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Conserved domains on  [gi|18699726|ref|NP_569053|]
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vacuolar protein sorting-associated protein 4A [Mus musculus]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
RecA-like_VPS4 cd19521
ATPase domain of vacuolar protein sorting-associated protein 4; Vacuolar protein ...
 121-291 4.80e-126

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: 361.87  E-value: 4.80e-126
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18699726 121 KPNIRWNDVAGLEGAKEALKEAVILPIKFPHLFTGKRTPWRGILLFGPPGTGKSYLAKAVATEANnSTFFSVSSSDLMSK 200
Cdd:cd19521   1 KPNVKWEDVAGLEGAKEALKEAVILPVKFPHLFTGNRKPWSGILLYGPPGTGKSYLAKAVATEAN-STFFSVSSSDLVSK 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18699726 201 WLGESEKLVKNLFELARQHKPSIIFIDEVDSLCGSRNENESEAARRIKTEFLVQMQGVGNNNDGTLVLGATNIPWVLDSA 280
Cdd:cd19521  80 WMGESEKLVKQLFAMARENKPSIIFIDEVDSLCGTRGEGESEASRRIKTELLVQMNGVGNDSQGVLVLGATNIPWQLDSA 159

                       170
                ....*....|.
gi 18699726 281 IRRRFEKRIYI 291
Cdd:cd19521 160 IRRRFEKRIYI 170
PTZ00454 super family cl36567
26S protease regulatory subunit 6B-like protein; Provisional
 4-348 3.57e-45

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


The actual alignment was detected with superfamily member PTZ00454:

Pssm-ID: 240423 [Multi-domain]  Cd Length: 398  Bit Score: 161.47  E-value: 3.57e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18699726    4 STLQKAIDLVTKATEED---KAKNYEEALRLYQHAVEYflhaIKYEAHSDKaKESIRAK------------CMQYLDRAE 68
Cdd:PTZ00454   3 TTAAAAVASSTTHTERDlyeKLKELEKELEFLDIQEEY----IKEEQKNLK-RELIRAKeevkriqsvplvIGQFLEMID 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18699726   69 KLK----------DYLRNKEKHGKKPVKENQSEGKGSDSDSEGDN-PEKKKLQEQLMGavVMEKPNIRWNDVAGLEGAKE 137
Cdd:PTZ00454  78 SNYgivsstsgsnYYVRILSTLNRELLKPNASVALHRHSHAVVDIlPPEADSSIQLLQ--MSEKPDVTYSDIGGLDIQKQ 155

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18699726  138 ALKEAVILPIKFPHLF--TGKRTPwRGILLFGPPGTGKSYLAKAVATEANnSTFFSVSSSDLMSKWLGESEKLVKNLFEL 215
Cdd:PTZ00454 156 EIREAVELPLTCPELYeqIGIDPP-RGVLLYGPPGTGKTMLAKAVAHHTT-ATFIRVVGSEFVQKYLGEGPRMVRDVFRL 233

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18699726  216 ARQHKPSIIFIDEVDSLCGSRNENESEAAR---RIKTEFLVQMQGVgNNNDGTLVLGATNIPWVLDSAIRR--RFEKRIY 290
Cdd:PTZ00454 234 ARENAPSIIFIDEVDSIATKRFDAQTGADRevqRILLELLNQMDGF-DQTTNVKVIMATNRADTLDPALLRpgRLDRKIE 312

                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 18699726  291 IPLPEEAARAQMFRLHLGSTphNLT-DANIHELARKTEGYSGADISIIVRDSLMQPVRK 348
Cdd:PTZ00454 313 FPLPDRRQKRLIFQTITSKM--NLSeEVDLEDFVSRPEKISAADIAAICQEAGMQAVRK 369
Vps4_C pfam09336
Vps4 C terminal oligomerization domain; This domain is found at the C terminal of ATPase ...
 374-434 1.55e-34

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


:

Pssm-ID: 462762 [Multi-domain]  Cd Length: 61  Bit Score: 122.61  E-value: 1.55e-34
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 18699726   374 LTPCSPGDPGAIEMTWMDVPGDKLLEPVVCMSDMLRSLATTRPTVNADDLLKVKKFSEDFG 434
Cdd:pfam09336   1 LTPCSPGDPGAIEMTWMDIPSDKLLEPPVTMKDFLKALKSSRPTVSKEDLEKYEEFTKEFG 61
 
Name Accession Description Interval E-value
RecA-like_VPS4 cd19521
ATPase domain of vacuolar protein sorting-associated protein 4; Vacuolar protein ...
 121-291 4.80e-126

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: 361.87  E-value: 4.80e-126
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18699726 121 KPNIRWNDVAGLEGAKEALKEAVILPIKFPHLFTGKRTPWRGILLFGPPGTGKSYLAKAVATEANnSTFFSVSSSDLMSK 200
Cdd:cd19521   1 KPNVKWEDVAGLEGAKEALKEAVILPVKFPHLFTGNRKPWSGILLYGPPGTGKSYLAKAVATEAN-STFFSVSSSDLVSK 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18699726 201 WLGESEKLVKNLFELARQHKPSIIFIDEVDSLCGSRNENESEAARRIKTEFLVQMQGVGNNNDGTLVLGATNIPWVLDSA 280
Cdd:cd19521  80 WMGESEKLVKQLFAMARENKPSIIFIDEVDSLCGTRGEGESEASRRIKTELLVQMNGVGNDSQGVLVLGATNIPWQLDSA 159

                       170
                ....*....|.
gi 18699726 281 IRRRFEKRIYI 291
Cdd:cd19521 160 IRRRFEKRIYI 170
RPT1 COG1222
ATP-dependent 26S proteasome regulatory subunit [Posttranslational modification, protein ...
 65-348 2.00e-88

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


Pssm-ID: 440835 [Multi-domain]  Cd Length: 326  Bit Score: 271.88  E-value: 2.00e-88
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18699726  65 DRAEKLKDYLRNKEKHGKKPVKENQSEgkgsDSDSEGDNPEKKKLQEQLMGAVVMEKPNIRWNDVAGLEGAKEALKEAVI 144
Cdd:COG1222  20 ALQERLGVELALLLQPVKALELLEEAP----ALLLNDANLTQKRLGTPRGTAVPAESPDVTFDDIGGLDEQIEEIREAVE 95

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18699726 145 LPIKFPHLFT--GKRTPwRGILLFGPPGTGKSYLAKAVATEANnSTFFSVSSSDLMSKWLGESEKLVKNLFELARQHKPS 222
Cdd:COG1222  96 LPLKNPELFRkyGIEPP-KGVLLYGPPGTGKTLLAKAVAGELG-APFIRVRGSELVSKYIGEGARNVREVFELAREKAPS 173

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18699726 223 IIFIDEVDSLCGSR-NENESEAARRIKTEFLVQMQGVGNNNDGtLVLGATNIPWVLDSAIRR--RFEKRIYIPLPEEAAR 299
Cdd:COG1222 174 IIFIDEIDAIAARRtDDGTSGEVQRTVNQLLAELDGFESRGDV-LIIAATNRPDLLDPALLRpgRFDRVIEVPLPDEEAR 252

                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|
gi 18699726 300 AQMFRLHLGSTPhnLTDA-NIHELARKTEGYSGADISIIVRDSLMQPVRK 348
Cdd:COG1222 253 EEILKIHLRDMP--LADDvDLDKLAKLTEGFSGADLKAIVTEAGMFAIRE 300
CDC48 TIGR01243
AAA family ATPase, CDC48 subfamily; This subfamily of the AAA family ATPases includes two ...
 107-437 1.61e-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: 231.33  E-value: 1.61e-68
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18699726   107 KKLQEQLMGAVVMEKPNIRWNDVAGLEGAKEALKEAVILPIKFPHLFT--GKRTPwRGILLFGPPGTGKSYLAKAVATEA 184
Cdd:TIGR01243 433 KMVEPSAIREVLVEVPNVRWSDIGGLEEVKQELREAVEWPLKHPEIFEkmGIRPP-KGVLLFGPPGTGKTLLAKAVATES 511

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18699726   185 NnSTFFSVSSSDLMSKWLGESEKLVKNLFELARQHKPSIIFIDEVDSLCGSRNENESEAAR-RIKTEFLVQMQGVgNNND 263
Cdd:TIGR01243 512 G-ANFIAVRGPEILSKWVGESEKAIREIFRKARQAAPAIIFFDEIDAIAPARGARFDTSVTdRIVNQLLTEMDGI-QELS 589

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18699726   264 GTLVLGATNIPWVLDSAIRR--RFEKRIYIPLPEEAARAQMFRLHLGSTPHNlTDANIHELARKTEGYSGADISIIVRDS 341
Cdd:TIGR01243 590 NVVVIAATNRPDILDPALLRpgRFDRLILVPPPDEEARKEIFKIHTRSMPLA-EDVDLEELAEMTEGYTGADIEAVCREA 668

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18699726   342 LMQPVRKVQSATHFKKVcgpsrtnpsvmiddlltpcspgdpgaiemtwMDVPGDKLLEPVVCMSDMLRSLATTRPTVNAD 421
Cdd:TIGR01243 669 AMAALRESIGSPAKEKL-------------------------------EVGEEEFLKDLKVEMRHFLEALKKVKPSVSKE 717

                         330
                  ....*....|....*.
gi 18699726   422 DLLKVKKFSEDFGQES 437
Cdd:TIGR01243 718 DMLRYERLAKELKRLT 733
PRK03992 PRK03992
proteasome-activating nucleotidase; Provisional
 118-348 1.54e-60

proteasome-activating nucleotidase; Provisional


Pssm-ID: 179699 [Multi-domain]  Cd Length: 389  Bit Score: 201.98  E-value: 1.54e-60
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18699726  118 VMEKPNIRWNDVAGLEGAKEALKEAVILPIKFPHLFtgKR---TPWRGILLFGPPGTGKSYLAKAVATEANnSTFFSVSS 194
Cdd:PRK03992 122 VIESPNVTYEDIGGLEEQIREVREAVELPLKKPELF--EEvgiEPPKGVLLYGPPGTGKTLLAKAVAHETN-ATFIRVVG 198

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18699726  195 SDLMSKWLGESEKLVKNLFELARQHKPSIIFIDEVDSLCGSRNENESEAAR---RIKTEFLVQMQGVgNNNDGTLVLGAT 271
Cdd:PRK03992 199 SELVQKFIGEGARLVRELFELAREKAPSIIFIDEIDAIAAKRTDSGTSGDRevqRTLMQLLAEMDGF-DPRGNVKIIAAT 277

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18699726  272 NIPWVLDSAIRR--RFEKRIYIPLPEEAARAQMFRLHLGSTphNLT-DANIHELARKTEGYSGADISIIVRDSLMQPVRK 348
Cdd:PRK03992 278 NRIDILDPAILRpgRFDRIIEVPLPDEEGRLEILKIHTRKM--NLAdDVDLEELAELTEGASGADLKAICTEAGMFAIRD 355
AAA pfam00004
ATPase family associated with various cellular activities (AAA); AAA family proteins often ...
 163-293 7.69e-57

ATPase family associated with various cellular activities (AAA); AAA family proteins often perform chaperone-like functions that assist in the assembly, operation, or disassembly of protein complexes.


Pssm-ID: 459627 [Multi-domain]  Cd Length: 130  Bit Score: 183.56  E-value: 7.69e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18699726   163 ILLFGPPGTGKSYLAKAVATEANnSTFFSVSSSDLMSKWLGESEKLVKNLFELARQHKPSIIFIDEVDSLCGSRNENESE 242
Cdd:pfam00004   1 LLLYGPPGTGKTTLAKAVAKELG-APFIEISGSELVSKYVGESEKRLRELFEAAKKLAPCVIFIDEIDALAGSRGSGGDS 79

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 18699726   243 AARRIKTEFLVQMQGVGNNNDGTLVLGATNIPWVLDSAIRRRFEKRIYIPL 293
Cdd:pfam00004  80 ESRRVVNQLLTELDGFTSSNSKVIVIAATNRPDKLDPALLGRFDRIIEFPL 130
PTZ00454 PTZ00454
26S protease regulatory subunit 6B-like protein; Provisional
 4-348 3.57e-45

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


Pssm-ID: 240423 [Multi-domain]  Cd Length: 398  Bit Score: 161.47  E-value: 3.57e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18699726    4 STLQKAIDLVTKATEED---KAKNYEEALRLYQHAVEYflhaIKYEAHSDKaKESIRAK------------CMQYLDRAE 68
Cdd:PTZ00454   3 TTAAAAVASSTTHTERDlyeKLKELEKELEFLDIQEEY----IKEEQKNLK-RELIRAKeevkriqsvplvIGQFLEMID 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18699726   69 KLK----------DYLRNKEKHGKKPVKENQSEGKGSDSDSEGDN-PEKKKLQEQLMGavVMEKPNIRWNDVAGLEGAKE 137
Cdd:PTZ00454  78 SNYgivsstsgsnYYVRILSTLNRELLKPNASVALHRHSHAVVDIlPPEADSSIQLLQ--MSEKPDVTYSDIGGLDIQKQ 155

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18699726  138 ALKEAVILPIKFPHLF--TGKRTPwRGILLFGPPGTGKSYLAKAVATEANnSTFFSVSSSDLMSKWLGESEKLVKNLFEL 215
Cdd:PTZ00454 156 EIREAVELPLTCPELYeqIGIDPP-RGVLLYGPPGTGKTMLAKAVAHHTT-ATFIRVVGSEFVQKYLGEGPRMVRDVFRL 233

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18699726  216 ARQHKPSIIFIDEVDSLCGSRNENESEAAR---RIKTEFLVQMQGVgNNNDGTLVLGATNIPWVLDSAIRR--RFEKRIY 290
Cdd:PTZ00454 234 ARENAPSIIFIDEVDSIATKRFDAQTGADRevqRILLELLNQMDGF-DQTTNVKVIMATNRADTLDPALLRpgRLDRKIE 312

                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 18699726  291 IPLPEEAARAQMFRLHLGSTphNLT-DANIHELARKTEGYSGADISIIVRDSLMQPVRK 348
Cdd:PTZ00454 313 FPLPDRRQKRLIFQTITSKM--NLSeEVDLEDFVSRPEKISAADIAAICQEAGMQAVRK 369
MIT_VPS4 cd02678
MIT: domain contained within Microtubule Interacting and Trafficking molecules. This ...
 4-79 3.92e-40

MIT: domain contained within Microtubule Interacting and Trafficking molecules. This sub-family of MIT domains is found in intracellular protein transport proteins of the AAA-ATPase family. The molecular function of the MIT domain is unclear.


Pssm-ID: 239141  Cd Length: 75  Bit Score: 138.17  E-value: 3.92e-40
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 18699726   4 STLQKAIDLVTKATEEDKAKNYEEALRLYQHAVEYFLHAIKYEAHSdKAKESIRAKCMQYLDRAEKLKDYLRNKEK 79
Cdd:cd02678   1 DFLQKAIELVKKAIEEDNAGNYEEALRLYQHALEYFMHALKYEKNP-KSKESIRAKCTEYLDRAEKLKEYLAKKEK 75
Vps4_C pfam09336
Vps4 C terminal oligomerization domain; This domain is found at the C terminal of ATPase ...
 374-434 1.55e-34

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


Pssm-ID: 462762 [Multi-domain]  Cd Length: 61  Bit Score: 122.61  E-value: 1.55e-34
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 18699726   374 LTPCSPGDPGAIEMTWMDVPGDKLLEPVVCMSDMLRSLATTRPTVNADDLLKVKKFSEDFG 434
Cdd:pfam09336   1 LTPCSPGDPGAIEMTWMDIPSDKLLEPPVTMKDFLKALKSSRPTVSKEDLEKYEEFTKEFG 61
MIT pfam04212
MIT (microtubule interacting and transport) domain; The MIT domain forms an asymmetric ...
 6-72 6.98e-27

MIT (microtubule interacting and transport) domain; The MIT domain forms an asymmetric three-helix bundle and binds ESCRT-III (endosomal sorting complexes required for transport) substrates.


Pssm-ID: 461228  Cd Length: 66  Bit Score: 102.23  E-value: 6.98e-27
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 18699726     6 LQKAIDLVTKATEEDKAKNYEEALRLYQHAVEYFLHAIKyEAHSDKAKESIRAKCMQYLDRAEKLKD 72
Cdd:pfam04212   1 LSKALELVKKAVEEDNAGNYEEALELYKEALDYLLLALK-ETKNEERRELLRAKIAEYLERAEELKE 66
MIT smart00745
Microtubule Interacting and Trafficking molecule domain;
2-79 1.06e-24

Microtubule Interacting and Trafficking molecule domain;


Pssm-ID: 197854  Cd Length: 77  Bit Score: 96.61  E-value: 1.06e-24
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 18699726      2 TTSTLQKAIDLVTKATEEDKAKNYEEALRLYQHAVEYFLHAIKYEaHSDKAKESIRAKCMQYLDRAEKLKDYLRNKEK 79
Cdd:smart00745   1 TRDYLSKAKELISKALKADEAGNYEEALELYKKAIEYLLEGIKVE-SDSKRREALKAKAAEYLDRAEEIKKSLLERLA 77
AAA smart00382
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ...
 159-295 3.27e-21

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


Pssm-ID: 214640 [Multi-domain]  Cd Length: 148  Bit Score: 89.35  E-value: 3.27e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18699726    159 PWRGILLFGPPGTGKSYLAKAVATEAN--NSTFFSVSSSDLMS--------------KWLGESEKLVKNLFELARQHKPS 222
Cdd:smart00382   1 PGEVILIVGPPGSGKTTLARALARELGppGGGVIYIDGEDILEevldqllliivggkKASGSGELRLRLALALARKLKPD 80

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 18699726    223 IIFIDEVDSLCGSRNENESEAARRIKTEFLVQMQGvgnnndGTLVLGATNIPWVLDSA-IRRRFEKRIYIPLPE 295
Cdd:smart00382  81 VLILDEITSLLDAEQEALLLLLEELRLLLLLKSEK------NLTVILTTNDEKDLGPAlLRRRFDRRIVLLLIL 148
IS21_help_AAA NF038214
IS21-like element helper ATPase IstB; This protein family model resembles PF01695, but was ...
 163-229 1.06e-05

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


Pssm-ID: 439516  Cd Length: 232  Bit Score: 46.31  E-value: 1.06e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 18699726  163 ILLFGPPGTGKSYLAKAV---ATEANNSTFFsVSSSDLMSKWlgESEKLVKNLFELARQH-KPSIIFIDEV 229
Cdd:NF038214  93 VLLLGPPGTGKTHLAIALgyaACRQGYRVRF-TTAADLVEQL--AQARADGRLGRLLRRLaRYDLLIIDEL 160
 
Name Accession Description Interval E-value
RecA-like_VPS4 cd19521
ATPase domain of vacuolar protein sorting-associated protein 4; Vacuolar protein ...
 121-291 4.80e-126

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: 361.87  E-value: 4.80e-126
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18699726 121 KPNIRWNDVAGLEGAKEALKEAVILPIKFPHLFTGKRTPWRGILLFGPPGTGKSYLAKAVATEANnSTFFSVSSSDLMSK 200
Cdd:cd19521   1 KPNVKWEDVAGLEGAKEALKEAVILPVKFPHLFTGNRKPWSGILLYGPPGTGKSYLAKAVATEAN-STFFSVSSSDLVSK 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18699726 201 WLGESEKLVKNLFELARQHKPSIIFIDEVDSLCGSRNENESEAARRIKTEFLVQMQGVGNNNDGTLVLGATNIPWVLDSA 280
Cdd:cd19521  80 WMGESEKLVKQLFAMARENKPSIIFIDEVDSLCGTRGEGESEASRRIKTELLVQMNGVGNDSQGVLVLGATNIPWQLDSA 159

                       170
                ....*....|.
gi 18699726 281 IRRRFEKRIYI 291
Cdd:cd19521 160 IRRRFEKRIYI 170
RecA-like_VPS4-like cd19509
ATPase domain of VPS4, ATAD1, K, KTNA1, Spastin, FIGL-1 and similar ATPase domains; This ...
 129-291 1.36e-93

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: 279.24  E-value: 1.36e-93
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18699726 129 VAGLEGAKEALKEAVILPIKFPHLFTGKRTPWRGILLFGPPGTGKSYLAKAVATEANnSTFFSVSSSDLMSKWLGESEKL 208
Cdd:cd19509   1 IAGLDDAKEALKEAVILPSLRPDLFPGLRGPPRGILLYGPPGTGKTLLARAVASESG-STFFSISASSLVSKWVGESEKI 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18699726 209 VKNLFELARQHKPSIIFIDEVDSLCGSRNENESEAARRIKTEFLVQMQGVGNN-NDGTLVLGATNIPWVLDSAIRRRFEK 287
Cdd:cd19509  80 VRALFALARELQPSIIFIDEIDSLLSERGSGEHEASRRVKTEFLVQMDGVLNKpEDRVLVLGATNRPWELDEAFLRRFEK 159


                ....
gi 18699726 288 RIYI 291
Cdd:cd19509 160 RIYI 163
RPT1 COG1222
ATP-dependent 26S proteasome regulatory subunit [Posttranslational modification, protein ...
 65-348 2.00e-88

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


Pssm-ID: 440835 [Multi-domain]  Cd Length: 326  Bit Score: 271.88  E-value: 2.00e-88
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18699726  65 DRAEKLKDYLRNKEKHGKKPVKENQSEgkgsDSDSEGDNPEKKKLQEQLMGAVVMEKPNIRWNDVAGLEGAKEALKEAVI 144
Cdd:COG1222  20 ALQERLGVELALLLQPVKALELLEEAP----ALLLNDANLTQKRLGTPRGTAVPAESPDVTFDDIGGLDEQIEEIREAVE 95

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18699726 145 LPIKFPHLFT--GKRTPwRGILLFGPPGTGKSYLAKAVATEANnSTFFSVSSSDLMSKWLGESEKLVKNLFELARQHKPS 222
Cdd:COG1222  96 LPLKNPELFRkyGIEPP-KGVLLYGPPGTGKTLLAKAVAGELG-APFIRVRGSELVSKYIGEGARNVREVFELAREKAPS 173

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18699726 223 IIFIDEVDSLCGSR-NENESEAARRIKTEFLVQMQGVGNNNDGtLVLGATNIPWVLDSAIRR--RFEKRIYIPLPEEAAR 299
Cdd:COG1222 174 IIFIDEIDAIAARRtDDGTSGEVQRTVNQLLAELDGFESRGDV-LIIAATNRPDLLDPALLRpgRFDRVIEVPLPDEEAR 252

                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|
gi 18699726 300 AQMFRLHLGSTPhnLTDA-NIHELARKTEGYSGADISIIVRDSLMQPVRK 348
Cdd:COG1222 253 EEILKIHLRDMP--LADDvDLDKLAKLTEGFSGADLKAIVTEAGMFAIRE 300
SpoVK COG0464
AAA+-type ATPase, SpoVK/Ycf46/Vps4 family [Cell wall/membrane/envelope biogenesis, Cell cycle ...
 95-347 9.59e-77

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


Pssm-ID: 440232 [Multi-domain]  Cd Length: 397  Bit Score: 244.44  E-value: 9.59e-77
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18699726  95 SDSDSEGDNPEKKKLQEQLMGAVVMEKPNIRWNDVAGLEGAKEALKEAVILPIKFPHLFT--GKRTPwRGILLFGPPGTG 172
Cdd:COG0464 125 SAEALALAAPLVTYEDIGGLEEELLELREAILDDLGGLEEVKEELRELVALPLKRPELREeyGLPPP-RGLLLYGPPGTG 203

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18699726 173 KSYLAKAVATEANnSTFFSVSSSDLMSKWLGESEKLVKNLFELARQHKPSIIFIDEVDSLCGSRNENESEAARRIKTEFL 252
Cdd:COG0464 204 KTLLARALAGELG-LPLIEVDLSDLVSKYVGETEKNLREVFDKARGLAPCVLFIDEADALAGKRGEVGDGVGRRVVNTLL 282

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18699726 253 VQMQGVgnnNDGTLVLGATNIPWVLDSAIRRRFEKRIYIPLPEEAARAQMFRLHLGSTPHNlTDANIHELARKTEGYSGA 332
Cdd:COG0464 283 TEMEEL---RSDVVVIAATNRPDLLDPALLRRFDEIIFFPLPDAEERLEIFRIHLRKRPLD-EDVDLEELAEATEGLSGA 358

                       250
                ....*....|....*
gi 18699726 333 DISIIVRDSLMQPVR 347
Cdd:COG0464 359 DIRNVVRRAALQALR 373
RecA-like_KTNA1 cd19522
Katanin p60 ATPase-containing subunit A1; Katanin p60 ATPase-containing subunit A1 (KTNA1) is ...
 128-291 6.99e-75

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: 231.41  E-value: 6.99e-75
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18699726 128 DVAGLEGAKEALKEAVILPIKFPHLFTGKRTPWRGILLFGPPGTGKSYLAKAVATEAnNSTFFSVSSSDLMSKWLGESEK 207
Cdd:cd19522   1 DIADLEEAKKLLEEAVVLPMWMPEFFKGIRRPWKGVLMVGPPGTGKTLLAKAVATEC-GTTFFNVSSSTLTSKYRGESEK 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18699726 208 LVKNLFELARQHKPSIIFIDEVDSLCGSR-NENESEAARRIKTEFLVQMQGVGNNNDG------TLVLGATNIPWVLDSA 280
Cdd:cd19522  80 LVRLLFEMARFYAPTTIFIDEIDSICSRRgTSEEHEASRRVKSELLVQMDGVGGASENddpskmVMVLAATNFPWDIDEA 159

                       170
                ....*....|.
gi 18699726 281 IRRRFEKRIYI 291
Cdd:cd19522 160 LRRRLEKRIYI 170
RecA-like_Figl-1 cd19525
ATPase domain of Fidgetin-Like 1 (FIGL-1); FIGL-1 may participate in DNA repair in the nucleus; ...
 108-291 7.02e-73

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: 227.18  E-value: 7.02e-73
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18699726 108 KLQEQLMGAVVMEKPNIRWNDVAGLEGAKEALKEAVILPIKFPHLFTGKRTPWRGILLFGPPGTGKSYLAKAVATEANnS 187
Cdd:cd19525   3 KMIELIMSEIMDHGPPINWADIAGLEFAKKTIKEIVVWPMLRPDIFTGLRGPPKGILLFGPPGTGKTLIGKCIASQSG-A 81

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18699726 188 TFFSVSSSDLMSKWLGESEKLVKNLFELARQHKPSIIFIDEVDSLCGSRNENESEAARRIKTEFLVQMQGVGNN-NDGTL 266
Cdd:cd19525  82 TFFSISASSLTSKWVGEGEKMVRALFSVARCKQPAVIFIDEIDSLLSQRGEGEHESSRRIKTEFLVQLDGATTSsEDRIL 161

                       170       180
                ....*....|....*....|....*
gi 18699726 267 VLGATNIPWVLDSAIRRRFEKRIYI 291
Cdd:cd19525 162 VVGATNRPQEIDEAARRRLVKRLYI 186
RecA-like_spastin cd19524
ATPase domain of spastin; Spastin is an ATP-dependent microtubule-severing protein involved in ...
 128-291 3.55e-70

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: 219.34  E-value: 3.55e-70
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18699726 128 DVAGLEGAKEALKEAVILPIKFPHLFTGKRTPWRGILLFGPPGTGKSYLAKAVATEANnSTFFSVSSSDLMSKWLGESEK 207
Cdd:cd19524   1 DIAGQDLAKQALQEMVILPSLRPELFTGLRAPARGLLLFGPPGNGKTMLAKAVAAESN-ATFFNISAASLTSKYVGEGEK 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18699726 208 LVKNLFELARQHKPSIIFIDEVDSLCGSRNENESEAARRIKTEFLVQMQGV-GNNNDGTLVLGATNIPWVLDSAIRRRFE 286
Cdd:cd19524  80 LVRALFAVARELQPSIIFIDEVDSLLSERSEGEHEASRRLKTEFLIEFDGVqSNGDDRVLVMGATNRPQELDDAVLRRFT 159


                ....*
gi 18699726 287 KRIYI 291
Cdd:cd19524 160 KRVYV 164
CDC48 TIGR01243
AAA family ATPase, CDC48 subfamily; This subfamily of the AAA family ATPases includes two ...
 107-437 1.61e-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: 231.33  E-value: 1.61e-68
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18699726   107 KKLQEQLMGAVVMEKPNIRWNDVAGLEGAKEALKEAVILPIKFPHLFT--GKRTPwRGILLFGPPGTGKSYLAKAVATEA 184
Cdd:TIGR01243 433 KMVEPSAIREVLVEVPNVRWSDIGGLEEVKQELREAVEWPLKHPEIFEkmGIRPP-KGVLLFGPPGTGKTLLAKAVATES 511

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18699726   185 NnSTFFSVSSSDLMSKWLGESEKLVKNLFELARQHKPSIIFIDEVDSLCGSRNENESEAAR-RIKTEFLVQMQGVgNNND 263
Cdd:TIGR01243 512 G-ANFIAVRGPEILSKWVGESEKAIREIFRKARQAAPAIIFFDEIDAIAPARGARFDTSVTdRIVNQLLTEMDGI-QELS 589

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18699726   264 GTLVLGATNIPWVLDSAIRR--RFEKRIYIPLPEEAARAQMFRLHLGSTPHNlTDANIHELARKTEGYSGADISIIVRDS 341
Cdd:TIGR01243 590 NVVVIAATNRPDILDPALLRpgRFDRLILVPPPDEEARKEIFKIHTRSMPLA-EDVDLEELAEMTEGYTGADIEAVCREA 668

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18699726   342 LMQPVRKVQSATHFKKVcgpsrtnpsvmiddlltpcspgdpgaiemtwMDVPGDKLLEPVVCMSDMLRSLATTRPTVNAD 421
Cdd:TIGR01243 669 AMAALRESIGSPAKEKL-------------------------------EVGEEEFLKDLKVEMRHFLEALKKVKPSVSKE 717

                         330
                  ....*....|....*.
gi 18699726   422 DLLKVKKFSEDFGQES 437
Cdd:TIGR01243 718 DMLRYERLAKELKRLT 733
PRK03992 PRK03992
proteasome-activating nucleotidase; Provisional
 118-348 1.54e-60

proteasome-activating nucleotidase; Provisional


Pssm-ID: 179699 [Multi-domain]  Cd Length: 389  Bit Score: 201.98  E-value: 1.54e-60
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18699726  118 VMEKPNIRWNDVAGLEGAKEALKEAVILPIKFPHLFtgKR---TPWRGILLFGPPGTGKSYLAKAVATEANnSTFFSVSS 194
Cdd:PRK03992 122 VIESPNVTYEDIGGLEEQIREVREAVELPLKKPELF--EEvgiEPPKGVLLYGPPGTGKTLLAKAVAHETN-ATFIRVVG 198

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18699726  195 SDLMSKWLGESEKLVKNLFELARQHKPSIIFIDEVDSLCGSRNENESEAAR---RIKTEFLVQMQGVgNNNDGTLVLGAT 271
Cdd:PRK03992 199 SELVQKFIGEGARLVRELFELAREKAPSIIFIDEIDAIAAKRTDSGTSGDRevqRTLMQLLAEMDGF-DPRGNVKIIAAT 277

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18699726  272 NIPWVLDSAIRR--RFEKRIYIPLPEEAARAQMFRLHLGSTphNLT-DANIHELARKTEGYSGADISIIVRDSLMQPVRK 348
Cdd:PRK03992 278 NRIDILDPAILRpgRFDRIIEVPLPDEEGRLEILKIHTRKM--NLAdDVDLEELAELTEGASGADLKAICTEAGMFAIRD 355
RecA-like_ATAD1 cd19520
ATPase domain of ATPase family AAA domain-containing protein 1 and similar ATPase domains; ...
 128-291 1.74e-58

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: 189.17  E-value: 1.74e-58
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18699726 128 DVAGLEGAKEALKEAVILPIKFPHLFTGKR--TPWRGILLFGPPGTGKSYLAKAVATEANnSTFFSVSSSDLMSKWLGES 205
Cdd:cd19520   1 DIGGLDEVITELKELVILPLQRPELFDNSRllQPPKGVLLYGPPGCGKTMLAKATAKEAG-ARFINLQVSSLTDKWYGES 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18699726 206 EKLVKNLFELARQHKPSIIFIDEVDSLCGSRNENESEAARRIKTEFLVQMQGVGNN-NDGTLVLGATNIPWVLDSAIRRR 284
Cdd:cd19520  80 QKLVAAVFSLASKLQPSIIFIDEIDSFLRQRSSTDHEATAMMKAEFMSLWDGLSTDgNCRVIVMGATNRPQDLDEAILRR 159


                ....*..
gi 18699726 285 FEKRIYI 291
Cdd:cd19520 160 MPKRFHI 166
AAA pfam00004
ATPase family associated with various cellular activities (AAA); AAA family proteins often ...
 163-293 7.69e-57

ATPase family associated with various cellular activities (AAA); AAA family proteins often perform chaperone-like functions that assist in the assembly, operation, or disassembly of protein complexes.


Pssm-ID: 459627 [Multi-domain]  Cd Length: 130  Bit Score: 183.56  E-value: 7.69e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18699726   163 ILLFGPPGTGKSYLAKAVATEANnSTFFSVSSSDLMSKWLGESEKLVKNLFELARQHKPSIIFIDEVDSLCGSRNENESE 242
Cdd:pfam00004   1 LLLYGPPGTGKTTLAKAVAKELG-APFIEISGSELVSKYVGESEKRLRELFEAAKKLAPCVIFIDEIDALAGSRGSGGDS 79

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 18699726   243 AARRIKTEFLVQMQGVGNNNDGTLVLGATNIPWVLDSAIRRRFEKRIYIPL 293
Cdd:pfam00004  80 ESRRVVNQLLTELDGFTSSNSKVIVIAATNRPDKLDPALLGRFDRIIEFPL 130
RecA-like_CDC48_r2-like cd19511
second of two ATPase domains of CDC48/p97, PEX1 and -6, VAT and NVL, and similar ATPase ...
 135-291 1.18e-54

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


Pssm-ID: 410919 [Multi-domain]  Cd Length: 159  Bit Score: 179.02  E-value: 1.18e-54
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18699726 135 AKEALKEAVILPIKFPHLFT--GKRTPwRGILLFGPPGTGKSYLAKAVATEANnSTFFSVSSSDLMSKWLGESEKLVKNL 212
Cdd:cd19511   1 VKRELKEAVEWPLKHPDAFKrlGIRPP-KGVLLYGPPGCGKTLLAKALASEAG-LNFISVKGPELFSKYVGESERAVREI 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18699726 213 FELARQHKPSIIFIDEVDSLCGSR-NENESEAARRIKTEFLVQMQGVGnNNDGTLVLGATNIPWVLDSAIRR--RFEKRI 289
Cdd:cd19511  79 FQKARQAAPCIIFFDEIDSLAPRRgQSDSSGVTDRVVSQLLTELDGIE-SLKGVVVIAATNRPDMIDPALLRpgRLDKLI 157


                ..
gi 18699726 290 YI 291
Cdd:cd19511 158 YV 159
RecA-like_CDC48_NLV2_r1-like cd19503
first of two ATPase domains of CDC48 and NLV2, and similar ATPase domains; CDC48 in yeast and ...
 128-291 4.28e-53

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: 175.17  E-value: 4.28e-53
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18699726 128 DVAGLEGAKEALKEAVILPIKFPHLFT--GKRTPwRGILLFGPPGTGKSYLAKAVATEANnSTFFSVSSSDLMSKWLGES 205
Cdd:cd19503   1 DIGGLDEQIASLKELIELPLKYPELFRalGLKPP-RGVLLHGPPGTGKTLLARAVANEAG-ANFLSISGPSIVSKYLGES 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18699726 206 EKLVKNLFELARQHKPSIIFIDEVDSLCGSRNENESEAARRIKTEFLVQMQGVGNNNdGTLVLGATNIPWVLDSAIRR-- 283
Cdd:cd19503  79 EKNLREIFEEARSHAPSIIFIDEIDALAPKREEDQREVERRVVAQLLTLMDGMSSRG-KVVVIAATNRPDAIDPALRRpg 157


                ....*...
gi 18699726 284 RFEKRIYI 291
Cdd:cd19503 158 RFDREVEI 165
FtsH_fam TIGR01241
ATP-dependent metalloprotease FtsH; HflB(FtsH) is a pleiotropic protein required for correct ...
 106-352 1.25e-52

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: 183.64  E-value: 1.25e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18699726   106 KKKLQEQlmgavvmEKPNIRWNDVAGLEGAKEALKEAVILpIKFPHLFT--GKRTPwRGILLFGPPGTGKSYLAKAVATE 183
Cdd:TIGR01241  41 KAKLLNE-------EKPKVTFKDVAGIDEAKEELMEIVDF-LKNPSKFTklGAKIP-KGVLLVGPPGTGKTLLAKAVAGE 111

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18699726   184 ANNStFFSVSSSDLMSKWLGESEKLVKNLFELARQHKPSIIFIDEVDS--------LCGSRNENEseaarRIKTEFLVQM 255
Cdd:TIGR01241 112 AGVP-FFSISGSDFVEMFVGVGASRVRDLFEQAKKNAPCIIFIDEIDAvgrqrgagLGGGNDERE-----QTLNQLLVEM 185

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18699726   256 QGVGnNNDGTLVLGATNIPWVLDSAIRR--RFEKRIYIPLPEEAARAQMFRLHLGSTPHNlTDANIHELARKTEGYSGAD 333
Cdd:TIGR01241 186 DGFG-TNTGVIVIAATNRPDVLDPALLRpgRFDRQVVVDLPDIKGREEILKVHAKNKKLA-PDVDLKAVARRTPGFSGAD 263

                         250
                  ....*....|....*....
gi 18699726   334 ISIIVRDSLMQPVRKVQSA 352
Cdd:TIGR01241 264 LANLLNEAALLAARKNKTE 282
CDC48 TIGR01243
AAA family ATPase, CDC48 subfamily; This subfamily of the AAA family ATPases includes two ...
 122-393 3.11e-51

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: 183.95  E-value: 3.11e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18699726   122 PNIRWNDVAGLEGAKEALKEAVILPIKFPHLFT--GKRTPwRGILLFGPPGTGKSYLAKAVATEANnSTFFSVSSSDLMS 199
Cdd:TIGR01243 173 PKVTYEDIGGLKEAKEKIREMVELPMKHPELFEhlGIEPP-KGVLLYGPPGTGKTLLAKAVANEAG-AYFISINGPEIMS 250

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18699726   200 KWLGESEKLVKNLFELARQHKPSIIFIDEVDSLCGSRNENESEAARRIKTEFLVQMQGVGNNNDgTLVLGATNIPWVLDS 279
Cdd:TIGR01243 251 KYYGESEERLREIFKEAEENAPSIIFIDEIDAIAPKREEVTGEVEKRVVAQLLTLMDGLKGRGR-VIVIGATNRPDALDP 329

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18699726   280 AIRR--RFEKRIYIPLPEEAARAQMFRLHLGSTPHNlTDANIHELARKTEGYSGADISIIVRDSLMQPVRKV--QSATHF 355
Cdd:TIGR01243 330 ALRRpgRFDREIVIRVPDKRARKEILKVHTRNMPLA-EDVDLDKLAEVTHGFVGADLAALAKEAAMAALRRFirEGKINF 408

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|
gi 18699726   356 KKVCGPSRT--NPSVMIDDLLTPCSPGDPGAIEMTWMDVP 393
Cdd:TIGR01243 409 EAEEIPAEVlkELKVTMKDFMEALKMVEPSAIREVLVEVP 448
RecA-like_protease cd19481
proteases similar to RecA; RecA-like NTPases. This family includes the NTP binding domain of ...
 135-291 2.77e-50

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: 167.46  E-value: 2.77e-50
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18699726 135 AKEALKEAVILPIKFPHLFTGKRTPWRGILLFGPPGTGKSYLAKAVATEANNStFFSVSSSDLMSKWLGESEKLVKNLFE 214
Cdd:cd19481   1 LKASLREAVEAPRRGSRLRRYGLGLPKGILLYGPPGTGKTLLAKALAGELGLP-LIVVKLSSLLSKYVGESEKNLRKIFE 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18699726 215 LARQHKPSIIFIDEVDSLCGSR-NENESEAARRIKTEFLVQMQGVgNNNDGTLVLGATNIPWVLDSAIRR--RFEKRIYI 291
Cdd:cd19481  80 RARRLAPCILFIDEIDAIGRKRdSSGESGELRRVLNQLLTELDGV-NSRSKVLVIAATNRPDLLDPALLRpgRFDEVIEF 158
COG1223 COG1223
Predicted ATPase, AAA+ superfamily [General function prediction only];
126-358 1.17e-47

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


Pssm-ID: 440836 [Multi-domain]  Cd Length: 246  Bit Score: 163.52  E-value: 1.17e-47
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18699726 126 WNDVAGLEGAKEALKEAVI------LPIKFphlftGKRTPwRGILLFGPPGTGKSYLAKAVATEANnSTFFSVSSSDLMS 199
Cdd:COG1223   1 LDDVVGQEEAKKKLKLIIKelrrreNLRKF-----GLWPP-RKILFYGPPGTGKTMLAEALAGELK-LPLLTVRLDSLIG 73

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18699726 200 KWLGESEKLVKNLFELARQHkPSIIFIDEVDSLCGSR-NENESEAARRIKTEFLVQMQGVgnnNDGTLVLGATNIPWVLD 278
Cdd:COG1223  74 SYLGETARNLRKLFDFARRA-PCVIFFDEFDAIAKDRgDQNDVGEVKRVVNALLQELDGL---PSGSVVIAATNHPELLD 149

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18699726 279 SAIRRRFEKRIYIPLPEEAARAQMFRLHLGSTPHNLtDANIHELARKTEGYSGADISIIVRDSLMQPV---RKVQSATHF 355
Cdd:COG1223 150 SALWRRFDEVIEFPLPDKEERKEILELNLKKFPLPF-ELDLKKLAKKLEGLSGADIEKVLKTALKKAIledREKVTKEDL 228


                ...
gi 18699726 356 KKV 358
Cdd:COG1223 229 EEA 231
RecA-like_fidgetin cd19523
ATPase domain of fidgetin; Fidgetin (FIGN) is a ATP-dependent microtubule severing protein. ...
 128-291 1.87e-45

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: 155.04  E-value: 1.87e-45
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18699726 128 DVAGLEGAKEALKEAVILPIKFPHLFTGKRTPWRGILLFGPPGTGKSYLAKAVATEAnNSTFFSVSSSDLMSKWLGESEK 207
Cdd:cd19523   1 DIAGLGALKAAIKEEVLWPLLRPDAFSGLLRLPRSILLFGPRGTGKTLLGRCLASQL-GATFLRLRGSTLVAKWAGEGEK 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18699726 208 LVKNLFELARQHKPSIIFIDEVDSLCGSRNENESeAARRIKTEFLVQMQGV-GNNNDGTLVLGATNIPWVLDSAIRRRFE 286
Cdd:cd19523  80 ILQASFLAARCRQPSVLFISDLDALLSSQDDEAS-PVGRLQVELLAQLDGVlGSGEDGVLVVCTTSKPEEIDESLRRYFS 158


                ....*
gi 18699726 287 KRIYI 291
Cdd:cd19523 159 KRLLV 163
PTZ00454 PTZ00454
26S protease regulatory subunit 6B-like protein; Provisional
 4-348 3.57e-45

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


Pssm-ID: 240423 [Multi-domain]  Cd Length: 398  Bit Score: 161.47  E-value: 3.57e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18699726    4 STLQKAIDLVTKATEED---KAKNYEEALRLYQHAVEYflhaIKYEAHSDKaKESIRAK------------CMQYLDRAE 68
Cdd:PTZ00454   3 TTAAAAVASSTTHTERDlyeKLKELEKELEFLDIQEEY----IKEEQKNLK-RELIRAKeevkriqsvplvIGQFLEMID 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18699726   69 KLK----------DYLRNKEKHGKKPVKENQSEGKGSDSDSEGDN-PEKKKLQEQLMGavVMEKPNIRWNDVAGLEGAKE 137
Cdd:PTZ00454  78 SNYgivsstsgsnYYVRILSTLNRELLKPNASVALHRHSHAVVDIlPPEADSSIQLLQ--MSEKPDVTYSDIGGLDIQKQ 155

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18699726  138 ALKEAVILPIKFPHLF--TGKRTPwRGILLFGPPGTGKSYLAKAVATEANnSTFFSVSSSDLMSKWLGESEKLVKNLFEL 215
Cdd:PTZ00454 156 EIREAVELPLTCPELYeqIGIDPP-RGVLLYGPPGTGKTMLAKAVAHHTT-ATFIRVVGSEFVQKYLGEGPRMVRDVFRL 233

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18699726  216 ARQHKPSIIFIDEVDSLCGSRNENESEAAR---RIKTEFLVQMQGVgNNNDGTLVLGATNIPWVLDSAIRR--RFEKRIY 290
Cdd:PTZ00454 234 ARENAPSIIFIDEVDSIATKRFDAQTGADRevqRILLELLNQMDGF-DQTTNVKVIMATNRADTLDPALLRpgRLDRKIE 312

                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 18699726  291 IPLPEEAARAQMFRLHLGSTphNLT-DANIHELARKTEGYSGADISIIVRDSLMQPVRK 348
Cdd:PTZ00454 313 FPLPDRRQKRLIFQTITSKM--NLSeEVDLEDFVSRPEKISAADIAAICQEAGMQAVRK 369
RecA-like_PAN_like cd19502
proteasome activating nucleotidase PAN and related proteasome subunits; This subfamily ...
 126-289 4.73e-45

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: 154.42  E-value: 4.73e-45
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18699726 126 WNDVAGLEGAKEALKEAVILPIKFPHLFT--GKRTPwRGILLFGPPGTGKSYLAKAVATEANnSTFFSVSSSDLMSKWLG 203
Cdd:cd19502   2 YEDIGGLDEQIREIREVVELPLKHPELFEelGIEPP-KGVLLYGPPGTGKTLLAKAVANHTD-ATFIRVVGSELVQKYIG 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18699726 204 ESEKLVKNLFELARQHKPSIIFIDEVDSLCGSRNENESEAAR---RIKTEFLVQMQGVGNNNDgTLVLGATNIPWVLDSA 280
Cdd:cd19502  80 EGARLVRELFEMAREKAPSIIFIDEIDAIGAKRFDSGTGGDRevqRTMLELLNQLDGFDPRGN-IKVIMATNRPDILDPA 158

                       170
                ....*....|.
gi 18699726 281 IRR--RFEKRI 289
Cdd:cd19502 159 LLRpgRFDRKI 169
RecA-like_FtsH cd19501
ATP-dependent zinc metalloprotease FtsH; FtsH ATPase is a processive, ATP-dependent zinc ...
 124-291 6.35e-45

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: 153.93  E-value: 6.35e-45
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18699726 124 IRWNDVAGLEGAKEALKEAVILpIKFPHLFT--GKRTPwRGILLFGPPGTGKSYLAKAVATEANNStFFSVSSSDLMSKW 201
Cdd:cd19501   1 VTFKDVAGCEEAKEELKEVVEF-LKNPEKFTklGAKIP-KGVLLVGPPGTGKTLLAKAVAGEAGVP-FFSISGSDFVEMF 77

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18699726 202 LGESEKLVKNLFELARQHKPSIIFIDEVDSLCGSRNENES---EAARRIKTEFLVQMQGVGnNNDGTLVLGATNIPWVLD 278
Cdd:cd19501  78 VGVGASRVRDLFEQAKKNAPCIVFIDEIDAVGRKRGAGLGgghDEREQTLNQLLVEMDGFE-SNTGVIVIAATNRPDVLD 156

                       170
                ....*....|....*
gi 18699726 279 SAIRR--RFEKRIYI 291
Cdd:cd19501 157 PALLRpgRFDRQVYV 171
RecA-like_VCP_r2 cd19529
second of two ATPase domains of Valosin-containing protein-like ATPase (VAT) and similar ...
 135-291 7.28e-45

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: 153.42  E-value: 7.28e-45
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18699726 135 AKEALKEAVILPIKFPHLFT--GKRTPwRGILLFGPPGTGKSYLAKAVATEANnSTFFSVSSSDLMSKWLGESEKLVKNL 212
Cdd:cd19529   1 VKQELKEAVEWPLLKPEVFKrlGIRPP-KGILLYGPPGTGKTLLAKAVATESN-ANFISVKGPELLSKWVGESEKAIREI 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18699726 213 FELARQHKPSIIFIDEVDSLCGSRNEN-ESEAARRIKTEFLVQMQGVGNNNDgTLVLGATNIPWVLDSAIRR--RFEKRI 289
Cdd:cd19529  79 FRKARQVAPCVIFFDEIDSIAPRRGTTgDSGVTERVVNQLLTELDGLEEMNG-VVVIAATNRPDIIDPALLRagRFDRLI 157


                ..
gi 18699726 290 YI 291
Cdd:cd19529 158 YI 159
HflB COG0465
ATP-dependent Zn proteases [Posttranslational modification, protein turnover, chaperones];
120-334 8.04e-45

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


Pssm-ID: 440233 [Multi-domain]  Cd Length: 583  Bit Score: 164.05  E-value: 8.04e-45
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18699726 120 EKPNIRWNDVAGLEGAKEALKEAV-ILpiKFPHLFT--GKRTPwRGILLFGPPGTGKSYLAKAVATEAnNSTFFSVSSSD 196
Cdd:COG0465 135 DKPKVTFDDVAGVDEAKEELQEIVdFL--KDPEKFTrlGAKIP-KGVLLVGPPGTGKTLLAKAVAGEA-GVPFFSISGSD 210

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18699726 197 LM--------SKwlgeseklVKNLFELARQHKPSIIFIDEVDSLCGSRNEN------ESEaarriKT--EFLVQMQGVGn 260
Cdd:COG0465 211 FVemfvgvgaSR--------VRDLFEQAKKNAPCIIFIDEIDAVGRQRGAGlggghdERE-----QTlnQLLVEMDGFE- 276

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 18699726 261 NNDGTLVLGATNIPWVLDSAIRR--RFEKRIYIPLPEEAARAQMFRLHLGSTPHNlTDANIHELARKTEGYSGADI 334
Cdd:COG0465 277 GNEGVIVIAATNRPDVLDPALLRpgRFDRQVVVDLPDVKGREAILKVHARKKPLA-PDVDLEVIARRTPGFSGADL 351
RecA-like_CDC48_r1-like cd19519
first of two ATPase domains of CDC48 and similar ATPase domains; CDC48 in yeast and p97 or VCP ...
 128-292 6.01e-42

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: 146.04  E-value: 6.01e-42
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18699726 128 DVAGLEGAKEALKEAVILPIKFPHLFtgKR---TPWRGILLFGPPGTGKSYLAKAVATEANnSTFFSVSSSDLMSKWLGE 204
Cdd:cd19519   1 DIGGCRKQLAQIREMVELPLRHPELF--KAigiKPPRGILLYGPPGTGKTLIARAVANETG-AFFFLINGPEIMSKLAGE 77

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18699726 205 SEKLVKNLFELARQHKPSIIFIDEVDSLCGSRNENESEAARRIKTEFLVQMQGVGNNNDgTLVLGATNIPWVLDSAIRR- 283
Cdd:cd19519  78 SESNLRKAFEEAEKNAPAIIFIDEIDAIAPKREKTHGEVERRIVSQLLTLMDGLKQRAH-VIVMAATNRPNSIDPALRRf 156

                       170
                ....*....|
gi 18699726 284 -RFEKRIYIP 292
Cdd:cd19519 157 gRFDREIDIG 166
RecA-like_CDC48_r2-like cd19528
second of two ATPase domains of CDC48 and similar ATPase domains; CDC48 in yeast and p97 or ...
 136-291 9.42e-41

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: 142.65  E-value: 9.42e-41
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18699726 136 KEALKEAVILPIKFPHLFTG-KRTPWRGILLFGPPGTGKSYLAKAVATEANnSTFFSVSSSDLMSKWLGESEKLVKNLFE 214
Cdd:cd19528   2 KRELQELVQYPVEHPDKFLKfGMTPSKGVLFYGPPGCGKTLLAKAIANECQ-ANFISVKGPELLTMWFGESEANVRDIFD 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18699726 215 LARQHKPSIIFIDEVDSLCGSRNEN---ESEAARRIKTEFLVQMQGVgNNNDGTLVLGATNIPWVLDSAIRR--RFEKRI 289
Cdd:cd19528  81 KARAAAPCVLFFDELDSIAKARGGNigdAGGAADRVINQILTEMDGM-NTKKNVFIIGATNRPDIIDPAILRpgRLDQLI 159


                ..
gi 18699726 290 YI 291
Cdd:cd19528 160 YI 161
MIT_VPS4 cd02678
MIT: domain contained within Microtubule Interacting and Trafficking molecules. This ...
 4-79 3.92e-40

MIT: domain contained within Microtubule Interacting and Trafficking molecules. This sub-family of MIT domains is found in intracellular protein transport proteins of the AAA-ATPase family. The molecular function of the MIT domain is unclear.


Pssm-ID: 239141  Cd Length: 75  Bit Score: 138.17  E-value: 3.92e-40
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 18699726   4 STLQKAIDLVTKATEEDKAKNYEEALRLYQHAVEYFLHAIKYEAHSdKAKESIRAKCMQYLDRAEKLKDYLRNKEK 79
Cdd:cd02678   1 DFLQKAIELVKKAIEEDNAGNYEEALRLYQHALEYFMHALKYEKNP-KSKESIRAKCTEYLDRAEKLKEYLAKKEK 75
PTZ00361 PTZ00361
26 proteosome regulatory subunit 4-like protein; Provisional
 118-337 5.69e-39

26 proteosome regulatory subunit 4-like protein; Provisional


Pssm-ID: 185575 [Multi-domain]  Cd Length: 438  Bit Score: 145.68  E-value: 5.69e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18699726  118 VMEKPNIRWNDVAGLEGAKEALKEAVILPIKFPHLF--TGKRTPwRGILLFGPPGTGKSYLAKAVATEANnSTFFSVSSS 195
Cdd:PTZ00361 174 VDKAPLESYADIGGLEQQIQEIKEAVELPLTHPELYddIGIKPP-KGVILYGPPGTGKTLLAKAVANETS-ATFLRVVGS 251

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18699726  196 DLMSKWLGESEKLVKNLFELARQHKPSIIFIDEVDSLCGSRNENESEAARRIKT---EFLVQMQGVGNNNDgTLVLGATN 272
Cdd:PTZ00361 252 ELIQKYLGDGPKLVRELFRVAEENAPSIVFIDEIDAIGTKRYDATSGGEKEIQRtmlELLNQLDGFDSRGD-VKVIMATN 330

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 18699726  273 IPWVLDSAIRR--RFEKRIYIPLPEEAARAQMFRLHlgSTPHNLT-DANIHELARKTEGYSGADISII 337
Cdd:PTZ00361 331 RIESLDPALIRpgRIDRKIEFPNPDEKTKRRIFEIH--TSKMTLAeDVDLEEFIMAKDELSGADIKAI 396
hflB PRK10733
ATP-dependent zinc metalloprotease FtsH;
128-357 8.07e-39

ATP-dependent zinc metalloprotease FtsH;


Pssm-ID: 182683 [Multi-domain]  Cd Length: 644  Bit Score: 148.26  E-value: 8.07e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18699726  128 DVAGLEGAKEALKEAVIL---PIKFPHLftGKRTPwRGILLFGPPGTGKSYLAKAVATEANnSTFFSVSSSDLMSKWLGE 204
Cdd:PRK10733 153 DVAGCDEAKEEVAELVEYlrePSRFQKL--GGKIP-KGVLMVGPPGTGKTLLAKAIAGEAK-VPFFTISGSDFVEMFVGV 228

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18699726  205 SEKLVKNLFELARQHKPSIIFIDEVDS--------LCGSRNENEseaarRIKTEFLVQMQGVgNNNDGTLVLGATNIPWV 276
Cdd:PRK10733 229 GASRVRDMFEQAKKAAPCIIFIDEIDAvgrqrgagLGGGHDERE-----QTLNQMLVEMDGF-EGNEGIIVIAATNRPDV 302

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18699726  277 LDSAIRR--RFEKRIYIPLPEEAARAQMFRLHLGSTPHNlTDANIHELARKTEGYSGADISIIVRDSLMQPVR---KVQS 351
Cdd:PRK10733 303 LDPALLRpgRFDRQVVVGLPDVRGREQILKVHMRRVPLA-PDIDAAIIARGTPGFSGADLANLVNEAALFAARgnkRVVS 381


                 ....*.
gi 18699726  352 ATHFKK 357
Cdd:PRK10733 382 MVEFEK 387
RecA-like_Yta7-like cd19517
ATPase domain of Saccharomyces cerevisiae Yta7 and similar ATPase domains; Saccharomyces ...
 128-290 5.94e-38

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: 135.71  E-value: 5.94e-38
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18699726 128 DVAGLEGAKEALKEAVILPIKFPHLFTG-KRTPWRGILLFGPPGTGKSYLAKAVATEA----NNSTFFSVSSSDLMSKWL 202
Cdd:cd19517   1 DIGGLSHYINQLKEMVFFPLLYPEVFAKfKITPPRGVLFHGPPGTGKTLMARALAAECskggQKVSFFMRKGADCLSKWV 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18699726 203 GESEKLVKNLFELARQHKPSIIFIDEVDSLCGSRNENESEAARRIKTEFLVQMQGVGNNNDgTLVLGATNIPWVLDSAIR 282
Cdd:cd19517  81 GEAERQLRLLFEEAYRMQPSIIFFDEIDGLAPVRSSKQEQIHASIVSTLLALMDGLDNRGQ-VVVIGATNRPDALDPALR 159

                       170
                ....*....|
gi 18699726 283 R--RFEKRIY 290
Cdd:cd19517 160 RpgRFDREFY 169
RecA-like_NVL_r2-like cd19530
second of two ATPase domains of NVL (nuclear VCP-like protein) and similar ATPase domains; NVL ...
 132-291 6.32e-38

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: 135.31  E-value: 6.32e-38
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18699726 132 LEGAKEALKEAVILPIKFPHLFT--GKRTPwRGILLFGPPGTGKSYLAKAVATEANnSTFFSVSSSDLMSKWLGESEKLV 209
Cdd:cd19530   1 LDHVREELTMSILRPIKRPDIYKalGIDLP-TGVLLYGPPGCGKTLLAKAVANESG-ANFISVKGPELLNKYVGESERAV 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18699726 210 KNLFELARQHKPSIIFIDEVDSLCGSRNENESEAARRIKTEFLVQMQGvGNNNDGTLVLGATNIPWVLDSAIRR--RFEK 287
Cdd:cd19530  79 RQVFQRARASAPCVIFFDEVDALVPKRGDGGSWASERVVNQLLTEMDG-LEERSNVFVIAATNRPDIIDPAMLRpgRLDK 157


                ....
gi 18699726 288 RIYI 291
Cdd:cd19530 158 TLYV 161
RecA-like_PEX1_r2 cd19526
second of two ATPase domains of Peroxisomal biogenesis factor 1 (PEX1); PEX1(also known as ...
 135-290 1.42e-37

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: 134.09  E-value: 1.42e-37
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18699726 135 AKEALKEAVILPIKFPHLFTGKRTPWR-GILLFGPPGTGKSYLAKAVATEANNStFFSVSSSDLMSKWLGESEKLVKNLF 213
Cdd:cd19526   1 VKKALEETIEWPSKYPKIFASSPLRLRsGILLYGPPGCGKTLLASAIASECGLN-FISVKGPELLNKYIGASEQNVRDLF 79

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 18699726 214 ELARQHKPSIIFIDEVDSLCGSRNENESEAARRIKTEFLVQMQGVgNNNDGTLVLGATNIPWVLDSAIRR--RFEKRIY 290
Cdd:cd19526  80 SRAQSAKPCILFFDEFDSIAPKRGHDSTGVTDRVVNQLLTQLDGV-EGLDGVYVLAATSRPDLIDPALLRpgRLDKLVY 157
RecA-like_PEX6_r2 cd19527
second of two ATPase domains of Peroxisomal biogenesis factor 6 (PEX6); PEX6(also known as ...
 136-291 2.32e-37

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


Pssm-ID: 410935 [Multi-domain]  Cd Length: 160  Bit Score: 133.79  E-value: 2.32e-37
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18699726 136 KEALKEAVILPIKFPHLFTGKRTPWRGILLFGPPGTGKSYLAKAVATEAnNSTFFSVSSSDLMSKWLGESEKLVKNLFEL 215
Cdd:cd19527   2 KKEILDTIQLPLEHPELFSSGLRKRSGILLYGPPGTGKTLLAKAIATEC-SLNFLSVKGPELINMYIGESEANVREVFQK 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18699726 216 ARQHKPSIIFIDEVDSLCGSR-NENESEAAR-RIKTEFLVQMQGVGNNNDGTLVLGATNIPWVLDSAIRR--RFEKRIYI 291
Cdd:cd19527  81 ARDAKPCVIFFDELDSLAPSRgNSGDSGGVMdRVVSQLLAELDGMSSSGQDVFVIGATNRPDLLDPALLRpgRFDKLLYL 160
RecA-like_NVL_r1-like cd19518
first of two ATPase domains of NVL (nuclear VCP-like protein) and similar ATPase domains; NVL ...
 128-289 6.70e-37

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: 132.91  E-value: 6.70e-37
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18699726 128 DVAGLEGAKEALKEAVILPIKFPHLF--TGKRTPwRGILLFGPPGTGKSYLAKAVATEANnSTFFSVSSSDLMSKWLGES 205
Cdd:cd19518   1 DIGGMDSTLKELCELLIHPILPPEYFqhLGVEPP-RGVLLHGPPGCGKTMLANAIAGELK-VPFLKISATEIVSGVSGES 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18699726 206 EKLVKNLFELARQHKPSIIFIDEVDSLCGSRNENESEAARRIKTEFLVQMQGVGNNND---GTLVLGATNIPWVLDSAIR 282
Cdd:cd19518  79 EEKIRELFDQAISNAPCIVFIDEIDAITPKRESAQREMERRIVSQLLTCMDELNNEKTaggPVLVIGATNRPDSLDPALR 158


                ....*....
gi 18699726 283 R--RFEKRI 289
Cdd:cd19518 159 RagRFDREI 167
ftsH CHL00176
cell division protein; Validated
 124-348 2.88e-36

cell division protein; Validated


Pssm-ID: 214386 [Multi-domain]  Cd Length: 638  Bit Score: 140.96  E-value: 2.88e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18699726  124 IRWNDVAGLEGAKEALKEAVILpIKFPHLFT--GKRTPwRGILLFGPPGTGKSYLAKAVATEAnNSTFFSVSSSDLMSKW 201
Cdd:CHL00176 180 ITFRDIAGIEEAKEEFEEVVSF-LKKPERFTavGAKIP-KGVLLVGPPGTGKTLLAKAIAGEA-EVPFFSISGSEFVEMF 256

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18699726  202 LGESEKLVKNLFELARQHKPSIIFIDEVDSL-------CGSRNEnESEaarRIKTEFLVQMQGVGNNNdGTLVLGATNIP 274
Cdd:CHL00176 257 VGVGAARVRDLFKKAKENSPCIVFIDEIDAVgrqrgagIGGGND-ERE---QTLNQLLTEMDGFKGNK-GVIVIAATNRV 331

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 18699726  275 WVLDSAIRR--RFEKRIYIPLPEEAARAQMFRLHLGSTPHNLtDANIHELARKTEGYSGADISIIVRDSLMQPVRK 348
Cdd:CHL00176 332 DILDAALLRpgRFDRQITVSLPDREGRLDILKVHARNKKLSP-DVSLELIARRTPGFSGADLANLLNEAAILTARR 406
Vps4_C pfam09336
Vps4 C terminal oligomerization domain; This domain is found at the C terminal of ATPase ...
 374-434 1.55e-34

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


Pssm-ID: 462762 [Multi-domain]  Cd Length: 61  Bit Score: 122.61  E-value: 1.55e-34
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 18699726   374 LTPCSPGDPGAIEMTWMDVPGDKLLEPVVCMSDMLRSLATTRPTVNADDLLKVKKFSEDFG 434
Cdd:pfam09336   1 LTPCSPGDPGAIEMTWMDIPSDKLLEPPVTMKDFLKALKSSRPTVSKEDLEKYEEFTKEFG 61
AAA cd00009
The AAA+ (ATPases Associated with a wide variety of cellular Activities) superfamily ...
 130-293 5.74e-29

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: 110.70  E-value: 5.74e-29
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18699726 130 AGLEGAKEALKEAVilpikfphlftgKRTPWRGILLFGPPGTGKSYLAKAVATEA--NNSTFFSVSSSDLMSKWLGESEK 207
Cdd:cd00009   1 VGQEEAIEALREAL------------ELPPPKNLLLYGPPGTGKTTLARAIANELfrPGAPFLYLNASDLLEGLVVAELF 68

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18699726 208 ---LVKNLFELARQHKPSIIFIDEVDSLcgsrneneSEAARRIKTEFLVQMQGVGNNNDGTLVLGATNIPWV--LDSAIR 282
Cdd:cd00009  69 ghfLVRLLFELAEKAKPGVLFIDEIDSL--------SRGAQNALLRVLETLNDLRIDRENVRVIGATNRPLLgdLDRALY 140

                       170
                ....*....|.
gi 18699726 283 RRFEKRIYIPL 293
Cdd:cd00009 141 DRLDIRIVIPL 151
MIT pfam04212
MIT (microtubule interacting and transport) domain; The MIT domain forms an asymmetric ...
 6-72 6.98e-27

MIT (microtubule interacting and transport) domain; The MIT domain forms an asymmetric three-helix bundle and binds ESCRT-III (endosomal sorting complexes required for transport) substrates.


Pssm-ID: 461228  Cd Length: 66  Bit Score: 102.23  E-value: 6.98e-27
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 18699726     6 LQKAIDLVTKATEEDKAKNYEEALRLYQHAVEYFLHAIKyEAHSDKAKESIRAKCMQYLDRAEKLKD 72
Cdd:pfam04212   1 LSKALELVKKAVEEDNAGNYEEALELYKEALDYLLLALK-ETKNEERRELLRAKIAEYLERAEELKE 66
MIT smart00745
Microtubule Interacting and Trafficking molecule domain;
2-79 1.06e-24

Microtubule Interacting and Trafficking molecule domain;


Pssm-ID: 197854  Cd Length: 77  Bit Score: 96.61  E-value: 1.06e-24
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 18699726      2 TTSTLQKAIDLVTKATEEDKAKNYEEALRLYQHAVEYFLHAIKYEaHSDKAKESIRAKCMQYLDRAEKLKDYLRNKEK 79
Cdd:smart00745   1 TRDYLSKAKELISKALKADEAGNYEEALELYKKAIEYLLEGIKVE-SDSKRREALKAKAAEYLDRAEEIKKSLLERLA 77
MIT cd02656
MIT: domain contained within Microtubule Interacting and Trafficking molecules. The MIT domain ...
 6-79 1.49e-23

MIT: domain contained within Microtubule Interacting and Trafficking molecules. The MIT domain is found in sorting nexins, the nuclear thiol protease PalBH, the AAA protein spastin and archaebacterial proteins with similar domain architecture, vacuolar sorting proteins and others. The molecular function of the MIT domain is unclear.


Pssm-ID: 239121  Cd Length: 75  Bit Score: 93.53  E-value: 1.49e-23
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 18699726   6 LQKAIDLVTKATEEDKAKNYEEALRLYQHAVEYFLHAIKYEAhSDKAKESIRAKCMQYLDRAEKLKDYLRNKEK 79
Cdd:cd02656   3 LQQAKELIKQAVKEDEDGNYEEALELYKEALDYLLQALKAEK-EPKLRKLLRKKVKEYLDRAEFLKELLKKQKQ 75
AAA smart00382
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ...
 159-295 3.27e-21

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


Pssm-ID: 214640 [Multi-domain]  Cd Length: 148  Bit Score: 89.35  E-value: 3.27e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18699726    159 PWRGILLFGPPGTGKSYLAKAVATEAN--NSTFFSVSSSDLMS--------------KWLGESEKLVKNLFELARQHKPS 222
Cdd:smart00382   1 PGEVILIVGPPGSGKTTLARALARELGppGGGVIYIDGEDILEevldqllliivggkKASGSGELRLRLALALARKLKPD 80

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 18699726    223 IIFIDEVDSLCGSRNENESEAARRIKTEFLVQMQGvgnnndGTLVLGATNIPWVLDSA-IRRRFEKRIYIPLPE 295
Cdd:smart00382  81 VLILDEITSLLDAEQEALLLLLEELRLLLLLKSEK------NLTVILTTNDEKDLGPAlLRRRFDRRIVLLLIL 148
RecA-like_NSF-SEC18_r1-like cd19504
first of two ATPase domains of NSF and SEC18, and similar ATPase domains; ...
 161-291 1.15e-18

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: 83.31  E-value: 1.15e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18699726 161 RGILLFGPPGTGKSYLAKAVATEANNSTFFSVSSSDLMSKWLGESEKLVKNLFELARQHKPS--------IIFIDEVDSL 232
Cdd:cd19504  36 KGILLYGPPGTGKTLMARQIGKMLNAREPKIVNGPEILNKYVGESEANIRKLFADAEEEQRRlgansglhIIIFDEIDAI 115

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 18699726 233 CGSRNE--NESEAARRIKTEFLVQMQGVGNNNDgTLVLGATNIPWVLDSAIRR--RFEKRIYI 291
Cdd:cd19504 116 CKQRGSmaGSTGVHDTVVNQLLSKIDGVEQLNN-ILVIGMTNRKDLIDEALLRpgRLEVQMEI 177
MIT_2 cd02684
MIT: domain contained within Microtubule Interacting and Trafficking molecules. This ...
 5-79 1.69e-16

MIT: domain contained within Microtubule Interacting and Trafficking molecules. This sub-family of MIT domains is found in proteins with an n-terminal serine/threonine kinase domain. The molecular function of the MIT domain is unclear.


Pssm-ID: 239147  Cd Length: 75  Bit Score: 73.70  E-value: 1.69e-16
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 18699726   5 TLQKAIDLVTKATEEDKAKNYEEALRLYQHAVEYFLHAIKYEAHSDKaKESIRAKCMQYLDRAEKLKDYLRNKEK 79
Cdd:cd02684   2 SLEKAIALVVQAVKKDQRGDAAAALSLYCSALQYFVPALHYETDAQR-KEALRQKVLQYVSRAEELKALIASDTQ 75
ycf46 CHL00195
Ycf46; Provisional
 105-337 2.00e-16

Ycf46; Provisional


Pssm-ID: 177094 [Multi-domain]  Cd Length: 489  Bit Score: 81.22  E-value: 2.00e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18699726  105 EKKKLQEQlmgAVVME--KPNIRWNDVAGLEGAKEALKeavilpiKFPHLFT------GKRTPwRGILLFGPPGTGKSYL 176
Cdd:CHL00195 207 EKKQIISQ---TEILEfySVNEKISDIGGLDNLKDWLK-------KRSTSFSkqasnyGLPTP-RGLLLVGIQGTGKSLT 275

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18699726  177 AKAVATEAnNSTFFSVSSSDLMSKWLGESEKLVKNLFELARQHKPSIIFIDEVD-SLCGSRNENESEAARRIKTEFLVQM 255
Cdd:CHL00195 276 AKAIANDW-QLPLLRLDVGKLFGGIVGESESRMRQMIRIAEALSPCILWIDEIDkAFSNSESKGDSGTTNRVLATFITWL 354

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18699726  256 QgvGNNNDGTLVLGATNIPWVLDSAIRR-RFEKRIYIPLPEEAARAQMFRLHLG-STPHNLTDANIHELARKTEGYSGAD 333
Cdd:CHL00195 355 S--EKKSPVFVVATANNIDLLPLEILRKgRFDEIFFLDLPSLEEREKIFKIHLQkFRPKSWKKYDIKKLSKLSNKFSGAE 432


                 ....*.
gi 18699726  334 I--SII 337
Cdd:CHL00195 433 IeqSII 438
RecA-like_Ycf46-like cd19507
ATPase domain of Ycf46 and similar ATPase domains; Ycf46 may play a role in the regulation of ...
 128-256 1.13e-15

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: 74.33  E-value: 1.13e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18699726 128 DVAGLEGAKEALKE---AVILPIKFPHLftgkrTPWRGILLFGPPGTGKSYLAKAVATEANnSTFFSVSSSDLMSKWLGE 204
Cdd:cd19507   1 DVGGLDNLKDWLKKrkaAFSKQASAYGL-----PTPKGLLLVGIQGTGKSLTAKAIAGVWQ-LPLLRLDMGRLFGGLVGE 74

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|...
gi 18699726 205 SEKLVKNLFELARQHKPSIIFIDEVDS-LCGSRNENESEAARRIKTEFLVQMQ 256
Cdd:cd19507  75 SESRLRQMIQTAEAIAPCVLWIDEIEKgFSNADSKGDSGTSSRVLGTFLTWLQ 127
RecA-like_Pch2-like cd19508
ATPase domain of Pachytene checkpoint 2 (Pch2) and similar ATPase domains; Pch2 (known as ...
 161-291 6.15e-14

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: 70.17  E-value: 6.15e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18699726 161 RGILLFGPPGTGKSYLAKAVATEAN--------NSTFFSVSSSDLMSKWLGESEKLVKNLF----ELARQHKPSI-IFID 227
Cdd:cd19508  53 RLVLLHGPPGTGKTSLCKALAQKLSirlssryrYGQLIEINSHSLFSKWFSESGKLVTKMFqkiqELIDDKDALVfVLID 132

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 18699726 228 EVDSLCGSRNE----NESEAARRIKTEFLVQMQGVgNNNDGTLVLGATNIPWVLDSAIRRRFEKRIYI 291
Cdd:cd19508 133 EVESLAAARSAsssgTEPSDAIRVVNAVLTQIDRI-KRYHNNVILLTSNLLEKIDVAFVDRADIKQYI 199
RecA-like_Ycf2 cd19505
ATPase domain of plant YCF2; Ycf2 is a chloroplast ATPase which has an essential function; ...
 159-281 2.93e-11

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: 61.62  E-value: 2.93e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18699726 159 PWRGILLFGPPGTGKSYLAKAVATEA--------------NNSTFFSVSSSDLMSKWlGESEKLVKNLFELARQHKPSII 224
Cdd:cd19505  11 PSKGILLIGSIETGRSYLIKSLAANSyvplirislnkllyNKPDFGNDDWIDGMLIL-KESLHRLNLQFELAKAMSPCII 89

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 18699726 225 FIDEVDSLCGSRNENESEAARRIKTEFLVQMQGVGNNNDGT---LVLGATNIPWVLDSAI 281
Cdd:cd19505  90 WIPNIHELNVNRSTQNLEEDPKLLLGLLLNYLSRDFEKSSTrniLVIASTHIPQKVDPAL 149
RecA-like_ATAD3-like cd19512
ATPase domains of ATPase AAA-domain protein 3A (ATAD3A), -3B, and -3C, and similar ATPase ...
 157-289 1.90e-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: 59.08  E-value: 1.90e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18699726 157 RTPWRGILLFGPPGTGKSYLAKAVATEANNStfFSVSSSDLMSKWLGESEKLVKNLFELARQHKPS-IIFIDEVDSLCGS 235
Cdd:cd19512  19 KGLYRNILFYGPPGTGKTLFAKKLALHSGMD--YAIMTGGDVAPMGREGVTAIHKVFDWANTSRRGlLLFVDEADAFLRK 96

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*
gi 18699726 236 RNENE-SEAARRIKTEFLVQMQgvGNNNDGTLVLgATNIPWVLDSAIRRRFEKRI 289
Cdd:cd19512  97 RSTEKiSEDLRAALNAFLYRTG--EQSNKFMLVL-ASNQPEQFDWAINDRIDEMV 148
RecA-like_BCS1 cd19510
Mitochondrial chaperone BCS1; Mitochondrial chaperone BCS1 is necessary for the assembly of ...
 139-291 7.85e-09

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: 54.28  E-value: 7.85e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18699726 139 LKEAVILPIKFPHLFTGKRTPW-RGILLFGPPGTGKSYLAKAVATEANNSTF-FSVSSSDLmskwlgeSEKLVKNLfeLA 216
Cdd:cd19510   1 IIDDLKDFIKNEDWYNDRGIPYrRGYLLYGPPGTGKSSFIAALAGELDYDICdLNLSEVVL-------TDDRLNHL--LN 71

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18699726 217 RQHKPSIIFIDEVDSLCGSRNENESEaarRIKTEFL--VQMQGVGNNNDG------TLVLGATNIPWVLDSAIRR--RFE 286
Cdd:cd19510  72 TAPKQSIILLEDIDAAFESREHNKKN---PSAYGGLsrVTFSGLLNALDGvasseeRIVFMTTNHIERLDPALIRpgRVD 148


                ....*
gi 18699726 287 KRIYI 291
Cdd:cd19510 149 MKIYM 153
AAA_lid_3 pfam17862
AAA+ lid domain; This entry represents the alpha helical AAA+ lid domain that is found to the ...
 316-358 1.15e-08

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


Pssm-ID: 465537 [Multi-domain]  Cd Length: 45  Bit Score: 50.61  E-value: 1.15e-08
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 18699726   316 DANIHELARKTEGYSGADISIIVRDSLMQPVRKVQSATHFKKV 358
Cdd:pfam17862   1 DVDLEELAERTEGFSGADLEALCREAALAALRRGLEAVTQEDL 43
RecA-like_IQCA1 cd19506
ATPase domain of IQ and AAA domain-containing protein 1 (IQCA1); IQCA1 (also known as dynein ...
 161-291 2.48e-08

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


Pssm-ID: 410914 [Multi-domain]  Cd Length: 160  Bit Score: 52.92  E-value: 2.48e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18699726 161 RGILLFGPPGTGKSYLAKAVATEAnNSTFFSVSSSDLMSKWLGES--EKLVKNLFELARQHKPSIIFIDEVDSLCGSR-- 236
Cdd:cd19506  27 KSLLLAGPSGVGKKMLVHAICTET-GANLFNLSPSNIAGKYPGKNglQMMLHLVLKVARQLQPSVIWIGDAEKTFYKKvp 105

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 18699726 237 NENESEAARRIKTEfLVQMQGVGNNNDGTLVLGATNIPWVLD-SAIRRRFEKRIYI 291
Cdd:cd19506 106 KTEKQLDPKRLKKD-LPKILKSLKPEDRVLIVGTTSRPFEADlKSFCKVYNKIILI 160
MIT_1 cd02683
MIT: domain contained within Microtubule Interacting and Trafficking molecules. This ...
 8-79 3.33e-08

MIT: domain contained within Microtubule Interacting and Trafficking molecules. This sub-family of MIT domains is found in proteins with unknown function, co-occuring with an as yet undescribed domain. The molecular function of the MIT domain is unclear.


Pssm-ID: 239146  Cd Length: 77  Bit Score: 50.50  E-value: 3.33e-08
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 18699726   8 KAIDLVTKATEEDKAKNYEEALRLYQHAVEYFLHAIKYEAHSDKaKESIRAKCMQYLDRAEKLKDYLrNKEK 79
Cdd:cd02683   5 AAKEVLKRAVELDQEGRFQEALVCYQEGIDLLMQVLKGTKDEAK-KKNLRQKISEYMDRAEAIKKRL-DQEK 74
T7SS_EccA TIGR03922
type VII secretion AAA-ATPase EccA; This model represents the AAA family ATPase, EccA, of the ...
 161-292 1.04e-06

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


Pssm-ID: 188437 [Multi-domain]  Cd Length: 557  Bit Score: 51.00  E-value: 1.04e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18699726   161 RGILLFGPPGTGKSYLAKAVA------TEANNSTFFSVSSSDLMSKWLGESEKLVKNLFELARQhkpSIIFIDEVDSLCG 234
Cdd:TIGR03922 313 NHMLFAGPPGTGKTTIARVVAkiycglGVLRKPLVREVSRADLIGQYIGESEAKTNEIIDSALG---GVLFLDEAYTLVE 389

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 18699726   235 SRNENESEAARRIKTEFLVQMQgvgNNNDGTLVLGA---TNIPWVLDS--AIRRRFEKRIYIP 292
Cdd:TIGR03922 390 TGYGQKDPFGLEAIDTLLARME---NDRDRLVVIGAgyrKDLDKFLEVneGLRSRFTRVIEFP 449
MIT_calpain7_2 cd02680
MIT: domain contained within Microtubule Interacting and Trafficking molecules. This ...
 6-74 3.80e-06

MIT: domain contained within Microtubule Interacting and Trafficking molecules. This sub-family of MIT domains is found in the nuclear thiol protease PalBH. The molecular function of the MIT domain is unclear.


Pssm-ID: 239143  Cd Length: 75  Bit Score: 44.60  E-value: 3.80e-06
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 18699726   6 LQKAIDLVTKATEEDKAKNYEEALRLYQHAVEYFLHAiKYEAHSDKAKESIRAKCMQYLDRAEKLKDYL 74
Cdd:cd02680   3 LERAHFLVTQAFDEDEKGNAEEAIELYTEAVELCINT-SNETMDQALQTKLKQLARQALDRAEALKESM 70
AAA_5 pfam07728
AAA domain (dynein-related subfamily); This Pfam entry includes some of the AAA proteins not ...
 162-285 4.15e-06

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: 46.13  E-value: 4.15e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18699726   162 GILLFGPPGTGKSYLAKAVATEANNSTFFSV------SSSDLMSKWLGESEKLVKNLFELARQHKPS-IIFIDEVdslcg 234
Cdd:pfam07728   1 GVLLVGPPGTGKTELAERLAAALSNRPVFYVqltrdtTEEDLFGRRNIDPGGASWVDGPLVRAAREGeIAVLDEI----- 75

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 18699726   235 srNENESEAA---------RRIKTEFLVQMQGVgnNNDGTLVLGATNIP----WVLDSAIRRRF 285
Cdd:pfam07728  76 --NRANPDVLnsllslldeRRLLLPDGGELVKA--APDGFRLIATMNPLdrglNELSPALRSRF 135
PRK13342 PRK13342
recombination factor protein RarA; Reviewed
 163-229 6.19e-06

recombination factor protein RarA; Reviewed


Pssm-ID: 237355 [Multi-domain]  Cd Length: 413  Bit Score: 48.16  E-value: 6.19e-06
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 18699726  163 ILLFGPPGTGKSYLAKAVATEAN------NSTFFSVsssdlmskwlgeseKLVKNLFELARQH----KPSIIFIDEV 229
Cdd:PRK13342  39 MILWGPPGTGKTTLARIIAGATDapfealSAVTSGV--------------KDLREVIEEARQRrsagRRTILFIDEI 101
TIP49 pfam06068
TIP49 P-loop domain; This family consists of the C-terminal region of several eukaryotic and ...
 131-212 8.02e-06

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


Pssm-ID: 399217 [Multi-domain]  Cd Length: 347  Bit Score: 47.69  E-value: 8.02e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18699726   131 GLEGAKEALKEA-VILpikfpHLFTGKRTPWRGILLFGPPGTGKSYLAKAVATEANNST-FFSVSSSDLMSKWLGESEKL 208
Cdd:pfam06068  25 GLVGQEKAREAAgVIV-----EMIKEGKIAGRAVLIAGPPGTGKTALAIAISKELGEDTpFTSISGSEVYSLEMKKTEAL 99


                  ....
gi 18699726   209 VKNL 212
Cdd:pfam06068 100 TQAF 103
IS21_help_AAA NF038214
IS21-like element helper ATPase IstB; This protein family model resembles PF01695, but was ...
 163-229 1.06e-05

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


Pssm-ID: 439516  Cd Length: 232  Bit Score: 46.31  E-value: 1.06e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 18699726  163 ILLFGPPGTGKSYLAKAV---ATEANNSTFFsVSSSDLMSKWlgESEKLVKNLFELARQH-KPSIIFIDEV 229
Cdd:NF038214  93 VLLLGPPGTGKTHLAIALgyaACRQGYRVRF-TTAADLVEQL--AQARADGRLGRLLRRLaRYDLLIIDEL 160
AAA_2 pfam07724
AAA domain (Cdc48 subfamily); This Pfam entry includes some of the AAA proteins not detected ...
 163-230 1.15e-05

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


Pssm-ID: 400187 [Multi-domain]  Cd Length: 168  Bit Score: 45.26  E-value: 1.15e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18699726   163 ILLFGPPGTGKSYLAKAVATEANNS--TFFSVSSSDLM-----SKWLGESEKLVK-----NLFELARQHKPSIIFIDEVD 230
Cdd:pfam07724   6 FLFLGPTGVGKTELAKALAELLFGDerALIRIDMSEYMeehsvSRLIGAPPGYVGyeeggQLTEAVRRKPYSIVLIDEIE 85
MIT_SNX15 cd02677
MIT: domain contained within Microtubule Interacting and Trafficking molecules. This MIT ...
 6-70 1.19e-05

MIT: domain contained within Microtubule Interacting and Trafficking molecules. This MIT domain sub-family is found in sorting nexin 15 and related proteins. The molecular function of the MIT domain is unclear.


Pssm-ID: 239140  Cd Length: 75  Bit Score: 43.10  E-value: 1.19e-05
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 18699726   6 LQKAIDLVTKATEEDKAKNYEEALRLYQHAVEYFLHAIKYEAHSDKaKESIRAKCMQYLDRAEKL 70
Cdd:cd02677   3 LEQAAELIRLALEKEEEGDYEAAFEFYRAGVDLLLKGVQGDSSPER-REAVKRKIAEYLKRAEEI 66
RarA COG2256
Replication-associated recombination protein RarA (DNA-dependent ATPase) [Replication, ...
 163-229 2.05e-05

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


Pssm-ID: 441857 [Multi-domain]  Cd Length: 439  Bit Score: 46.59  E-value: 2.05e-05
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 18699726 163 ILLFGPPGTGKSYLAKAVATEAnNSTFFSVS--SSdlmskwlGESEklVKNLFELARQH----KPSIIFIDEV 229
Cdd:COG2256  52 MILWGPPGTGKTTLARLIANAT-DAEFVALSavTS-------GVKD--IREVIEEARERraygRRTILFVDEI 114
COG1373 COG1373
Predicted ATPase, AAA+ superfamily [General function prediction only];
163-229 3.93e-05

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


Pssm-ID: 440984 [Multi-domain]  Cd Length: 405  Bit Score: 45.71  E-value: 3.93e-05
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 18699726 163 ILLFGPPGTGKSYLAKAVATEANNSTFFSVSSSDLMSKWLGESEKLVKNLFELARQHKPsiIFIDEV 229
Cdd:COG1373  23 VVITGPRQVGKTTLLKQLAKELENILYINLDDPRLRALAEEDPDDLLEALKELYPGKTY--LFLDEI 87
TIP49 COG1224
DNA helicase TIP49, TBP-interacting protein [Transcription];
161-208 4.43e-05

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


Pssm-ID: 440837 [Multi-domain]  Cd Length: 452  Bit Score: 45.73  E-value: 4.43e-05
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*....
gi 18699726 161 RGILLFGPPGTGKSYLAKAVATEANNST-FFSVSSSDLMSKWLGESEKL 208
Cdd:COG1224  65 KGILIVGPPGTGKTALAVAIARELGEDTpFVAISGSEIYSAELKKTEFL 113
McrB COG1401
5-methylcytosine-specific restriction endonuclease McrBC, GTP-binding regulatory subunit McrB ...
 163-228 7.18e-05

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


Pssm-ID: 441011 [Multi-domain]  Cd Length: 477  Bit Score: 45.15  E-value: 7.18e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18699726 163 ILLFGPPGTGKSYLAKAVA---TEANNSTFFSV------SSSDLMskwLGESEKLVKNLFEL-------------ARQHK 220
Cdd:COG1401 224 VILAGPPGTGKTYLARRLAealGGEDNGRIEFVqfhpswSYEDFL---LGYRPSLDEGKYEPtpgiflrfclkaeKNPDK 300


                ....*...
gi 18699726 221 PSIIFIDE 228
Cdd:COG1401 301 PYVLIIDE 308
DnaC COG1484
DNA replication protein DnaC [Replication, recombination and repair];
161-184 1.28e-04

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


Pssm-ID: 441093 [Multi-domain]  Cd Length: 242  Bit Score: 43.23  E-value: 1.28e-04
                        10        20
                ....*....|....*....|....
gi 18699726 161 RGILLFGPPGTGKSYLAKAVATEA 184
Cdd:COG1484 100 ENLILLGPPGTGKTHLAIALGHEA 123
PRK04195 PRK04195
replication factor C large subunit; Provisional
 127-234 6.86e-04

replication factor C large subunit; Provisional


Pssm-ID: 235250 [Multi-domain]  Cd Length: 482  Bit Score: 41.83  E-value: 6.86e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18699726  127 NDVAGLEGAKEALKEAVIlpiKFPHlftgkRTPWRGILLFGPPGTGKSYLAKAVAT-------EANNStffSVSSSDLMS 199
Cdd:PRK04195  14 SDVVGNEKAKEQLREWIE---SWLK-----GKPKKALLLYGPPGVGKTSLAHALANdygweviELNAS---DQRTADVIE 82

                         90       100       110
                 ....*....|....*....|....*....|....*
gi 18699726  200 KWLGESEKlVKNLFELARQhkpsIIFIDEVDSLCG 234
Cdd:PRK04195  83 RVAGEAAT-SGSLFGARRK----LILLDEVDGIHG 112
ycf2 CHL00206
Ycf2; Provisional
 158-377 6.98e-04

Ycf2; Provisional


Pssm-ID: 214396 [Multi-domain]  Cd Length: 2281  Bit Score: 42.21  E-value: 6.98e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18699726   158 TPWRGILLFGPPGTGKSYLAKAVATeanNSTFFSVSSSdlmskwlgeSEKLVKNlfelarqhKPSIIFIDEVDSLCGSRN 237
Cdd:CHL00206 1628 SPSRGILVIGSIGTGRSYLVKYLAT---NSYVPFITVF---------LNKFLDN--------KPKGFLIDDIDIDDSDDI 1687

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18699726   238 ENESEAARRIKTEFLVQMQGVGNNndgtlvlgatnipwvLDSAIRrrfekRIYIPLPEEAARAQmfrlhlgsTPHNLTDA 317
Cdd:CHL00206 1688 DDSDDIDRDLDTELLTMMNALTMD---------------MMPKID-----RFYITLQFELAKAM--------SPCIIWIP 1739

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 18699726   318 NIHELARKTEGY--SGADISIIVRDSLMQPVRK--VQSATHFkkvcgPSRTNPSVMIDDLLTPC 377
Cdd:CHL00206 1740 NIHDLNVNESNYlsLGLLVNSLSRDCERCSTRNilVIASTHI-----PQKVDPALIAPNKLNTC 1798
AAA_18 pfam13238
AAA domain;
163-248 9.41e-04

AAA domain;


Pssm-ID: 433052 [Multi-domain]  Cd Length: 128  Bit Score: 38.95  E-value: 9.41e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18699726   163 ILLFGPPGTGKSYLAKAVATEANNSTFFS--VSSSDLMSKWLGES-----------EKLVKNLFELARQHKPSIIFIDEV 229
Cdd:pfam13238   1 ILITGTPGVGKTTLAKELSKRLGFGDNVRdlALENGLVLGDDPETreskrldedklDRLLDLLEENAALEEGGNLIIDGH 80

                          90
                  ....*....|....*....
gi 18699726   230 dslcgsRNENESEAARRIK 248
Cdd:pfam13238  81 ------LAELEPERAKDLV 93
IstB_IS21 pfam01695
IstB-like ATP binding protein; This protein contains an ATP/GTP binding P-loop motif. It is ...
 163-238 1.25e-03

IstB-like ATP binding protein; This protein contains an ATP/GTP binding P-loop motif. It is found associated with IS21 family insertion sequences. The function of this protein is unknown, but it may perform a transposase function.


Pssm-ID: 426385 [Multi-domain]  Cd Length: 238  Bit Score: 40.12  E-value: 1.25e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 18699726   163 ILLFGPPGTGKSYLAKAVATEA---NNSTFFsVSSSDLMSKwLGESEKLVKNLFELARQHKPSIIFIDEVDSLCGSRNE 238
Cdd:pfam01695  95 VVLLGPPGVGKTHLAIALGVEAcraGYSVRF-TSAADLVNQ-LKRAHGDGKLTRKLQQLLKPDVLILDEWGYLPLDQAE 171
RecA-like_superfamily cd01120
RecA-like_NTPases; RecA-like NTPases. This superfamily includes the NTP binding domain of F1 ...
 163-268 1.29e-03

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


Pssm-ID: 410865 [Multi-domain]  Cd Length: 119  Bit Score: 38.64  E-value: 1.29e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18699726 163 ILLFGPPGTGKSYLAKAVATEANNSTFFSVSSSDLmskwlgesEKLVKNLFELARQHKPSIIFIDEVDSLCGSRNENESE 242
Cdd:cd01120   1 ILITGPPGSGKTTLLLQFAEQALLSDEPVIFISFL--------DTILEAIEDLIEEKKLDIIIIDSLSSLARASQGDRSS 72

                        90       100
                ....*....|....*....|....*.
gi 18699726 243 AARRIKTEFLvqmqGVGNNNDGTLVL 268
Cdd:cd01120  73 ELLEDLAKLL----RAARNTGITVIA 94
AAA_22 pfam13401
AAA domain;
163-232 1.36e-03

AAA domain;


Pssm-ID: 379165 [Multi-domain]  Cd Length: 129  Bit Score: 38.48  E-value: 1.36e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18699726   163 ILLFGPPGTGKSYLAKAVATEAN--NSTFFSV------SSSDLMSKWLGE---------SEKLVKNLFE--LARQHKPSI 223
Cdd:pfam13401   8 LVLTGESGTGKTTLLRRLLEQLPevRDSVVFVdlpsgtSPKDLLRALLRAlglplsgrlSKEELLAALQqlLLALAVAVV 87


                  ....*....
gi 18699726   224 IFIDEVDSL 232
Cdd:pfam13401  88 LIIDEAQHL 96
PRK08116 PRK08116
hypothetical protein; Validated
 161-183 1.41e-03

hypothetical protein; Validated


Pssm-ID: 236153 [Multi-domain]  Cd Length: 268  Bit Score: 40.39  E-value: 1.41e-03
                         10        20
                 ....*....|....*....|...
gi 18699726  161 RGILLFGPPGTGKSYLAKAVATE 183
Cdd:PRK08116 115 VGLLLWGSVGTGKTYLAACIANE 137
PRK12402 PRK12402
replication factor C small subunit 2; Reviewed
 128-199 1.69e-03

replication factor C small subunit 2; Reviewed


Pssm-ID: 237090 [Multi-domain]  Cd Length: 337  Bit Score: 40.36  E-value: 1.69e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 18699726  128 DVAGLEGAKEALKEAVILPIkFPHLftgkrtpwrgiLLFGPPGTGKSYLAKAVATEA------NNSTFFSVssSDLMS 199
Cdd:PRK12402  16 DILGQDEVVERLSRAVDSPN-LPHL-----------LVQGPPGSGKTAAVRALARELygdpweNNFTEFNV--ADFFD 79
RecA-like_Lon cd19500
lon protease homolog 2 peroxisomal; Lon protease (also known as Lon peptidase) is an ...
 127-193 1.78e-03

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


Pssm-ID: 410908 [Multi-domain]  Cd Length: 182  Bit Score: 39.08  E-value: 1.78e-03
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18699726 127 NDVAGLEGAKEALKEavilpikfpHLFTGKRTP-WRG-ILLF-GPPGTGKSYLAKAVAtEANNSTFFSVS 193
Cdd:cd19500  10 ADHYGLEDVKERILE---------YLAVRKLKGsMKGpILCLvGPPGVGKTSLGKSIA-RALGRKFVRIS 69
clpC CHL00095
Clp protease ATP binding subunit
 161-296 2.85e-03

Clp protease ATP binding subunit


Pssm-ID: 214361 [Multi-domain]  Cd Length: 821  Bit Score: 40.04  E-value: 2.85e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18699726  161 RGILLFGPPGTGKSYLAKAVATE-ANNSTFFSVSSSDLM----------SKWLGESEKLVKNLFELARQHKPSIIFIDEV 229
Cdd:CHL00095 201 NNPILIGEPGVGKTAIAEGLAQRiVNRDVPDILEDKLVItldiglllagTKYRGEFEERLKRIFDEIQENNNIILVIDEV 280

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 18699726  230 DSLCGSRNENESEAARRIKTEFLVQmqgvgnnndGTL-VLGATNIPWV-----LDSAIRRRFEKrIYI--PLPEE 296
Cdd:CHL00095 281 HTLIGAGAAEGAIDAANILKPALAR---------GELqCIGATTLDEYrkhieKDPALERRFQP-VYVgePSVEE 345
Mg_chelatase pfam01078
Magnesium chelatase, subunit ChlI; Magnesium-chelatase is a three-component enzyme that ...
 126-182 3.42e-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: 38.67  E-value: 3.42e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 18699726   126 WNDVAGLEGAKEALKEAVIlpikfphlftgkrtpwrG---ILLFGPPGTGKSYLAKAVAT 182
Cdd:pfam01078   2 LADVKGQEQAKRALEIAAA-----------------GghnLLMIGPPGSGKTMLAKRLPG 44
clpA PRK11034
ATP-dependent Clp protease ATP-binding subunit; Provisional
 164-296 4.89e-03

ATP-dependent Clp protease ATP-binding subunit; Provisional


Pssm-ID: 236828 [Multi-domain]  Cd Length: 758  Bit Score: 39.43  E-value: 4.89e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18699726  164 LLFGPPGTGKSYLAKAVA---TEAN------NSTFFSVSSSDLM--SKWLGESEKLVKNLFELARQHKPSIIFIDEVDSL 232
Cdd:PRK11034 211 LLVGESGVGKTAIAEGLAwriVQGDvpevmaDCTIYSLDIGSLLagTKYRGDFEKRFKALLKQLEQDTNSILFIDEIHTI 290

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 18699726  233 --CGSRNENESEAARRIKTEFlvqmqgvgnnNDGTL-VLGAT------NIpWVLDSAIRRRFEK-RIYIPLPEE 296
Cdd:PRK11034 291 igAGAASGGQVDAANLIKPLL----------SSGKIrVIGSTtyqefsNI-FEKDRALARRFQKiDITEPSIEE 353
PRK13341 PRK13341
AAA family ATPase;
164-229 7.23e-03

AAA family ATPase;


Pssm-ID: 237354 [Multi-domain]  Cd Length: 725  Bit Score: 38.88  E-value: 7.23e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 18699726  164 LLFGPPGTGKSYLAKAVATEAnNSTFFSVSS-----SDLMSKwlgeseklVKNLFELARQH-KPSIIFIDEV 229
Cdd:PRK13341  56 ILYGPPGVGKTTLARIIANHT-RAHFSSLNAvlagvKDLRAE--------VDRAKERLERHgKRTILFIDEV 118
ABC_ATPase cd00267
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ...
 163-231 7.30e-03

ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.


Pssm-ID: 213179 [Multi-domain]  Cd Length: 157  Bit Score: 37.22  E-value: 7.30e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18699726 163 ILLFGPPGTGKSYLAKAVATEANNS----TFFSVSSSDLMSKWL------------GESEKLvknlfELARQ--HKPSII 224
Cdd:cd00267  28 VALVGPNGSGKSTLLRAIAGLLKPTsgeiLIDGKDIAKLPLEELrrrigyvpqlsgGQRQRV-----ALARAllLNPDLL 102


                ....*..
gi 18699726 225 FIDEVDS 231
Cdd:cd00267 103 LLDEPTS 109
COG0645 COG0645
Predicted kinase, contains AAA domain [General function prediction only];
163-183 7.55e-03

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


Pssm-ID: 440410 [Multi-domain]  Cd Length: 164  Bit Score: 37.20  E-value: 7.55e-03
                        10        20
                ....*....|....*....|.
gi 18699726 163 ILLFGPPGTGKSYLAKAVATE 183
Cdd:COG0645   2 ILVCGLPGSGKSTLARALAER 22
RNA_helicase pfam00910
RNA helicase; This family includes RNA helicases thought to be involved in duplex unwinding ...
 163-183 9.62e-03

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


Pssm-ID: 459992  Cd Length: 102  Bit Score: 35.66  E-value: 9.62e-03
                          10        20
                  ....*....|....*....|.
gi 18699726   163 ILLFGPPGTGKSYLAKAVATE 183
Cdd:pfam00910   1 IWLYGPPGCGKSTLAKYLARA 21
RecA-like_HslU cd19498
ATP-dependent protease ATPase subunit HslU; HslU is a component of the ATP-dependent protease ...
 163-245 9.88e-03

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: 36.97  E-value: 9.88e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18699726 163 ILLFGPPGTGKSYLAKAVATEANnSTFFSVSSSDLMS-KWLG-ESEKLVKNLFElarqhkpSIIFIDEVDSLCGSRNENE 240
Cdd:cd19498  49 ILMIGPTGVGKTEIARRLAKLAG-APFIKVEATKFTEvGYVGrDVESIIRDLVE-------GIVFIDEIDKIAKRGGSSG 120


                ....*
gi 18699726 241 SEAAR 245
Cdd:cd19498 121 PDVSR 125
 
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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