSGATFFSISASSL 91

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008337 260 VQMFIGDGAKLVRDAFALAKEKAPSIIFIDELDAIGTKRFDSEKAGDRevqRTMLELLNQLDGFQ--PNTQVKVIAATNR 337
Cdd:cd19525   92 TSKWVGEGEKMVRALFSVARCKQPAVIFIDEIDSLLSQRGEGEHESSR---RIKTEFLVQLDGATtsSEDRILVVGATNR 168

                        170
                 ....*....|....*...
gi 228008337 338 VDILDPALLRsgRLDRKI 355
Cdd:cd19525  169 PQEIDEAARR--RLVKRL 184
RecA-like_VPS4 cd19521
ATPase domain of vacuolar protein sorting-associated protein 4; Vacuolar protein ...
 183-355 7.12e-38

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: 135.37  E-value: 7.12e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008337 183 RPTEQYSDIGGLDKQIQELVEAIVLPMNHKEKFENlGIQPPKGVLMYGPPGTGKTLLARACAAQTKATFLKLAGPQLVQM 262
Cdd:cd19521    1 KPNVKWEDVAGLEGAKEALKEAVILPVKFPHLFTG-NRKPWSGILLYGPPGTGKSYLAKAVATEANSTFFSVSSSDLVSK 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008337 263 FIGDGAKLVRDAFALAKEKAPSIIFIDELDAIGTKRFDSEKAGDRevqRTMLELLNQLDGFQPNTQ-VKVIAATNRVDIL 341
Cdd:cd19521   80 WMGESEKLVKQLFAMARENKPSIIFIDEVDSLCGTRGEGESEASR---RIKTELLVQMNGVGNDSQgVLVLGATNIPWQL 156

                        170
                 ....*....|....
gi 228008337 342 DPALLRsgRLDRKI 355
Cdd:cd19521  157 DSAIRR--RFEKRI 168
RecA-like_KTNA1 cd19522
Katanin p60 ATPase-containing subunit A1; Katanin p60 ATPase-containing subunit A1 (KTNA1) is ...
 190-355 1.92e-35

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


Pssm-ID: 410930 [Multi-domain]  Cd Length: 170  Bit Score: 128.95  E-value: 1.92e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008337 190 DIGGLDKQIQELVEAIVLPMNHKEKFEnlGIQPP-KGVLMYGPPGTGKTLLARACAAQTKATFLKLAGPQLVQMFIGDGA 268
Cdd:cd19522    1 DIADLEEAKKLLEEAVVLPMWMPEFFK--GIRRPwKGVLMVGPPGTGKTLLAKAVATECGTTFFNVSSSTLTSKYRGESE 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008337 269 KLVRDAFALAKEKAPSIIFIDELDAIGTKR-FDSEKAGDREVQRtmlELLNQLDGF-------QPNTQVKVIAATNRVDI 340
Cdd:cd19522   79 KLVRLLFEMARFYAPTTIFIDEIDSICSRRgTSEEHEASRRVKS---ELLVQMDGVggasendDPSKMVMVLAATNFPWD 155

                        170
                 ....*....|....*
gi 228008337 341 LDPALLRsgRLDRKI 355
Cdd:cd19522  156 IDEALRR--RLEKRI 168
RecA-like_fidgetin cd19523
ATPase domain of fidgetin; Fidgetin (FIGN) is a ATP-dependent microtubule severing protein. ...
 190-347 3.00e-31

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: 117.68  E-value: 3.00e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008337 190 DIGGLDKQIQELVEAIVLPMNHKEKFENLgIQPPKGVLMYGPPGTGKTLLARACAAQTKATFLKLAGPQLVQMFIGDGAK 269
Cdd:cd19523    1 DIAGLGALKAAIKEEVLWPLLRPDAFSGL-LRLPRSILLFGPRGTGKTLLGRCLASQLGATFLRLRGSTLVAKWAGEGEK 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008337 270 LVRDAFALAKEKAPSIIFIDELDAIGTKRFDSEKAGDrevqRTMLELLNQLDGF--QPNTQVKVIAATNRVDILDPALLR 347
Cdd:cd19523   80 ILQASFLAARCRQPSVLFISDLDALLSSQDDEASPVG----RLQVELLAQLDGVlgSGEDGVLVVCTTSKPEEIDESLRR 155
RecA-like_NSF-SEC18_r1-like cd19504
first of two ATPase domains of NSF and SEC18, and similar ATPase domains; ...
 191-356 9.06e-28

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: 108.35  E-value: 9.06e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008337 191 IGGLDKQIQELVE----AIVLPmnhKEKFENLGIQPPKGVLMYGPPGTGKTLLARACAAQTKATFLKLA-GPQLVQMFIG 265
Cdd:cd19504    2 IGGLDKEFSDIFRrafaSRVFP---PEIVEQLGCKHVKGILLYGPPGTGKTLMARQIGKMLNAREPKIVnGPEILNKYVG 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008337 266 DGAKLVRDAFALAKEKAPS--------IIFIDELDAIGTKRfdSEKAGDREVQRTML-ELLNQLDGFQPNTQVKVIAATN 336
Cdd:cd19504   79 ESEANIRKLFADAEEEQRRlgansglhIIIFDEIDAICKQR--GSMAGSTGVHDTVVnQLLSKIDGVEQLNNILVIGMTN 156

                        170       180
                 ....*....|....*....|
gi 228008337 337 RVDILDPALLRSGRLDRKIE 356
Cdd:cd19504  157 RKDLIDEALLRPGRLEVQME 176
AAA cd00009
The AAA+ (ATPases Associated with a wide variety of cellular Activities) superfamily ...
 192-358 4.55e-24

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: 97.60  E-value: 4.55e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008337 192 GGLDKQIQELVEAIVLPmnhkekfenlgiqPPKGVLMYGPPGTGKTLLARACAAQT---KATFLKLAGPQLVQMFIG--- 265
Cdd:cd00009    1 VGQEEAIEALREALELP-------------PPKNLLLYGPPGTGKTTLARAIANELfrpGAPFLYLNASDLLEGLVVael 67

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008337 266 DGAKLVRDAFALAKEKAPSIIFIDELDAIGtkrfdsekagdREVQRTMLELLNQL-DGFQPNTQVKVIAATNRVDILDPA 344
Cdd:cd00009   68 FGHFLVRLLFELAEKAKPGVLFIDEIDSLS-----------RGAQNALLRVLETLnDLRIDRENVRVIGATNRPLLGDLD 136

                        170
                 ....*....|....
gi 228008337 345 LLRSGRLDRKIEFP 358
Cdd:cd00009  137 RALYDRLDIRIVIP 150
ycf46 CHL00195
Ycf46; Provisional
 186-410 2.00e-23

Ycf46; Provisional


Pssm-ID: 177094 [Multi-domain]  Cd Length: 489  Bit Score: 102.41  E-value: 2.00e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008337 186 EQYSDIGGLD---KQIQELVEAIvlpmnhKEKFENLGIQPPKGVLMYGPPGTGKTLLARACAAQTKATFLKLAGPQLVQM 262
Cdd:CHL00195 225 EKISDIGGLDnlkDWLKKRSTSF------SKQASNYGLPTPRGLLLVGIQGTGKSLTAKAIANDWQLPLLRLDVGKLFGG 298

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008337 263 FIGDGAKLVRDAFALAKEKAPSIIFIDELDaigtKRF-DSEKAGD----REVQRTMLELLNqldgfQPNTQVKVIAATNR 337
Cdd:CHL00195 299 IVGESESRMRQMIRIAEALSPCILWIDEID----KAFsNSESKGDsgttNRVLATFITWLS-----EKKSPVFVVATANN 369

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 228008337 338 VDILDPALLRSGRLDRKIEFPMPNEEARARIMQIHSRKmnVSPD----VNYEELARCTDDFNGAQCKAVCVEAGMIA 410
Cdd:CHL00195 370 IDLLPLEILRKGRFDEIFFLDLPSLEEREKIFKIHLQK--FRPKswkkYDIKKLSKLSNKFSGAEIEQSIIEAMYIA 444
RecA-like_Ycf46-like cd19507
ATPase domain of Ycf46 and similar ATPase domains; Ycf46 may play a role in the regulation of ...
 216-353 4.57e-20

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


Pssm-ID: 410915 [Multi-domain]  Cd Length: 161  Bit Score: 86.65  E-value: 4.57e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008337 216 ENLGIQPPKGVLMYGPPGTGKTLLARACAAQTKATFLKLAGPQLVQMFIGDGAKLVRDAFALAKEKAPSIIFIDELD-AI 294
Cdd:cd19507   24 SAYGLPTPKGLLLVGIQGTGKSLTAKAIAGVWQLPLLRLDMGRLFGGLVGESESRLRQMIQTAEAIAPCVLWIDEIEkGF 103

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 228008337 295 GTKRFDSEKAGDREVQRTMLELLNqldgfQPNTQVKVIAATNRVDILDPALLRSGRLDR 353
Cdd:cd19507  104 SNADSKGDSGTSSRVLGTFLTWLQ-----EKKKPVFVVATANNVQSLPPELLRKGRFDE 157
AAA smart00382
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ...
 222-358 2.70e-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: 81.27  E-value: 2.70e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008337   222 PPKGVLMYGPPGTGKTLLARACAAQTKAT-----------------FLKLAGPQLVQMFIGDGAKLVRDAFALAKEKAPS 284
Cdd:smart00382   1 PGEVILIVGPPGSGKTTLARALARELGPPgggviyidgedileevlDQLLLIIVGGKKASGSGELRLRLALALARKLKPD 80

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 228008337   285 IIFIDELDAIGTKRFdsekagdrEVQRTMLELLNQLDGFQPNTQVKVIAATNRVDILDPALLRSgRLDRKIEFP 358
Cdd:smart00382  81 VLILDEITSLLDAEQ--------EALLLLLEELRLLLLLKSEKNLTVILTTNDEKDLGPALLRR-RFDRRIVLL 145
RecA-like_BCS1 cd19510
Mitochondrial chaperone BCS1; Mitochondrial chaperone BCS1 is necessary for the assembly of ...
 201-357 3.08e-14

Mitochondrial chaperone BCS1; Mitochondrial chaperone BCS1 is necessary for the assembly of mitochondrial respiratory chain complex III and plays an important role in the maintenance of mitochondrial tubular networks, respiratory chain assembly and formation of the LETM1 complex. RecA-like NTPases. This family includes the NTP binding domain of F1 and V1 H(+)ATPases, DnaB and related helicases as well as bacterial RecA and related eukaryotic and archaeal recombinases. This group also includes bacterial conjugation proteins and related DNA transfer proteins involved in type II and type IV secretion.


Pssm-ID: 410918 [Multi-domain]  Cd Length: 153  Bit Score: 70.07  E-value: 3.08e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008337 201 LVEAIVLPMNHKEKFENLGIQPPKGVLMYGPPGTGKTLLARACAAQTKATF--LKLAGpqlvqmfIGDGAKLVRDAFALA 278
Cdd:cd19510    1 IIDDLKDFIKNEDWYNDRGIPYRRGYLLYGPPGTGKSSFIAALAGELDYDIcdLNLSE-------VVLTDDRLNHLLNTA 73

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008337 279 KEKapSIIFIDELDAIGTKRFDSEK---AGDREVQRTMLELLNQLDGFQPNTQVKVIAATNRVDILDPALLRSGRLDRKI 355
Cdd:cd19510   74 PKQ--SIILLEDIDAAFESREHNKKnpsAYGGLSRVTFSGLLNALDGVASSEERIVFMTTNHIERLDPALIRPGRVDMKI 151


                 ..
gi 228008337 356 EF 357
Cdd:cd19510  152 YM 153
AAA_lid_3 pfam17862
AAA+ lid domain; This entry represents the alpha helical AAA+ lid domain that is found to the ...
 381-425 2.72e-10

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


Pssm-ID: 465537 [Multi-domain]  Cd Length: 45  Bit Score: 55.24  E-value: 2.72e-10
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 228008337  381 DVNYEELARCTDDFNGAQCKAVCVEAGMIALRRGATELTHEDYME 425
Cdd:pfam17862   1 DVDLEELAERTEGFSGADLEALCREAALAALRRGLEAVTQEDLEE 45
Prot_ATP_ID_OB pfam16450
Proteasomal ATPase OB C-terminal domain; This is the interdomain (ID) or oligonucleotide ...
 116-168 6.74e-10

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


Pssm-ID: 465118 [Multi-domain]  Cd Length: 56  Bit Score: 54.44  E-value: 6.74e-10
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 228008337  116 LDSQRkgkcAVIKTSTRQTYFLPVIGLVDAEKLKPGDLVGVNKDSYLILETLP 168
Cdd:pfam16450   8 LDDGR----ALVKSSGGEERVVRLAGSLDEEKLRPGDRVLLDPRSGYALEVLP 56
RecA-like_ATAD3-like cd19512
ATPase domains of ATPase AAA-domain protein 3A (ATAD3A), -3B, and -3C, and similar ATPase ...
 224-357 9.01e-10

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: 57.15  E-value: 9.01e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008337 224 KGVLMYGPPGTGKTLLARACAAQTKATFLKLAGPQLVQMFiGDGAKLVRDAFALA-KEKAPSIIFIDELDAIGTKRfDSE 302
Cdd:cd19512   23 RNILFYGPPGTGKTLFAKKLALHSGMDYAIMTGGDVAPMG-REGVTAIHKVFDWAnTSRRGLLLFVDEADAFLRKR-STE 100

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 228008337 303 KAGdrEVQRTMLELLNQLDGFQPNTQVKVIaATNRVDILDPALlrSGRLDRKIEF 357
Cdd:cd19512  101 KIS--EDLRAALNAFLYRTGEQSNKFMLVL-ASNQPEQFDWAI--NDRIDEMVEF 150
AAA_5 pfam07728
AAA domain (dynein-related subfamily); This Pfam entry includes some of the AAA proteins not ...
 225-347 4.35e-09

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


Pssm-ID: 400191 [Multi-domain]  Cd Length: 135  Bit Score: 54.61  E-value: 4.35e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008337  225 GVLMYGPPGTGKTLLA-RACAAQTKATFLKLAGP------QLVQ-MFIGDGAKLVRDAFALAKEKAPSIIFIDELDAIgt 296
Cdd:pfam07728   1 GVLLVGPPGTGKTELAeRLAAALSNRPVFYVQLTrdtteeDLFGrRNIDPGGASWVDGPLVRAAREGEIAVLDEINRA-- 78

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 228008337  297 krfdsekagDREVQRTMLELLN-----QLDGFQ----PNTQVKVIAATNRVDI----LDPALLR 347
Cdd:pfam07728  79 ---------NPDVLNSLLSLLDerrllLPDGGElvkaAPDGFRLIATMNPLDRglneLSPALRS 133
RarA COG2256
Replication-associated recombination protein RarA (DNA-dependent ATPase) [Replication, ...
 226-290 4.87e-09

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


Pssm-ID: 441857 [Multi-domain]  Cd Length: 439  Bit Score: 58.14  E-value: 4.87e-09
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 228008337 226 VLMYGPPGTGKTLLARACAAQTKATFLKLAGpqlvqmfIGDGAKLVRDAFALAKEKA----PSIIFIDE 290
Cdd:COG2256   52 MILWGPPGTGKTTLARLIANATDAEFVALSA-------VTSGVKDIREVIEEARERRaygrRTILFVDE 113
RecA-like_HslU cd19498
ATP-dependent protease ATPase subunit HslU; HslU is a component of the ATP-dependent protease ...
 223-317 8.35e-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: 55.08  E-value: 8.35e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008337 223 PKGVLMYGPPGTGKTLLARACAAQTKATFLKLAGPQLVQM-FIGdgaklvRDAFALAKEKAPSIIFIDELDAIGTKRFDS 301
Cdd:cd19498   46 PKNILMIGPTGVGKTEIARRLAKLAGAPFIKVEATKFTEVgYVG------RDVESIIRDLVEGIVFIDEIDKIAKRGGSS 119

                         90
                 ....*....|....*..
gi 228008337 302 EKAGDRE-VQRTMLELL 317
Cdd:cd19498  120 GPDVSREgVQRDLLPIV 136
RecA-like_Ycf2 cd19505
ATPase domain of plant YCF2; Ycf2 is a chloroplast ATPase which has an essential function; ...
 218-357 2.04e-08

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: 53.53  E-value: 2.04e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008337 218 LGIQPPKGVLMYGPPGTGKTLLARACAAQTKATFLKLAGPQLV--------------QMFIGDGAKLVRDAFALAKEKAP 283
Cdd:cd19505    7 LGLSPSKGILLIGSIETGRSYLIKSLAANSYVPLIRISLNKLLynkpdfgnddwidgMLILKESLHRLNLQFELAKAMSP 86

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 228008337 284 SIIFIDELDAIGTKRFDSEKAGDRevqRTMLELLNQL---DGFQPNTQ-VKVIAATNRVDILDPALLRSGRLDRKIEF 357
Cdd:cd19505   87 CIIWIPNIHELNVNRSTQNLEEDP---KLLLGLLLNYlsrDFEKSSTRnILVIASTHIPQKVDPALIAPNRLDTCINI 161
PRK13342 PRK13342
recombination factor protein RarA; Reviewed
 229-290 9.09e-08

recombination factor protein RarA; Reviewed


Pssm-ID: 237355 [Multi-domain]  Cd Length: 413  Bit Score: 53.94  E-value: 9.09e-08
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 228008337 229 YGPPGTGKTLLARACAAQTKATFLKLAGpqlvqmfIGDGAKLVRDAFALAKEKAPS----IIFIDE 290
Cdd:PRK13342  42 WGPPGTGKTTLARIIAGATDAPFEALSA-------VTSGVKDLREVIEEARQRRSAgrrtILFIDE 100
44 PHA02544
clamp loader, small subunit; Provisional
 202-369 9.12e-08

clamp loader, small subunit; Provisional


Pssm-ID: 222866 [Multi-domain]  Cd Length: 316  Bit Score: 53.46  E-value: 9.12e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008337 202 VEAIVLPMNHKEKFenLGI----QPPKGVLMYGPPGTGKTLLARACAAQTKATFlklagpqlvqMFI-GDGAKL--VRD- 273
Cdd:PHA02544  20 IDECILPAADKETF--KSIvkkgRIPNMLLHSPSPGTGKTTVAKALCNEVGAEV----------LFVnGSDCRIdfVRNr 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008337 274 --AFALAK--EKAPSIIFIDELDAIGTKrfdsekagdrEVQRTMLELLNQldgFQPNtqVKVIAATNRVD-ILDPalLRS 348
Cdd:PHA02544  88 ltRFASTVslTGGGKVIIIDEFDRLGLA----------DAQRHLRSFMEA---YSKN--CSFIITANNKNgIIEP--LRS 150

                        170       180
                 ....*....|....*....|.
gi 228008337 349 gRLdRKIEFPMPNEEARARIM 369
Cdd:PHA02544 151 -RC-RVIDFGVPTKEEQIEMM 169
RecA-like_Pch2-like cd19508
ATPase domain of Pachytene checkpoint 2 (Pch2) and similar ATPase domains; Pch2 (known as ...
 226-345 6.32e-07

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


Pssm-ID: 410916 [Multi-domain]  Cd Length: 199  Bit Score: 49.75  E-value: 6.32e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008337 226 VLMYGPPGTGKTLLARACAAQ---------TKATFLKLAGPQLVQMFIGDGAKLVRDAF----ALAKEKAPSI-IFIDEL 291
Cdd:cd19508   55 VLLHGPPGTGKTSLCKALAQKlsirlssryRYGQLIEINSHSLFSKWFSESGKLVTKMFqkiqELIDDKDALVfVLIDEV 134

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 228008337 292 DAIGTKRfDSEKAGD--REVQRTMLELLNQLDGFQPNTQVKVIAATNRVDILDPAL 345
Cdd:cd19508  135 ESLAAAR-SASSSGTepSDAIRVVNAVLTQIDRIKRYHNNVILLTSNLLEKIDVAF 189
RecA-like_superfamily cd01120
RecA-like_NTPases; RecA-like NTPases. This superfamily includes the NTP binding domain of F1 ...
 226-342 1.96e-06

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


Pssm-ID: 410865 [Multi-domain]  Cd Length: 119  Bit Score: 46.73  E-value: 1.96e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008337 226 VLMYGPPGTGKTLLARACAAQTKATflklaGPQLVqmFIGDGAKLVRDAFALAKEKAPSIIFIDELDAIGTkrfdsekAG 305
Cdd:cd01120    1 ILITGPPGSGKTTLLLQFAEQALLS-----DEPVI--FISFLDTILEAIEDLIEEKKLDIIIIDSLSSLAR-------AS 66

                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 228008337 306 DREVQRTMLELLNQLDGFQPNTQVKVIAATNRVDILD 342
Cdd:cd01120   67 QGDRSSELLEDLAKLLRAARNTGITVIATIHSDKFDI 103
RecA-like_ClpX cd19497
ATP-dependent Clp protease ATP-binding subunit ClpX; ClpX is a component of the ATP-dependent ...
 210-297 2.79e-05

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: 45.28  E-value: 2.79e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008337 210 NHKEKFENLGIQPPKG-VLMYGPPGTGKTLLARACA-------AQTKATFLKLAGpqlvqmFIGDG-----AKLVRDA-F 275
Cdd:cd19497   36 RNNLKQKDDDVELEKSnILLIGPTGSGKTLLAQTLAkildvpfAIADATTLTEAG------YVGEDvenilLKLLQAAdY 109

                         90       100
                 ....*....|....*....|...
gi 228008337 276 ALAK-EKApsIIFIDELDAIGTK 297
Cdd:cd19497  110 DVERaQRG--IVYIDEIDKIARK 130
CDC6 COG1474
Cdc6-related protein, AAA superfamily ATPase [Replication, recombination and repair];
195-358 1.92e-04

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


Pssm-ID: 441083 [Multi-domain]  Cd Length: 389  Bit Score: 43.30  E-value: 1.92e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008337 195 DKQIQELVEAIVLPMNHkekfenlgiQPPKGVLMYGPPGTGKTLLARACAAQTKATFLKLAGP----------------- 257
Cdd:COG1474   32 EEEIEELASALRPALRG---------ERPSNVLIYGPTGTGKTAVAKYVLEELEEEAEERGVDvrvvyvncrqastryrv 102

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008337 258 --QLVQMFIGD--------GAKLVRDAF--ALAKEKAPSIIFIDELDAIGtkrfdsEKAGDrevqrtmlELLNQL---DG 322
Cdd:COG1474  103 lsRILEELGSGedipstglSTDELFDRLyeALDERDGVLVVVLDEIDYLV------DDEGD--------DLLYQLlraNE 168

                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 228008337 323 FQPNTQVKVIAATNRVDI---LDPALLRSGRlDRKIEFP 358
Cdd:COG1474  169 ELEGARVGVIGISNDLEFlenLDPRVKSSLG-EEEIVFP 206
DnaC COG1484
DNA replication protein DnaC [Replication, recombination and repair];
220-320 5.32e-04

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


Pssm-ID: 441093 [Multi-domain]  Cd Length: 242  Bit Score: 41.30  E-value: 5.32e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008337 220 IQPPKGVLMYGPPGTGKTLLA-----RACAAQTKATFLKLagPQLVQMF---IGDG--AKLVRdafALAKekaPSIIFID 289
Cdd:COG1484   96 IERGENLILLGPPGTGKTHLAialghEACRAGYRVRFTTA--PDLVNELkeaRADGrlERLLK---RLAK---VDLLILD 167

                         90       100       110
                 ....*....|....*....|....*....|.
gi 228008337 290 EldaIGTKRFDSEKAGDrevqrtMLELLNQL 320
Cdd:COG1484  168 E---LGYLPLDAEGAEL------LFELISDR 189
ruvB TIGR00635
Holliday junction DNA helicase, RuvB subunit; All proteins in this family for which functions ...
 226-295 7.26e-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: 41.52  E-value: 7.26e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008337  226 VLMYGPPGTGKTLLARACAAQTKATFLKLAGPQLVQMfiGDGAKLvrdafaLAKEKAPSIIFIDELDAIG 295
Cdd:TIGR00635  33 LLLYGPPGLGKTTLAHIIANEMGVNLKITSGPALEKP--GDLAAI------LTNLEEGDVLFIDEIHRLS 94
PRK13341 PRK13341
AAA family ATPase;
227-290 9.09e-04

AAA family ATPase;


Pssm-ID: 237354 [Multi-domain]  Cd Length: 725  Bit Score: 41.58  E-value: 9.09e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 228008337 227 LMYGPPGTGKTLLARACAAQTKATFLKLAGpqlvqmfIGDGAKLVRDAFALAKEKAP-----SIIFIDE 290
Cdd:PRK13341  56 ILYGPPGVGKTTLARIIANHTRAHFSSLNA-------VLAGVKDLRAEVDRAKERLErhgkrTILFIDE 117
PRK04195 PRK04195
replication factor C large subunit; Provisional
 185-244 9.15e-04

replication factor C large subunit; Provisional


Pssm-ID: 235250 [Multi-domain]  Cd Length: 482  Bit Score: 41.44  E-value: 9.15e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 228008337 185 TEQY-----SDIGGLDKQIQELVEAIvlpmnhkEKFENLgiQPPKGVLMYGPPGTGKTLLARACA 244
Cdd:PRK04195   5 VEKYrpktlSDVVGNEKAKEQLREWI-------ESWLKG--KPKKALLLYGPPGVGKTSLAHALA 60
YifB COG0606
Predicted Mg-chelatase, contains ChlI-like and ATPase domains, YifB family [Posttranslational ...
 226-241 1.10e-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: 41.18  E-value: 1.10e-03
                         10
                 ....*....|....*.
gi 228008337 226 VLMYGPPGTGKTLLAR 241
Cdd:COG0606  214 LLMIGPPGSGKTMLAR 229
MoxR COG0714
MoxR-like ATPase [General function prediction only]; MoxR-like ATPase is part of the Pathway ...
 226-389 1.36e-03

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


Pssm-ID: 440478 [Multi-domain]  Cd Length: 292  Bit Score: 40.54  E-value: 1.36e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008337 226 VLMYGPPGTGKTLLARACAAQTKATFlklagpQLVQMFIG-DGAKLVRDAFALAKEKAP---------SIIFIDELDaig 295
Cdd:COG0714   34 LLLEGVPGVGKTTLAKALARALGLPF------IRIQFTPDlLPSDILGTYIYDQQTGEFefrpgplfaNVLLADEIN--- 104

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008337 296 tkrfdseKAgDREVQRTMLELlnqLDGFQ---PNTQVK------VIAATNRVDI-----LDPALLRsgRLDRKIEFPMPN 361
Cdd:COG0714  105 -------RA-PPKTQSALLEA---MEERQvtiPGGTYKlpepflVIATQNPIEQegtypLPEAQLD--RFLLKLYIGYPD 171

                        170       180       190
                 ....*....|....*....|....*....|
gi 228008337 362 EEARARIMQIHSRKM--NVSPDVNYEELAR 389
Cdd:COG0714  172 AEEEREILRRHTGRHlaEVEPVLSPEELLA 201
Mg_chelatase pfam01078
Magnesium chelatase, subunit ChlI; Magnesium-chelatase is a three-component enzyme that ...
 226-242 1.66e-03

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


Pssm-ID: 426032 [Multi-domain]  Cd Length: 207  Bit Score: 39.44  E-value: 1.66e-03
                          10
                  ....*....|....*..
gi 228008337  226 VLMYGPPGTGKTLLARA 242
Cdd:pfam01078  25 LLMIGPPGSGKTMLAKR 41
ruvB PRK00080
Holliday junction branch migration DNA helicase RuvB;
226-290 1.69e-03

Holliday junction branch migration DNA helicase RuvB;


Pssm-ID: 234619 [Multi-domain]  Cd Length: 328  Bit Score: 40.11  E-value: 1.69e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 228008337 226 VLMYGPPGTGKTLLARACAAQTKATFLKLAGPQLVQMfiGDGAKLvrdafaLAKEKAPSIIFIDE 290
Cdd:PRK00080  54 VLLYGPPGLGKTTLANIIANEMGVNIRITSGPALEKP--GDLAAI------LTNLEEGDVLFIDE 110
RuvB_N pfam05496
Holliday junction DNA helicase RuvB P-loop domain; The RuvB protein makes up part of the ...
 216-290 1.70e-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: 39.02  E-value: 1.70e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008337  216 ENLGI---------QPPKGVLMYGPPGTGKTLLARACAAQTKATFLKLAGPQLVQMfiGDGAKLvrdafaLAKEKAPSII 286
Cdd:pfam05496  17 ENLKIfieaakqrgEALDHVLLYGPPGLGKTTLANIIANEMGVNIRITSGPAIERP--GDLAAI------LTNLEPGDVL 88


                  ....
gi 228008337  287 FIDE 290
Cdd:pfam05496  89 FIDE 92
COG0645 COG0645
Predicted kinase, contains AAA domain [General function prediction only];
226-252 3.17e-03

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


Pssm-ID: 440410 [Multi-domain]  Cd Length: 164  Bit Score: 38.36  E-value: 3.17e-03
                         10        20
                 ....*....|....*....|....*..
gi 228008337 226 VLMYGPPGTGKTLLARACAAQTKATFL 252
Cdd:COG0645    2 ILVCGLPGSGKSTLARALAERLGAVRL 28
DnaA COG0593
Chromosomal replication initiation ATPase DnaA [Replication, recombination and repair];
229-382 4.20e-03

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


Pssm-ID: 440358 [Multi-domain]  Cd Length: 303  Bit Score: 39.02  E-value: 4.20e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008337 229 YGPPGTGKTLLARACAAQTKATFLK-----LAGPQLVQMFIgdgAKLVRDAFALAKEKAPSI--IFIDELDAIgtkrfds 301
Cdd:COG0593   40 YGGVGLGKTHLLHAIGNEALENNPGarvvyLTAEEFTNDFI---NAIRNNTIEEFKEKYRSVdvLLIDDIQFL------- 109

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008337 302 ekAGDREVQRTMLELLNQLdgFQPNTQVkVIAAT---NRVDILDPAlLRSgRLDR----KIEfpMPNEEARARIMQ--IH 372
Cdd:COG0593  110 --AGKEATQEEFFHTFNAL--REAGKQI-VLTSDrppKELPGLEER-LRS-RLEWglvvDIQ--PPDLETRIAILRkkAA 180

                        170
                 ....*....|
gi 228008337 373 SRKMNVSPDV 382
Cdd:COG0593  181 DRGLELPDEV 190
McrB COG1401
5-methylcytosine-specific restriction endonuclease McrBC, GTP-binding regulatory subunit McrB ...
 24-246 6.78e-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: 6.78e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008337  24 WDEAEQDGIGEEVLKMSTEEIVQRTRLLDSEIKI-MKSEVLRVTHELQAMKDKIKENSEKIKVNKTLPYLVSNVIELLDV 102
Cdd:COG1401    4 PVLEFKFLIVGLRLKPLESEDAVRELGIRADDLRgAAELATRLAERLSEELLRADRAARATELVEELSAALEVVVLLLDL 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008337 103 DPNDQEEDGANIDLDSQRKGKCAVIKTSTRQTYFLPVIGLVDAEKLKPGDLVGVNKDSYLILETLPTEYDSRVKAMEVDE 182
Cdd:COG1401   84 EKVELNEKLALSEAAVAIEELYELEADSEIEAVGLLLELAERSDALEALERARLLLELADLEERAALETEVLEALEAELE 163

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228008337 183 RPTEQYSDIGGLDKQ----------IQELVEAIVLPMNH-KEKFEN------LGIQPPKGVLMYGPPGTGKTLLARACAA 245
Cdd:COG1401  164 ELLAAPEDLSADALAaelsaaeelySEDLESEDDYLKDLlREKFEEtleaflAALKTKKNVILAGPPGTGKTYLARRLAE 243


                 .
gi 228008337 246 Q 246
Cdd:COG1401  244 A 244
TIGR02928 TIGR02928
orc1/cdc6 family replication initiation protein; Members of this protein family are found ...
 191-242 8.59e-03

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


Pssm-ID: 274354 [Multi-domain]  Cd Length: 365  Bit Score: 38.00  E-value: 8.59e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 228008337  191 IGGLDKQIQELVEAIVlPMnhkekfenLGIQPPKGVLMYGPPGTGKTLLARA 242
Cdd:TIGR02928  17 IVHRDEQIEELAKALR-PI--------LRGSRPSNVFIYGKTGTGKTAVTKY 59
 
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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