NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|1780598789|emb|VYS53703|]
View 

unnamed protein product [Arabidopsis thaliana]

Protein Classification

vacuolar protein sorting-associated protein 4( domain architecture ID 15269737)

vacuolar protein sorting-associated protein 4 is an ATP-binding protein with an AAA (ATPases Associated with various cellular Activities) domain.

CATH:  1.10.8.60
Gene Ontology:  GO:0005524|GO:0016887|GO:0007033|GO:0015031

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

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 ...
 126-296 9.11e-120

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: 346.08  E-value: 9.11e-120
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1780598789 126 KPNIKWSDVAGLESAKQALQEAVILPVKFPQFFTGKRRPWRAFLLYGPPGTGKSYLAKAVATEADSTFFSVSSSDLVSKW 205
Cdd:cd19521     1 KPNVKWEDVAGLEGAKEALKEAVILPVKFPHLFTGNRKPWSGILLYGPPGTGKSYLAKAVATEANSTFFSVSSSDLVSKW 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1780598789 206 MGESEKLVSNLFEMARESAPSIIFVDEIDSLCGTRGEGnESEASRRIKTELLVQMQGVGHNDEKVLVLAATNTPYALDQA 285
Cdd:cd19521    81 MGESEKLVKQLFAMARENKPSIIFIDEVDSLCGTRGEG-ESEASRRIKTELLVQMNGVGNDSQGVLVLGATNIPWQLDSA 159

                         170
                  ....*....|.
gi 1780598789 286 IRRRFDKRIYI 296
Cdd:cd19521   160 IRRRFEKRIYI 170
cell_div_CdvC super family cl49147
cell division protein CdvC;
7-431 3.76e-75

cell division protein CdvC;


The actual alignment was detected with superfamily member NF041006:

Pssm-ID: 468935 [Multi-domain]  Cd Length: 371  Bit Score: 239.25  E-value: 3.76e-75
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1780598789   7 EQAIEYVKQAVHEDNAGNYNKAFPLYMNALEYFKTHLK-YEKNPkIREAITQKFTEYLRRAEeiraVLDEGGSGPGSNGD 85
Cdd:NF041006    9 EMARKYAIAAVKADKEGRYEEAINNYKKAIEILTQIVRlYPDSP-LRHAYEQMINEYKKRIE----VLEELVPAEPAGPD 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1780598789  86 AAVATrpktkpkdgegggkdgedpeqsklragLNSAIVREKPNIKWSDVAGLESAKQALQEAVILPVKFPQFFtgkrrP- 164
Cdd:NF041006   84 VEKES---------------------------DEELVVKEKPKVTFSDIVGLEDVKEALKEAIVYPSKRPDLF-----Pl 131

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1780598789 165 -W-RAFLLYGPPGTGKSYLAKAVATEADSTFFSVSSSDLVSKWMGESEKLVSNLFEMARESA-----PSIIFVDEIDSLC 237
Cdd:NF041006  132 gWpRGILLYGPPGCGKTMLAAAVANEIDSEFIHVDAASIMSKWLGEAEKNVAKIFKKAREKSkeegkPAIIFIDEIDALL 211

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1780598789 238 GTRGEGNESEAsrRIKTELLVQMQGVGHNDE--KVLVLAATNTPYALDQAIRRRFDKRIYIPLPEAKARQHMFKVHlgdT 315
Cdd:NF041006  212 GVYSSEVGGEV--RVRNQFLKEMDGLQDKSEnyHVYVIGATNKPWRLDEPFLRRFQKRIYIPLPDREQRLELLKYY---T 286

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1780598789 316 PHNLTEP--DFEYLGQKTEGFSGSDvsvcVKDVLFEPVRKTQDAMFffkspdgtwmpcgprhpgaiqttmqdlaTKGLAE 393
Cdd:NF041006  287 SKIKLENdvDLDELAEMTEGYTASD----IRDIVQAAHMRVVKEMF----------------------------EKGLGE 334

                         410       420       430
                  ....*....|....*....|....*....|....*...
gi 1780598789 394 kiiPPPITRTDFEKVLARQRPTVSKSDLDVHERFTQEF 431
Cdd:NF041006  335 ---PRPITMEDFKEVLKIRKPSVNQEMLKAYEAWHEKF 369
 
Name Accession Description Interval E-value
RecA-like_VPS4 cd19521
ATPase domain of vacuolar protein sorting-associated protein 4; Vacuolar protein ...
 126-296 9.11e-120

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: 346.08  E-value: 9.11e-120
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1780598789 126 KPNIKWSDVAGLESAKQALQEAVILPVKFPQFFTGKRRPWRAFLLYGPPGTGKSYLAKAVATEADSTFFSVSSSDLVSKW 205
Cdd:cd19521     1 KPNVKWEDVAGLEGAKEALKEAVILPVKFPHLFTGNRKPWSGILLYGPPGTGKSYLAKAVATEANSTFFSVSSSDLVSKW 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1780598789 206 MGESEKLVSNLFEMARESAPSIIFVDEIDSLCGTRGEGnESEASRRIKTELLVQMQGVGHNDEKVLVLAATNTPYALDQA 285
Cdd:cd19521    81 MGESEKLVKQLFAMARENKPSIIFIDEVDSLCGTRGEG-ESEASRRIKTELLVQMNGVGNDSQGVLVLGATNIPWQLDSA 159

                         170
                  ....*....|.
gi 1780598789 286 IRRRFDKRIYI 296
Cdd:cd19521   160 IRRRFEKRIYI 170
RPT1 COG1222
ATP-dependent 26S proteasome regulatory subunit [Posttranslational modification, protein ...
 60-342 2.99e-87

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


Pssm-ID: 440835 [Multi-domain]  Cd Length: 326  Bit Score: 268.80  E-value: 2.99e-87
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1780598789  60 TEYLRRAEEIRAVLDEGGSGPGSNGDAAVATRPKTKPKDGEGGGKDGEDPEQSKLRAGLNSAIVREKPNIKWSDVAGLES 139
Cdd:COG1222     6 TIDENIKALLALIDALQERLGVELALLLQPVKALELLEEAPALLLNDANLTQKRLGTPRGTAVPAESPDVTFDDIGGLDE 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1780598789 140 AKQALQEAVILPVKFPQFFT--GKRRPwRAFLLYGPPGTGKSYLAKAVATEADSTFFSVSSSDLVSKWMGESEKLVSNLF 217
Cdd:COG1222    86 QIEEIREAVELPLKNPELFRkyGIEPP-KGVLLYGPPGTGKTLLAKAVAGELGAPFIRVRGSELVSKYIGEGARNVREVF 164

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1780598789 218 EMARESAPSIIFVDEIDSLCGTRGEGNESEASRRIKTELLVQMQGVgHNDEKVLVLAATNTPYALDQAIRR--RFDKRIY 295
Cdd:COG1222   165 ELAREKAPSIIFIDEIDAIAARRTDDGTSGEVQRTVNQLLAELDGF-ESRGDVLIIAATNRPDLLDPALLRpgRFDRVIE 243

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*....
gi 1780598789 296 IPLPEAKARQHMFKVHLGDTPhnLTEP-DFEYLGQKTEGFSGSDV-SVC 342
Cdd:COG1222   244 VPLPDEEAREEILKIHLRDMP--LADDvDLDKLAKLTEGFSGADLkAIV 290
cell_div_CdvC NF041006
cell division protein CdvC;
7-431 3.76e-75

cell division protein CdvC;


Pssm-ID: 468935 [Multi-domain]  Cd Length: 371  Bit Score: 239.25  E-value: 3.76e-75
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1780598789   7 EQAIEYVKQAVHEDNAGNYNKAFPLYMNALEYFKTHLK-YEKNPkIREAITQKFTEYLRRAEeiraVLDEGGSGPGSNGD 85
Cdd:NF041006    9 EMARKYAIAAVKADKEGRYEEAINNYKKAIEILTQIVRlYPDSP-LRHAYEQMINEYKKRIE----VLEELVPAEPAGPD 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1780598789  86 AAVATrpktkpkdgegggkdgedpeqsklragLNSAIVREKPNIKWSDVAGLESAKQALQEAVILPVKFPQFFtgkrrP- 164
Cdd:NF041006   84 VEKES---------------------------DEELVVKEKPKVTFSDIVGLEDVKEALKEAIVYPSKRPDLF-----Pl 131

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1780598789 165 -W-RAFLLYGPPGTGKSYLAKAVATEADSTFFSVSSSDLVSKWMGESEKLVSNLFEMARESA-----PSIIFVDEIDSLC 237
Cdd:NF041006  132 gWpRGILLYGPPGCGKTMLAAAVANEIDSEFIHVDAASIMSKWLGEAEKNVAKIFKKAREKSkeegkPAIIFIDEIDALL 211

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1780598789 238 GTRGEGNESEAsrRIKTELLVQMQGVGHNDE--KVLVLAATNTPYALDQAIRRRFDKRIYIPLPEAKARQHMFKVHlgdT 315
Cdd:NF041006  212 GVYSSEVGGEV--RVRNQFLKEMDGLQDKSEnyHVYVIGATNKPWRLDEPFLRRFQKRIYIPLPDREQRLELLKYY---T 286

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1780598789 316 PHNLTEP--DFEYLGQKTEGFSGSDvsvcVKDVLFEPVRKTQDAMFffkspdgtwmpcgprhpgaiqttmqdlaTKGLAE 393
Cdd:NF041006  287 SKIKLENdvDLDELAEMTEGYTASD----IRDIVQAAHMRVVKEMF----------------------------EKGLGE 334

                         410       420       430
                  ....*....|....*....|....*....|....*...
gi 1780598789 394 kiiPPPITRTDFEKVLARQRPTVSKSDLDVHERFTQEF 431
Cdd:NF041006  335 ---PRPITMEDFKEVLKIRKPSVNQEMLKAYEAWHEKF 369
CDC48 TIGR01243
AAA family ATPase, CDC48 subfamily; This subfamily of the AAA family ATPases includes two ...
 122-432 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: 230.95  E-value: 1.61e-68
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1780598789 122 IVREKPNIKWSDVAGLESAKQALQEAVILPVKFPQFFTG-KRRPWRAFLLYGPPGTGKSYLAKAVATEADSTFFSVSSSD 200
Cdd:TIGR01243 443 VLVEVPNVRWSDIGGLEEVKQELREAVEWPLKHPEIFEKmGIRPPKGVLLFGPPGTGKTLLAKAVATESGANFIAVRGPE 522

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1780598789 201 LVSKWMGESEKLVSNLFEMARESAPSIIFVDEIDSLCGTRGEGNESEASRRIKTELLVQMQGVGHNDEkVLVLAATNTPY 280
Cdd:TIGR01243 523 ILSKWVGESEKAIREIFRKARQAAPAIIFFDEIDAIAPARGARFDTSVTDRIVNQLLTEMDGIQELSN-VVVIAATNRPD 601

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1780598789 281 ALDQAIRR--RFDKRIYIPLPEAKARQHMFKVHLGDTPhnLTEP-DFEYLGQKTEGFSGSDVSVCVKDVLFEPVRKTqda 357
Cdd:TIGR01243 602 ILDPALLRpgRFDRLILVPPPDEEARKEIFKIHTRSMP--LAEDvDLEELAEMTEGYTGADIEAVCREAAMAALRES--- 676

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1780598789 358 mfffkspdgtwmpcgprhpgaIQTTMQDLATKGLAEKIIPPPITRTDFEKVLARQRPTVSKSDLDVHERFTQEFG 432
Cdd:TIGR01243 677 ---------------------IGSPAKEKLEVGEEEFLKDLKVEMRHFLEALKKVKPSVSKEDMLRYERLAKELK 730
PRK03992 PRK03992
proteasome-activating nucleotidase; Provisional
 123-343 1.18e-61

proteasome-activating nucleotidase; Provisional


Pssm-ID: 179699 [Multi-domain]  Cd Length: 389  Bit Score: 204.68  E-value: 1.18e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1780598789 123 VREKPNIKWSDVAGLESAKQALQEAVILPVKFPQFFtgkRR----PWRAFLLYGPPGTGKSYLAKAVATEADSTFFSVSS 198
Cdd:PRK03992  122 VIESPNVTYEDIGGLEEQIREVREAVELPLKKPELF---EEvgiePPKGVLLYGPPGTGKTLLAKAVAHETNATFIRVVG 198

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1780598789 199 SDLVSKWMGESEKLVSNLFEMARESAPSIIFVDEIDSLCGTRGEGNESeASR---RIKTELLVQMQGVGHNDEkVLVLAA 275
Cdd:PRK03992  199 SELVQKFIGEGARLVRELFELAREKAPSIIFIDEIDAIAAKRTDSGTS-GDRevqRTLMQLLAEMDGFDPRGN-VKIIAA 276

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1780598789 276 TNTPYALDQAIRR--RFDKRIYIPLPEAKARQHMFKVHLGDTphNLTEP-DFEYLGQKTEGFSGSDV-SVCV 343
Cdd:PRK03992  277 TNRIDILDPAILRpgRFDRIIEVPLPDEEGRLEILKIHTRKM--NLADDvDLEELAELTEGASGADLkAICT 346
AAA pfam00004
ATPase family associated with various cellular activities (AAA); AAA family proteins often ...
 169-298 2.85e-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: 184.72  E-value: 2.85e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1780598789 169 LLYGPPGTGKSYLAKAVATEADSTFFSVSSSDLVSKWMGESEKLVSNLFEMARESAPSIIFVDEIDSLCGTRGEGNESEa 248
Cdd:pfam00004   2 LLYGPPGTGKTTLAKAVAKELGAPFIEISGSELVSKYVGESEKRLRELFEAAKKLAPCVIFIDEIDALAGSRGSGGDSE- 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 1780598789 249 SRRIKTELLVQMQGVGHNDEKVLVLAATNTPYALDQAIRRRFDKRIYIPL 298
Cdd:pfam00004  81 SRRVVNQLLTELDGFTSSNSKVIVIAATNRPDKLDPALLGRFDRIIEFPL 130
MIT_VPS4 cd02678
MIT: domain contained within Microtubule Interacting and Trafficking molecules. This ...
 4-78 4.40e-37

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: 130.08  E-value: 4.40e-37
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1780598789   4 NFKEQAIEYVKQAVHEDNAGNYNKAFPLYMNALEYFKTHLKYEKNPKIREAITQKFTEYLRRAEEIRAVLDEGGS 78
Cdd:cd02678     1 DFLQKAIELVKKAIEEDNAGNYEEALRLYQHALEYFMHALKYEKNPKSKESIRAKCTEYLDRAEKLKEYLAKKEK 75
Vps4_C pfam09336
Vps4 C terminal oligomerization domain; This domain is found at the C terminal of ATPase ...
 368-432 6.77e-27

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: 102.19  E-value: 6.77e-27
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1780598789 368 WMPCGPRHPGAIQTTMQDLAtkglAEKIIPPPITRTDFEKVLARQRPTVSKSDLDVHERFTQEFG 432
Cdd:pfam09336   1 LTPCSPGDPGAIEMTWMDIP----SDKLLEPPVTMKDFLKALKSSRPTVSKEDLEKYEEFTKEFG 61
MIT smart00745
Microtubule Interacting and Trafficking molecule domain;
3-75 1.79e-20

Microtubule Interacting and Trafficking molecule domain;


Pssm-ID: 197854  Cd Length: 77  Bit Score: 85.05  E-value: 1.79e-20
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1780598789    3 SNFKEQAIEYVKQAVHEDNAGNYNKAFPLYMNALEYFKTHLKYEKNPKIREAITQKFTEYLRRAEEIRAVLDE 75
Cdd:smart00745   2 RDYLSKAKELISKALKADEAGNYEEALELYKKAIEYLLEGIKVESDSKRREALKAKAAEYLDRAEEIKKSLLE 74
AAA smart00382
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ...
 164-300 1.25e-19

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: 85.12  E-value: 1.25e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1780598789  164 PWRAFLLYGPPGTGKSYLAKAVATEADST---FFSVSSSDL--------------VSKWMGESEKLVSNLFEMARESAPS 226
Cdd:smart00382   1 PGEVILIVGPPGSGKTTLARALARELGPPgggVIYIDGEDIleevldqllliivgGKKASGSGELRLRLALALARKLKPD 80

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1780598789  227 IIFVDEIDSLCGTRGEGNESEASRRIKTELLVQmqgvghnDEKVLVLAATNTPYALDQA-IRRRFDKRIYIPLPE 300
Cdd:smart00382  81 VLILDEITSLLDAEQEALLLLLEELRLLLLLKS-------EKNLTVILTTNDEKDLGPAlLRRRFDRRIVLLLIL 148
IS21_help_AAA NF038214
IS21-like element helper ATPase IstB; This protein family model resembles PF01695, but was ...
 169-189 1.19e-03

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


Pssm-ID: 439516  Cd Length: 232  Bit Score: 40.15  E-value: 1.19e-03
                          10        20
                  ....*....|....*....|.
gi 1780598789 169 LLYGPPGTGKSYLAKAVATEA 189
Cdd:NF038214   94 LLLGPPGTGKTHLAIALGYAA 114
McrB COG1401
5-methylcytosine-specific restriction endonuclease McrBC, GTP-binding regulatory subunit McrB ...
 4-186 1.54e-03

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


Pssm-ID: 441011 [Multi-domain]  Cd Length: 477  Bit Score: 40.91  E-value: 1.54e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1780598789   4 NFKEQAIEYVKQAVHEDNAGNYNKAFPLYMNALEYFKTHLKYEKNPKI---REAITQKFTEYLRRAEEIRAVLDEGGSGP 80
Cdd:COG1401    48 ERLSEELLRADRAARATELVEELSAALEVVVLLLDLEKVELNEKLALSeaaVAIEELYELEADSEIEAVGLLLELAERSD 127

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1780598789  81 GSNGDAAVATRPKTKPKDGEGGGKDGEDPEQSKLRAGLNSAIVREKPNIKWSDVAGLESAKQalQEAVILPVKFPQFFTG 160
Cdd:COG1401   128 ALEALERARLLLELADLEERAALETEVLEALEAELEELLAAPEDLSADALAAELSAAEELYS--EDLESEDDYLKDLLRE 205

                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 1780598789 161 KRRPW-RAFL----------LYGPPGTGKSYLAKAVA 186
Cdd:COG1401   206 KFEETlEAFLaalktkknviLAGPPGTGKTYLARRLA 242
 
Name Accession Description Interval E-value
RecA-like_VPS4 cd19521
ATPase domain of vacuolar protein sorting-associated protein 4; Vacuolar protein ...
 126-296 9.11e-120

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: 346.08  E-value: 9.11e-120
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1780598789 126 KPNIKWSDVAGLESAKQALQEAVILPVKFPQFFTGKRRPWRAFLLYGPPGTGKSYLAKAVATEADSTFFSVSSSDLVSKW 205
Cdd:cd19521     1 KPNVKWEDVAGLEGAKEALKEAVILPVKFPHLFTGNRKPWSGILLYGPPGTGKSYLAKAVATEANSTFFSVSSSDLVSKW 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1780598789 206 MGESEKLVSNLFEMARESAPSIIFVDEIDSLCGTRGEGnESEASRRIKTELLVQMQGVGHNDEKVLVLAATNTPYALDQA 285
Cdd:cd19521    81 MGESEKLVKQLFAMARENKPSIIFIDEVDSLCGTRGEG-ESEASRRIKTELLVQMNGVGNDSQGVLVLGATNIPWQLDSA 159

                         170
                  ....*....|.
gi 1780598789 286 IRRRFDKRIYI 296
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 ...
 134-296 9.96e-90

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: 269.22  E-value: 9.96e-90
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1780598789 134 VAGLESAKQALQEAVILPVKFPQFFTGKRRPWRAFLLYGPPGTGKSYLAKAVATEADSTFFSVSSSDLVSKWMGESEKLV 213
Cdd:cd19509     1 IAGLDDAKEALKEAVILPSLRPDLFPGLRGPPRGILLYGPPGTGKTLLARAVASESGSTFFSISASSLVSKWVGESEKIV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1780598789 214 SNLFEMARESAPSIIFVDEIDSLCGTRGEGnESEASRRIKTELLVQMQGVGHNDE-KVLVLAATNTPYALDQAIRRRFDK 292
Cdd:cd19509    81 RALFALARELQPSIIFIDEIDSLLSERGSG-EHEASRRVKTEFLVQMDGVLNKPEdRVLVLGATNRPWELDEAFLRRFEK 159


                  ....
gi 1780598789 293 RIYI 296
Cdd:cd19509   160 RIYI 163
RPT1 COG1222
ATP-dependent 26S proteasome regulatory subunit [Posttranslational modification, protein ...
 60-342 2.99e-87

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


Pssm-ID: 440835 [Multi-domain]  Cd Length: 326  Bit Score: 268.80  E-value: 2.99e-87
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1780598789  60 TEYLRRAEEIRAVLDEGGSGPGSNGDAAVATRPKTKPKDGEGGGKDGEDPEQSKLRAGLNSAIVREKPNIKWSDVAGLES 139
Cdd:COG1222     6 TIDENIKALLALIDALQERLGVELALLLQPVKALELLEEAPALLLNDANLTQKRLGTPRGTAVPAESPDVTFDDIGGLDE 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1780598789 140 AKQALQEAVILPVKFPQFFT--GKRRPwRAFLLYGPPGTGKSYLAKAVATEADSTFFSVSSSDLVSKWMGESEKLVSNLF 217
Cdd:COG1222    86 QIEEIREAVELPLKNPELFRkyGIEPP-KGVLLYGPPGTGKTLLAKAVAGELGAPFIRVRGSELVSKYIGEGARNVREVF 164

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1780598789 218 EMARESAPSIIFVDEIDSLCGTRGEGNESEASRRIKTELLVQMQGVgHNDEKVLVLAATNTPYALDQAIRR--RFDKRIY 295
Cdd:COG1222   165 ELAREKAPSIIFIDEIDAIAARRTDDGTSGEVQRTVNQLLAELDGF-ESRGDVLIIAATNRPDLLDPALLRpgRFDRVIE 243

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*....
gi 1780598789 296 IPLPEAKARQHMFKVHLGDTPhnLTEP-DFEYLGQKTEGFSGSDV-SVC 342
Cdd:COG1222   244 VPLPDEEAREEILKIHLRDMP--LADDvDLDKLAKLTEGFSGADLkAIV 290
RecA-like_KTNA1 cd19522
Katanin p60 ATPase-containing subunit A1; Katanin p60 ATPase-containing subunit A1 (KTNA1) is ...
 133-296 1.23e-80

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: 246.43  E-value: 1.23e-80
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1780598789 133 DVAGLESAKQALQEAVILPVKFPQFFTGKRRPWRAFLLYGPPGTGKSYLAKAVATEADSTFFSVSSSDLVSKWMGESEKL 212
Cdd:cd19522     1 DIADLEEAKKLLEEAVVLPMWMPEFFKGIRRPWKGVLMVGPPGTGKTLLAKAVATECGTTFFNVSSSTLTSKYRGESEKL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1780598789 213 VSNLFEMARESAPSIIFVDEIDSLCGTRGEGNESEASRRIKTELLVQMQGVG---HNDEK---VLVLAATNTPYALDQAI 286
Cdd:cd19522    81 VRLLFEMARFYAPTTIFIDEIDSICSRRGTSEEHEASRRVKSELLVQMDGVGgasENDDPskmVMVLAATNFPWDIDEAL 160

                         170
                  ....*....|
gi 1780598789 287 RRRFDKRIYI 296
Cdd:cd19522   161 RRRLEKRIYI 170
cell_div_CdvC NF041006
cell division protein CdvC;
7-431 3.76e-75

cell division protein CdvC;


Pssm-ID: 468935 [Multi-domain]  Cd Length: 371  Bit Score: 239.25  E-value: 3.76e-75
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1780598789   7 EQAIEYVKQAVHEDNAGNYNKAFPLYMNALEYFKTHLK-YEKNPkIREAITQKFTEYLRRAEeiraVLDEGGSGPGSNGD 85
Cdd:NF041006    9 EMARKYAIAAVKADKEGRYEEAINNYKKAIEILTQIVRlYPDSP-LRHAYEQMINEYKKRIE----VLEELVPAEPAGPD 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1780598789  86 AAVATrpktkpkdgegggkdgedpeqsklragLNSAIVREKPNIKWSDVAGLESAKQALQEAVILPVKFPQFFtgkrrP- 164
Cdd:NF041006   84 VEKES---------------------------DEELVVKEKPKVTFSDIVGLEDVKEALKEAIVYPSKRPDLF-----Pl 131

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1780598789 165 -W-RAFLLYGPPGTGKSYLAKAVATEADSTFFSVSSSDLVSKWMGESEKLVSNLFEMARESA-----PSIIFVDEIDSLC 237
Cdd:NF041006  132 gWpRGILLYGPPGCGKTMLAAAVANEIDSEFIHVDAASIMSKWLGEAEKNVAKIFKKAREKSkeegkPAIIFIDEIDALL 211

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1780598789 238 GTRGEGNESEAsrRIKTELLVQMQGVGHNDE--KVLVLAATNTPYALDQAIRRRFDKRIYIPLPEAKARQHMFKVHlgdT 315
Cdd:NF041006  212 GVYSSEVGGEV--RVRNQFLKEMDGLQDKSEnyHVYVIGATNKPWRLDEPFLRRFQKRIYIPLPDREQRLELLKYY---T 286

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1780598789 316 PHNLTEP--DFEYLGQKTEGFSGSDvsvcVKDVLFEPVRKTQDAMFffkspdgtwmpcgprhpgaiqttmqdlaTKGLAE 393
Cdd:NF041006  287 SKIKLENdvDLDELAEMTEGYTASD----IRDIVQAAHMRVVKEMF----------------------------EKGLGE 334

                         410       420       430
                  ....*....|....*....|....*....|....*...
gi 1780598789 394 kiiPPPITRTDFEKVLARQRPTVSKSDLDVHERFTQEF 431
Cdd:NF041006  335 ---PRPITMEDFKEVLKIRKPSVNQEMLKAYEAWHEKF 369
SpoVK COG0464
AAA+-type ATPase, SpoVK/Ycf46/Vps4 family [Cell wall/membrane/envelope biogenesis, Cell cycle ...
 80-352 3.60e-74

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: 237.50  E-value: 3.60e-74
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1780598789  80 PGSNGDAAVATRPKTKPKDGEGGGKDGEDPEQSKLRAGLNSAIVREKPNIKWSDVAGLESAKQALQEAVILPVKFPQFFT 159
Cdd:COG0464   105 LLLLLLLLDLERALLELLRESAEALALAAPLVTYEDIGGLEEELLELREAILDDLGGLEEVKEELRELVALPLKRPELRE 184

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1780598789 160 --GKRRPwRAFLLYGPPGTGKSYLAKAVATEADSTFFSVSSSDLVSKWMGESEKLVSNLFEMARESAPSIIFVDEIDSLC 237
Cdd:COG0464   185 eyGLPPP-RGLLLYGPPGTGKTLLARALAGELGLPLIEVDLSDLVSKYVGETEKNLREVFDKARGLAPCVLFIDEADALA 263

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1780598789 238 GTRGEGNESeASRRIKTELLVQMQGVGHNdekVLVLAATNTPYALDQAIRRRFDKRIYIPLPEAKARQHMFKVHLGDTPH 317
Cdd:COG0464   264 GKRGEVGDG-VGRRVVNTLLTEMEELRSD---VVVIAATNRPDLLDPALLRRFDEIIFFPLPDAEERLEIFRIHLRKRPL 339

                         250       260       270
                  ....*....|....*....|....*....|....*
gi 1780598789 318 NlTEPDFEYLGQKTEGFSGSDVSVCVKDVLFEPVR 352
Cdd:COG0464   340 D-EDVDLEELAEATEGLSGADIRNVVRRAALQALR 373
RecA-like_Figl-1 cd19525
ATPase domain of Fidgetin-Like 1 (FIGL-1); FIGL-1 may participate in DNA repair in the nucleus; ...
 118-296 3.01e-69

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: 217.55  E-value: 3.01e-69
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1780598789 118 LNSAIVREKPNIKWSDVAGLESAKQALQEAVILPVKFPQFFTGKRRPWRAFLLYGPPGTGKSYLAKAVATEADSTFFSVS 197
Cdd:cd19525     8 IMSEIMDHGPPINWADIAGLEFAKKTIKEIVVWPMLRPDIFTGLRGPPKGILLFGPPGTGKTLIGKCIASQSGATFFSIS 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1780598789 198 SSDLVSKWMGESEKLVSNLFEMARESAPSIIFVDEIDSLCGTRGEGnESEASRRIKTELLVQMQGVG-HNDEKVLVLAAT 276
Cdd:cd19525    88 ASSLTSKWVGEGEKMVRALFSVARCKQPAVIFIDEIDSLLSQRGEG-EHESSRRIKTEFLVQLDGATtSSEDRILVVGAT 166

                         170       180
                  ....*....|....*....|
gi 1780598789 277 NTPYALDQAIRRRFDKRIYI 296
Cdd:cd19525   167 NRPQEIDEAARRRLVKRLYI 186
CDC48 TIGR01243
AAA family ATPase, CDC48 subfamily; This subfamily of the AAA family ATPases includes two ...
 122-432 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: 230.95  E-value: 1.61e-68
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1780598789 122 IVREKPNIKWSDVAGLESAKQALQEAVILPVKFPQFFTG-KRRPWRAFLLYGPPGTGKSYLAKAVATEADSTFFSVSSSD 200
Cdd:TIGR01243 443 VLVEVPNVRWSDIGGLEEVKQELREAVEWPLKHPEIFEKmGIRPPKGVLLFGPPGTGKTLLAKAVATESGANFIAVRGPE 522

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1780598789 201 LVSKWMGESEKLVSNLFEMARESAPSIIFVDEIDSLCGTRGEGNESEASRRIKTELLVQMQGVGHNDEkVLVLAATNTPY 280
Cdd:TIGR01243 523 ILSKWVGESEKAIREIFRKARQAAPAIIFFDEIDAIAPARGARFDTSVTDRIVNQLLTEMDGIQELSN-VVVIAATNRPD 601

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1780598789 281 ALDQAIRR--RFDKRIYIPLPEAKARQHMFKVHLGDTPhnLTEP-DFEYLGQKTEGFSGSDVSVCVKDVLFEPVRKTqda 357
Cdd:TIGR01243 602 ILDPALLRpgRFDRLILVPPPDEEARKEIFKIHTRSMP--LAEDvDLEELAEMTEGYTGADIEAVCREAAMAALRES--- 676

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1780598789 358 mfffkspdgtwmpcgprhpgaIQTTMQDLATKGLAEKIIPPPITRTDFEKVLARQRPTVSKSDLDVHERFTQEFG 432
Cdd:TIGR01243 677 ---------------------IGSPAKEKLEVGEEEFLKDLKVEMRHFLEALKKVKPSVSKEDMLRYERLAKELK 730
RecA-like_spastin cd19524
ATPase domain of spastin; Spastin is an ATP-dependent microtubule-severing protein involved in ...
 133-296 1.72e-68

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: 214.71  E-value: 1.72e-68
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1780598789 133 DVAGLESAKQALQEAVILPVKFPQFFTGKRRPWRAFLLYGPPGTGKSYLAKAVATEADSTFFSVSSSDLVSKWMGESEKL 212
Cdd:cd19524     1 DIAGQDLAKQALQEMVILPSLRPELFTGLRAPARGLLLFGPPGNGKTMLAKAVAAESNATFFNISAASLTSKYVGEGEKL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1780598789 213 VSNLFEMARESAPSIIFVDEIDSLCGTRGEgNESEASRRIKTELLVQMQGVGHN-DEKVLVLAATNTPYALDQAIRRRFD 291
Cdd:cd19524    81 VRALFAVARELQPSIIFIDEVDSLLSERSE-GEHEASRRLKTEFLIEFDGVQSNgDDRVLVMGATNRPQELDDAVLRRFT 159


                  ....*
gi 1780598789 292 KRIYI 296
Cdd:cd19524   160 KRVYV 164
PRK03992 PRK03992
proteasome-activating nucleotidase; Provisional
 123-343 1.18e-61

proteasome-activating nucleotidase; Provisional


Pssm-ID: 179699 [Multi-domain]  Cd Length: 389  Bit Score: 204.68  E-value: 1.18e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1780598789 123 VREKPNIKWSDVAGLESAKQALQEAVILPVKFPQFFtgkRR----PWRAFLLYGPPGTGKSYLAKAVATEADSTFFSVSS 198
Cdd:PRK03992  122 VIESPNVTYEDIGGLEEQIREVREAVELPLKKPELF---EEvgiePPKGVLLYGPPGTGKTLLAKAVAHETNATFIRVVG 198

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1780598789 199 SDLVSKWMGESEKLVSNLFEMARESAPSIIFVDEIDSLCGTRGEGNESeASR---RIKTELLVQMQGVGHNDEkVLVLAA 275
Cdd:PRK03992  199 SELVQKFIGEGARLVRELFELAREKAPSIIFIDEIDAIAAKRTDSGTS-GDRevqRTLMQLLAEMDGFDPRGN-VKIIAA 276

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1780598789 276 TNTPYALDQAIRR--RFDKRIYIPLPEAKARQHMFKVHLGDTphNLTEP-DFEYLGQKTEGFSGSDV-SVCV 343
Cdd:PRK03992  277 TNRIDILDPAILRpgRFDRIIEVPLPDEEGRLEILKIHTRKM--NLADDvDLEELAELTEGASGADLkAICT 346
RecA-like_CDC48_r2-like cd19511
second of two ATPase domains of CDC48/p97, PEX1 and -6, VAT and NVL, and similar ATPase ...
 140-296 7.10e-60

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: 192.50  E-value: 7.10e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1780598789 140 AKQALQEAVILPVKFPQFFT--GKRRPwRAFLLYGPPGTGKSYLAKAVATEADSTFFSVSSSDLVSKWMGESEKLVSNLF 217
Cdd:cd19511     1 VKRELKEAVEWPLKHPDAFKrlGIRPP-KGVLLYGPPGCGKTLLAKALASEAGLNFISVKGPELFSKYVGESERAVREIF 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1780598789 218 EMARESAPSIIFVDEIDSLCGTRGEGNESEASRRIKTELLVQMQGVGHNDEkVLVLAATNTPYALDQAIRR--RFDKRIY 295
Cdd:cd19511    80 QKARQAAPCIIFFDEIDSLAPRRGQSDSSGVTDRVVSQLLTELDGIESLKG-VVVIAATNRPDMIDPALLRpgRLDKLIY 158


                  .
gi 1780598789 296 I 296
Cdd:cd19511   159 V 159
AAA pfam00004
ATPase family associated with various cellular activities (AAA); AAA family proteins often ...
 169-298 2.85e-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: 184.72  E-value: 2.85e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1780598789 169 LLYGPPGTGKSYLAKAVATEADSTFFSVSSSDLVSKWMGESEKLVSNLFEMARESAPSIIFVDEIDSLCGTRGEGNESEa 248
Cdd:pfam00004   2 LLYGPPGTGKTTLAKAVAKELGAPFIEISGSELVSKYVGESEKRLRELFEAAKKLAPCVIFIDEIDALAGSRGSGGDSE- 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 1780598789 249 SRRIKTELLVQMQGVGHNDEKVLVLAATNTPYALDQAIRRRFDKRIYIPL 298
Cdd:pfam00004  81 SRRVVNQLLTELDGFTSSNSKVIVIAATNRPDKLDPALLGRFDRIIEFPL 130
RecA-like_CDC48_NLV2_r1-like cd19503
first of two ATPase domains of CDC48 and NLV2, and similar ATPase domains; CDC48 in yeast and ...
 133-296 8.51e-54

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: 176.71  E-value: 8.51e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1780598789 133 DVAGLESAKQALQEAVILPVKFPQFFT--GKRRPwRAFLLYGPPGTGKSYLAKAVATEADSTFFSVSSSDLVSKWMGESE 210
Cdd:cd19503     1 DIGGLDEQIASLKELIELPLKYPELFRalGLKPP-RGVLLHGPPGTGKTLLARAVANEAGANFLSISGPSIVSKYLGESE 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1780598789 211 KLVSNLFEMARESAPSIIFVDEIDSLCGTRGEGNEsEASRRIKTELLVQMQGVGhNDEKVLVLAATNTPYALDQAIRR-- 288
Cdd:cd19503    80 KNLREIFEEARSHAPSIIFIDEIDALAPKREEDQR-EVERRVVAQLLTLMDGMS-SRGKVVVIAATNRPDAIDPALRRpg 157


                  ....*...
gi 1780598789 289 RFDKRIYI 296
Cdd:cd19503   158 RFDREVEI 165
RecA-like_ATAD1 cd19520
ATPase domain of ATPase family AAA domain-containing protein 1 and similar ATPase domains; ...
 133-296 4.81e-53

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: 174.92  E-value: 4.81e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1780598789 133 DVAGLESAKQALQEAVILPVKFPQFFTGKR--RPWRAFLLYGPPGTGKSYLAKAVATEADSTFFSVSSSDLVSKWMGESE 210
Cdd:cd19520     1 DIGGLDEVITELKELVILPLQRPELFDNSRllQPPKGVLLYGPPGCGKTMLAKATAKEAGARFINLQVSSLTDKWYGESQ 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1780598789 211 KLVSNLFEMARESAPSIIFVDEIDSLCGTRgEGNESEASRRIKTELLVQMQGVGHND-EKVLVLAATNTPYALDQAIRRR 289
Cdd:cd19520    81 KLVAAVFSLASKLQPSIIFIDEIDSFLRQR-SSTDHEATAMMKAEFMSLWDGLSTDGnCRVIVMGATNRPQDLDEAILRR 159


                  ....*..
gi 1780598789 290 FDKRIYI 296
Cdd:cd19520   160 MPKRFHI 166
RecA-like_protease cd19481
proteases similar to RecA; RecA-like NTPases. This family includes the NTP binding domain of ...
 140-296 2.02e-52

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


Pssm-ID: 410889 [Multi-domain]  Cd Length: 158  Bit Score: 172.85  E-value: 2.02e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1780598789 140 AKQALQEAVILPVKFPQFFTGKRRPWRAFLLYGPPGTGKSYLAKAVATEADSTFFSVSSSDLVSKWMGESEKLVSNLFEM 219
Cdd:cd19481     1 LKASLREAVEAPRRGSRLRRYGLGLPKGILLYGPPGTGKTLLAKALAGELGLPLIVVKLSSLLSKYVGESEKNLRKIFER 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1780598789 220 ARESAPSIIFVDEIDSLCGTRGEGNESEASRRIKTELLVQMQGVGHnDEKVLVLAATNTPYALDQAIRR--RFDKRIYI 296
Cdd:cd19481    81 ARRLAPCILFIDEIDAIGRKRDSSGESGELRRVLNQLLTELDGVNS-RSKVLVIAATNRPDLLDPALLRpgRFDEVIEF 158
HflB COG0465
ATP-dependent Zn proteases [Posttranslational modification, protein turnover, chaperones];
122-338 4.07e-50

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


Pssm-ID: 440233 [Multi-domain]  Cd Length: 583  Bit Score: 178.69  E-value: 4.07e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1780598789 122 IVREKPNIKWSDVAGLESAKQALQEAV-ILpvKFPQFFT--GKRRPwRAFLLYGPPGTGKSYLAKAVATEADSTFFSVSS 198
Cdd:COG0465   132 YDEDKPKVTFDDVAGVDEAKEELQEIVdFL--KDPEKFTrlGAKIP-KGVLLVGPPGTGKTLLAKAVAGEAGVPFFSISG 208

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1780598789 199 SDLVSkwM----GESEklVSNLFEMARESAPSIIFVDEIDSLCGTRGEGN-----ESEasrriKT--ELLVQMQGVGHNd 267
Cdd:COG0465   209 SDFVE--MfvgvGASR--VRDLFEQAKKNAPCIIFIDEIDAVGRQRGAGLggghdERE-----QTlnQLLVEMDGFEGN- 278

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1780598789 268 EKVLVLAATNTPYALDQAIRR--RFDKRIYIPLPEAKARQHMFKVHLGDTPhnLTEP-DFEYLGQKTEGFSGSD 338
Cdd:COG0465   279 EGVIVIAATNRPDVLDPALLRpgRFDRQVVVDLPDVKGREAILKVHARKKP--LAPDvDLEVIARRTPGFSGAD 350
RecA-like_VCP_r2 cd19529
second of two ATPase domains of Valosin-containing protein-like ATPase (VAT) and similar ...
 140-296 5.95e-50

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: 166.52  E-value: 5.95e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1780598789 140 AKQALQEAVILPVKFPQFFTGKR-RPWRAFLLYGPPGTGKSYLAKAVATEADSTFFSVSSSDLVSKWMGESEKLVSNLFE 218
Cdd:cd19529     1 VKQELKEAVEWPLLKPEVFKRLGiRPPKGILLYGPPGTGKTLLAKAVATESNANFISVKGPELLSKWVGESEKAIREIFR 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1780598789 219 MARESAPSIIFVDEIDSLCGTRGEGNESEASRRIKTELLVQMQGVgHNDEKVLVLAATNTPYALDQAIRR--RFDKRIYI 296
Cdd:cd19529    81 KARQVAPCVIFFDEIDSIAPRRGTTGDSGVTERVVNQLLTELDGL-EEMNGVVVIAATNRPDIIDPALLRagRFDRLIYI 159
CDC48 TIGR01243
AAA family ATPase, CDC48 subfamily; This subfamily of the AAA family ATPases includes two ...
 124-353 7.38e-50

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: 180.10  E-value: 7.38e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1780598789 124 REKPNIKWSDVAGLESAKQALQEAVILPVKFPQFFtgKR---RPWRAFLLYGPPGTGKSYLAKAVATEADSTFFSVSSSD 200
Cdd:TIGR01243 170 RKVPKVTYEDIGGLKEAKEKIREMVELPMKHPELF--EHlgiEPPKGVLLYGPPGTGKTLLAKAVANEAGAYFISINGPE 247

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1780598789 201 LVSKWMGESEKLVSNLFEMARESAPSIIFVDEIDSLCGTRGEGNeSEASRRIKTELLVQMQGVGHNDeKVLVLAATNTPY 280
Cdd:TIGR01243 248 IMSKYYGESEERLREIFKEAEENAPSIIFIDEIDAIAPKREEVT-GEVEKRVVAQLLTLMDGLKGRG-RVIVIGATNRPD 325

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1780598789 281 ALDQAIRR--RFDKRIYIPLPEAKARQHMFKVHLGDTPHNlTEPDFEYLGQKTEGFSGSDVSVCVKDVLFEPVRK 353
Cdd:TIGR01243 326 ALDPALRRpgRFDREIVIRVPDKRARKEILKVHTRNMPLA-EDVDLDKLAEVTHGFVGADLAALAKEAAMAALRR 399
RecA-like_FtsH cd19501
ATP-dependent zinc metalloprotease FtsH; FtsH ATPase is a processive, ATP-dependent zinc ...
 129-296 1.34e-49

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: 166.25  E-value: 1.34e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1780598789 129 IKWSDVAGLESAKQALQEAVILpVKFPQFFT--GKRRPwRAFLLYGPPGTGKSYLAKAVATEADSTFFSVSSSDLVSKWM 206
Cdd:cd19501     1 VTFKDVAGCEEAKEELKEVVEF-LKNPEKFTklGAKIP-KGVLLVGPPGTGKTLLAKAVAGEAGVPFFSISGSDFVEMFV 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1780598789 207 GESEKLVSNLFEMARESAPSIIFVDEIDSLCGTRGEGNESEASRRIKT--ELLVQMQGVGHNdEKVLVLAATNTPYALDQ 284
Cdd:cd19501    79 GVGASRVRDLFEQAKKNAPCIVFIDEIDAVGRKRGAGLGGGHDEREQTlnQLLVEMDGFESN-TGVIVIAATNRPDVLDP 157

                         170
                  ....*....|....
gi 1780598789 285 AIRR--RFDKRIYI 296
Cdd:cd19501   158 ALLRpgRFDRQVYV 171
RecA-like_PAN_like cd19502
proteasome activating nucleotidase PAN and related proteasome subunits; This subfamily ...
 131-294 3.50e-48

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: 162.51  E-value: 3.50e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1780598789 131 WSDVAGLESAKQALQEAVILPVKFPQFFT--GKRRPwRAFLLYGPPGTGKSYLAKAVATEADSTFFSVSSSDLVSKWMGE 208
Cdd:cd19502     2 YEDIGGLDEQIREIREVVELPLKHPELFEelGIEPP-KGVLLYGPPGTGKTLLAKAVANHTDATFIRVVGSELVQKYIGE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1780598789 209 SEKLVSNLFEMARESAPSIIFVDEIDSLCGTR---GEGNESEAsRRIKTELLVQMQGVGHNDEkVLVLAATNTPYALDQA 285
Cdd:cd19502    81 GARLVRELFEMAREKAPSIIFIDEIDAIGAKRfdsGTGGDREV-QRTMLELLNQLDGFDPRGN-IKVIMATNRPDILDPA 158

                         170
                  ....*....|.
gi 1780598789 286 IRR--RFDKRI 294
Cdd:cd19502   159 LLRpgRFDRKI 169
COG1223 COG1223
Predicted ATPase, AAA+ superfamily [General function prediction only];
131-347 1.43e-45

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


Pssm-ID: 440836 [Multi-domain]  Cd Length: 246  Bit Score: 158.12  E-value: 1.43e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1780598789 131 WSDVAGLESAKQALQEAVilpvkfpQFFTGKRRPwRAF--------LLYGPPGTGKSYLAKAVATEADSTFFSVSSSDLV 202
Cdd:COG1223     1 LDDVVGQEEAKKKLKLII-------KELRRRENL-RKFglwpprkiLFYGPPGTGKTMLAEALAGELKLPLLTVRLDSLI 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1780598789 203 SKWMGESEKLVSNLFEMAREsAPSIIFVDEIDSLCGTRGEGNESEASRRIKTELLVQMQGVghnDEKVLVLAATNTPYAL 282
Cdd:COG1223    73 GSYLGETARNLRKLFDFARR-APCVIFFDEFDAIAKDRGDQNDVGEVKRVVNALLQELDGL---PSGSVVIAATNHPELL 148

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1780598789 283 DQAIRRRFDKRIYIPLPEAKARQHMFKVHLGDTPHNLtEPDFEYLGQKTEGFSGSDVSVCVKDVL 347
Cdd:COG1223   149 DSALWRRFDEVIEFPLPDKEERKEILELNLKKFPLPF-ELDLKKLAKKLEGLSGADIEKVLKTAL 212
PTZ00454 PTZ00454
26S protease regulatory subunit 6B-like protein; Provisional
 123-353 2.36e-45

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


Pssm-ID: 240423 [Multi-domain]  Cd Length: 398  Bit Score: 161.85  E-value: 2.36e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1780598789 123 VREKPNIKWSDVAGLESAKQALQEAVILPVKFPQFF--TGKRRPwRAFLLYGPPGTGKSYLAKAVATEADSTFFSVSSSD 200
Cdd:PTZ00454  136 MSEKPDVTYSDIGGLDIQKQEIREAVELPLTCPELYeqIGIDPP-RGVLLYGPPGTGKTMLAKAVAHHTTATFIRVVGSE 214

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1780598789 201 LVSKWMGESEKLVSNLFEMARESAPSIIFVDEIDSLCGTRGEGnESEASR---RIKTELLVQMQGVGHNdEKVLVLAATN 277
Cdd:PTZ00454  215 FVQKYLGEGPRMVRDVFRLARENAPSIIFIDEVDSIATKRFDA-QTGADRevqRILLELLNQMDGFDQT-TNVKVIMATN 292

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1780598789 278 TPYALDQAIRR--RFDKRIYIPLPEAKARQHMFKVHLGDTphNLT-EPDFEYLGQKTEGFSGSDVSVCVKDVLFEPVRK 353
Cdd:PTZ00454  293 RADTLDPALLRpgRLDRKIEFPLPDRRQKRLIFQTITSKM--NLSeEVDLEDFVSRPEKISAADIAAICQEAGMQAVRK 369
RecA-like_fidgetin cd19523
ATPase domain of fidgetin; Fidgetin (FIGN) is a ATP-dependent microtubule severing protein. ...
 133-296 4.79e-44

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: 151.58  E-value: 4.79e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1780598789 133 DVAGLESAKQALQEAVILPVKFPQFFTGKRRPWRAFLLYGPPGTGKSYLAKAVATEADSTFFSVSSSDLVSKWMGESEKL 212
Cdd:cd19523     1 DIAGLGALKAAIKEEVLWPLLRPDAFSGLLRLPRSILLFGPRGTGKTLLGRCLASQLGATFLRLRGSTLVAKWAGEGEKI 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1780598789 213 VSNLFEMARESAPSIIFVDEIDSLCGTRGEgnESEASRRIKTELLVQMQGV-GHNDEKVLVLAATNTPYALDQAIRRRFD 291
Cdd:cd19523    81 LQASFLAARCRQPSVLFISDLDALLSSQDD--EASPVGRLQVELLAQLDGVlGSGEDGVLVVCTTSKPEEIDESLRRYFS 158


                  ....*
gi 1780598789 292 KRIYI 296
Cdd:cd19523   159 KRLLV 163
RecA-like_CDC48_r1-like cd19519
first of two ATPase domains of CDC48 and similar ATPase domains; CDC48 in yeast and p97 or VCP ...
 133-297 2.35e-43

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: 149.51  E-value: 2.35e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1780598789 133 DVAGLESAKQALQEAVILPVKFPQFFtgKR---RPWRAFLLYGPPGTGKSYLAKAVATEADSTFFSVSSSDLVSKWMGES 209
Cdd:cd19519     1 DIGGCRKQLAQIREMVELPLRHPELF--KAigiKPPRGILLYGPPGTGKTLIARAVANETGAFFFLINGPEIMSKLAGES 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1780598789 210 EKLVSNLFEMARESAPSIIFVDEIDSLCGTRGEGNeSEASRRIKTELLVQMQGVGHNDEkVLVLAATNTPYALDQAIRR- 288
Cdd:cd19519    79 ESNLRKAFEEAEKNAPAIIFIDEIDAIAPKREKTH-GEVERRIVSQLLTLMDGLKQRAH-VIVMAATNRPNSIDPALRRf 156

                         170
                  ....*....|
gi 1780598789 289 -RFDKRIYIP 297
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 ...
 141-296 1.97e-42

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: 146.89  E-value: 1.97e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1780598789 141 KQALQEAVILPVKFPQFFTG-KRRPWRAFLLYGPPGTGKSYLAKAVATEADSTFFSVSSSDLVSKWMGESEKLVSNLFEM 219
Cdd:cd19528     2 KRELQELVQYPVEHPDKFLKfGMTPSKGVLFYGPPGCGKTLLAKAIANECQANFISVKGPELLTMWFGESEANVRDIFDK 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1780598789 220 ARESAPSIIFVDEIDSLCGTRG--EGNESEASRRIKTELLVQMQGVghNDEK-VLVLAATNTPYALDQAIRR--RFDKRI 294
Cdd:cd19528    82 ARAAAPCVLFFDELDSIAKARGgnIGDAGGAADRVINQILTEMDGM--NTKKnVFIIGATNRPDIIDPAILRpgRLDQLI 159


                  ..
gi 1780598789 295 YI 296
Cdd:cd19528   160 YI 161
hflB PRK10733
ATP-dependent zinc metalloprotease FtsH;
131-345 9.24e-41

ATP-dependent zinc metalloprotease FtsH;


Pssm-ID: 182683 [Multi-domain]  Cd Length: 644  Bit Score: 153.65  E-value: 9.24e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1780598789 131 WSDVAGLESAKQALQEAVIL---PVKFPQFftGKRRPwRAFLLYGPPGTGKSYLAKAVATEADSTFFSVSSSDLVSKWMG 207
Cdd:PRK10733  151 FADVAGCDEAKEEVAELVEYlrePSRFQKL--GGKIP-KGVLMVGPPGTGKTLLAKAIAGEAKVPFFTISGSDFVEMFVG 227

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1780598789 208 ESEKLVSNLFEMARESAPSIIFVDEIDSLCGTRGEGNESEASRRIKT--ELLVQMQGVGHNdEKVLVLAATNTPYALDQA 285
Cdd:PRK10733  228 VGASRVRDMFEQAKKAAPCIIFIDEIDAVGRQRGAGLGGGHDEREQTlnQMLVEMDGFEGN-EGIIVIAATNRPDVLDPA 306

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1780598789 286 IRR--RFDKRIYIPLPEAKARQHMFKVHLGDTPHNlTEPDFEYLGQKTEGFSGSDVSVCVKD 345
Cdd:PRK10733  307 LLRpgRFDRQVVVGLPDVRGREQILKVHMRRVPLA-PDIDAAIIARGTPGFSGADLANLVNE 367
PTZ00361 PTZ00361
26 proteosome regulatory subunit 4-like protein; Provisional
 123-311 2.07e-40

26 proteosome regulatory subunit 4-like protein; Provisional


Pssm-ID: 185575 [Multi-domain]  Cd Length: 438  Bit Score: 149.54  E-value: 2.07e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1780598789 123 VREKPNIKWSDVAGLESAKQALQEAVILPVKFPQFF--TGKRRPwRAFLLYGPPGTGKSYLAKAVATEADSTFFSVSSSD 200
Cdd:PTZ00361  174 VDKAPLESYADIGGLEQQIQEIKEAVELPLTHPELYddIGIKPP-KGVILYGPPGTGKTLLAKAVANETSATFLRVVGSE 252

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1780598789 201 LVSKWMGESEKLVSNLFEMARESAPSIIFVDEIDSLcGTRGEGNESEASRRIKT---ELLVQMQGV-GHNDEKVLVlaAT 276
Cdd:PTZ00361  253 LIQKYLGDGPKLVRELFRVAEENAPSIVFIDEIDAI-GTKRYDATSGGEKEIQRtmlELLNQLDGFdSRGDVKVIM--AT 329

                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 1780598789 277 NTPYALDQAIRR--RFDKRIYIPLPEAKARQHMFKVH 311
Cdd:PTZ00361  330 NRIESLDPALIRpgRIDRKIEFPNPDEKTKRRIFEIH 366
RecA-like_NVL_r1-like cd19518
first of two ATPase domains of NVL (nuclear VCP-like protein) and similar ATPase domains; NVL ...
 133-294 5.92e-40

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: 140.62  E-value: 5.92e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1780598789 133 DVAGLESAKQALQEAVILPVKFPQFF--TGKRRPwRAFLLYGPPGTGKSYLAKAVATEADSTFFSVSSSDLVSKWMGESE 210
Cdd:cd19518     1 DIGGMDSTLKELCELLIHPILPPEYFqhLGVEPP-RGVLLHGPPGCGKTMLANAIAGELKVPFLKISATEIVSGVSGESE 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1780598789 211 KLVSNLFEMARESAPSIIFVDEIDSLCGTRgEGNESEASRRIKTELLVQMQGVGHNDEK---VLVLAATNTPYALDQAIR 287
Cdd:cd19518    80 EKIRELFDQAISNAPCIVFIDEIDAITPKR-ESAQREMERRIVSQLLTCMDELNNEKTAggpVLVIGATNRPDSLDPALR 158


                  ....*....
gi 1780598789 288 R--RFDKRI 294
Cdd:cd19518   159 RagRFDREI 167
ftsH CHL00176
cell division protein; Validated
 129-338 1.33e-39

cell division protein; Validated


Pssm-ID: 214386 [Multi-domain]  Cd Length: 638  Bit Score: 150.20  E-value: 1.33e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1780598789 129 IKWSDVAGLESAKQALQEAVILpVKFPQFFT--GKRRPwRAFLLYGPPGTGKSYLAKAVATEADSTFFSVSSSDLVSKWM 206
Cdd:CHL00176  180 ITFRDIAGIEEAKEEFEEVVSF-LKKPERFTavGAKIP-KGVLLVGPPGTGKTLLAKAIAGEAEVPFFSISGSEFVEMFV 257

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1780598789 207 GESEKLVSNLFEMARESAPSIIFVDEIDSLCGTRGEG-----NESEasrRIKTELLVQMQGVGHNDEkVLVLAATNTPYA 281
Cdd:CHL00176  258 GVGAARVRDLFKKAKENSPCIVFIDEIDAVGRQRGAGigggnDERE---QTLNQLLTEMDGFKGNKG-VIVIAATNRVDI 333

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1780598789 282 LDQAIRR--RFDKRIYIPLPEAKARQHMFKVHLGDTPhnlTEPD--FEYLGQKTEGFSGSD 338
Cdd:CHL00176  334 LDAALLRpgRFDRQITVSLPDREGRLDILKVHARNKK---LSPDvsLELIARRTPGFSGAD 391
RecA-like_NVL_r2-like cd19530
second of two ATPase domains of NVL (nuclear VCP-like protein) and similar ATPase domains; NVL ...
 137-296 3.40e-39

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: 138.39  E-value: 3.40e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1780598789 137 LESAKQALQEAVILPVKFPQFFT--GKRRPwRAFLLYGPPGTGKSYLAKAVATEADSTFFSVSSSDLVSKWMGESEKLVS 214
Cdd:cd19530     1 LDHVREELTMSILRPIKRPDIYKalGIDLP-TGVLLYGPPGCGKTLLAKAVANESGANFISVKGPELLNKYVGESERAVR 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1780598789 215 NLFEMARESAPSIIFVDEIDSLCGTRGEGnESEASRRIKTELLVQMQGvGHNDEKVLVLAATNTPYALDQAIRR--RFDK 292
Cdd:cd19530    80 QVFQRARASAPCVIFFDEVDALVPKRGDG-GSWASERVVNQLLTEMDG-LEERSNVFVIAATNRPDIIDPAMLRpgRLDK 157


                  ....
gi 1780598789 293 RIYI 296
Cdd:cd19530   158 TLYV 161
RecA-like_PEX6_r2 cd19527
second of two ATPase domains of Peroxisomal biogenesis factor 6 (PEX6); PEX6(also known as ...
 141-296 8.85e-38

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


Pssm-ID: 410935 [Multi-domain]  Cd Length: 160  Bit Score: 134.56  E-value: 8.85e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1780598789 141 KQALQEAVILPVKFPQFFTGKRRPWRAFLLYGPPGTGKSYLAKAVATEADSTFFSVSSSDLVSKWMGESEKLVSNLFEMA 220
Cdd:cd19527     2 KKEILDTIQLPLEHPELFSSGLRKRSGILLYGPPGTGKTLLAKAIATECSLNFLSVKGPELINMYIGESEANVREVFQKA 81

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1780598789 221 RESAPSIIFVDEIDSLCGTRGEGNESEASR-RIKTELLVQMQGVGHNDEKVLVLAATNTPYALDQAIRR--RFDKRIYI 296
Cdd:cd19527    82 RDAKPCVIFFDELDSLAPSRGNSGDSGGVMdRVVSQLLAELDGMSSSGQDVFVIGATNRPDLLDPALLRpgRFDKLLYL 160
MIT_VPS4 cd02678
MIT: domain contained within Microtubule Interacting and Trafficking molecules. This ...
 4-78 4.40e-37

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: 130.08  E-value: 4.40e-37
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1780598789   4 NFKEQAIEYVKQAVHEDNAGNYNKAFPLYMNALEYFKTHLKYEKNPKIREAITQKFTEYLRRAEEIRAVLDEGGS 78
Cdd:cd02678     1 DFLQKAIELVKKAIEEDNAGNYEEALRLYQHALEYFMHALKYEKNPKSKESIRAKCTEYLDRAEKLKEYLAKKEK 75
RecA-like_PEX1_r2 cd19526
second of two ATPase domains of Peroxisomal biogenesis factor 1 (PEX1); PEX1(also known as ...
 140-295 3.24e-36

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: 130.63  E-value: 3.24e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1780598789 140 AKQALQEAVILPVKFPQFFTGKRRPWRA-FLLYGPPGTGKSYLAKAVATEADSTFFSVSSSDLVSKWMGESEKLVSNLFE 218
Cdd:cd19526     1 VKKALEETIEWPSKYPKIFASSPLRLRSgILLYGPPGCGKTLLASAIASECGLNFISVKGPELLNKYIGASEQNVRDLFS 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1780598789 219 MARESAPSIIFVDEIDSLCGTRGEGNeSEASRRIKTELLVQMQGVgHNDEKVLVLAATNTPYALDQAIRR--RFDKRIY 295
Cdd:cd19526    81 RAQSAKPCILFFDEFDSIAPKRGHDS-TGVTDRVVNQLLTQLDGV-EGLDGVYVLAATSRPDLIDPALLRpgRLDKLVY 157
RecA-like_Yta7-like cd19517
ATPase domain of Saccharomyces cerevisiae Yta7 and similar ATPase domains; Saccharomyces ...
 133-295 2.68e-35

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: 128.40  E-value: 2.68e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1780598789 133 DVAGLESAKQALQEAVILPVKFPQFFTG-KRRPWRAFLLYGPPGTGKSYLAKAVATEADS-----TFFSVSSSDLVSKWM 206
Cdd:cd19517     1 DIGGLSHYINQLKEMVFFPLLYPEVFAKfKITPPRGVLFHGPPGTGKTLMARALAAECSKggqkvSFFMRKGADCLSKWV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1780598789 207 GESEKLVSNLFEMARESAPSIIFVDEIDSLCGTRGEGNESEASRRIKTeLLVQMQGVgHNDEKVLVLAATNTPYALDQAI 286
Cdd:cd19517    81 GEAERQLRLLFEEAYRMQPSIIFFDEIDGLAPVRSSKQEQIHASIVST-LLALMDGL-DNRGQVVVIGATNRPDALDPAL 158

                         170
                  ....*....|.
gi 1780598789 287 RR--RFDKRIY 295
Cdd:cd19517   159 RRpgRFDREFY 169
Vps4_C pfam09336
Vps4 C terminal oligomerization domain; This domain is found at the C terminal of ATPase ...
 368-432 6.77e-27

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: 102.19  E-value: 6.77e-27
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1780598789 368 WMPCGPRHPGAIQTTMQDLAtkglAEKIIPPPITRTDFEKVLARQRPTVSKSDLDVHERFTQEFG 432
Cdd:pfam09336   1 LTPCSPGDPGAIEMTWMDIP----SDKLLEPPVTMKDFLKALKSSRPTVSKEDLEKYEEFTKEFG 61
AAA cd00009
The AAA+ (ATPases Associated with a wide variety of cellular Activities) superfamily ...
 135-298 2.45e-26

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: 103.77  E-value: 2.45e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1780598789 135 AGLESAKQALQEAVilpvkfpqfftgKRRPWRAFLLYGPPGTGKSYLAKAVATEA---DSTFFSVSSSDLVSKWMGESEK 211
Cdd:cd00009     1 VGQEEAIEALREAL------------ELPPPKNLLLYGPPGTGKTTLARAIANELfrpGAPFLYLNASDLLEGLVVAELF 68

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1780598789 212 ---LVSNLFEMARESAPSIIFVDEIDSLcgtrgegneseaSRRIKTELLVQMQGV---GHNDEKVLVLAATNTPYA--LD 283
Cdd:cd00009    69 ghfLVRLLFELAEKAKPGVLFIDEIDSL------------SRGAQNALLRVLETLndlRIDRENVRVIGATNRPLLgdLD 136

                         170
                  ....*....|....*
gi 1780598789 284 QAIRRRFDKRIYIPL 298
Cdd:cd00009   137 RALYDRLDIRIVIPL 151
MIT pfam04212
MIT (microtubule interacting and transport) domain; The MIT domain forms an asymmetric ...
 7-71 2.53e-21

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: 86.83  E-value: 2.53e-21
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1780598789   7 EQAIEYVKQAVHEDNAGNYNKAFPLYMNALEYFKTHLKYEKNPKIREAITQKFTEYLRRAEEIRA 71
Cdd:pfam04212   2 SKALELVKKAVEEDNAGNYEEALELYKEALDYLLLALKETKNEERRELLRAKIAEYLERAEELKE 66
MIT cd02656
MIT: domain contained within Microtubule Interacting and Trafficking molecules. The MIT domain ...
 7-74 1.47e-20

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: 85.05  E-value: 1.47e-20
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1780598789   7 EQAIEYVKQAVHEDNAGNYNKAFPLYMNALEYFKTHLKYEKNPKIREAITQKFTEYLRRAEEIRAVLD 74
Cdd:cd02656     4 QQAKELIKQAVKEDEDGNYEEALELYKEALDYLLQALKAEKEPKLRKLLRKKVKEYLDRAEFLKELLK 71
MIT smart00745
Microtubule Interacting and Trafficking molecule domain;
3-75 1.79e-20

Microtubule Interacting and Trafficking molecule domain;


Pssm-ID: 197854  Cd Length: 77  Bit Score: 85.05  E-value: 1.79e-20
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1780598789    3 SNFKEQAIEYVKQAVHEDNAGNYNKAFPLYMNALEYFKTHLKYEKNPKIREAITQKFTEYLRRAEEIRAVLDE 75
Cdd:smart00745   2 RDYLSKAKELISKALKADEAGNYEEALELYKKAIEYLLEGIKVESDSKRREALKAKAAEYLDRAEEIKKSLLE 74
AAA smart00382
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ...
 164-300 1.25e-19

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: 85.12  E-value: 1.25e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1780598789  164 PWRAFLLYGPPGTGKSYLAKAVATEADST---FFSVSSSDL--------------VSKWMGESEKLVSNLFEMARESAPS 226
Cdd:smart00382   1 PGEVILIVGPPGSGKTTLARALARELGPPgggVIYIDGEDIleevldqllliivgGKKASGSGELRLRLALALARKLKPD 80

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1780598789  227 IIFVDEIDSLCGTRGEGNESEASRRIKTELLVQmqgvghnDEKVLVLAATNTPYALDQA-IRRRFDKRIYIPLPE 300
Cdd:smart00382  81 VLILDEITSLLDAEQEALLLLLEELRLLLLLKS-------EKNLTVILTTNDEKDLGPAlLRRRFDRRIVLLLIL 148
RecA-like_Pch2-like cd19508
ATPase domain of Pachytene checkpoint 2 (Pch2) and similar ATPase domains; Pch2 (known as ...
 166-296 5.87e-17

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: 79.03  E-value: 5.87e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1780598789 166 RAFLLYGPPGTGKSYLAKAVA---------TEADSTFFSVSSSDLVSKWMGESEKLVSNLFEMARESAP---SIIFV--D 231
Cdd:cd19508    53 RLVLLHGPPGTGKTSLCKALAqklsirlssRYRYGQLIEINSHSLFSKWFSESGKLVTKMFQKIQELIDdkdALVFVliD 132

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1780598789 232 EIDSLCGTR---GEGNESEASRRIKTELLVQMQGVGHNDeKVLVLAATNTPYALDQAIRRRFDKRIYI 296
Cdd:cd19508   133 EVESLAAARsasSSGTEPSDAIRVVNAVLTQIDRIKRYH-NNVILLTSNLLEKIDVAFVDRADIKQYI 199
ycf46 CHL00195
Ycf46; Provisional
 127-340 1.75e-16

Ycf46; Provisional


Pssm-ID: 177094 [Multi-domain]  Cd Length: 489  Bit Score: 81.22  E-value: 1.75e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1780598789 127 PNIKWSDVAGLESAKQ-------ALQEAVI---LPVKfpqfftgkrrpwRAFLLYGPPGTGKSYLAKAVATEADSTFFSV 196
Cdd:CHL00195  223 VNEKISDIGGLDNLKDwlkkrstSFSKQASnygLPTP------------RGLLLVGIQGTGKSLTAKAIANDWQLPLLRL 290

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1780598789 197 SSSDLVSKWMGESEKLVSNLFEMARESAPSIIFVDEID-SLCGTRGEGnESEASRRIKTELLVQMQgvghndEK---VLV 272
Cdd:CHL00195  291 DVGKLFGGIVGESESRMRQMIRIAEALSPCILWIDEIDkAFSNSESKG-DSGTTNRVLATFITWLS------EKkspVFV 363

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1780598789 273 LAATNTPYALDQAIRR--RFDKRIYIPLPEAKARQHMFKVHLGDT-PHNLTEPDFEYLGQKTEGFSGSDVS 340
Cdd:CHL00195  364 VATANNIDLLPLEILRkgRFDEIFFLDLPSLEEREKIFKIHLQKFrPKSWKKYDIKKLSKLSNKFSGAEIE 434
RecA-like_Ycf46-like cd19507
ATPase domain of Ycf46 and similar ATPase domains; Ycf46 may play a role in the regulation of ...
 133-296 3.64e-16

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: 75.48  E-value: 3.64e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1780598789 133 DVAGLESAKQALQeavilpvKFPQFFTGKRRPW-----RAFLLYGPPGTGKSYLAKAVATEADSTFFSVSSSDLVSKWMG 207
Cdd:cd19507     1 DVGGLDNLKDWLK-------KRKAAFSKQASAYglptpKGLLLVGIQGTGKSLTAKAIAGVWQLPLLRLDMGRLFGGLVG 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1780598789 208 ESEKLVSNLFEMARESAPSIIFVDEIDSLCGTRGEGNESEASRRIKTELLVQMQgvghndEK---VLVLAATNTPYALDQ 284
Cdd:cd19507    74 ESESRLRQMIQTAEAIAPCVLWIDEIEKGFSNADSKGDSGTSSRVLGTFLTWLQ------EKkkpVFVVATANNVQSLPP 147

                         170
                  ....*....|....
gi 1780598789 285 AIRR--RFDKRIYI 296
Cdd:cd19507   148 ELLRkgRFDEIFFV 161
RecA-like_NSF-SEC18_r1-like cd19504
first of two ATPase domains of NSF and SEC18, and similar ATPase domains; ...
 166-296 3.91e-16

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: 75.99  E-value: 3.91e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1780598789 166 RAFLLYGPPGTGKSYLAKAVATEADSTFFS-VSSSDLVSKWMGESEKLVSNLFEMARE--------SAPSIIFVDEIDSL 236
Cdd:cd19504    36 KGILLYGPPGTGKTLMARQIGKMLNAREPKiVNGPEILNKYVGESEANIRKLFADAEEeqrrlganSGLHIIIFDEIDAI 115

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1780598789 237 CGTRGE-GNESEASRRIKTELLVQMQGVGHNDeKVLVLAATNTPYALDQAIRR--RFDKRIYI 296
Cdd:cd19504   116 CKQRGSmAGSTGVHDTVVNQLLSKIDGVEQLN-NILVIGMTNRKDLIDEALLRpgRLEVQMEI 177
MIT_2 cd02684
MIT: domain contained within Microtubule Interacting and Trafficking molecules. This ...
 7-73 2.93e-13

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: 64.84  E-value: 2.93e-13
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1780598789   7 EQAIEYVKQAVHEDNAGNYNKAFPLYMNALEYFKTHLKYEKNPKIREAITQKFTEYLRRAEEIRAVL 73
Cdd:cd02684     4 EKAIALVVQAVKKDQRGDAAAALSLYCSALQYFVPALHYETDAQRKEALRQKVLQYVSRAEELKALI 70
RecA-like_BCS1 cd19510
Mitochondrial chaperone BCS1; Mitochondrial chaperone BCS1 is necessary for the assembly of ...
 155-296 3.69e-13

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: 66.61  E-value: 3.69e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1780598789 155 PQFFTGKRRPW-RAFLLYGPPGTGKSYLAKAVATEADSTFFSVSSSDLVSkwmgeSEKLVSNLfeMARESAPSIIFVDEI 233
Cdd:cd19510    12 EDWYNDRGIPYrRGYLLYGPPGTGKSSFIAALAGELDYDICDLNLSEVVL-----TDDRLNHL--LNTAPKQSIILLEDI 84

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1780598789 234 DSLCGTR----GEGNESEASRRIK-TELLVQMQGVGHNDEKVLVLaATNTPYALDQAIRR--RFDKRIYI 296
Cdd:cd19510    85 DAAFESRehnkKNPSAYGGLSRVTfSGLLNALDGVASSEERIVFM-TTNHIERLDPALIRpgRVDMKIYM 153
RecA-like_ATAD3-like cd19512
ATPase domains of ATPase AAA-domain protein 3A (ATAD3A), -3B, and -3C, and similar ATPase ...
 162-294 7.02e-13

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: 66.01  E-value: 7.02e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1780598789 162 RRPWRAFLLYGPPGTGKSYLAKAVATEADSTFFSVSSSDLVSkwMG-ESEKLVSNLFEMARESAPS-IIFVDEIDSLCGT 239
Cdd:cd19512    19 KGLYRNILFYGPPGTGKTLFAKKLALHSGMDYAIMTGGDVAP--MGrEGVTAIHKVFDWANTSRRGlLLFVDEADAFLRK 96

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1780598789 240 RGEGNESEASRRIKTELLVQMqgvGHNDEKVLVLAATNTPYALDQAIRRRFDKRI 294
Cdd:cd19512    97 RSTEKISEDLRAALNAFLYRT---GEQSNKFMLVLASNQPEQFDWAINDRIDEMV 148
MIT_SNX15 cd02677
MIT: domain contained within Microtubule Interacting and Trafficking molecules. This MIT ...
 7-69 3.83e-09

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: 53.12  E-value: 3.83e-09
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1780598789   7 EQAIEYVKQAVHEDNAGNYNKAFPLYMNALEYFKTHLKYEKNPKIREAITQKFTEYLRRAEEI 69
Cdd:cd02677     4 EQAAELIRLALEKEEEGDYEAAFEFYRAGVDLLLKGVQGDSSPERREAVKRKIAEYLKRAEEI 66
RecA-like_Ycf2 cd19505
ATPase domain of plant YCF2; Ycf2 is a chloroplast ATPase which has an essential function; ...
 164-296 3.92e-09

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: 55.46  E-value: 3.92e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1780598789 164 PWRAFLLYGPPGTGKSYLAKAVATEADSTFFSVSSSDLVSKW--------------MGESEKLVSNLFEMARESAPSIIF 229
Cdd:cd19505    11 PSKGILLIGSIETGRSYLIKSLAANSYVPLIRISLNKLLYNKpdfgnddwidgmliLKESLHRLNLQFELAKAMSPCIIW 90

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1780598789 230 VDEIDSLcGTRGEGNESEASRRIKTELLVQMqgVGHNDEK-----VLVLAATNTPYALDQAI--RRRFDKRIYI 296
Cdd:cd19505    91 IPNIHEL-NVNRSTQNLEEDPKLLLGLLLNY--LSRDFEKsstrnILVIASTHIPQKVDPALiaPNRLDTCINI 161
RecA-like_IQCA1 cd19506
ATPase domain of IQ and AAA domain-containing protein 1 (IQCA1); IQCA1 (also known as dynein ...
 166-294 4.53e-09

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: 55.23  E-value: 4.53e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1780598789 166 RAFLLYGPPGTGKSYLAKAVATEADSTFFSVSSSDLVSKWMGES--EKLVSNLFEMARESAPSIIFVDEIDSLCGTRGEG 243
Cdd:cd19506    27 KSLLLAGPSGVGKKMLVHAICTETGANLFNLSPSNIAGKYPGKNglQMMLHLVLKVARQLQPSVIWIGDAEKTFYKKVPK 106

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1780598789 244 NESEAS-RRIKTELLVQMQGVGHNDeKVLVLAATNTPYALDQAIRRRFDKRI 294
Cdd:cd19506   107 TEKQLDpKRLKKDLPKILKSLKPED-RVLIVGTTSRPFEADLKSFCKVYNKI 157
T7SS_EccA TIGR03922
type VII secretion AAA-ATPase EccA; This model represents the AAA family ATPase, EccA, of the ...
 169-297 1.00e-08

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: 57.16  E-value: 1.00e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1780598789 169 LLYGPPGTGKSYLAKAVATE-------ADSTFFSVSSSDLVSKWMGESEKLVSNLFEMAREsapSIIFVDEIDSLCGTRG 241
Cdd:TIGR03922 316 LFAGPPGTGKTTIARVVAKIycglgvlRKPLVREVSRADLIGQYIGESEAKTNEIIDSALG---GVLFLDEAYTLVETGY 392

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1780598789 242 EGNESEASRRIKTeLLVQMQgvGHNDEKVLVLAAtntpYALD--------QAIRRRFDKRIYIP 297
Cdd:TIGR03922 393 GQKDPFGLEAIDT-LLARME--NDRDRLVVIGAG----YRKDldkflevnEGLRSRFTRVIEFP 449
AAA_5 pfam07728
AAA domain (dynein-related subfamily); This Pfam entry includes some of the AAA proteins not ...
 168-290 2.08e-07

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


Pssm-ID: 400191 [Multi-domain]  Cd Length: 135  Bit Score: 49.60  E-value: 2.08e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1780598789 168 FLLYGPPGTGKSYLAK--AVATEADSTFF-----SVSSSDLVSKW---MGESEKLVSNLFEMARESApsIIFVDEIDslc 237
Cdd:pfam07728   2 VLLVGPPGTGKTELAErlAAALSNRPVFYvqltrDTTEEDLFGRRnidPGGASWVDGPLVRAAREGE--IAVLDEIN--- 76

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1780598789 238 gtrgegnesEASRRIKTEL--------LVQMQG---VGHNDEKVLVLAATNTPYA----LDQAIRRRF 290
Cdd:pfam07728  77 ---------RANPDVLNSLlsllderrLLLPDGgelVKAAPDGFRLIATMNPLDRglneLSPALRSRF 135
PRK13342 PRK13342
recombination factor protein RarA; Reviewed
 168-233 1.91e-06

recombination factor protein RarA; Reviewed


Pssm-ID: 237355 [Multi-domain]  Cd Length: 413  Bit Score: 49.70  E-value: 1.91e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1780598789 168 FLLYGPPGTGKSYLAKAVATEADSTFFSVSSS-----DLvskwmgesEKLVSNLFEMARESAPSIIFVDEI 233
Cdd:PRK13342   39 MILWGPPGTGKTTLARIIAGATDAPFEALSAVtsgvkDL--------REVIEEARQRRSAGRRTILFIDEI 101
RarA COG2256
Replication-associated recombination protein RarA (DNA-dependent ATPase) [Replication, ...
 168-233 7.47e-06

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


Pssm-ID: 441857 [Multi-domain]  Cd Length: 439  Bit Score: 48.13  E-value: 7.47e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1780598789 168 FLLYGPPGTGKSYLAKAVATEADSTFFSVS--SS---DLvskwmgesEKLVSNLFEMARESAPSIIFVDEI 233
Cdd:COG2256    52 MILWGPPGTGKTTLARLIANATDAEFVALSavTSgvkDI--------REVIEEARERRAYGRRTILFVDEI 114
PRK04195 PRK04195
replication factor C large subunit; Provisional
 132-254 2.49e-05

replication factor C large subunit; Provisional


Pssm-ID: 235250 [Multi-domain]  Cd Length: 482  Bit Score: 46.45  E-value: 2.49e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1780598789 132 SDVAGLESAKQALQEAVIlpvKFPqfftgKRRPWRAFLLYGPPGTGKSYLAKAVATEADSTFFSVSSSD-----LVSKWM 206
Cdd:PRK04195   14 SDVVGNEKAKEQLREWIE---SWL-----KGKPKKALLLYGPPGVGKTSLAHALANDYGWEVIELNASDqrtadVIERVA 85

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 1780598789 207 GESEKlVSNLFEMAResapSIIFVDEIDSLCGTRGEGNESEASRRIKT 254
Cdd:PRK04195   86 GEAAT-SGSLFGARR----KLILLDEVDGIHGNEDRGGARAILELIKK 128
ruvB PRK00080
Holliday junction branch migration DNA helicase RuvB;
169-236 3.40e-05

Holliday junction branch migration DNA helicase RuvB;


Pssm-ID: 234619 [Multi-domain]  Cd Length: 328  Bit Score: 45.51  E-value: 3.40e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1780598789 169 LLYGPPGTGKSYLAKAVATEADSTFFSVS------SSDLVSkwmgesekLVSNLFEMaresapSIIFVDEIDSL 236
Cdd:PRK00080   55 LLYGPPGLGKTTLANIIANEMGVNIRITSgpalekPGDLAA--------ILTNLEEG------DVLFIDEIHRL 114
AAA_2 pfam07724
AAA domain (Cdc48 subfamily); This Pfam entry includes some of the AAA proteins not detected ...
 168-234 3.47e-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: 44.11  E-value: 3.47e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1780598789 168 FLLYGPPGTGKSYLAKAVA----------TEADSTFFSVSSSdlVSKWMGESEKLVS-----NLFEMARESAPSIIFVDE 232
Cdd:pfam07724   6 FLFLGPTGVGKTELAKALAellfgderalIRIDMSEYMEEHS--VSRLIGAPPGYVGyeeggQLTEAVRRKPYSIVLIDE 83


                  ..
gi 1780598789 233 ID 234
Cdd:pfam07724  84 IE 85
MIT_1 cd02683
MIT: domain contained within Microtubule Interacting and Trafficking molecules. This ...
 7-74 5.87e-05

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: 41.26  E-value: 5.87e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1780598789   7 EQAIEYVKQAVHEDNAGNYNKAFPLYMNALEYFKTHLKYEKNPKIREAITQKFTEYLRRAEEIRAVLD 74
Cdd:cd02683     4 LAAKEVLKRAVELDQEGRFQEALVCYQEGIDLLMQVLKGTKDEAKKKNLRQKISEYMDRAEAIKKRLD 71
TIP49 pfam06068
TIP49 P-loop domain; This family consists of the C-terminal region of several eukaryotic and ...
 166-216 8.85e-05

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: 44.22  E-value: 8.85e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1780598789 166 RAFLLYGPPGTGKSYLAKAVATE--ADSTFFSVSSSDLVSKWMGESEKLVSNL 216
Cdd:pfam06068  51 RAVLIAGPPGTGKTALAIAISKElgEDTPFTSISGSEVYSLEMKKTEALTQAF 103
DnaC COG1484
DNA replication protein DnaC [Replication, recombination and repair];
169-202 2.73e-04

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


Pssm-ID: 441093 [Multi-domain]  Cd Length: 242  Bit Score: 42.46  E-value: 2.73e-04
                          10        20        30
                  ....*....|....*....|....*....|....*....
gi 1780598789 169 LLYGPPGTGKSYLAKAVATEA-----DSTFFSVssSDLV 202
Cdd:COG1484   103 ILLGPPGTGKTHLAIALGHEAcragyRVRFTTA--PDLV 139
RecA-like_HslU cd19498
ATP-dependent protease ATPase subunit HslU; HslU is a component of the ATP-dependent protease ...
 169-250 3.89e-04

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: 41.21  E-value: 3.89e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1780598789 169 LLYGPPGTGKSYLAKAVATEADSTFFSVSSSDLVSkwMGESEKLVSNlfeMARESAPSIIFVDEIDSLCgTRGEGNESEA 248
Cdd:cd19498    50 LMIGPTGVGKTEIARRLAKLAGAPFIKVEATKFTE--VGYVGRDVES---IIRDLVEGIVFIDEIDKIA-KRGGSSGPDV 123


                  ..
gi 1780598789 249 SR 250
Cdd:cd19498   124 SR 125
RecA-like_ClpB_Hsp104-like cd19499
Chaperone protein ClpB/Hsp104 subfamily; Bacterial Caseinolytic peptidase B (ClpB) and ...
 134-234 4.70e-04

Chaperone protein ClpB/Hsp104 subfamily; Bacterial Caseinolytic peptidase B (ClpB) and eukaryotic Heat shock protein 104 (Hsp104) are ATP-dependent molecular chaperones and essential proteins of the heat-shock response. ClpB/Hsp104 ATPases, in concert with the DnaK/Hsp70 chaperone system, disaggregate and reactivate aggregated proteins. This RecA-like_ClpB_Hsp104_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: 410907 [Multi-domain]  Cd Length: 178  Bit Score: 41.01  E-value: 4.70e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1780598789 134 VAGLESAKQALQEAVILPVkfpqffTGKRRPWR---AFLLYGPPGTGKSYLAKAVA-----TEADSTFFSVSS---SDLV 202
Cdd:cd19499    13 VVGQDEAVKAVSDAIRRAR------AGLSDPNRpigSFLFLGPTGVGKTELAKALAellfgDEDNLIRIDMSEymeKHSV 86

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 1780598789 203 SKWMGESEKLVSN-----LFEMARESAPSIIFVDEID 234
Cdd:cd19499    87 SRLIGAPPGYVGYteggqLTEAVRRKPYSVVLLDEIE 123
Mg_chelatase pfam01078
Magnesium chelatase, subunit ChlI; Magnesium-chelatase is a three-component enzyme that ...
 131-187 8.25e-04

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: 40.60  E-value: 8.25e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1780598789 131 WSDVAGLESAKQALQEAVIlpvkfpqfftGKRRpwraFLLYGPPGTGKSYLAKAVAT 187
Cdd:pfam01078   2 LADVKGQEQAKRALEIAAA----------GGHN----LLMIGPPGSGKTMLAKRLPG 44
TIP49 COG1224
DNA helicase TIP49, TBP-interacting protein [Transcription];
166-212 8.82e-04

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


Pssm-ID: 440837 [Multi-domain]  Cd Length: 452  Bit Score: 41.49  E-value: 8.82e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 1780598789 166 RAFLLYGPPGTGKSYLAKAVATE--ADSTFFSVSSSDLVSKWMGESEKL 212
Cdd:COG1224    65 KGILIVGPPGTGKTALAVAIARElgEDTPFVAISGSEIYSAELKKTEFL 113
IS21_help_AAA NF038214
IS21-like element helper ATPase IstB; This protein family model resembles PF01695, but was ...
 169-189 1.19e-03

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


Pssm-ID: 439516  Cd Length: 232  Bit Score: 40.15  E-value: 1.19e-03
                          10        20
                  ....*....|....*....|.
gi 1780598789 169 LLYGPPGTGKSYLAKAVATEA 189
Cdd:NF038214   94 LLLGPPGTGKTHLAIALGYAA 114
PRK08116 PRK08116
hypothetical protein; Validated
 168-188 1.50e-03

hypothetical protein; Validated


Pssm-ID: 236153 [Multi-domain]  Cd Length: 268  Bit Score: 40.00  E-value: 1.50e-03
                          10        20
                  ....*....|....*....|.
gi 1780598789 168 FLLYGPPGTGKSYLAKAVATE 188
Cdd:PRK08116  117 LLLWGSVGTGKTYLAACIANE 137
McrB COG1401
5-methylcytosine-specific restriction endonuclease McrBC, GTP-binding regulatory subunit McrB ...
 4-186 1.54e-03

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


Pssm-ID: 441011 [Multi-domain]  Cd Length: 477  Bit Score: 40.91  E-value: 1.54e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1780598789   4 NFKEQAIEYVKQAVHEDNAGNYNKAFPLYMNALEYFKTHLKYEKNPKI---REAITQKFTEYLRRAEEIRAVLDEGGSGP 80
Cdd:COG1401    48 ERLSEELLRADRAARATELVEELSAALEVVVLLLDLEKVELNEKLALSeaaVAIEELYELEADSEIEAVGLLLELAERSD 127

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1780598789  81 GSNGDAAVATRPKTKPKDGEGGGKDGEDPEQSKLRAGLNSAIVREKPNIKWSDVAGLESAKQalQEAVILPVKFPQFFTG 160
Cdd:COG1401   128 ALEALERARLLLELADLEERAALETEVLEALEAELEELLAAPEDLSADALAAELSAAEELYS--EDLESEDDYLKDLLRE 205

                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 1780598789 161 KRRPW-RAFL----------LYGPPGTGKSYLAKAVA 186
Cdd:COG1401   206 KFEETlEAFLaalktkknviLAGPPGTGKTYLARRLA 242
AAA_lid_3 pfam17862
AAA+ lid domain; This entry represents the alpha helical AAA+ lid domain that is found to the ...
 323-358 1.76e-03

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: 35.98  E-value: 1.76e-03
                          10        20        30
                  ....*....|....*....|....*....|....*.
gi 1780598789 323 DFEYLGQKTEGFSGSDVSVCVKDVLFEPVRKTQDAM 358
Cdd:pfam17862   3 DLEELAERTEGFSGADLEALCREAALAALRRGLEAV 38
MIT_AAA_Arch cd02682
MIT: domain contained within Microtubule Interacting and Trafficking molecules. This ...
 4-73 1.80e-03

MIT: domain contained within Microtubule Interacting and Trafficking molecules. This sub-family of MIT domains is found in mostly archaebacterial AAA-ATPases. The molecular function of the MIT domain is unclear.


Pssm-ID: 239145  Cd Length: 75  Bit Score: 37.12  E-value: 1.80e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1780598789   4 NFKEQAIEYVKQAVHEDNAGNYNKAFPLYMNALEYFKTHLKYEKNPKIREAITQKFTEYLRRAEEIRAVL 73
Cdd:cd02682     1 MLEEMARKYAINAVKAEKEGNAEDAITNYKKAIEVLSQIVKNYPDSPTRLIYEQMINEYKRRIEVLEKQN 70
DnaX COG2812
DNA polymerase III, gamma/tau subunits [Replication, recombination and repair];
130-186 2.19e-03

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


Pssm-ID: 442061 [Multi-domain]  Cd Length: 340  Bit Score: 39.79  E-value: 2.19e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1780598789 130 KWSDVAGLESAKQALQEAVILPvKFPQfftgkrrpwrAFLLYGPPGTGKSYLAKAVA 186
Cdd:COG2812     8 TFDDVVGQEHVVRTLKNALASG-RLAH----------AYLFTGPRGVGKTTLARILA 53
clpA PRK11034
ATP-dependent Clp protease ATP-binding subunit; Provisional
 169-292 2.70e-03

ATP-dependent Clp protease ATP-binding subunit; Provisional


Pssm-ID: 236828 [Multi-domain]  Cd Length: 758  Bit Score: 40.21  E-value: 2.70e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1780598789 169 LLYGPPGTGKSYLAKAVATE----------ADSTFFSVSSSDLV--SKWMGESEKLVSNLFEMARESAPSIIFVDEIDSL 236
Cdd:PRK11034  211 LLVGESGVGKTAIAEGLAWRivqgdvpevmADCTIYSLDIGSLLagTKYRGDFEKRFKALLKQLEQDTNSILFIDEIHTI 290

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1780598789 237 CGT-RGEGNESEASRRIKTELlvqmqgvghNDEKVLVLAAT-----NTPYALDQAIRRRFDK 292
Cdd:PRK11034  291 IGAgAASGGQVDAANLIKPLL---------SSGKIRVIGSTtyqefSNIFEKDRALARRFQK 343
RuvB_N pfam05496
Holliday junction DNA helicase RuvB P-loop domain; The RuvB protein makes up part of the ...
 169-233 5.85e-03

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


Pssm-ID: 398900 [Multi-domain]  Cd Length: 159  Bit Score: 37.48  E-value: 5.85e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1780598789 169 LLYGPPGTGKSYLAKAVATEADSTFFSVS------SSDLVSkwmgesekLVSNLFEMaresapSIIFVDEI 233
Cdd:pfam05496  37 LLYGPPGLGKTTLANIIANEMGVNIRITSgpaierPGDLAA--------ILTNLEPG------DVLFIDEI 93
PRK06851 PRK06851
hypothetical protein; Provisional
 166-200 6.10e-03

hypothetical protein; Provisional


Pssm-ID: 235878  Cd Length: 367  Bit Score: 38.79  E-value: 6.10e-03
                          10        20        30
                  ....*....|....*....|....*....|....*....
gi 1780598789 166 RAFLLYGPPGTGKSYLAKAVATEADSTFFSV----SSSD 200
Cdd:PRK06851   31 RIFILKGGPGTGKSTLMKKIGEEFLEKGYDVeflhCSSD 69
COG1373 COG1373
Predicted ATPase, AAA+ superfamily [General function prediction only];
166-233 7.24e-03

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


Pssm-ID: 440984 [Multi-domain]  Cd Length: 405  Bit Score: 38.39  E-value: 7.24e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1780598789 166 RAFLLYGPPGTGKSYLAKAVATEADST-FFSVSSSDLVSKWMGESEKLVSNLFEMARESAPsiIFVDEI 233
Cdd:COG1373    21 KAVVITGPRQVGKTTLLKQLAKELENIlYINLDDPRLRALAEEDPDDLLEALKELYPGKTY--LFLDEI 87
IstB_IS21 pfam01695
IstB-like ATP binding protein; This protein contains an ATP/GTP binding P-loop motif. It is ...
 169-244 9.59e-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: 37.42  E-value: 9.59e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1780598789 169 LLYGPPGTGKSYLAKAVATEA----DSTFFsVSSSDLVSKWMGESE--KLVSNLFEMAResaPSIIFVDEIDSLCGTRGE 242
Cdd:pfam01695  96 VLLGPPGVGKTHLAIALGVEAcragYSVRF-TSAADLVNQLKRAHGdgKLTRKLQQLLK---PDVLILDEWGYLPLDQAE 171


                  ..
gi 1780598789 243 GN 244
Cdd:pfam01695 172 AN 173
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH